ID AM406670; SV 1; circular; genomic DNA; STD; PRO; 4376040 BP. XX AC AM406670; XX PR Project:PRJNA13217; XX DT 19-DEC-2006 (Rel. 90, Created) DT 05-NOV-2010 (Rel. 106, Last updated, Version 2) XX DE Azoarcus sp. BH72, complete genome XX KW complete genome. XX OS Azoarcus sp. BH72 OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. XX RN [1] RP 1-4376040 RA Reinhold-Hurek B., Krause A.; RT ; RL Submitted (19-SEP-2006) to the INSDC. RL Reinhold-Hurek B., Krause A., University of Bremen, General Microbiology, RL PO. Box 33 04 40, D-28334 Bremen, GERMANY. XX RN [2] RP 1-4376040 RX DOI; 10.1038/nbt1243. RX PUBMED; 17057704. RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. RT strain BH72"; RL Nat. Biotechnol. 24(11):1385-1391(2006). XX DR GR; AM406670_GR. DR RFAM; RF00001; 5S_rRNA. DR RFAM; RF00005; tRNA. DR RFAM; RF00010; RNaseP_bact_a. DR RFAM; RF00013; 6S. DR RFAM; RF00023; tmRNA. DR RFAM; RF00059; TPP. DR RFAM; RF00140; Alpha_RBS. DR RFAM; RF00169; Bacteria_small_SRP. DR RFAM; RF00174; Cobalamin. DR RFAM; RF00177; SSU_rRNA_bacteria. DR RFAM; RF00504; Glycine. DR RFAM; RF01057; SAH_riboswitch. DR RFAM; RF01086; LR-PK1. DR RFAM; RF01118; PK-G12rRNA. DR RFAM; RF01854; Bacteria_large_SRP. DR SILVA-LSU; AM406670. DR SILVA-SSU; AM406670. DR StrainInfo; 49226; 0. XX FH Key Location/Qualifiers FH FT source 1..4376040 FT /organism="Azoarcus sp. BH72" FT /strain="BH72" FT /mol_type="genomic DNA" FT /db_xref="taxon:62928" FT CDS 1..1443 FT /transl_table=11 FT /gene="dnaA" FT /locus_tag="azo0001" FT /product="chromosomal replication initiator protein" FT /function="ATPase involved in DNA replication initiation" FT /note="Chromosomal replication initiator protein dnaA. FT Plays an important role in the initiation and regulation of FT chromosomal replication. Binds to the origin of FT replication; it binds specifically double-stranded DNA at a FT 9 bp consensus (dnaA box): 5-TTATC(C/A)A(C/A)A-3. DnaA FT binds to ATP and to acidic phospholipids (By similarity). FT InterPro: Bacterial chromosomal replication initiator FT protein DnaA" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1B4" FT /db_xref="InterPro:IPR001957" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR010921" FT /db_xref="InterPro:IPR013159" FT /db_xref="InterPro:IPR013317" FT /db_xref="InterPro:IPR018312" FT /db_xref="InterPro:IPR020591" FT /db_xref="UniProtKB/Swiss-Prot:A1K1B4" FT /protein_id="CAL92619.1" FT /translation="MNQDFWPFCLARLEQELPQQQFNTWIKTLQAAESDADGAVALTLT FT APNRFVLQWVRERYMRRIGELGEEFHGQPIQLELQLPVAGAKSAPVAPARVRPAGANGG FT AAANSPMAPPVSEAAPPQIIVRPSEPEPVSANELAYDKTRLNADFTFDTLVTGRANDLA FT RAAAMQVAQNPGTSYNPLFVYGGVGLGKTHLVHAIGNAVYRHNPRMVIRYVHVEDYYAD FT VVRAYQQKSFDAFKRYYRSLDMLIIDDIQFFNNKNRTQEEFFHAFNALTEAKKQIVITC FT DTYPKDIQGLEDRLISRFDWGLTVQIEPPELEMRVAILQKKAEALRVSVDDDVAFLIAK FT NLRSNVRELEGALNKVVAYARFHGRGISLEVAKEALKDLLHAHNRQLSIEHIQKTVADY FT YKIKVADMHSKKRTRVIARPRQVAMWLAKELTPMSLPAIGEAFGGRDHTTVLHACRTIT FT ELRLGDHQLNHDVHVLTQVLRG" FT CDS 1502..2611 FT /transl_table=11 FT /gene="dnaN" FT /locus_tag="azo0002" FT /product="DNA-directed DNA polymerase" FT /function="DNA polymerase sliding clamp subunit (PCNA FT homolog)" FT /EC_number="2.7.7.7" FT /note="DNA polymerase III beta chain (EC 2.7.7.7). DNA FT polymerase III is a complex multichain enzyme responsible FT for most of the replicative synthesis in bacteria. This DNA FT polymerase also exhibits 3 to 5 exonuclease activity. The FT beta chain is required for initiation of replication once FT it is clamped onto DNA It slides freely (bidirectional and FT ATP- independent) along duplex DNA (By similarity). FT InterPro: DNA polymerase III beta chain dnan: DNA FT polymerase III beta subunit" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1B5" FT /db_xref="InterPro:IPR001001" FT /db_xref="InterPro:IPR022634" FT /db_xref="InterPro:IPR022635" FT /db_xref="InterPro:IPR022637" FT /db_xref="InterPro:IPR024693" FT /db_xref="UniProtKB/TrEMBL:A1K1B5" FT /protein_id="CAL92620.1" FT /translation="MLLLNTTRDALLAPLQSVAGIVEKRHTLPILSNVLIEKRGDQLTL FT LATDIEIQIRTTTAGHIGGEDSSITVGARKLQDILRALSDSVDIVLTLEDKRLTVKAGK FT SRFQLQTLPAADYPRMNLPDGDAVRFSVPQRAFKRQLAQVSYSMAQQDIRYYLNGLLLI FT ADGSELRMVATDGHRLAYAAGDLAVPVQARTEAILPRKTVLELARQLADTDDPLEIILA FT GNQAVFRFGSIELVTKLIDGKFPDYERVIPQNHPRMVTFDRQPLLASLQRAAILTNEKF FT RGVRMVLGEGALKIISSNTEQEEAQEELEIDYHDTPLDIGFNVTYLLDVLNNLSSEQVE FT WRFNDGNSSALVTLPGNDKFKYVVMPMRI" FT CDS 2821..5310 FT /transl_table=11 FT /gene="gyrB" FT /locus_tag="azo0003" FT /product="DNA topoisomerase (ATP-hydrolysing)" FT /function="DNA gyrase (topoisomerase II) B subunit" FT /EC_number="5.99.1.3" FT /note="DNA gyrase subunit B (EC 5.99.1.3). DNA gyrase FT negatively supercoils closed circular double- stranded DNA FT in an ATP-dependent manner and also catalyzes the FT interconversion of other topological isomers of FT double-stranded DNA rings including catenanes and knotted FT rings. InterPro: DNA topoisomerase II recJ: FT single-stranded-DNA-specific ex" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1B6" FT /db_xref="InterPro:IPR001241" FT /db_xref="InterPro:IPR002288" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR011557" FT /db_xref="InterPro:IPR013506" FT /db_xref="InterPro:IPR013759" FT /db_xref="InterPro:IPR013760" FT /db_xref="InterPro:IPR014721" FT /db_xref="InterPro:IPR018522" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/TrEMBL:A1K1B6" FT /protein_id="CAL92621.1" FT /translation="MSEPQNTPAPSGNDYDESSIQQLEGLEAVRKRPGMYIGDTSDGTG FT LHHMVFEVVDNAIDEALAGHCDDIVITIHADNSISVTDNGRGIPVGVKMDDKHEPKRSA FT AEIVMCVLHAGGKFNQNSYKVSGGLHGVGVSCVNALSKWLRLTIRRDGKKHFMEFHRGA FT PQDRVIDVVDGVEVSPLKVLGETSKRGTEVHYLADEEIFGTVEYHYEILAKRLRELSFL FT NNGVKIRLVDQRTGKEEDFAFAGGVRGFVEYINRTKAVLHPSVFYAAGTTRIPTGAGEA FT ELSVEVAMQWNDSYAEQVLCYTNNIPQADGGTHLTGLRTAMTRVINKYIEENEIAKKAK FT VDITGDDMREGLACVLSVKMPDPKFASQTKMKLVSSEARPAVEEVVAAKLTDFLLENPI FT DAKTICNKIVEAARARDAARKAREMTRRKGVLDGVGLPGKLADCQEKDPALSELYLVEG FT DSAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKLLQSQEIATLITALGTSIGKDDYK FT PEKLRYHRIILMTDADVDGAHIRTLLLTFFYRQMPELVERGHIYIAQPPLYKIKHGKTE FT LYIKDDHELNGHLLKLALDGAVLVPREGADAITDDALGGLARSYLLAEAVIKRLASYID FT PEVLQAMLAHDLEISLDDEAAARASADRIQPHLPEGLRIYAEYHEETEAWRLTIERLHH FT GNLKFGWVETAFLVSGDYRSIRTAAASIAGLIGPGAEIRRGEKRQTVTRFADAITWLLA FT EVERGLSKQRYKGLGEMNPEQLWETTMDPAVRRLLRVQIDDAIAADEIFTTLMGDNVEP FT RRAFIESNALYAQNIDV" FT CDS 5505..7346 FT /transl_table=11 FT /gene="hsdM" FT /locus_tag="azo0004" FT /product="Site-specific DNA-methyltransferase FT (adenine-specific)" FT /function="Type I restriction-modification system FT methyltransferase subunit" FT /EC_number="2.1.1.72" FT /note="METHYLATION OF SPECIFIC ADENINE RESIDUES; REQUIRED FT FOR BOTH RESTRICTION AND MODIFICATION ACTIVITIES (BY FT SIMILARITY), TREMBL:Q7VCN2 (55% identity). InterPro FT (IPR002296): N6 adenine-specific DNA methyltransferase,N12 FT class. InterPro (IPR003356): N-6 DNA methylase. InterPro FT (IPR003665): Type I restriction-modification system M FT subunit. Pfam (PF02384): N-6 DNA Methylase. Pfam (PF02506): FT Type I restriction modification system, M protein." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1B7" FT /db_xref="InterPro:IPR002052" FT /db_xref="InterPro:IPR002296" FT /db_xref="InterPro:IPR003356" FT /db_xref="InterPro:IPR022749" FT /db_xref="UniProtKB/TrEMBL:A1K1B7" FT /protein_id="CAL92622.1" FT /translation="MNHQALSSFIWSVADLLRGDYKQSEYGKVILPFTVLRRLDCVLEA FT TKPSVLAELEAKTKAGLNPDPFLLRKSGQSFYNTAPLDLVKLLGDQDHIRQNLYTYVQA FT FSPAARDIFERFDFFTQVERLAKANLLYLVTEKFANIDLHPEAVDNTSMGLVFEELIRK FT FAEISNETAGEHFTPREVIRLMVNLLFIEDDDVLTPGNAVVRTIYDPTAGTGGMLSVAG FT EFLLEHNPQARLTMFGQELNDESYAICKADMLIKGQDVANIVAGNTLSDDGHGARKFDY FT MLSNPPFGVEWKKVEKAVRQEHEQKGFDGRFGPGLPRVSDGSMLFLMHLLSKMRPAQDG FT GSRFGIVLNGSPLFTGGAGSGESEIRRYVLENDLVEAIVGLPTDMFYNTGIATYVWIIS FT NRKKADRKGQVQLIDASSFWQKMRKSLGSKRKEMSDAHIATVTRLFGSFTEAEYITVFD FT AAGQQLGEPQLVTNTDTPPKAPEGGRLKRVPIARIFRNQDFGYTTITVERPLKDEAGKP FT VLGSKGARRGKPQADSALRDTENVPLGEDISAYFKREVLPHAPDAWIDETKSKVGYEIP FT FNRHFYVFEPPRSLHAIDEELKTVSANIMKMLEGLAE" FT CDS 7453..8910 FT /transl_table=11 FT /gene="mloB" FT /locus_tag="azo0005" FT /product="putative restriction modification gene" FT /function="predicted transcriptional regulator containing FT an HTH domain and an uncharacterized domain shared with the FT mammalian protein Schlafen" FT /note="Putative restriction modification gene," FT /note="Function unclear" FT /db_xref="GOA:A1K1B8" FT /db_xref="InterPro:IPR007421" FT /db_xref="UniProtKB/TrEMBL:A1K1B8" FT /protein_id="CAL92623.1" FT /translation="MTKHWLKQAQAWLKASREPVPHEINELDWKADISGNKERLIEHLI FT AFANHPNGGYLVFGIQDSGAELIGVSQSQVEEIVSRLTNLGRDAIEPPLLLDHAVVEQD FT GTPLLFVHVREQPNKPAHRRGKTIEDAWVRSGGTTRAASRNEIGSLMLHSQAPSWETLR FT ASALLPAEEVLARLDLPSIAKLLQRPLPEDPAELMHWLADEGMVVADGNGYYITNLGGI FT AAARELDQFESLARKRIRVIHYRGTNKIDTIDELLGHKGYAVGFEGLIGYLKRLLPHSE FT VIQQSLREQVTVYPEIALRELIANALIHQDFSVTGAGPTIEIFDDRISFTNPGTLLPSK FT RLDRLIGTTPESRNERLASKFRLYRICEERGTGFQKIVAAVEIFGLPPVSFKPLENAFQ FT VTLHAPRKFADMSQAERIEACYQHAVLQYFSSQTLTNTTLRTRFKVSERQRNQITNLIA FT DAVEAGRIKRKDETSGNKFAEYLPYWA" FT CDS 8919..9038 FT /transl_table=11 FT /locus_tag="azo0006" FT /product="hypothetical protein predicted by FT Glimmer/Critica" FT /note="Hypothetical protein predicted by Glimmer/Critica. FT No homology to the data bank no domains predicted no signal FT peptide no TMHS" FT /db_xref="UniProtKB/TrEMBL:A1K1B9" FT /protein_id="CAL92624.1" FT /translation="MMKHPDRRAHPRPCSLHAIDEELKTVSANIMKMLEGLAE" FT CDS 9035..10384 FT /transl_table=11 FT /gene="hsdS" FT /locus_tag="azo0007" FT /product="Type I site-specific deoxyribonuclease" FT /function="Restriction endonuclease S subunits" FT /EC_number="3.1.21.3" FT /note="S subunit, DNA SPECIFICITY SUBUNIT REQUIRED FOR FT RESTRICTION AND MODIFICATION, TREMBL:Q9AAH7 (31% identity); FT TREMBL:Q8PIJ8 (28% identity). Pfam (PF01420): Type I FT restriction modification DNA specificity domain. InterPro FT (IPR000055): Restriction modification system DNA FT specificity domain." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1C0" FT /db_xref="InterPro:IPR000055" FT /db_xref="UniProtKB/TrEMBL:A1K1C0" FT /protein_id="CAL92625.1" FT /translation="MSLPRYAEYKDSGVALLATIPAHWEPSPLKRVVALVESGVSVNAV FT DEPAGPDAVGVLKTSCVYSGNFSHGENKAVVAEELDRVACPVRAGTLIVSRMNTPALVG FT AAGLVEENADNLFLPDRLWQVHFSGAVPKFAHYWTASPSYRAQVQMACAGTSASMQNLS FT QDEFLRFVMPLPPKDEQTAIAAFLDRETAKIDALIAKQEKLIALLAEKRQATISHAVTR FT GLNPDAPMKDSGVAWLGEVPAHWSVSALSYLASLETGATPDRGEPSYWNGTIPWLKTGE FT INWAPICEAEEFITDAGLENSAAKIAKPGTLLMAMYGQGVTRGRVALLEIEATYNQACA FT AINFRSRIIPEFGRYFFMAAYDHVRDAGNETSQMNLSAGLISKIRLPVPPLDEQQAVVR FT FLDVETAKLDVLGAESERGITLLKERRSALIAAAVTGQIDVRNTAERAST" FT CDS 10381..11256 FT /transl_table=11 FT /locus_tag="azo0008" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to RB11641 FT of R.baltica of 42% (tremble:Q7TTG8). No domains predicted. FT No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K1C1" FT /protein_id="CAL92626.1" FT /translation="MKTQAKTIQIFLPGGDPQGIRVAEITTRIVQLIEVPRALLPEFLK FT MPESNQVALYFLVGEAEDGAERRVYIGQTGDLPARLATHNKEKAFWTRALVLISRTNSL FT TQTHALFLEWYSLQRAKQAARYDLSENRNGGSKPHTPAPLEADCLEIFETGQTLLATLG FT YPVFEPVAKPSEAGNPAEFFHCKRSGIDGKGLYTPEGFVVLKGSLGHQADAPSITGTWA FT GHLRQKLRDSGVVQVKGGNIEFLKDHLFASPSTAAVALLGRTANGWVEWKSAEGKTLDA FT LKRQGVGGTD" FT CDS 11468..11794 FT /transl_table=11 FT /locus_tag="azo0009" FT /product="transcriptional regulatory protein" FT /function="uncharacterized conserved protein" FT /note="Transcriptional regulatory protein, 35% identity to FT TrEMBL;Q89JK0. Has Prosite, PS01117; HTH_MARR_1 domain; The FT marR-type HTH domain is a DNA-binding, winged FT helix-turn-helix (wHTH)domain of about 135 amino acids FT present in transcription regulators of the marR/slyA FT family,involved in the development of antibiotic FT resistance" FT /note="Function unclear" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1C2" FT /protein_id="CAL92627.1" FT /translation="MRFFLKGVAETASKGRDVFGQILHLRTEAEQQILSLGKRAPTARQ FT GLNLLYRNPVVSAGDLATGLAISTPTANALIKDFERLGILRESTGRQKDRVFVFDRYLR FT LFVS" FT CDS 11948..15061 FT /transl_table=11 FT /gene="hsdR" FT /locus_tag="azo0010" FT /product="Type I site-specific deoxyribonuclease" FT /function="Type I site-specific restriction-modification FT system R (restriction) subunit and related helicases" FT /EC_number="3.1.21.3" FT /note="SUBUNIT R IS REQUIRED FOR BOTH NUCLEASE AND ATPASE FT ACTIVITIES BUT NOT FOR MODIFICATION (BY FT SIMILARITY),TREMBL:Q9AAH5 (64% identity); TREMBL:Q8FUH0 FT (40% identity). InterPro (IPR001410): DEAD/DEAH box FT helicase TIGRFAM (TIGR00348): Type I site-specific FT deoxyribonuclease, HsdR family." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1C3" FT /db_xref="InterPro:IPR006935" FT /db_xref="InterPro:IPR007409" FT /db_xref="InterPro:IPR014001" FT /db_xref="UniProtKB/TrEMBL:A1K1C3" FT /protein_id="CAL92628.1" FT /translation="MNLHQEHHFEAEICAHLAANGWLYAEGDAALFDRATGLFLPDLLA FT WVEETQPESFQRLTKTHGAALPQVLAERVRKSLNLPERGTLDVLRRGVEMLGLKEPLML FT AQFKPALAINPATQAKYAANRLRVVRQVCHSPNNPKEELDLVLFLNGIAVATAELKSNF FT TQSVQDAVDQYRYDRHPQPKGGVLEPLLGFPGGALVHFAVSQSEVMMSTRLAGKDSFFL FT PFNRGNAGGAGNAPNPQGFATAYLWEEVWARESWLDILHRYIIGKRDDKKQLKSLIFPR FT YHQLDATRKLVADVLQNGTGERYLIQHSAGSGKTNSIAWTAHFLADLHDAQHNKLFDSV FT LVVSDRNVLDAQLQEAIFDFERTTGVVATITNEHGSKSAQLGQALKDGKKIIVCTIQTF FT PFALQAVQELAATEGKRFAVIADEAHSSQTGEAAAKLKQLLSAEEWAELQDGGEVDTEA FT LLAAQMEAKAGATKGLTYIAFTATPKGKTLELFGRRGEDGLPQPFHVYSMRQAIEEGFI FT LDVLKNYTSYKLAFKLAHDGQEYDEKEVERSTAMKGIMQWVRLHPYNIAQKVQVVVEHY FT RENVQPLLQGRAKAMVVVGSRREAVRWQKAIRAYIAKQNYPLGVLVAFSGEVNDAESFP FT EPVTETNAQLNPGLKGRDIREVFKEPDFHLLLVANKFQTGFDQPLLCGMYVDKMLGGIQ FT AVQTLSRLNRAHPGKDTTYILDFVNEPAEVLKAFKTYYETAELEATTDPHAVYDLRAKL FT DATGYYDEFEVERVAKVDLDPNGTQKQLDAAIAPVADRLLKRYKAAQQDKAAAAEHGDE FT NAAKTAKDTLEALVLFKNDMGAYVRLYAFLGQIFDYGNTDIEKRFLFYKRLIPLLEFGR FT ERDTVDLSKVVLTHHHLKNRGKQTLSLNSDGNYKLPPMDAVGSGSVQDKQQAYLVEIIE FT KVNGLFEGELSDDDQLVYVNGVLKGKLLENETLVKQAVNNTKEQFGNSPDLSQALLHAI FT MDALEAHQSMSTQALGSERVRDGLKDVLLGPAQLYESLRARANQPARM" FT CDS complement(15231..16085) FT /transl_table=11 FT /locus_tag="azo0011" FT /product="Short-chain dehydrogenase family protein" FT /function="Dehydrogenases with different specificities FT (related to short-chain alcohol dehydrogenases)" FT /note="The short-chain dehydrogenases/reductases family is FT a very large family of enzymes, most of which are known to FT be NAD- or NADP-dependent oxidoreductases, similarity to FT SWISSPROT:P37959 (35% identity); TREMBL:Q930L8 (44% FT identity); TREMBL:Q9I3W5 (41% identity). Pfam (PF00106): FT Short chain dehydrogenase. InterPro (IPR002198): FT Short-chain dehydrogenase/reductase (SDR). InterPro FT (IPR002347): Glucose/ribitol dehydrogenase." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1C4" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K1C4" FT /protein_id="CAL92629.1" FT /translation="MNTKQTTFKRVWFITGASRGLGALIARAALDDGNAVVATGRNADV FT VRERLGDHPGLLALALDVTVETQAQAAIEAAVRRFGRIDVLINNAGHGLLGAVEESSDA FT DTRRMYETNVFGLLNVTRAVLPVMRAQRAGHLINFSSIGGYSSAVGFGVYCSTKFAVEG FT LSEALHAELAPLGVAVTVVEPGYFRTDFLDSTSLVVAPQVIPDYAATAGQVREGAKQLN FT HKQPGDPVRLAQAMLRLVDAERPPLRLALGSDTLRAIAEKNARVDAETAEWAELSRSTD FT FPG" FT CDS 16203..17150 FT /transl_table=11 FT /gene="bdhR" FT /locus_tag="azo0012" FT /product="transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="Transcriptional regulator, LysR family," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1C5" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1C5" FT /protein_id="CAL92630.1" FT /translation="MNEVRALSLFVRAATLGSLRRAAIDQGISPQAASHAVMQLEKSLG FT VRLFHRTTRRLSLTEDGRMLFERSSPALDVLFAAIEDVRKARDDVGGLLTLSAPTALGR FT TMLWPLIVEFARLHPEIRVDAHFDDHLTDLVAERADVGFRGGASPAEGTIARRLLPIQL FT IVCAAPDYLARHGAPRTIDDLVHHRCSGYRQANTGKLAPWEFLVDGETIRRDVPAVLSC FT NDVDAEVDAVLSGSAIGQLASFSAVTHIRAGRLVPLLVRHVAERDGIHLYYRRRSEQPR FT RTRAFIDFIVGRLADHPDFHLGREELERLVAEQS" FT CDS 17232..17876 FT /transl_table=11 FT /gene="rluA1" FT /locus_tag="azo0013" FT /product="pseudouridine synthase A" FT /function="Pseudouridylate synthases 23S RNA-specific" FT /EC_number="4.2.1.70" FT /note="Ribosomal large subunit pseudouridine synthase A (EC FT 4.2.1.70) (Pseudouridylate synthase) (Uracil hydrolyase). FT Responsible for synthesis of pseudouridine from uracil-746 FT in 23S ribosomal RNA and from uracil-32 in the anticodon FT stem and loop of transfer RNAs ." FT /note="Family membership" FT /db_xref="GOA:A1K1C6" FT /db_xref="InterPro:IPR006145" FT /db_xref="InterPro:IPR006224" FT /db_xref="InterPro:IPR020103" FT /db_xref="UniProtKB/TrEMBL:A1K1C6" FT /protein_id="CAL92631.1" FT /translation="MPQLTPTLLYTDDSLIVADKPAGLLSVPAGGEDRQDCLAHRVQAQ FT FDDALIVHRLDAATSGLVLLARGMEMLRRMSLGFEQRVVGKRYVALVHGRVAQDDGEIA FT LPLAADPLNRPRQIVDAARGRPALTRYRVLERSGAGDAAVSRLELKPMTGRSHQLRVHL FT MAIGHPIVGDPLYAPPESAAAHPRMFLHAAGIAFMHPDRRVPMQFDSPVPF" FT CDS complement(18010..18567) FT /transl_table=11 FT /gene="nifF1" FT /locus_tag="azo0014" FT /product="probable flavodoxin" FT /function="Flavodoxins" FT /note="Probable flavodoxin. Homology to nifF of A. FT vinelandii of 49% (pir|FXAVEP) Flavodoxins are FT electron-transfer proteins that function in various FT electron transport systems. Flavodoxins bind one FMN FT molecule,which serves as a redox-active prosthetic group FT and are functionally interchangeable with ferredoxins. FT InterPro: Flavodoxin (IPR001226) Pfam: Flavodoxin no signal FT peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1C7" FT /db_xref="InterPro:IPR008254" FT /db_xref="InterPro:IPR010086" FT /db_xref="UniProtKB/TrEMBL:A1K1C7" FT /protein_id="CAL92632.1" FT /translation="MNKIGMFFGTETGTTRLIAKKIHKKLGDEIADKPVNVNRIEPADM FT LKYDVLILGTPSYGIEEVPGLSAGCLEPNWAEFLVKMDKPDFSGKRIALFGLGAQERYS FT ERFCSSLMRIYEIFKGYGAEIVGDDWPTDGYTFQQSAAVKDGRFVGLVIDERTQGMYTN FT ERIDTWVAKVKPLLLEKLGVEA" FT CDS complement(18971..19501) FT /transl_table=11 FT /locus_tag="azo0015" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein, 50% identitcal(67% FT similarity) to TrEMBL;Q888U7.TrEMBL;Q747X0(33% identity). FT Has PF03473, MOSC domain;IPR005302; The MOSC (MOCO FT sulfurase C-terminal) domain is a superfamily of FT beta-strand-rich domains identified in the molybdenum FT cofactor sulfurase and several other proteins from both FT prokaryotes and eukaryotes. These MOSC domains contain an FT absolutely conserved cysteine and occur either as FT stand-alone forms such as P32157, or fused to other domains FT such as NifS-like catalytic domain in Molybdenum cofactor FT sulfurase. The MOSC domain is predicted to be a FT sulfur-carrier domain that receives sulfur abstracted by FT the pyridoxal phosphate-dependent NifS-like enzymes, on its FT conserved cysteine,and delivers it for the formation of FT diverse sulfur-metal clusters." FT /note="Function unclear" FT /db_xref="GOA:A1K1C8" FT /db_xref="InterPro:IPR005302" FT /db_xref="InterPro:IPR011037" FT /db_xref="InterPro:IPR015808" FT /db_xref="UniProtKB/TrEMBL:A1K1C8" FT /protein_id="CAL92633.1" FT /translation="MDADDDLRALTARFPRAGRLDAVLLRSARRGEVVRAEAAEAIAGR FT GLAGDHRTSGGRGGGKRQVTLIQAEHLPVIAALVGRDALDPALLRRNLVVSGINLHAAR FT SLFDDQALVLRIGEVVLEVTGPCDPCSRMEAVLGPGAYNAMRGHGGMTARVLVGGPLRV FT GDVVRCSLEAAAS" FT CDS complement(19505..19855) FT /transl_table=11 FT /locus_tag="azo0016" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT Daro03002995 of Dechloromonas aromatica of 34% FT (ZP_00348572.1). No signal peptide present. TMHMM reporting FT one transmembrane helix. No domains predicted." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K1C9" FT /protein_id="CAL92634.1" FT /translation="MQFDRDPAAGPGSLPPPSARPAGVLKKALAIVVAAALFVLAMMAS FT VVLFAVVLTAGAVLWGYLWWKTRAARKAMAERMAEAQAWQQRQQQGSSGAGGLVLEGEV FT IREIRPGDEDRR" FT CDS complement(19882..20355) FT /transl_table=11 FT /locus_tag="azo0017" FT /product="Hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Hypothetical protein, 28% identity to TrEMBL;Q8E8U4. FT Has PF07049, Protein of unknown function (DUF1332); FT IPR010755;This family consists of several hypothetical FT bacterial proteins of around 165 residues in length. The FT function of this family is unknown." FT /note="Function unclear" FT /db_xref="InterPro:IPR007791" FT /db_xref="UniProtKB/TrEMBL:A1K1D0" FT /protein_id="CAL92635.1" FT /translation="MLRTLKELFASFAAPDDSAPATEHRLQLAAAVLLVEVMRADAVSG FT AVEREAVIDALRNKFGLGEDEVARLLELAEATADDAPDFYAFTSQLNKGFSPEQKLRMV FT EHLWQVAFADGALSHFENQLMLKLGDLLYIPRGEFVAAKQRARATAPSLDPSP" FT CDS complement(20480..21061) FT /transl_table=11 FT /locus_tag="azo0018" FT /product="ThiJ/PfpI family protein" FT /function="Putative intracellular protease/amidase" FT /note="InterPro (IPR002818): ThiJ/PfpI. Pfam (PF01965): FT DJ-1/PfpI family." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1D1" FT /db_xref="InterPro:IPR002818" FT /db_xref="InterPro:IPR006286" FT /db_xref="UniProtKB/TrEMBL:A1K1D1" FT /protein_id="CAL92636.1" FT /translation="MAAKKILMITGDYTEDYETMVPFQALLMAGHTVHAACPGKKAGEQ FT VRTAIHDFEGDQTYSEKPGHNFTLNAEFDSLRAEDYDALVIPGGRAPEYLRLNPKVIAA FT VQHFFAADKPVAAICHGAQVLAAAGVLKGRTCSAYPACAPEVKAAGGEYAEIPVDKARV FT DGKLVTAPAWPAHPDWLAKFLQVLGTTITP" FT CDS 21263..22402 FT /transl_table=11 FT /locus_tag="azo0019" FT /product="extracellular ligand binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems periplasmic component" FT /note="This family includes extracellular ligand binding FT domains of a wide range of receptors and it also includes FT the bacterial amino acid binding proteins of known FT structure. Similar to trembl|Q8XVG7 (38%). Pfam (PF01094): FT Receptor family ligand binding region SignalP reporting FT Signal peptide." FT /note="Function unclear" FT /db_xref="InterPro:IPR001828" FT /db_xref="UniProtKB/TrEMBL:A1K1D2" FT /protein_id="CAL92637.1" FT /translation="MIGRRSFALALCCALVAALSFHTLPARAEPGAITVGQSIVLSGPQ FT AANGLLYARGIKLQLDAVNAAGGVNGKPVRLVTLDDGYDPERCKENTRRLIAQDKVVAL FT FGYTGTGPTAACAPLAEAARVPLLAPLTGAPELREDTARYLFHTRASYLDEMRKMVEYL FT TTVGVRDIAVVYQDDGFGRSGLRSAETVLAAYQLKPAAVGSIPPQTYDPAQAVAALGSR FT APGAVILATAGQASVNFIRAYLKSGKRTQFFGLSVVSSNQLLKELGQDTDGVVISQVVP FT SPWSQSTQVVRDFQRDAAAAKDVEVNHTTLEGYIAARVLVEGLRRAGPDPSPEKLTQAL FT ENLHSLNLGGYEVGFGPGRRAGSRYVDLSLVRGSGRYVQ" FT CDS complement(22404..23309) FT /transl_table=11 FT /locus_tag="azo0020" FT /product="probable transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="Probable transcriptional regulator, LysR family," FT /note="Family membership" FT /db_xref="GOA:A1K1D3" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1D3" FT /protein_id="CAL92638.1" FT /translation="MIEPSLLPALAAFECVARHASFSRAAAELGLSASALSQSVSTLER FT RLGLRLLARTTRHVGLTEEGARLLDGVRRGLAELGGALASVDHAREQPSGTVRITLPRL FT AFALYFAPHVDEFARRYPEVGIEFSLDDKLADLVADRFDIGLRMADNIAGDMVAIPLGR FT PQRLIVAAAPAYFARHPVPLQPADLAEHDCIRFRFPTSGRNARWLFRQDDGDFELEVRG FT RFTVNDADAELDLLRRGLGISQVVESMVQDDLAAGRLREVLAEYAWPMPVAHLYFPSRA FT QMPARLRVFIDFFRAMNAPA" FT CDS 23470..23928 FT /transl_table=11 FT /gene="iorA" FT /locus_tag="azo0021" FT /product="probable isoquinoline 1-oxidoreductase, alpha FT subunit" FT /function="Aerobic-type carbon monoxide dehydrogenase small FT subunit CoxS/CutS homologs" FT /EC_number="1.3.99.16" FT /note="Probable isoquinoline 1-oxidoreductase, alpha FT subunit Homology to iroA of B. diminuta of 58% FT (sprot|IORA_BREDI). InterPro: [2Fe-2S] binding domain FT (IPR002888); Ferredoxin (IPR001041) Pfam: 2FE-2S FT iron-sulfur cluster binding domein, [2Fe-2S] binding domain FT no signal peptide no TMHs" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1D4" FT /db_xref="InterPro:IPR001041" FT /db_xref="InterPro:IPR002888" FT /db_xref="InterPro:IPR006058" FT /db_xref="InterPro:IPR012675" FT /db_xref="UniProtKB/TrEMBL:A1K1D4" FT /protein_id="CAL92639.1" FT /translation="MTRFTLNGKPVETALPDDTPLLWVLRDGLDQTGTKFGCGMGLCGA FT CTVHLDGQPIRSCSTPLSAAAGKKITTIEGVGKARVGAAVQKAWQKLDVVQCGYCQSGQ FT IMSATALLTANPKPTDADIDAAMGGNICRCATYVRIRAAIHEAAKSLA" FT CDS 23939..26152 FT /transl_table=11 FT /gene="iorB" FT /locus_tag="azo0022" FT /product="putative isoquinoline 1-oxidoreductase, beta FT subunit" FT /function="Aerobic-type carbon monoxide dehydrogenase large FT subunit CoxL/CutL homologs" FT /note="Putative isoquinoline 1-oxidoreductase, beta subunit FT Homology to iorB of B. diminuta of 34% (sprot|IORB_BREDI). FT InterPro: Aldehyde oxidase and xanthine dehydrogenase C FT terminus (IPR000674) Pfam: Aldehyde oxidase and xanthine FT dehydrogenase signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1D5" FT /db_xref="InterPro:IPR000674" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR008274" FT /db_xref="InterPro:IPR012368" FT /db_xref="InterPro:IPR019546" FT /db_xref="UniProtKB/TrEMBL:A1K1D5" FT /protein_id="CAL92640.1" FT /translation="MKMQITNVSRRDFLKAGAGLTLSVSLPGAVLAAAGGPGIAGSATA FT AGDFTPNAFVRIGADSTVTVLSKHLEMGQGVYTGLTTLVAEELDADWAQVVVEGAPAEA FT KRYNNLFWGPVQGTGGSTAIGNSFEQLRQAGAAARAMLVQAAAERWKVPAAEISVKNGV FT VSHAKSGRKARFGELAEAAAALPVPQQVTLKDPKNFSLIGRHVPRKDSVAKTTGTAQFT FT QDVKLPGMLVAVVAHPPRFGGKVRSVDDKAARAVPGVADVVTIPNGVAVLAGDYWTAKK FT GRDALQVVWDESAAYHGSSDAILADYRKLAGTPGLVARKDGDGDGAAALAKATKVIEAE FT YAFPFLAHAAMEPINCVMRLGPDSCEVWNGEQFQTVDQANLAAFFGLKPEQVTLHMLYA FT GGSFGRRANPMSDYLLETAQIVKAIGGRAPVKLVWSREDDMRAGYYRPAFLHRLRATLG FT ADGTPQAWEQRIVGQSIIKGSPFEGVMIKDGIDATSVEGAANLPYAIPNLQIELHTTND FT AVKVPVQWWRSVGSTHTGHATEVFLDELATAAGADPVAYRMALLGSHPRHAGVLKLAAD FT KAGWGKPLAAARDKGARRGRGVAVHESFHSYVAQVVEVTVAADGGFKVDRVVCAVDCGV FT AVNPDVIRAQMEGGIGFALAAALTGVVTLKDGVVEQSNFHDYPVLRIGEMPKVEVHIVP FT SAEKPTGVGEPGVPPLAPALANALHAATGKRIRSLPIAEQLKA" FT CDS 26175..27197 FT /transl_table=11 FT /locus_tag="azo0023" FT /product="conserved hypothetical protein" FT /function="Xanthine and CO dehydrogenases maturation factor FT XdhC/CoxF family" FT /note="Conserved hypothetical protein (Xanthine FT like-dehydrogenase accessory factor). Homology to Rsc1464 FT (hyp. protein) of R. solanacearum of 66% (CAD15165). FT InterPro: DUF182 Pfam: uncharacterized BCR, COG1975 no FT signal peptide no TMHs" FT /db_xref="GOA:A1K1D6" FT /db_xref="InterPro:IPR003777" FT /db_xref="InterPro:IPR013817" FT /db_xref="UniProtKB/TrEMBL:A1K1D6" FT /protein_id="CAL92641.1" FT /translation="MDSLDHDVLTRARDWLAAGRRVLLATVVRTWGSSPRPPGALLALR FT DDGRAVGSVSGGCIEDDLIDRLHRDGLPATPQLVSYGVGAEEARRFGLPCGGTMELVLE FT PLADPAPLDALLARLAAGELVERRLGMASGRATLAAAHPEQGLAYDGRTLTSVFGPRYR FT LLLIGAGQLSESLARIALGLDFAVTVCDPREEYHEEWRVAGTTLTRDMPDDVVIAMRPD FT ARTAVIALTHDPKLDDLALMEALRSPAFYVAALGSRRNNAARRERLREFDLSEAQVATL FT RGPAGLYIGSRTPAEIAVSIAAELVAVKNGVTPERVLPVAEAKAALELAADTLSSCAAR FT " FT CDS 27194..27763 FT /transl_table=11 FT /locus_tag="azo0024" FT /product="conserved hypothetical protein" FT /function="uncharacterized MobA-related protein" FT /note="Purine catabolism protein pucB. TREMBL:Q8XZ0: 40% FT identity, 47% similarity Required for xanthine FT dehydrogenase activity. Could be involved in formation of FT the molybdenum cofactor required by xanthine dehydrogenase. FT FUNCTION: Links a guanosine 5'-phosphate to molydopterin FT (MPT) forming molybdopterin guanine dinucleotide (MGD) (By FT similarity). PATHWAY: Molybdenum cofactor biosynthesis. FT SUBCELLULAR LOCATION: Cytoplasmic (By similarity). FT SIMILARITY: Belongs to the mobA family. FT Pfam:UPF0007:Uncharacterized protein family UPF000 ispD: FT 4-diphosphocytidyl-2C-methyl-D-er Non-secretory protein FT with signal peptide probability: 0 No TMH's (TMHMM FT predicted)." FT /note="Function unclear" FT /db_xref="UniProtKB/TrEMBL:A1K1D7" FT /protein_id="CAL92642.1" FT /translation="MMQGILLAAGYGRRFDPDGVQDKLLAPLADGRPVIWHAARALCAA FT LPASIAVLRPRQRERELWLRDAGCEVVKSTAAETGMGAALAAAIAASANADGWVVALAD FT MPWLPVEAVAAVAGAIDDPQRVAAAMHAGRRGHPVGFGAAWGAKLMTLTGDSGARELLR FT ETEILLIDNADPGVLRDVDTPADLGR" FT CDS 28052..28618 FT /transl_table=11 FT /locus_tag="azo0025" FT /product="conserved hypothetical protein" FT /function="Conserved protein/domain typically associated FT with flavoprotein oxygenases DIM6/NTAB family" FT /note="Hypothetical protein yddH. TREMBL:Q7NTI1:66% FT identity, 76% similarity InterPro:IPR002563; Flavin_Reduct. FT Pfam:PF01613; Flavin_Reduct; InterPro: Flavin FT reductase-like domain Non-secretory protein with no signal FT peptide. No transmembrane helices TIGR00357: PilB-related FT protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1D8" FT /db_xref="InterPro:IPR002563" FT /db_xref="InterPro:IPR009002" FT /db_xref="InterPro:IPR012349" FT /db_xref="UniProtKB/TrEMBL:A1K1D8" FT /protein_id="CAL92643.1" FT /translation="MTPPHTLPVPLEKSYRLINHGPTVLVASAHGGRRNVMAAAWNMPL FT DFAPPKVAVVIDKATYSRGLIEASGEFVLAVPTRAAAAQALATGSRSGRDEDKFAALGI FT EAYSADKVGAPLPGGCIAWLECRVIPEPHIQQTYDLFLGEVVAARADARLFRDGHWHFD FT EAGTRSIHYIAGGNFFATGDAFTVE" FT CDS complement(28631..29569) FT /transl_table=11 FT /gene="acbB" FT /locus_tag="azo0026" FT /product="putative dTDP-glucose 4-6-dehydratase" FT /function="dTDP-glucose 4-6-dehydratase" FT /EC_number="4.2.1.46" FT /note="dTDP-glucose 4,6-dehydratase, AcbB,probably involved FT in the biosynthesis of the acarviose moiety of the FT alpha-glucosidase inhibitor acarbose. Belongs to the sugar FT epimerase family. dTDP-glucose dehydratase subfamily. 30% FT dTDP_gluc_dehyt.IPR001509; Epimerase_Dh. Pfam:PF01370; FT Epimerase; 1. TIGRFAMs:TIGR01181; dTDP_gluc_dehyt; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1D9" FT /db_xref="InterPro:IPR001509" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K1D9" FT /protein_id="CAL92644.1" FT /translation="MRVLVTGGAGFIGSHLCRRLLADGHEVLSADNYFTGSRRNIHDLL FT GNPDFEALRHDITFPLYVEVDRIYNFACPASPVHYQYDPVQTTKTSVHGAINMLGLAKR FT TGARVLQASTSEVYGDPEVHPQTEDYWGRVNPIGPRSCYDEGKRCAETLFFDYHRQHRV FT EIKVVRIFNTYGPGMQPNDGRVISNFIVQALRGEDITLYGDGAQTRSFCHVSDLVDGVV FT RMMDSPAGFTGPVNLGNPTEYRIDALAELILRLCGSRSRLVFRPLPEDDPCQRQPDITL FT ARERLAWTPRVALEDGLRDTIDHFRRLLETQ" FT CDS 29590..30477 FT /transl_table=11 FT /gene="exoU" FT /locus_tag="azo0027" FT /product="Glycosyltransferase" FT /EC_number="2.4.1.-" FT /note="Putative glycosyl transferase. Weak Homology with FT hits spanning the entire length of protein. 24% identitcal FT to TrEMBL;Q8F209.TrEMBL; Q89D69(33% identity) Has FT PF00535,Glycosyl transferase:IPR001173;Diverse FT family,transferring sugar from UDP-glucose, FT UDP-N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to FT a range of substrates including cellulose, dolichol FT phosphate and teichoic acids. The biosynthesis of FT disaccharides,oligosaccharides and polysaccharides involves FT the action of hundreds of different glycosyltransferases. FT These are enzymes that catalyse the transfer of sugar FT moieties from activated donor molecules to specific FT acceptor molecules,forming glycosidic bonds." FT /note="Family membership" FT /db_xref="GOA:A1K1E0" FT /db_xref="InterPro:IPR001173" FT /db_xref="InterPro:IPR003859" FT /db_xref="UniProtKB/TrEMBL:A1K1E0" FT /protein_id="CAL92645.1" FT /translation="MQQIAFVTTSKGRLHHIRETLPRIVGQAPHEIIVVDYGCPDGTAA FT WVETHYPDVKVLRVDDDPGFCLPRARNLGARLSSARWICFIDADIRIQPGWVEWMRQRL FT VPGHFYRAAADAKGKRDGETFGTVICERAAFERIGGYDEAFRGWGGEDTDLYARLAAQP FT GLREAGYPAHFVEPIPHDDGERTQFHEVKRKDTQGRINVAYIRIKQQLLAHHVDALSIE FT VRRALMEQIKRQLGGNGDAAPRKTYAARVLTGQVLSRTGLPRSFVVDIARRRRFVLFGP FT RRFVIRVRPEPVEG" FT CDS complement(30502..30732) FT /transl_table=11 FT /locus_tag="azo0028" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein Homology to FT cv0580 of C. violaceum of 41% (trembl|Q7P0I7(SRS)) no FT domains predicted no signal peptide 2 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR021529" FT /db_xref="UniProtKB/TrEMBL:A1K1E1" FT /protein_id="CAL92646.1" FT /translation="MQIKPQHVQPVIMSGIMAFLMTAVITWLNLGFPPDFLSRWLHAFV FT VAWPLAALAAFIAIPIAQRATRRIVAAFGTR" FT CDS 30906..31676 FT /transl_table=11 FT /locus_tag="azo0029" FT /product="conserved hypothetical membrane protein" FT /function="Membrane protein TerC possibly involved in FT tellurium resistance" FT /note="Similar to a tellurium resistance protein TerC. FT Belongs to the terC family. This family contains a number FT of integral membrane proteins that also contains the TerC FT protein. TerC has been implicated in resistance to FT tellurium. Similar to a putative membrane protein TerC,80% FT identity to TrEMBL; Q5P410 from Azoarcus sp EnN1. 50% FT RNA_rec_mot.IPR005496; TerC. Pfam:PF03741; TerC; 1. FT TIGR:SPTO2691. TMHelix:5." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1E2" FT /db_xref="InterPro:IPR005496" FT /db_xref="UniProtKB/TrEMBL:A1K1E2" FT /protein_id="CAL92647.1" FT /translation="MLEFLTDPQLLVAFLTLTMLELVLGIDNIIFISILVDKLPPERRT FT FARRLGLFLAMFMRIGLLAALAWLAGLTKPLFELFGAGFSGRDLILICGGLFLVWKSTG FT EIHQLLEGEEGEASSAVKATFGAVILQIIVIDLVFSLDSIITAIGMVNNLPVMIAAVVA FT SVGLMMVASAPIGEFVSRHPTVKMLALSFLMVVGVVLIADGFGHHVPKGYIYSAMAFSV FT VVEMLNIRLRKNAEKPVDLHEAYVPEQTPAPEKR" FT CDS complement(31735..32625) FT /transl_table=11 FT /gene="gltR" FT /locus_tag="azo0030" FT /product="probable transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="HTH-type transcriptional regulator gltR. POSITIVE FT REGULATOR OF GLUTAMATE BIOSYNTHESIS (GLTAB GENES). FT NEGATIVELY REGULATES ITS OWN EXPRESSION. Similar to FT SWISSPROT: sprot|GLTR_BACSU (33% Bacillus subtilis, FT HTH-type transcriptional regulator GltR) InterPro: FT IPR000847 HTH_LysR. IPR009058 Winged helix DNA-binding. FT Pfam: PF00126 Bacterial regulatory helix-turn-helix FT protein,lysR family. HTH reporting nucleic acid binding FT motif." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1E3" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1E3" FT /protein_id="CAL92648.1" FT /translation="MLSPTRFNPQLLRYFRAVVEQGSLSAASRQLNCVPSNVSARLRQL FT EEQLGSVLLERNGPQFTLTAAGERLLPHARQLDALCSAAWNSVHLDTLQGRLRLGSMET FT TAAMRLPDVLARFHRHAPRVEVELETGTSATLIERVLGHELDAALVAGPLEHPRLLANE FT VWREELRLVVPPGEPAPAPGTEVSLIAFPEGCHYRARLFTHARDCGWRVRGQQSYASVE FT AIIGCVGAGLGLGVLPASLLAAHPRGRQVASHPLPPSLAVSPTVLVRRRVAEPHPALDA FT WVEVLLGGASGTQTQ" FT CDS 32784..34019 FT /transl_table=11 FT /locus_tag="azo0031" FT /product="putative permease member of the MFS transporters" FT /function="Permeases of the major facilitator superfamily" FT /note="Permease member of the Major Facilitator Superfamily FT (MFS).MFS are single-polypeptide secondary carriers capable FT only of transporting small solutes in response to FT chemiosmotic ion gradients. 25% MFS.IPR005828; FT Sub_transporter. Pfam:PF00083; sugar_tr; 1. TMHelix: 10." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR010645" FT /db_xref="InterPro:IPR016196" FT /db_xref="UniProtKB/TrEMBL:A1K1E4" FT /protein_id="CAL92649.1" FT /translation="MTAPPPSPPPSPPRLWIPLLAAALALVVVHGIGRFAYTPLLPLLV FT GDGFMGLDTGAAVATWNYVGYLLGAMLAIRLHEPAQIRRILPLALLINAACTLAQGFTD FT NATAFLVLRLINGISNGVVFVQAPALVLEWLARHGLASLSGLMYFGVGGGLLLSNALAN FT LPAELLHGAARWWPMALAALPLALWSARQLAHLDRPQAGAPAPAAAPRATALLDRASLP FT VFMAYAGAGLGYILPTTFLPVVAREQLPAGHWLQSGAWLILALCTLAAAWLWNRLGTRM FT GDRNALVLNYVVQGIGVAGPLLWPGTVGILACALMVGSTFLGSVLLTQRLARALHPHQG FT PRISAALITLYGFAQLTGPWMARMWLERGGSMSDTYWLGAGALVWATVWTLKTQQAPEH FT AGAPKLQAVRGD" FT CDS complement(34326..34814) FT /transl_table=11 FT /locus_tag="azo0032" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to nfa21510 FT of Nocardia farcinica of 31% (trembl:Q5YXU4). No domains FT predicted. No TMHs. No signal peptide.," FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR014710" FT /db_xref="UniProtKB/TrEMBL:A1K1E5" FT /protein_id="CAL92650.1" FT /translation="MSVMLCTAESQKTHGSAARDRITLPYPKFQKLDPIPWRPWVMDGV FT QYKLLSVNSRTGGFTCMLKVLPGVEAPIHHHLGAIEVMVMEGDICYEDADIGGPGDYMF FT EPAGDIHQPRTKAGCVLFCVFDGPIAGLAPDGSIAGIVDYKVMLEMAARDGVAEGVHR" FT CDS 35113..35601 FT /transl_table=11 FT /locus_tag="azo0033" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to nfa21510 FT of Nocardia farcinica of 42% (trembl:Q5YXU4). No domains FT predicted. No TMHs. No signal peptide.," FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR014710" FT /db_xref="UniProtKB/TrEMBL:A1K1E6" FT /protein_id="CAL92651.1" FT /translation="MTAAVLSHSPSSQAALSARHGKDFVNLAEVPWTPWVMEGTHFKLL FT AINELSGGFSMLLKVDPGVQAPVHGHLGSAEAYLVEGGFYYEEDDPGYAGYYTYERGGS FT IHQPVSPQGCVMFAVTHGPLAGCNPDGSVSAVVDCRLMLQLAEANAAAGHVVQLVSGR" FT CDS 35640..37502 FT /transl_table=11 FT /locus_tag="azo0034" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT PP2042 of P. putida of 34% (TrEMBL;Q88L93) Has FT PF06980:(IPR010727)Protein of unknown function FT (DUF1302);This family contains a number of hypothetical FT bacterial proteins of unknown function that are FT approximately 600 residues long. Most family members seem FT to be from Pseudomonas. No TMHs signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR010727" FT /db_xref="UniProtKB/TrEMBL:A1K1E7" FT /protein_id="CAL92652.1" FT /translation="MNGTFRRPGLRPAVLAAAVAACGGAHAGDFRLGDELTGTWTLNAS FT LGTNVRTQDRDAKLTSFGNANHNGGKPGGGGGSTDDGDLNFDRGDVTSTTLKLVGDVEL FT RYRNYGALLRAKAWHDFTLANKKVDHGHFDNGYVPNERLNDGHYDSAAKFTGAELLDAF FT VFADWELGNDSRLNMRLGNQVVNWGESIFIQGVNVVNPIDVPAARRAGAQVREILLPVP FT LLYGNLGLPGGVSLEAFYQLKWKKTVIDGCGTFFSPADVINCGGSQFGPDVFSDREQYE FT GVAALGGLNLRSLRLNDDKPSDAGQYGLALHWLEPNSETDIGLYYINYHTRTPFLSLSS FT RPSEPSSLYGTAAPLSYLLDYSAEDIKTFGLSLSNTLGGVSVMAELSYTRDLPVQINGG FT DLVQFGVSGGTQGPLVGKRIYDPAGATIRGYDRMDKIQLQFGAINVFSQVLGAQSLLAV FT GEVGMSWLPDLPNAKTDVRYGRAFTFGTAWHPAYTNPALSTRAGCNAANSAGMVTPANC FT AQDGFVTPFSWGYRLFGELEYPNAVAGWTAKPRLYWAHDVKGNAADGAFMENRRTLGTG FT VGLSRLVDGQRWTVDLAYTRFIDAARWDTNRDKDFLAASLSVAF" FT CDS 37514..38869 FT /transl_table=11 FT /locus_tag="azo0035" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT PA3421 of P. aeruginosa of 50% (TrEMBL;Q9HYI4) Has FT (IPR010752)PF07044:Protein of unknown function FT (DUF1329);This family consists of several hypothetical FT bacterial proteins of around 475 residues in length. The FT majority of family members are from Pseudomonas species but FT the family also contains sequences from Shewanella FT oneidensis and Thauera aromatica. No TMHs signal peptide FT present" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR010752" FT /db_xref="UniProtKB/TrEMBL:A1K1E8" FT /protein_id="CAL92653.1" FT /translation="MTRLHPALRLASLLLPLAAGAAHAAMSAEEIARLGKDLTPLGAER FT AGNAAGTIPAWTGGLTKPPAGFDIAQGHANPYADEKPLYTITAQNWEQHKDKLSDGHIA FT MLKRYPETYRLNVYPTHRSAALPQAEYDRIREQAGRIAVTASGTGLENWDRSATPFPIP FT KNGLEAIWNHQVRSRAGGIERRHLIGAVNPNGSFNAYGVDESWIFAQNMDRQEDNRFWY FT FMARMYSPADVTGEVVMVHEPLDFARDGRLAWVYNAGLRRVRRAPQIIYDSPGSFSEGT FT RTEDDYDMFNGPTDRYEWKLVGKREMLIPYNSYAIHSKKLKAKDVVKPHHLDPALTRYE FT LHRVWVVEATLKDGARHIYGKRVFYLDEDSWTIAVKEQYDGRGQLWRVGEAQLMQYYDL FT PLPYYAFENMYDLQDGRYYVAGLSNEEGPWRFGAKARRADFDPDALRRSGTK" FT CDS 38945..40102 FT /transl_table=11 FT /locus_tag="azo0036" FT /product="conserved hypothetical BNR domain protein" FT /function="uncharacterized protein related to plant FT photosystem II stability/assembly factor" FT /note="Conserved hypothetical BNR domain protein. Homology FT to pp3201 of P. putida of 40% (trembl|Q88I01). InterPro: FT BNR repeat (IPR002860) Pfam: BNR repeat BNR repeats are FT short repeats never found closer than 40 residues together, FT which suggests that the repeat is structurally longer. FT These repeats are found in many glycosyl hydrolases as well FT as other extracellular proteins of unknown function. singal FT peptide no TMHs" FT /note="Function unclear" FT /db_xref="InterPro:IPR002860" FT /db_xref="InterPro:IPR015943" FT /db_xref="UniProtKB/TrEMBL:A1K1E9" FT /protein_id="CAL92654.1" FT /translation="MTRLPLATLAAAAVLVAAAASAGLAPRPAAAPPIDLLETAAPQSP FT RAAAQLMNALVHAGHRLVAAGARGTIVYSDDGGRSWTQAAVPVAVMLTALHFPTPQLGW FT AVGHDGVILHSRDSGASWARQFDGNQANAQMLAWAQTRVEAARAALEAAPAPQREAAED FT ALAAAEDGLAGIEQTAGFGPSRPFMSVWFRDAREGYAVGAFGMAFATTDGGEHWTLFAD FT RLPNPEDLHLYAVASPAPEVVLIAGERGLVLRSEDAGAHWQAQADLADGGLYGLVTLPD FT GSATLAYGFDGAVLRSTDLGASWQALDSGTRSALYGAALADGELQLVGNNGARLRLAGE FT RFETLPAGDGRPLTAAARGKDGWVLAGWGGLARIETATAGDGRHE" FT CDS 40095..42521 FT /transl_table=11 FT /locus_tag="azo0037" FT /product="probable exporter of RND superfamily" FT /function="predicted exporters of the RND superfamily" FT /note="Putative membrane protein MJ1562. TREMBL:Q88LB6: 47% FT identity, 63% similarity InterPro:IPR000731; SSD_5TM FT InterPro: HMGCR/Patched 5TM box Pfam:Patched:Patched family FT 2A067: efflux transporter putative Signal peptide absent. FT Presence of 12 transmembrane helices" FT /note="Family membership" FT /db_xref="GOA:A1K1F0" FT /db_xref="InterPro:IPR000731" FT /db_xref="InterPro:IPR004869" FT /db_xref="UniProtKB/TrEMBL:A1K1F0" FT /protein_id="CAL92655.1" FT /translation="MSETTVTSARAPHGGLLKRLERRLEGALFRHRAATVAVFALLTVW FT LGWVALGLRPDASFEKMIPTHHPAIANYLAHEDNLRGLSNVVRVVVENRKGDIFDPGFQ FT EVLRKVNDEVFYIPGVDRAGMRSLWTPNVMWGEVTAEGFEAGPVIPDGYDGSPRALEQL FT RANVFRSGEVGTLVANDLRSALVLVPLMERNPETGERLDYGRFATDLEERIRARYENEA FT VGIRIVGFAKVIGELIDGAVPILGYFLLTLVLTAALLFWYSRCLRSTLTTLVCCLIAVV FT WQLGIVRLLGYGLDPYSILVPFLTFAIGISHAVQNINATANAALDGADRVEAAKRSFRS FT LFVAGTVALLCDAVGFATLLVIRIGVIQELAISASIGVAVIIFSKMFLLPVLMSWTGVS FT PAAVAHARRRRDHLPWLWQQVARCAQPRPAVVVTLAGAALLALGYWGARDLQIGDLDPG FT APELRTDSRYNRDAAFLVEHYATSTDVFVVMAETPPQGCRDYQVLAGMDLLAAELERVP FT GVQRTVSMSDFAYRVLAGNNEGNPKWYAISRNKYALGGAFQKTPKEYIGNGCAMTPFVV FT YLNDHKAATLSAVMATVRDFAARHDSDKVRFTLVGGNAGIEAATNEVIRDAERTMLMLV FT YAIVALLLLIEFRSLRVTICIVVPLYITSVLCEAIMAWMGLGVKVATLPVIALGVGIGV FT DYGIYIYNRLQSCLDRGLPLAEAYLLTVATTGRAVAFTGLTLAVGVLTWIGSDIKFQAD FT MGLLLTFMFLWNMVGALVLLPALARLLLPATRPAAATATPRHPEPHLRLADAQRS" FT CDS 42527..43336 FT /transl_table=11 FT /locus_tag="azo0038" FT /product="Short-chain dehydrogenase family protein" FT /function="Dehydrogenases with different specificities FT (related to short-chain alcohol dehydrogenases)" FT /note="The short-chain dehydrogenases/reductases family FT (SDR) is a very large family of enzymes, most of which are FT known to be NAD- or NADP-dependent oxidoreductases. EntA,a FT 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase enzyme,is FT involved in the third stage of enterobactin biosynthesis FT and converts isochorismate to 2,3-dihydroxybenzoic acid FT (DHBA), SWISSPROT:Q10855 (37% identity); TREMBL:Q89M15 (36% FT identity). InterPro (IPR002198): Short-chain FT dehydrogenase/reductase (SDR). InterPro (IPR002347): FT Glucose/ribitol dehydrogenase. InterPro (IPR003560): FT 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. Pfam FT (PF00106): Short chain dehydrogenase." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1F1" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K1F1" FT /protein_id="CAL92656.1" FT /translation="MTTTIETRLMDLTGRVAFVTGGASGIGRATAHALAAQGARVIVAD FT INETGGWETADAIGTAAGFVHLDVTEETAWCRALDYVISTEGRLDILANVAGIGLGGDF FT EDLALADWNRLMAVNATGPFLGCKHAIRAMAGSGRPGAIINVGSIAATHAAPDLGGYCA FT SKGALRMLSKSVALYCAHKGYPIRCNAVHPTYVDSEMLDPIAALYGSREAMVQAMARLV FT PVGRLAKPADVAAAVVYLASDAAGMVTGTELFVDGGQTAGIAPSHFG" FT CDS 43466..45670 FT /transl_table=11 FT /locus_tag="azo0039" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conservd hypothetical protein, 79% identity(85% FT similarity) to TrEMBL;Q88GU7. Has PF02566, OsmC-like FT protein; IPR003718; Osmotically inducible protein C (OsmC) FT (P23929) is a stress -induced protein found in E. Coli. FT This family also contains a organic hydroperoxide FT detoxification protein (O68390) that has a novel pattern of FT oxidative stress regulation. Has PF02624, YcaO-like fatty FT acid binding protein;IPR003776, DUF181;This is a family of FT proteins of unknown function." FT /db_xref="GOA:A1K1F2" FT /db_xref="InterPro:IPR003718" FT /db_xref="InterPro:IPR003776" FT /db_xref="InterPro:IPR015946" FT /db_xref="InterPro:IPR019938" FT /db_xref="UniProtKB/TrEMBL:A1K1F2" FT /protein_id="CAL92657.1" FT /translation="MEIKVNFLDKLRLEAKFDDFTVIADQPIRYKGDGSAPGPFDYFLA FT SSALCAAYFVKLYCNTRNIPTDNIRLSQNNIVDPENRYQQTFKIQVELPEDISAKDRLG FT ILRSIERCTVKKVVQTGPEFVIEEVENLDADAQALLTLRPDPAHRTYIAGKDLPLEQTI FT ANMSEVLAGLGIKIEIASWRNLVPNVWSLHIRDAHSPMCFTNGKGASKESALASALGEY FT IERLNCNHFYNDQFWGEDIANAPFVHYPDERWFKPGPADALPAGLLDDYCLQIYNPDGD FT LRGSHLYDTNSGNVRRGICALPYVRQSDGAVVYFPSNLIDNLFLSNGMSAGNTLAEAQV FT QCLSEIFERAVKREILEGELALPDVPPEVLAKYPGILAGIEALEKQGFPVLVKDASLGG FT TYPVMCVTLMNPHTGGVFASFGAHPSLEVALERSLTELLQGRSFEGLNDLPRPTFNSNA FT VTEPNNFVEHFIDSSGVVSWRFFSARADFDFVEWDFSSQGQNANAQEAARLLGILEDMG FT KEVYMAVYDQLGAIACRILVPDYSEIYPVEDLIWDNTNKALAFRADILNLHRLDDAGLE FT ALLERLEDSELDDYTDIITLIGIEFDENTVWGQLTILELKLLIHLALQQFEAAKERVEA FT FLQYNENTVERVLFYQALDAVLEVVLDDALELDDYVVNFRRMFGDARMDAVLGSVDGSV FT RFFGLTPTSMKLEGLDRHQRLIDSYRKLHTARARRASAPA" FT CDS complement(45701..46612) FT /transl_table=11 FT /locus_tag="azo0040" FT /product="putative AraC-family transcriptional regulator" FT /function="AraC-type DNA-binding domain-containing FT proteins" FT /note="Putative AraC-family transcriptional regulator," FT /note="Family membership" FT /db_xref="GOA:A1K1F3" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR018060" FT /db_xref="InterPro:IPR018062" FT /db_xref="InterPro:IPR020449" FT /db_xref="UniProtKB/TrEMBL:A1K1F3" FT /protein_id="CAL92658.1" FT /translation="MTGVFASTPQLIARATASAPDYVMEGHNGDIFGARWNHPAGESQL FT RRNAEHVLVYHLSGNTDVERLQQGVVTGFRSRVGSVTFMPRDSESDWRLGGNTQVIHLY FT LSQDLMDAFARDTLERDACPEIDDFFAVNDTWLDGFFRMLASEAPPSAGAGTRLETLVL FT DQIQSLLVRHLVTRYARERRADTERALVRGGSGSQLRQSVLKKITALIHERLHEDICLQ FT DLADLACISKDHFLRAFRDTVGQTPYHYVLSQRLERARALLREEPNLPVAEIARRCGFK FT NLSHFSATFRRMTGVSPKGYRG" FT CDS 46800..47561 FT /transl_table=11 FT /locus_tag="azo0041" FT /product="Short-chain dehydrogenase family protein" FT /function="Dehydrogenases with different specificities FT (related to short-chain alcohol dehydrogenases)" FT /note="The short-chain dehydrogenases/reductases family FT (SDR) is a very large family of enzymes, most of which are FT known to be NAD- or NADP-dependent FT oxidoreductases,TREMBL:Q9I376 (49% identity); FT SWISSPROT:P50197 (44% identity). InterPro (IPR002198): FT Short-chain dehydrogenase/reductase (SDR). InterPro FT (IPR002347): Glucose/ribitol dehydrogenase. Pfam (PF00106): FT Short chain dehydrogenase." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1F4" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K1F4" FT /protein_id="CAL92659.1" FT /translation="MQGMLEQKVVIVTGAGSGIGRAAAELMAREGAIVIASDLKLDTVE FT DTAHRITLAGGRAVAVRTDVAKLAELDALHDLAIAEFGRLDGAFNNAGIPGPGVALADH FT EEAAFDALIAINLKAVWYGMKRQIELMLPGGGGAIVNTASVGGIVGKPGLSVYCATKHA FT VIGLTKTAALEYGSRGVRVNAVCPGVIRTPMVDQVIAGQPGAEEEWNRLQPIGRMGTPE FT ELAETVVWLMSPRASLVHGHALVADGGLTVA" FT CDS 47901..48494 FT /transl_table=11 FT /locus_tag="azo0042" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein. Homology to FT bll2189 of B. japonicum of 48% (trembl|Q89T61). Has FT PF06577, Protein of unknown function FT (DUF1134);IPR008325,UCP033924; This family consists of FT several hypothetical bacterial proteins of unknown FT function. Signal peptide. TMH present in signal peptide." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR008325" FT /db_xref="UniProtKB/TrEMBL:A1K1F5" FT /protein_id="CAL92660.1" FT /translation="MFTPTHPVRSGHSWVLALIAALGLAFAVPAVAAGDDASTYDKDSI FT IKDAAEFFGETTEGLAKVIEKAFNEQGRPNGYIKGEEIAGAVGVGLRYGDGTLTLKKGG FT SAKVYWQGPSIGFDVGANASKVFILVYNLPRTQDIYQRFPGIDGSVYYVAGAGINYQQR FT DNIVLAPIRVGVGLRTGASVGYMHYTPTKTLNPL" FT CDS complement(48804..49574) FT /transl_table=11 FT /locus_tag="azo0043" FT /product="conserved hypothetical protein" FT /function="uncharacterized proteins homologs of lactam FT utilization protein B" FT /note="Hypothetical UPF0271 protein PYRAB09930. This family FT includes LamB. The lam locus of Aspergillus nidulans FT consists of two divergently transcribed genes,lamA and FT lamB, involved in the utilization of lactams such as FT 2-pyrrolidinone. Both genes are under the control of the FT positive regulatory gene amdR and are subject to carbon and FT nitrogen metabolite repression [1]. The exact molecular FT function of the proteins in this family is unknown. FT SPROT:Q89LH6: 47% identity, 62% similarity FT InterPro:IPR005501; LamB_YcsF. Pfam:PF03746; LamB_YcsF FT urease_gam: urease gamma subunit Nonsecretory protein with FT Signal peptide probability 0 No transmembrane helices" FT /note="Family membership" FT /db_xref="GOA:A1K1F6" FT /db_xref="InterPro:IPR005501" FT /db_xref="InterPro:IPR011330" FT /db_xref="UniProtKB/Swiss-Prot:A1K1F6" FT /protein_id="CAL92661.1" FT /translation="MMKINLNADLGESFGAWKMGEDDALLQVVRSANIACGFHAGDPLV FT MRNTVRMALAAGVSLGAHPAYPDLQGFGRRPMKMAPAELEAAVIYQLGALAGIAAAEGG FT RLSHVKPHGALSNQACEDAELAATVVRAVRAFDRELILLAPALSELHAVGERAGLRVAA FT EIFADRAYTDAATLAARTQPGAVIHDHDEIIAHVLRMLDAGGIVAQSGKVMKTVMHSVC FT VHGDTPGAVQSARRLAETLAAKGWELVGLPEMGE" FT CDS complement(49571..50671) FT /transl_table=11 FT /locus_tag="azo0044" FT /product="conserved hypothetical urea amidolyase-related FT protein" FT /function="Allophanate hydrolase subunit 2" FT /note="Conserved hypothetical urea amidolyase-related FT protein. Homology to ybgK of E. coli of 36% FT (sprot|YBGK_ECOLI). InterPro: DUF183 (IPR003778) FT Uncharacterized domain in proteins of unknown function. FT This domain is found in a multifunctional enzyme, urea FT amidolyase, from yeast. Pfam: DFU182, uncharcterized FT ACR,COG1984 no signal peptide no TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K1F7" FT /db_xref="InterPro:IPR003778" FT /db_xref="UniProtKB/TrEMBL:A1K1F7" FT /protein_id="CAL92662.1" FT /translation="MSAVQLEVLAPGAYASLQDGGRRGYRRIGVPWAGVLDTRLMRIAN FT VLVGNAEGAPVIECFDGGLLLAARGGPLRLAVAGDAVLEIERGGERSALAPWRSLTLGD FT GELLRLRRMSGGRIAVVAVEGLVLTPVLGSVSTYARAGLGGLDGPLAGRALTTGMLLPA FT QAARADGERMLPLPPQVDEGPIRVVPGPQADHFSAAAFATLLGEEYRVSAEADRMGLRL FT EGPALEHAGAREIVSDATVPGAIQVPGNGQPIVLLADAQTAGGYPKIATVIGADLGRLA FT ALRPGQVLRFATVTAGEGEHLARAAEAGTRALLAGVRPLAADGIDLAALQAANLVSGVV FT HALAAEYRPLTAAADQAAAPTPPEPR" FT CDS complement(50668..51462) FT /transl_table=11 FT /locus_tag="azo0045" FT /product="conserved hypothetical protein" FT /function="Allophanate hydrolase subunit 1" FT /note="Conserved hypothetical protein ybgJ. Homology to FT ybgJ of E. coli of 41% (sprot|YBGJ_ECOLI) InterPro: DUF213 FT (IPR003833) Pfam: DUF213, uncharacterized ACR, COG2049 no FT signal peptide no TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K1F8" FT /db_xref="InterPro:IPR002130" FT /db_xref="InterPro:IPR003833" FT /db_xref="InterPro:IPR010016" FT /db_xref="UniProtKB/TrEMBL:A1K1F8" FT /protein_id="CAL92663.1" FT /translation="MKPRVLDAGDAAFTVEFGDAIEPRLLAAVNALDAAIARLQADGGL FT PGVIETMPTFRSLTVFFDPLVTGRAALLAALQPLLAGDADRAAAPGRRWRLPVCYEGEA FT APDLAVTARATGLDEAAVVALHSGTEYRVYMLGFLPGFPFMGDLPEPLRLPRRAEPRLR FT VPSGSVAIATGLTAIYPWESPGGWHLLGRCPVPLFDVRRAAPALLAAGDRVVFAPVSGA FT EYVRLAAALQGGEIDPQEWLCSGVAEGDGTAAPSAAPEGGAR" FT CDS complement(51590..52516) FT /transl_table=11 FT /gene="dehH" FT /locus_tag="azo0046" FT /product="haloacetate dehalogenase" FT /function="predicted hydrolases or acyltransferases FT (alpha/beta hydrolase superfamily)" FT /EC_number="3.8.1.3" FT /note="Hypothetical haloacetate dehalogenase H-1 (EC FT 3.8.1.3). Haloacetate + H(2)O = glycolate + halide FT TREMBL:Q8Y2S9: 58% identity, 67% similarity Gene name:dehH FT from Ralstonia solanacearum genome project. InterPro: FT Alpha/beta hydrolase fold InterPro:IPR000073; FT A/b_hydrolase. IPR000379: Ser_estrs. Pfam:PF00561; FT Abhydrolase_1 nadp_idh_euk: isocitrate dehydrogenase No TMH FT present absence of signal peptide." FT /note="Family membership" FT /db_xref="GOA:A1K1F9" FT /db_xref="UniProtKB/TrEMBL:A1K1F9" FT /protein_id="CAL92664.1" FT /translation="MSVVTEVAAAADAVLFPGFARRRIEVGAGVSIPCVSGGDGPPLLL FT LHGHPQTHAIWHKVAARLARHFTVVASDLRGYGDASRPATTADHVRYSKREMAADQVAL FT MRALGHDRFSVLAHDRGARVAHRLAADHPQAVSRMVLLDIAPTLAMYEQTTETFARAYW FT HWFFLIQRAPLPERLIEADPTAYLRDVMGSRHAGLAAFDPTAFAEYARCLSQPGAAHSL FT CEDYRAAATIDLEHDRADRAAGRRLAMPLQVLWGQSGIVQRCFRPLDEWRRVADDVRGG FT TLPCGHYIPEEAPAELLAAALPFLLAD" FT CDS complement(52582..53337) FT /transl_table=11 FT /locus_tag="azo0047" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein Homology to FT pa4487 of P. aeruginosa of 52% (trembl|Q9HVT4(SRS)) no FT domains predicted signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR019220" FT /db_xref="UniProtKB/TrEMBL:A1K1G0" FT /protein_id="CAL92665.1" FT /translation="MSKPSCSERALSALLLALAAAPALAEIEMPVGGWRQGNAEAPYSQ FT EVNYPASRPAIDAGVPGVAQIRGRIARHTKGPATLVVNGNAMPLEVDEEGRYGRAYSFA FT TGSNSVEVRAGDGRPQRVQFYQTAAGQAEARLRVVLSWDTDGTDLDLHLITPDGEHAWY FT GNRAVKGGAIDVDVTTGYGPEIFASPAPLKGPYQIWVNYYGGGRGEMLTTARVAVISNE FT GTSSERRQEFDVPMRAAGELTLVRQFVYP" FT CDS complement(53315..54151) FT /transl_table=11 FT /locus_tag="azo0048" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein. Homology to FT rsc3028 of R. solanacearum of 57% (trembl|Q8XV04(SRS)) no FT domains predicted signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR019220" FT /db_xref="UniProtKB/TrEMBL:A1K1G1" FT /protein_id="CAL92666.1" FT /translation="MTAFPSRPWWRLCVALWAVAAAGAAAAMPPATLEAPSGGWNRGTL FT TDHSGDGAVAYPNPPIDRGVQAGRTLIRGRLAAEHRARDANRRPRTPPTLVVNGNPMPL FT YSDADGHFARPYAFGPGSNSVEIRSADGQPLRRLQFFEADPGRPRAQLRAILAWDDDQA FT EVDLHVLTPDGQHAFWAHPVLANGGGMDVDSVDGAGPEMFSMTAPLRGPYQLYVNYWGN FT FGDAGYHFDESTRQKKIITCRITLVFHENTPQERRESFVVPLRKIGDLTHVKTVMF" FT CDS complement(54285..56000) FT /transl_table=11 FT /locus_tag="azo0049" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT PA4488 of P. aeruginosa of 47% (trembl|Q9HVT3(SRS)) No FT domains predicted. No TMHs. Singal Peptide Present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR013693" FT /db_xref="InterPro:IPR018748" FT /db_xref="UniProtKB/TrEMBL:A1K1G2" FT /protein_id="CAL92667.1" FT /translation="MFPHLSSAFRLRLLVALACALLIRPAAAALDLAYRDPASGELVLQ FT RVDGEGRPLAGVQPPAAVPLGSVWKLFVFAWLVEHGVPAPDYACRAGRGSDAASRRLRE FT EESYCCESGGSIGRDAALVASCGLFFEPARLGIDAADWRAFWTARAPALPWLADLGALV FT PDTAVSPAALIGALEAVPPRARAEAASVLLARAFAPGGEAGAVGTLGGRLRVKTFSWYL FT PGTRTRYGGGAGWLADGTPLWFGGAGTGQQVLVRDAAALAAALPAGVGSLAPGCVDVAF FT FSRYPLRRVDGADGRPARAGALRGRHVAVFANGVSLPFRASGQMRLDLADGAPRVYGRF FT GVDEYVARVLDREADAGETEAARALAVVARSYLFNEARRAGNCLAIADSSRTQRVSPNP FT PSVAALAVAGFTTELVLRGAPVGYHLDTPGPDRLVWREAVAEARAGARWDAMLRRAFPA FT ADLVAARDPAGLPCDRLEVAERWLAEQVPRWRPQLAALPGFETPAPPRVCRLAWGTPFS FT ELDRGRIHVRALHSVEDRITLAHEYLHLGLRHHPASGDENWVEGWARRLVLGTP" FT CDS complement(56050..57162) FT /transl_table=11 FT /gene="phaZ" FT /locus_tag="azo0050" FT /product="Poly (3-hydroxybutyrate) depolymerase" FT /function="Poly(3-hydroxybutyrate) depolymerase" FT /EC_number="3.1.1.75" FT /note="This protein degrades water-insoluble and FT water-soluble PHB to monomeric FT D(-)-3-hydroxybutyrate,TREMBL:Q9LBN6 (35% identity); FT TREMBL:Q46334 (34% identity). SignalP predicting signal FT peptide." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1G3" FT /db_xref="UniProtKB/TrEMBL:A1K1G3" FT /protein_id="CAL92668.1" FT /translation="MKKTVRIIAGAALAVAFQATAAPPLPAFNIDIAETSISGISSGAF FT MAVQFQVAHSSIIKGAGIIAGGPYYCARDDFFRATTTCSCTGEPFLDCKVTDASAEVPA FT LVEATRRFHAERRIDDPANLARQRVVTVVGTADGLVPPTITAQLHAYYAASGMPWSSVS FT PVVVDGAGHTLPTLDFGRDCGLTETPYIGRCRFDSAKAILDWIYGQGVPLPPAPVRAPR FT RPTGRFVEFDQRPYLPADAPSPFTWGNGLDNSGWLYVPAACARGERCRLHIALHGCKQG FT QNFLPLRPPPGGGLYYGTTFVKNAGYHRWADDNRLVVLYPQAVSIPGWNPNGCWDWWGY FT TGAHYADRDGVQIRTIRAMVDRLASGRRDN" FT CDS complement(57268..58020) FT /transl_table=11 FT /locus_tag="azo0051" FT /product="conserved hypothetical membrane protein" FT /function="Small-conductance mechanosensitive channel" FT /note="Conserved hypothetical membrane protein. Homology to FT ebA624 of Azoarcus sp. EbN1 of 52% FT (gnl|keqq|eba:ebA624(KEGG)) . no domains predicted. no FT signal peptide. 3 TMHs" FT /db_xref="GOA:A1K1G4" FT /db_xref="InterPro:IPR006685" FT /db_xref="InterPro:IPR010920" FT /db_xref="UniProtKB/TrEMBL:A1K1G4" FT /protein_id="CAL92669.1" FT /translation="MELAHQRRCRCKRGMPSDMHRGRGAAPQGPAAAGLRWRRATVPPP FT VMTPPYNHGLAAFPPAFRECVMKQLLPAWADPWLDLIHLGLQIALILFGAALLRMVLRR FT LLRRLGEHYNLPPELVIGARRTISFVIYSGALLLVLDRFGVSGTVLWTAFTGFAAVAAV FT AFFAAWSVLSNIFCTLLIFTTRPFRLYDHIELLENGEKPGLKGQVVDINLIYTTLQESA FT GEHGDTVLQVPNSLFFQRCLRRWRGNPG" FT CDS 58066..59952 FT /transl_table=11 FT /locus_tag="azo0052" FT /product="hypothetical secreted protein" FT /function="predicted acetyltransferases and hydrolases with FT the alpha/beta hydrolase fold" FT /note="Hypothetical secreted protein. No homology of the FT entire protein to the data bank. FT InterPro:Esterase/lipase/thioesterase family active site FT Pfam:Putative serine esterase (DUF676) This family of FT proteins are probably serine esterase type enzymes. Signal FT peptide present (Signal P predicted) No transmembrane FT helices." FT /db_xref="UniProtKB/TrEMBL:A1K1G5" FT /protein_id="CAL92670.1" FT /translation="MPRWLRLLGLAGACLALAGCTLIRLGDEAQAFYTSTVLVGRVAAP FT AGWSGPVIVAAHREEDGDAPPAHRTLLHEAGGFELIVPAGDYRLFAFGDTNRNGRFDAG FT EPAGEYSGGKPVAASGSGVIALLDFALGDAAAASAAARRAAGWPPLDSRHSTQAGALAE FT LDAPAFSAANGVDGYWAPMAFFRASGGNVYFLEPYDPARIPVLFVHGAAGSAQDWRYFY FT EHLDRSRYQAWIFQYPSGAAVDSMAYLLYWKLFNLQLRHRFERLHIVAHSMGGLVARSF FT LINHGSQVRGLSLFISISTPWAGEPTAALGVKHAPAVVPSWHDMAPGGSFMRALFARPL FT PAGLDYYLLFGHRGGYSLLRPNHDGTVTLASQLRQAAQAEARMIYGFDEDHVGILSSPQ FT VLAQVQALLDSHAGGPRADIASGGQLRAAFATADGVLPAGVPLLVLQPLGEGARVAPIT FT VPLAATDSGRSLGPFPPGDYAASLLVQGYRAEPARQPLHIGDGAAATARFRLLPRGELA FT GYVGDEADAVGNPAGSYRRPHDTVRIREVDLRGAGVQRTLRPLDTAADDALALHLRGED FT SAERAHFAFFDLAAGDYELTIRADGYETHRSRHTVVPGQGGPMAPIVLQPRR" FT CDS complement(59974..61287) FT /transl_table=11 FT /gene="rstB" FT /locus_tag="azo0053" FT /product="probable sensor histidine kinase" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.13.1" FT /note="Probable two component sensor histidine kinase," FT /note="Specificity unclear" FT /db_xref="GOA:A1K1G6" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="UniProtKB/TrEMBL:A1K1G6" FT /protein_id="CAL92671.1" FT /translation="MKSLAGRVFLILVVATVLIQVLSFGGALAVSARDSRHQMFEFMGA FT DIAFLHRLLGRMPPAERETWIPALDRGFYQPALEPAGRTHPPADTPHLRESMVPMRRLL FT GPAIDVRAVMLAPPVPGEDGIPALAVALDEAHTLLVRFPTRKAPLAPPPLGVIAAYVAA FT VSLAVMLAAWGAVRLATRPLRRLADAARALGHNLDAPALPERGASELVEASRAFNAMQA FT ALQKNLAERTQILAAISHDLKTPLTRLRLRVGALPADEQARARIEADIDAMSHLVEEGL FT DYARSARPSEASTRVDLQALVESLAEQAADLGQAVRIEGRLAAPVRCAPRALQRALQNL FT LDNALKYGGGATTLRLAHEGDGVEIRIEDDGPGLPPALLEQVFEPFFRAEDSRSRQTGG FT AGLGLAIARNLLRAQGGDIRLENRGGGGLAAIVSLPQG" FT CDS complement(61284..62054) FT /transl_table=11 FT /gene="rstA" FT /locus_tag="azo0054" FT /product="probable two-component response regulator" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="Two component response regulator," FT /note="Specificity unclear" FT /db_xref="GOA:A1K1G7" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:A1K1G7" FT /protein_id="CAL92672.1" FT /translation="MNRPDHVLIVDDDPDIRDLLADYLGKQALQVSAAADGRQMRAALL FT AGPVDVVVLDLMLPGEDGMALFRWLRETPAHAQIPVVMLTARADDVDRIIGLEMGADDY FT LGKPFVARELLARVRAVLRRARMLPPGTVRTEVARYLAFGDWLLDTVERHLVARGGTVT FT LLQAAEYTLLRFLLDHPQCVVNRDQLLVGLAGREADVFDRSIDLRVSRLRKRLGDDARE FT PAYIKTVRNEGYVLCKTVAAHVTRPPGFGDGDGA" FT CDS 62241..62975 FT /transl_table=11 FT /locus_tag="azo0055" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type antimicrobial peptide transport system FT ATPase component" FT /note="ATP-binding cassette (ABC) transporters form a large FT family of proteins responsible for translocation of a FT variety of compounds across biological membranes. They are FT composed of two transmembrane domains responsible for FT binding and transport and two nucleotide-binding domains FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the TMDs, TREMBL:O54136 (41% FT identity); TREMBL:Q8RCZ7 (40% identity). Pfam (PF00005): FT ABC transporter. TC (3.A.1): The ATP-binding Cassette (ABC) FT Superfamily." FT /note="Family membership" FT /db_xref="GOA:A1K1G8" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K1G8" FT /protein_id="CAL92673.1" FT /translation="MTTESPAAAVRTEPVAVLRGIRKRYRLDNTAVLALDGVDLDIPPA FT RFTVITGPSGSGKSTLLHLLGALDRADAGTLHVDGRDLARLDDDALSAFRARHIGFVFQ FT SFNLLPVLTALENVEYPLRLGMLSAAARRARALDLLGAVGLADKARHRPAELSGGQRQR FT VAIARALANSPRLLLADEPTANLDRATGAGIIALLRRLQRETGTSVVFSSHDAAVLDAA FT DLRVTLVDGRVARLETGAEVAA" FT CDS 62972..64369 FT /transl_table=11 FT /locus_tag="azo0056" FT /product="conserved hypothetical membrane protein" FT /function="ABC-type transport system involved in FT lipoprotein release permease component" FT /note="Conserved hypothetical membrane protein. Homology to FT cv3942 of C. violaceum of 30% (trembl|Q7NR42) InterPro: FT DUF214 (IPR003838) Pfam: Predicted permease This is a FT family of predicted permeases and hypothetical FT transmembrane proteins. One member has been shown to FT transport lipids targeted to the outer membrane across the FT inner membrane, a step which requires ATP. Signal peptide 3 FT TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1G9" FT /db_xref="InterPro:IPR003838" FT /db_xref="UniProtKB/TrEMBL:A1K1G9" FT /protein_id="CAL92674.1" FT /translation="MSTLFLAWRNVLRNRRRSAITLATIAVAAMAVVMLGGYVAATIKG FT LETLTVRQVGHLQVMSRGYLEFGRANPARHALRDYAPLAGRLRADPQLAPLLHVVTPTL FT QVQGVAGHFASASSSTFSAAGWVADDRARMLAWDGLRLGTPPLPTALRADRPDDGVIGV FT GLAQLLDLCDALAIADCVRAPAAVPAAAAAIDADLAALSRQAREAGPAAPAAGAVVVDL FT LAAGASGAPNIVRMTATRAERQGVRELDMVHVGLPLALAQRLVFGTGAAGASALVLQLE FT DSARLDEARARVAAVVHDYAGDTLEVRTFAEVSPSYNQVVRMFRTLFGFVSLLMAVVTL FT FAVANTVNMAVSERTGEIGSLRAIGLPRARIRRMFVLEGGLVGAFGAVLGVALAVVLAG FT GLINHAGFSWTPPGNITPVPITIDVQGSARLCLGTVLAMTLIACISSWWPARRAARLEI FT VEALRHA" FT CDS 64362..65171 FT /transl_table=11 FT /locus_tag="azo0057" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT BPSS2323 of Burkholderia pseudomallei of 45% FT (trembl:Q63HU7). no domains predicted. singal peptide. no FT TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR011220" FT /db_xref="UniProtKB/TrEMBL:A1K1H0" FT /protein_id="CAL92675.1" FT /translation="MRDVLFPRGGRRRLLLAACCLAAGAALPGWVRADDDALALLAGSD FT RVRNLPGSFSVQIALTEFRHGKQTGSSVLTVYSRPAPDSGQYNNLVRFVAPARDAGKLM FT LRRGLDLWFHDPASGASVRISPQQRLLGQASNGDVMSTNLARDYRAELLGRESLRDGEG FT QPREAARLRLTALRDDVPYPLADYWIEPGSHHPLMARYHSAEGRLLKTAYFRKYREVLG FT VLRPTETVIIDGLDPDWVTLMQLSRHTAREVPEAWLQRDYLPRFSGE" FT CDS 65168..66349 FT /transl_table=11 FT /locus_tag="azo0058" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. signal peptide TMHs inside FT of the signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K1H1" FT /protein_id="CAL92676.1" FT /translation="MSAAARPARMLRVLGAALPLLLGAAGAPAAAAFDPLALQPEPPAD FT DTTTAPPPWHGSGPGLRLELAREQQDRAGGGSQGYSSVVLDFRGEWRTEAGLRLALSDR FT YERRIGGDAARNRNALREAYASLAAAPGWYVDFGRINWRNGVGSGYNPTDYLKRGADIE FT QGSLDPRAQRENRLGTVMLRQQWVGAAGSAQLALIPALADGPESSLTAPGWSRTNRERA FT ALLKLAPTVDERTSLDLLAYTRAGDAPQVGANLTRLLGDAWVLHAEFSRGRRAAAPGAP FT LRQADDSAIGLAWTTPPGAVLTLEHQHDGGARQRALFARLAWDDAFGLAGLDVSAFVRR FT TLDSRARRWQIELGWAAGDRDDLRLRWAGSDGTTDPAAPTPRHSLNLAWLHAF" FT CDS complement(66440..71053) FT /transl_table=11 FT /locus_tag="azo0059" FT /product="conserved hypothetical secreted protein" FT /function="Large extracellular alpha-helical protein" FT /note="Conserved hypothetical secreted protein. Homology to FT rsc3030 of R. solanacearum of 48% (sprot|YU30_RALSO) Pfam: FT Alpha-2-macroglobulin family Nterminal region (PF01835, FT PF07703) signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1H2" FT /db_xref="InterPro:IPR001599" FT /db_xref="InterPro:IPR002890" FT /db_xref="InterPro:IPR008930" FT /db_xref="InterPro:IPR011625" FT /db_xref="InterPro:IPR019565" FT /db_xref="UniProtKB/TrEMBL:A1K1H2" FT /protein_id="CAL92677.1" FT /translation="MTTLLRPSLPRLLSAALLALACTVAPPPAAAQSELGLSSGYVPFE FT SMPFFILADRQFGSGDEALLRVEVPARDGGRQMLEAYGGVDVVLYRVPKPLDFLKAQKN FT LHRVDVRARPRDEGLPNTLSYLWDNAWKKSRFAWRDLFDPRTRSTVTAAAPALQSRRAL FT LEPTEFRAPQRFKALEGYELVDRFRYPVWQAQPIKPPEVKLQGSSSDFIPASEGNIHVP FT LGKLKPGLYLVEAIIGTHRALTLLFVSDTVAVTKIAAGALTVWTANRNDGRPVADSRLL FT WTDGVGTLKSATTAADGLATLAHASPERTYLLGEDAAGGVFVSENFYYDSEIHDTKLYA FT VTDRPLYRPGDLVRIKFLGRDFQSASRSRPARAGELRIEVHDPNGTPVLTTSAPLVPDS FT GADTAFRLPDNAVAGGYDIRIGYEDKQYGAAFRVAEYVKPHFEIELLADQKSYKTGEPV FT SGKVRLAYPDGKPVKNAAVELTLRAQTLTMVQGELRYSGLFPVQLSTASLTTDGSGEAK FT FTLPAAKEPSRLILTLLATDGAAYRVRSSRELLVERAAASWKLASTRSFTMAGDKPAFR FT LEAEGENAAAPVKWEIVRLEDQSRSGGDFDPAQREWKPALDRPGSYSLMLRDAAGNIVA FT ATAHWVGGATDKDSLKVAPGSIEMVTDKVSYQPGDTAEVLISFPEPVDEALLTLERDGV FT DATALLSRPGSWLRTERLAPNQWRARIPVSEAHAPNITFSAVYVKHGDYVFQNAGLVVE FT PPRIALDIRSDHETVQPGDTVTVDIQAQLRGKPAPALLTVSVVDEMVYALQPEIAPSLP FT EFLQHIRRNNVRTSASLNFIAYDEAADWSAAASRQPPARHQYNERGVKVLERPRRDDTD FT TAAWLPALKTDAQGRARFSFRMPDALSRWRITVRAVGLDAADGVPGQRTAYVRSDKPLY FT AKWTSPDWLREGDKPQAALAVFNNAAEERKAEVVLTLAGKEIKQEASLHRGVNYLQFAL FT PDFKGRETARVEVKEGGKTVDALETPLDARGAKWRGPREQILALHGDAPAAFTLPADAR FT DLRLRLVAGGGEHFLRIADDLIDYPWGCTEQTASRLIPLALVTPLLAPDRRAEGEGGRL FT WQTLYSQRLRLAALAGPQAVFGWWGDGTENSALMTAYAYYADWYAARTLGITLPAAHWE FT RVLTAYRNHANHEPLLHRALALWFAQEIGLPVRTQSEGLLQALAEAKAPEDGRTGGESW FT SPFLAAPDSALGIAHARVLAAVVAQRAQAPLPAGFEATVAEAQAQLAASNRPAARALLL FT LAGKEARTAAADILASAGSAAPTLDRALTLVWTRKALGEIAPGASAARPAGAWQAARAA FT FGLAEWRWPSSSPLPNGLQVEGGRGGEALTAVLRYEAEEGAGPGTLPVTVERRLYRLER FT TDKGYTRTPVKPADGLSVQSLYLDEIVLKSDAGYRRGLLEAALPPGAAVERGTWGIALA FT DDGPQPVALERARAEERSGSYGVPVDRLEGTVTIRHLLRVAQPGRFVLPPARYYRMYQP FT EEKALADKGESGVWVVK" FT CDS complement(71064..71747) FT /transl_table=11 FT /locus_tag="azo0060" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT RS04726 of R. solanacearum of 55% (trembl|Q8XV01(SRS)) Has FT PF06672;(IPR009558)Protein of unknown function FT (DUF1175):This family consists of several hypothetical FT bacterial proteins of around 210 residues in length. The FT function of this family is unknown. No TMHs signal peptide FT present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR009558" FT /db_xref="UniProtKB/TrEMBL:A1K1H3" FT /protein_id="CAL92678.1" FT /translation="MSVRLAARRRALGAGLLLLGAATPLRALMPVAPGRAAEPVAQLDA FT EQSRALRAWVVRIAEAQIRRGPTPRWTHRDCAGLVRFAVAEALAEHDARWRQAMGISRR FT LPPDTVPAALRAELRHRWKRPDGSTGAYVNAIGLVQENSRPVGRDLRLARPADLLFFDQ FT GDAQHLMLWTGYRIVYHNGAEPRPGDDGLRAVTPRELLQWTDTRWRPDATNPNFAGVHT FT LAFLA" FT CDS complement(71744..73438) FT /transl_table=11 FT /locus_tag="azo0061" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein. Homology to FT RS04725 of Ralstonia solanacearum of 43% FT (trembl|Q8XV00(SRS)) No domains predicted. Signal Peptide FT Present. NO TMH reported present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR018671" FT /db_xref="UniProtKB/TrEMBL:A1K1H4" FT /protein_id="CAL92679.1" FT /translation="MTSASRSPRRKLLFGVIVLALVVGAVALFWLKRFDGHVNALALDL FT ARPDALIRTRSLARLPADLLRVPLARDVLTEDFVDYYERHEQRLALSGTLRRIAFEHRL FT SLPERVLESVFDEPAEVALWRGADGSLKHFVVAMTRNGLARALQMALPVLPDTQLESAG FT TLRGGKARLLVLQYGYGRQLLLAVEGDRVVALSDPGMLLVADDGDEHAGEEGAEPVQDA FT RAAALVARLLESDAERDSPFDAHFALAPAGADEGHQLVVSSAFYTFGYGAFAPGVEALS FT FAFDDKGGWRTAALIDGARLPAGGLDGAGLWPALPHGPSLCALLPADWGALAPLAARIG FT AGAGGESARAGVGELARELFGGPAAVCWYGESRHYTPLFATTLRRDVDEAWAKELAALF FT DSAIGKGEPAQRAPVEAGQRGSARLWRRTVETPYGARRGEDEPALAPTLAVSGRTLVFS FT PDAALVDKALDVGAKLYPAVGDSLPDGARTLALLEPAALAKLVRKEVFAALPRDEEAVL FT RNAADANLLPRLEALAKYPPLRLVRAEGALEGRGWHALQWESAGNRP" FT CDS 73627..75072 FT /transl_table=11 FT /locus_tag="azo0062" FT /product="conserved hypothetical protein" FT /function="Fe-S oxidoreductases" FT /note="Conserved hypothetical protein. Homology to MCA0287 FT of Methylococcus capsulatus of 48% (trembl:Q60C24). no FT domains predicted. no signal peptide. no TMHs" FT /db_xref="GOA:A1K1H5" FT /db_xref="InterPro:IPR012285" FT /db_xref="UniProtKB/TrEMBL:A1K1H5" FT /protein_id="CAL92680.1" FT /translation="MNGTALASYPCGLPPCLFRPPAPEPDRIRRAHMKHQLDWSSYETA FT GQGDAYAGIPATGGDFAKAVAVCISDRSCLKKPKGVMCPSFRATDEAAHSPGERVKVLK FT DALNGEFGDNPFADPRIRDALELCVGCKGCKRECANQVDMAAIKIEVLAQRNAALGVSP FT RDRLFASLPRLLGERRWLASLVRWRNRSPWLARLGERWLGIAAGRALPEPAAQPYAAPA FT ARATAPADTADDRRVILFVDTFARHFEPEIAAAAHAVLDAAGYQVEVLAPAAADGEQRP FT LCCGRTWLSLGQVDAARAEARRMQAALRPALEKGWPVVGLEPSCILSLRDDHLKLGLGA FT EAEALAKQVYLFEEFIAREHDRKRLQLKLKPLAGGKTLVHGHCHQKAVGAMKSLRKVLR FT LIPEFDFEFVEASCCGMAGHFGLEAEHAEISRRMAELDLLPALRAAPDAPVLANGFSCR FT HQIREGVARQPRHVALLLQAALA" FT CDS 75089..75535 FT /transl_table=11 FT /locus_tag="azo0063" FT /product="hypothetical protein" FT /note="Hypothetical protein. No good homology to the data FT bank. No domains predicted. No TMHs Probable signal FT peptide." FT /db_xref="UniProtKB/TrEMBL:A1K1H6" FT /protein_id="CAL92681.1" FT /translation="MSDSSDAFRAAGALPIHPATAAVPAADIGRALWCAGLLGNLHDAG FT VAISLCTSGWDQAAFFESRAARKKALQCLNVMVDSARDLPDAVTARLGRIDWLAWEALR FT AVLKARTADERDRLWYAIGTLVPATVIELRRYRRQMPQLFEFSL" FT CDS complement(75546..76649) FT /transl_table=11 FT /locus_tag="azo0064" FT /product="probable permease" FT /function="predicted permease" FT /note="Hypothetical protein ydiK.Integral membrane protein FT (potential). similarity:belongs to the upf0118 (perm) FT family TREMBL:Q7WQ94: 68% identity; 81% similarity. FT PIR:AD2790; AD2790.C97569; C97569. InterPro:IPR000585; FT Hemopexin. IPR002549; UPF0118. Pfam: PF01594; UPF0118; FT 2A0604s01: protein-export membrane pro Pfam: presence of FT DUF20 domain and branched chain amino acid transport. FT TIGRFAM: general nitrate transport. Signal P predicted FT signal peptide and TMHMM predicted transmembrane helices." FT /note="Function unclear" FT /db_xref="InterPro:IPR002549" FT /db_xref="UniProtKB/TrEMBL:A1K1H7" FT /protein_id="CAL92682.1" FT /translation="MPSIFPAHLVARWLLFLLLLAGVYFLSGFIVPVLAALIIGFASWP FT LYERLLRRCGGRSAVAASLALMTVILVLVVPLSLAGSYAMREADTLIEWLLAANRNGMA FT PPRWVEALPLVGGRLAALWQEYLGAPQALGEWVQILSGQHLGNIYRILLAATGDLLHAV FT LTLLFMLITLFFIYKDGDRIAAQLDRVGEQVLPARWQRFSRVVPATVSATVTGMGLIAI FT GEGVVLGLAYWIAGVPSPVLLGVATAFMALIPGGAPLAFTLVSLYLVGSGDPMAGLALF FT TWGTCELFIVDKTLRPRLVGGPVKLPFLPTFFGLVGGVKTMGLVGLFVGPVLMALLVAI FT WREWLHHTEEEAAAAVGIEDGRPASDA" FT CDS complement(76751..77287) FT /transl_table=11 FT /locus_tag="azo0065" FT /product="conserved hypothetical protein" FT /note="64% similarity with ABC-type multidrug transport FT system, ATPase and permease components [Dechloromonas FT aromatica RCB]. and" FT /db_xref="InterPro:IPR021332" FT /db_xref="UniProtKB/TrEMBL:A1K1H8" FT /protein_id="CAL92683.1" FT /translation="MSTDGTACSPRPWPQVPACYGWLSLDRRGRWRLQGEPVTHRGLLA FT FLNQHYASEEDGAWFVQNGPQRVFVRLDYTPFVLRMGADGGLLTHTEAAAGPASAVHVD FT DEGSVLIATAAGIGLLDDRELPAFVDECRGADGAAAEIEAVLACAGVSWRGLPLQPIGR FT AEVAARYGFRADPQP" FT CDS complement(77284..78402) FT /transl_table=11 FT /locus_tag="azo0066" FT /product="probable enoyl-CoA hydratase/isomerase" FT /function="Enoyl-CoA hydratase/carnithine racemase" FT /EC_number="4.2.1.17" FT /note="Enoyl-CoA hydratase and 3-2trans-enoyl-CoA isomerase FT are two enzymes involved in fatty acid metabolism. ECH FT catalyzes the hydratation of 2-trans-enoyl-CoA into FT 3-hydroxyacyl-CoA and ECI shifts the 3- double bond of the FT intermediates of unsaturated fatty acid oxidation to the FT 2-trans position.In Escherichia coli (gene fadB) and FT Pseudomonas fragi (gene faoA), ECH and ECI are also part of FT a multifunctional enzyme which contains both a HCDH and a FT 3-hydroxybutyryl-CoA epimerase domain. InterPro: Enoyl-CoA FT hydratase/isomerase Entry name TREMBL:Q8PMW0 Prim. FT accession # Q8PMW0 InterPro IPR001753; EnCoA_hydrtse. Pfam FT PF00378; ECH; 1 Identities = 169/379 (44%) Number of FT predicted TMHs: 0 Signal peptide probability: 0.000" FT /note="Family membership" FT /db_xref="GOA:A1K1H9" FT /db_xref="InterPro:IPR001753" FT /db_xref="UniProtKB/TrEMBL:A1K1H9" FT /protein_id="CAL92684.1" FT /translation="MTAAVLLREIPTACGRRFGHATLNAERALNALSLEMIDLLAPQLD FT AWAADPDIVGVVLDGSGDKAFCAGGDVAALYRALRAHDGDAPPQAVTDFFEREYRLDYR FT IHTYPKPLLCWGHGIVMGGGIGLLAGASHRVATLQTRMAMPEITIGLYPDVGGSWFLPR FT MPGRAGLFLALTGAPLNAADARFAGLADFVLDHGARGGVLAALGATRWAGDAAADRLRL FT DHLLGEFSVREGMPAAPLRTHLDRIEAVVGRGSLAEIAVRLHALAADPDPWLAAAAGSF FT VRGAPSSAALSLELWRRARHLSLAEVFRLEYIVSVAATGRADFVEGVRALLIDKDRKPR FT WQHADVGAVDTAFIADNFRARFDGAHPLADLA" FT CDS 78461..79156 FT /transl_table=11 FT /gene="polC" FT /locus_tag="azo0067" FT /product="DNA-directed DNA polymerase" FT /function="DNA polymerase III alpha subunit (gram-positive FT type)" FT /EC_number="2.7.7.7" FT /note="DNA polymerase III polC-type (EC 2.7.7.7) (PolIII). FT Required for replicative DNA synthesis. This DNA polymerase FT also exhibits 3 to 5 exonuclease activity (By similarity). FT InterPro: Exonuclease dnaq: DNA polymerase III epsilon FT subun" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1I0" FT /db_xref="InterPro:IPR006054" FT /db_xref="InterPro:IPR006055" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR013520" FT /db_xref="UniProtKB/TrEMBL:A1K1I0" FT /protein_id="CAL92685.1" FT /translation="MHHGLRRRAIVRALRWISLTLVAAEDHLDTYAVIDFETTGMAPEH FT GARPTEIAVVLVRNGCVIDRYQSLMNAGVHVPYEIQALTGITNAMVRAAPPLAQVMAQA FT ADFVGSHALVAHNAAFDRKFWDAELDRLGRRREADFVCSLLLSRRVFPDSPNHKLGTLV FT RTLGLPASGRFHRALADAEATAQLFARIAHTLCERYALAALDHALLMKIQKTARGALDG FT CIARHRAAA" FT CDS complement(79164..79916) FT /transl_table=11 FT /locus_tag="azo0068" FT /product="Hypothetical protein" FT /note="Hypothetical protein. No good homology with any hits FT of this length protein. No Domains/Features/motifs/signal FT peptide present." FT /db_xref="GOA:A1K1I1" FT /db_xref="InterPro:IPR009097" FT /db_xref="UniProtKB/TrEMBL:A1K1I1" FT /protein_id="CAL92686.1" FT /translation="MIESAPPSPRPGSLAAVRAQFVAAGRTLRNVRRDFAEWHGGRPRY FT ALWAIPLDLPAVAARVAAADAHLAGLLLTGYRRQPHVTLALCGFPQRQPRRRDDYGPAA FT LAAQLGSLRSAPPGPFEIEIGGLATFGSAPFLTVHDSGGGLAMVRARLAAADLNRPDGP FT YTPHVTVGLYAGAWPAAEVLCRIDGFVAPPPLRLRVDRIALLTYDTRDIAGPLLQAAEF FT DLRDGALLPGGAAAAGFDEAFFAPAEID" FT CDS 80013..80393 FT /transl_table=11 FT /locus_tag="azo0069" FT /product="conserved hypothetical globin-like protein" FT /function="Truncated hemoglobins" FT /note="Conserved hypothetical globin-like protein. Homology FT to rpa2719 of R. palustris of 46% (tremblnew|CAE28161). FT Interpro: IPR009050 Globin-like. Globins are FT heme-containing proteins involved in binding and/or FT transporting oxygen. This family of heme binding proteins FT are found mainly in bacteria. No signal peptide. No TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K1I2" FT /db_xref="InterPro:IPR001486" FT /db_xref="InterPro:IPR009050" FT /db_xref="InterPro:IPR012292" FT /db_xref="UniProtKB/TrEMBL:A1K1I2" FT /protein_id="CAL92687.1" FT /translation="MTELTEQHIRNLVHTFYGRARQHPSLGPVFNAAVSDWDHHLGVIV FT DFWSNSLLHTQRYKGHAFPVHMNLPIKREHFGQWLELFREAARETLPEEAARAAIGRAE FT FMAESFRAGLFPLDPPGRPLAG" FT CDS complement(80397..80645) FT /transl_table=11 FT /locus_tag="azo0070" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. no homology to the FT data bank. no domains predicted.signal peptide. 1 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K1I3" FT /protein_id="CAL92688.1" FT /translation="MPRATPTLRQRKIFALTRILGGLVAALYLGYVVVANLAAGAPFDR FT TLMFTAAVAAAGFGYAAWYLRDLQAVAREERAAANKE" FT CDS 80784..82139 FT /transl_table=11 FT /locus_tag="azo0071" FT /product="sigma-54 dependent response regulator" FT /function="Response regulator containing CheY-like receiver FT AAA-type ATPase and DNA-binding domains" FT /note="Sigma-54 dependent response regulator," FT /note="Specificity unclear" FT /db_xref="GOA:A1K1I4" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR002078" FT /db_xref="InterPro:IPR002197" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR020441" FT /db_xref="UniProtKB/TrEMBL:A1K1I4" FT /protein_id="CAL92689.1" FT /translation="MNPESAPASAPQQSVLVVDDEQGMRNFLSRALALRGFVVDTAESA FT EEGAEKLAATRFDLVILDIALPGKAGIEWLQDLTAAGFAGEVILITAFADMQTAIDALR FT AGAADFILKPFRIDQILNSIHRSTERARLARENFLLRRQVAGSGSASDGMIGASPAIGQ FT LRQILHRIAPTPSTVLIQGESGVGKEVVARALHQLSPRAEQPFVAVNCAAISAELIESE FT LFGHVKGAFTGAREARNGLFHYAHGGTLFLDEIGELPLALQSRLLRVLEERKVRPVGTE FT QEVPVDVRVLAATNRDLRAEVAACRFREDLFYRLEVITLTVPPLRERAEDVPALAAAFM FT QQLAMQLGLPPLLISPEVSARLMAHPWPGNVRELRNFVERSLLFGDFPLASLAGAVAPP FT PPASAAPLLLEEVEKRHILAVLDQCGGNKTRAAELLGVSRKTLERKCAEWSV" FT CDS 82158..84344 FT /transl_table=11 FT /locus_tag="azo0072" FT /product="putative sensor histidine kinase" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.3.-" FT /note="Putative two component sensor histidine kinase," FT /note="Specificity unclear" FT /db_xref="GOA:A1K1I5" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="UniProtKB/TrEMBL:A1K1I5" FT /protein_id="CAL92690.1" FT /translation="MAERALRRWRKRWPVPRSVRARLLLLVLAPLLIGVPVLLGIVWVW FT GTHGYDRLLVNKVSADLLTARQYFERVQQGVAGDLAAVASSHALALALQGQGPDSVEVL FT LDTSASRLGLDYLLFLDPQGRVTVPSAPLPSALAERGNWPAVRSALQGRAEHTLAVFPP FT EHLEALDPALRAHATLGLVPTQRAAPDPRPREERGLMVQVAVPVTDLGGRLLGVLEGGV FT MLNRNLGIVDRINAAVYQDSSLPLDSQGTATLFLDDIRIATNVRLFEGSRALGTRVSAA FT VRDKVLGRGETWLGSAFVVNADYISGYAPLFDGDGKAVGMLYVGFLQAPLQQALYLALG FT GLFLVFLLLSGLGTLAAVRWARSIFQPIERMAAVMGRIESGEEQARVGAVVRDDELGGL FT ARSFDRLLDLLAARRAELQRWGQELDSKVAARTAELEAANATLRRAHQQLVMNEKLTAI FT GELTAGVAHEINNPVAVIQGNLELVRELLGGDSAPVADELAQIDAQVGRIHGIVTKLLQ FT FARPGDFAGYTEQVDASGLVGDCLLLTRHNLSRGRIEVTTALDARGTVEINRGELQQVL FT INLIVNAMQAMPDGGRLRLSTADIDEGGEDDDAGHGAGRNGKSEHRHGFAGVCIRVEDT FT GCGIAADDLDRIFDPFFTTKKQEGTGLGLSISYAIVTRYGGHLNVDSQPGQGTRFTVCL FT RREARFDGEPSAPGFASRFFRSAGIDNLNDGHHD" FT CDS 84372..85583 FT /transl_table=11 FT /locus_tag="azo0073" FT /product="putative MFS permease" FT /function="Permeases of the major facilitator superfamily" FT /note="Permease,member of the Major Facilitator FT Superfamiliy (MFS)transporters. MFS are single-polypeptide FT secondary carriers capable only of transporting small FT solutes in response to chemiosmotic ion gradients. Probable FT sugar-proton symporter transmembrane protein ProP FT proline/betaine transporter. Low homology to the FT hypothetical protein ycxA (ORF5)involved in the FT biosynthesis of the pepitde antibiotic Bacitracin in B. FT subtilis. Signal peptide" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1I6" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:A1K1I6" FT /protein_id="CAL92691.1" FT /translation="MLRTLNQPGLWLITLTAAGILMVTMGVRQSTGLFVSPLNSATGLG FT ITTISFALAIAQFTWGAVQPLAGAAADRYGPGPVLAGGILLLALGSALTPFMQSSFGLV FT VSLGLLSAMGSGAASFSVLIGAAAQRLPLEARGAASGVVNAGGSFGQFVFAPIAQKLIQ FT GVGWMGAMWGLALLTLAALPLVRKLVPPGSHPRHTASDGSLRRALGEALRDRSYRLLHL FT GFFTCGFHIAFLVTHLPGEVALCGLPADVASWSLAIIGLANIAGSIYAGGCVARYRSKH FT ILFWMYASRAVLVALYLMAPKTAMTFYLFAAGLGFTWLATVPPTAAIVGKLFGVRHLGT FT LFGLTLLSHQIGGFLGAWLGGIAVSLQGDYTWMWYADMALAAAAALVNLPIREAPVAVA FT PAAA" FT CDS 85691..87382 FT /transl_table=11 FT /locus_tag="azo0074" FT /product="conseved hypothetical exported protein" FT /function="uncharacterized protein containing a von FT Willebrand factor type A (vWA) domain" FT /note="Hypothetical protein yfbK. The von Willebrand factor FT is a large multimeric glycoprotein found in blood plasma. FT Mutant forms are involved in the aetiology of bleeding FT disorders [1]. In von Willebrand factor, the type A domain FT (vWF) is the prototype for a protein superfamily. FT trembl:Q8P6Q2: 55% identity; 66% similarity FT InterPro:IPR002016; Peroxidase. IPR002035; VWF_A. Pfam: FT PF00092; VWA; 1. SMART: SM00327; VWA; 1. cdhD: CO FT dehydrogenase/acetyl-CoA syn Signal peptide present (0.927 FT probability); SignalP predicted. No transmembrane helices FT (TMHMM predicted)." FT /note="Function unclear" FT /db_xref="InterPro:IPR002035" FT /db_xref="InterPro:IPR021908" FT /db_xref="InterPro:IPR022156" FT /db_xref="UniProtKB/TrEMBL:A1K1I7" FT /protein_id="CAL92692.1" FT /translation="MNTARHRIVLLALPLLFACSAQEPLRPLVQEPAAASASGEQADRA FT AEAAAPAAPPPVAPARVQRHDAMGAAKIAPPAVAPLPLAEPADRERYQAIERHGIQRVA FT EAPVSTFSIDVDTGSYSNLRRMLNAGQLPPRDAVRVEELVNYFPYRYSLPQGDAPFAVD FT TEIAPTPWNPRSLLLRVGIQAADPAKQALPPANLVFLVDVSGSMNSPDKLPLLQNALKL FT FVAQLRPQDRVALVTYASGTRVVLEPTAGDRKAAITAAIDGLVPGGATAGAAGIDLAYR FT MAEQGFVEHGINRILLATDGDFNVGITRFETLKDRVAERRKSGIALSTLGFGGGNYNDQ FT LMEQLADAGDGAYRYIDSLAEAQKVLVDEFTSTLATVASDVKIQLEFNPAQVAEYRQIG FT FENRKLRREDFANDKVDAGEIGAGHRVTALYEITLAGQPGAIEPLRYGQRAATPARATS FT GELAFLRLRYKPAHGAASRLLEVPLARSQIRSQGSDDFRFAAAVAAFGQRLGDGGRYLG FT DFDFAAIGALAAAARGDDRYGHRGEFLNLVRLAGSLASAPQAAARE" FT CDS 87379..87978 FT /transl_table=11 FT /gene="rpoE" FT /locus_tag="azo0075" FT /product="probable RNA polymerase sigma-E factor FT (sigma-24)" FT /function="DNA-directed RNA polymerase specialized sigma FT subunit sigma24 homolog" FT /note="Probable RNA polymerase sigma-E factor (sigma-24)," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1I8" FT /db_xref="InterPro:IPR007627" FT /db_xref="InterPro:IPR007630" FT /db_xref="InterPro:IPR013324" FT /db_xref="InterPro:IPR013325" FT /db_xref="InterPro:IPR014284" FT /db_xref="UniProtKB/TrEMBL:A1K1I8" FT /protein_id="CAL92693.1" FT /translation="MNDGALSGGAADDGALMLAYAAGDAAAFEQLYARHRRGLYAYLQR FT QAPRPGWVDDLFQETWLAVIGARAGYRPSAAFRTWLYGIARNKLIDRIRRSDAVLLSDF FT LADDGDDGELLDRLGADAGHDPAQLLARRRDGDALHAALRTLPAPQREVFLLREQADMS FT LTEIAALVGVPLETAKSRLRYAIARLRAALAEEVAG" FT CDS 87975..88751 FT /transl_table=11 FT /locus_tag="azo0076" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT BB3269 of Bordetella bronchiseptica of 31% FT (trembl|Q7WHD9(SRS)). No domains predicted. no signal FT peptide 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K1I9" FT /protein_id="CAL92694.1" FT /translation="MTRPTPEHEPQDAAVSAAFRGLDTPEPPPALDAAILAAARAAVAE FT APPSSAEVVAFPRRRRETRRWLALAATLVLAVGVSWQLRDSADHGLPAPAPATAPVEQE FT APAVLATPPATEAEQRAAKPAAPAPARRAESAAAPAPRAEPQAAAEAAPPVAAPPAPAA FT TAPAAPPLAAPAAAEATADAAAPAAKALAPAIAAQRARADHTDGAEAEREAAITTIRRL FT LAAGRPDEARERLQDFRRRWPDAVLPPDLTALAAAP" FT CDS complement(88772..88993) FT /transl_table=11 FT /locus_tag="azo0077" FT /product="Hypothetical protein" FT /note="Hypothetical protein. No Good homologs. No FT Domains/Features/Motifs reported present." FT /db_xref="UniProtKB/TrEMBL:A1K1J0" FT /protein_id="CAL92695.1" FT /translation="MSRKHKQRRDLPLVVPPSPPPRNPLATAPKMRRGVQVHDKSRGAL FT RRAEHMALRRLAVPAVHGEEGDDSDEDG" FT CDS complement(89004..89966) FT /transl_table=11 FT /locus_tag="azo0078" FT /product="Hypothetical protein" FT /note="Hypothetical protein. Weak homology with hits over FT entire length. PS50821; PAZ domain present(Prosite)" FT /db_xref="UniProtKB/TrEMBL:A1K1J1" FT /protein_id="CAL92696.1" FT /translation="MQMQEIDSLRALLPRGRTLFPYFKDKYSLQLLRYALPRPTAVAAL FT RGHAAAQLLQKPALRALLAGCGGMLDRATVDAAWLPGMLQPEHYTLSLGVWGNGRWRAA FT QTSRRGANLVLQLNFNHGHNRAFGRLVRPHGGEDPFNAWGHPALRDPTAPEPRYTLAWA FT RLDVDFERGEALIEELQTDWLRRAARVRDNALRLDDATFARRYQRSFGGSRADVVAYHD FT RHLAPHRALWDEALLAATLFFLREELGIADIWMHTPRSGVLLKDIRHGAAPPVSVYSSL FT PQRFCFRPGTTLPAFLAADRSVLRRLRRAEGVQLLKFSL" FT CDS complement(90144..91352) FT /transl_table=11 FT /gene="rtcB" FT /locus_tag="azo0079" FT /product="rtcB protein" FT /note="rtcB protein, 57% identical(70% similairty) to FT TrEMBL;Q7NZ85 TrEMBL;Q8FCS7(56% identity). Has FT IPR001233;UPF0027(PF01139, Uncharacterized protein FT family):A number of uncharacterized proteins including FT Escherichia coli rtcB, Mycobacterium tuberculosis FT MtCY441.01., Caenorhabditis elegans F16A11.2 and FT Methanococcus jannaschii MJ0682 belong to this family. Has FT no Signal peptide or TMH present." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR001233" FT /db_xref="UniProtKB/TrEMBL:A1K1J2" FT /protein_id="CAL92697.1" FT /translation="MAIQLTLNKGRVPIKLWTRDIEHEALQQLVNLSQLPIVDHPIAAM FT PDVHAGIGATIGSVIPTAHAIIPAAVGVDIGCGMNALRLSLDAGRLPDNLGRLRSAIEA FT AVPVGFEQHDESRVRGSAHARQARRLGDRLDAIVGRHPGLMKMQRRFNTTWICQLGSLG FT GGNHFIELCVDEADQLWVMLHSGSRGIGNVIGRYFIAAAKKDMGRHLHALPDKDLAYFS FT EGSALFDDYVDAVHWAQDYAMENRRMMMALVVEAIRPLLPAFSITEEAINCHHNYVARE FT THFGESLYVTRKGAIRAGAGELGIIPGSMGVKSYIVRGLGNAASYCSCSHGAGRRMSRS FT EAKRRFSRFDLEAQTAGVECRKDGGVIDEIPAAYKNIDEVMANQTDLVEVVHTLKQVLC FT VKG" FT CDS 91812..93434 FT /transl_table=11 FT /gene="prfC" FT /locus_tag="azo0080" FT /product="peptide chain release factor" FT /function="Peptide chain release factor RF-3" FT /note="Peptide chain release factor 3 (RF-3). Increases the FT formation of ribosomal termination complexes and stimulates FT activities of RF-1 and RF-2. It binds guanine nucleotides FT and has strong preference for UGA stop codons. It may FT interact directly with the ribosome. The stimulation of RF- FT 1 and RF-2 is significantly reduced by GTP and GDP but not FT by GMP" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1J3" FT /db_xref="InterPro:IPR000795" FT /db_xref="InterPro:IPR004161" FT /db_xref="InterPro:IPR004548" FT /db_xref="InterPro:IPR005225" FT /db_xref="InterPro:IPR009000" FT /db_xref="InterPro:IPR009022" FT /db_xref="UniProtKB/TrEMBL:A1K1J3" FT /protein_id="CAL92698.1" FT /translation="MSSTPFPPELLRDVDKRRTFAIISHPDAGKTTLTEKLLLFGGAIQ FT LAGTVKARKSARHATSDWMEVEKQRGISVTSSVMQFEYQDHTINLLDTPGHEDFSEDTY FT RVLTAVDAAVMVIDAAKGVEAQTIKLLEVCRLRNTPIITFVNKMDREVREPFELLAEIE FT DVLKISCAPVTWPIGMGKAFRGVYHLLQDHVLTFTPGEERRSDAEVLSGIGNPELDARF FT PMEIGQVRENVDLLNDASPPFDLDEFLAGKQSPVFFGSGINNFGVQEILQALIDWAPPP FT QQRIAGTKGNDTRMVQPAEPAFTGFVFKIQANMDPKHRDRIAFFRICSGRYQSGMKVKH FT VRAGREMKLANALTFMANERVLKDDGVAGDIIGIHNHGQLQIGDTLTEGEILGFKGIPY FT FSPEMFRAARLRDPLKSKQLQKGLQELGEEGAIQVFEQDGGQMLLGAVGQLQFEVVAQR FT LKDEYKVDAIFETADIHTARWLTFPDDLTRRNFEREQALRLGKDVDGNLVYLASSRYNL FT EVTREKWPTVGFHATREHGQVIA" FT CDS 93454..93981 FT /transl_table=11 FT /locus_tag="azo0081" FT /product="conserved hypothetical membrane protein" FT /function="predicted aspartyl protease" FT /note="Conserved hypothetical membrane protein. Homology to FT pa4965 ao P. aeruginosa of 50% (trembl|Q9HUK0) Pfam: FT Retroviral aspartyl protease no signal peptide 1 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR011969" FT /db_xref="InterPro:IPR018061" FT /db_xref="InterPro:IPR021109" FT /db_xref="UniProtKB/TrEMBL:A1K1J4" FT /protein_id="CAL92699.1" FT /translation="MSNTDHADTRRLGRVMAWLAALALLGLLWLYFENELEHRNNPNRG FT LVADPGGGAELVLKRNRAGHYVAPGTINGRPVTFLLDTGASQVSVPARLADQLDLKPGA FT PAQVMTANGAVQVRLTRIDELVLGPFRVRGVQGHLNPGMNAHDEILLGMSVLKALEFTQ FT RGDTLILRAPTP" FT CDS complement(94431..95405) FT /transl_table=11 FT /gene="rdgC" FT /locus_tag="azo0082" FT /product="recombination associated protein RdgC" FT /function="DNA recombination-dependent growth factor C" FT /note="Recombination associated protein rdgC. Not known; FT may be involved in recombination (By similarity). hemC: FT porphobilinogen deaminase." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1J5" FT /db_xref="InterPro:IPR007476" FT /db_xref="UniProtKB/TrEMBL:A1K1J5" FT /protein_id="CAL92700.1" FT /translation="MWFKNLQLYRLPAPWDISLERFEEQLAKRRFQPCGSQDMESRGWV FT APVADDVLVHPVGDQWLIALGVEGKLLPSSVVKQVADERAEEIAEQQGYKLGRKQLKEL FT REQVTQELLPRAFTRRRRIHAWIDPVHGWLAVDASSAARAEDVLEHLRQTLDSLPLALL FT RTERSPSSAMADWLAGGEAPANFTIDQDCELRSVTEDKAAVRYVRHTLEGDEIKGHLTA FT GKLPTRLAMTFDDRVSFVLTEKLEIKRLDFLDVVRDQIDGEAEDAIALFNAEFALMTGE FT LQKLLPAVVDALGGELATPEVQPAVTAFDRPAVEPALAGDPPF" FT CDS complement(95476..95943) FT /transl_table=11 FT /locus_tag="azo0083" FT /product="conserved hypothetical protein" FT /db_xref="InterPro:IPR015075" FT /db_xref="UniProtKB/TrEMBL:A1K1J6" FT /protein_id="CAL92701.1" FT /translation="MKFEHLVEVNDLADPHTTRLTREELWFGLLCRAEDARPFLPGLES FT CRIVERSPNELVRDLHFGAAVIRDRVRFAELEWISFESEANAEHAGGSLTIRIEEPQPG FT ALFLRFIYATTLPDVGGEDAKYADIVRSAYHQSDLDTLKMIRMIAESGRLQ" FT CDS 96022..96768 FT /transl_table=11 FT /gene="rsuA" FT /locus_tag="azo0084" FT /product="pseudouridylate synthase" FT /function="16S rRNA uridine-516 pseudouridylate synthase FT and related pseudouridylate synthases" FT /EC_number="4.2.1.70" FT /note="Ribosomal small subunit pseudouridine synthase A (EC FT 4.2.1.70) (16S pseudouridylate 516 synthase) (16S FT pseudouridine 516 synthase) (Uracil hydrolyase). FT Responsible for synthesis of pseudouridine from uracil-516 FT in 16S ribosomal RNA." FT /note="Family membership" FT /db_xref="GOA:A1K1J7" FT /db_xref="InterPro:IPR000748" FT /db_xref="InterPro:IPR002942" FT /db_xref="InterPro:IPR006145" FT /db_xref="InterPro:IPR018496" FT /db_xref="InterPro:IPR020103" FT /db_xref="UniProtKB/TrEMBL:A1K1J7" FT /protein_id="CAL92702.1" FT /translation="MQAMQIERLLHSQGFGSRKDCRALLRAGYVSVAGVPCDDPRAEFD FT PGSKDGSPGLEFTVDDEIWHFRAQAYLMLHKPAGYECSHKPTFHPSVFTLLPPQLLNRG FT VQCIGRLDQDTTGLLLLSDDGQFIHQWSSGKKRTPKVYEIGLKHAADDALVAALLAGVE FT LHDEPTPIAAAACEITASHALRLTITEGKYHQVKRMVAAAGNRVETLHRSRVGGLTLDP FT ALKPGEWRWLEAADIAALAAGAADGD" FT CDS 97020..98186 FT /transl_table=11 FT /locus_tag="azo0085" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to RS04117 FT of R.solanacearum of 52% (tremble:Q8Y0H4) No domains FT predicted. No signal peptide. No TMHs" FT /db_xref="InterPro:IPR016633" FT /db_xref="UniProtKB/TrEMBL:A1K1J8" FT /protein_id="CAL92703.1" FT /translation="MNPIAPQTPPEWEIFCRVVDNYGDIGVCWRLARMLAATGATVRLW FT VDDWSALGRLCPAVADATGAALLAGVELRQWSSPFPAPAPGANVIEAFACELPSSQVHA FT MARCSPPPAWINLEYLSAEDWVAGCHRLASPHPALGLVKHFFFPGFDAGSGGLLREPGL FT LAARDRYRAGGGRAALLQGLGLGADTADALVVSLFAYEQPALAELVGAWRHSPQPLVLL FT VPEGRVLADLAGALGGDPLAVGERRRLDALQVAVLPFSDQDGYDRLLWSCDLNFVRGED FT SFVRAQWAAAPFVWQIYRQPDDAHADKLDAFLARYAAGLDDAPRTALGRFWKAWNGEGS FT AAAAWPDFAAALPLLADHTARWSAALAAQDDLATQLKRFCNHIRQPAG" FT CDS 98247..98804 FT /transl_table=11 FT /gene="efp" FT /locus_tag="azo0086" FT /product="putative elongation factor P" FT /function="Translation elongation factor P FT (EF-P)/translation initiation factor 5A (eIF-5A)" FT /note="Elongation factor P (EF-P). Involved in peptide bond FT synthesis. Stimulates efficient translation and FT peptide-bond synthesis on native or reconstituted 70S FT ribosomes in vitro. Probably functions indirectly by FT altering the affinity of the ribosome for aminoacyl-tRNA FT thus increasing their reactivity as acceptors for peptidyl FT transferase." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1J9" FT /db_xref="InterPro:IPR001059" FT /db_xref="InterPro:IPR008991" FT /db_xref="InterPro:IPR011768" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR013185" FT /db_xref="InterPro:IPR013852" FT /db_xref="InterPro:IPR014722" FT /db_xref="InterPro:IPR015365" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR020599" FT /db_xref="UniProtKB/Swiss-Prot:A1K1J9" FT /protein_id="CAL92704.1" FT /translation="MKTAQELRSGNVIMVGSDPLVVQKAEYNKSGRNAAVVKMKLKNLL FT TGAPSESVYKADDKFEVVQLDRKEVTYSYFADPMYVFMDADYEQFEVEAENMTDALKYL FT EDGLQCEVVFYNGKAISVELPTTVVREVVYTEPAVKGDTSGKVMKPAKIATGFELPVPA FT FVEIGDKIEIDTRTDEYKNRVK" FT CDS 98928..99359 FT /transl_table=11 FT /locus_tag="azo0087" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. Homology to RS00193 FT of R. solanacearum of 26% (tremble:Q8XVC9) PF02987, Late FT embryogenesis abundant protein;IPR004238;Different types of FT LEA proteins are expressed at different stages of late FT embryogenesis in higher plant seed embryos and under FT conditions of dehydration stress. The function of these FT proteins is unknown. No TMHs Signal peptide present" FT /db_xref="UniProtKB/TrEMBL:A1K1K0" FT /protein_id="CAL92705.1" FT /translation="MSVRSSPTRVVALSLALTMLPLLPACSDGPGSEARRSAQEAASAA FT REALDKAGEAAQKAGEAGKAALEAVEQGTRAGTERGGEKLEALTDATGEHARDAQEAAE FT RAAQRIADATRDAARRLATAGRDAVEAVRRPDQGETGPR" FT CDS 99435..105044 FT /transl_table=11 FT /gene="uvrA1" FT /locus_tag="azo0088" FT /product="putative excinuclease ABC subunit" FT /function="Excinuclease ATPase subunit" FT /note="UvrABC system protein A (UvrA protein) (Excinuclease FT ABC subunit A). The UvrABC repair system catalyzes the FT recognition and processing of DNA lesions. UvrA is an FT ATPase and a DNA-binding protein. A damage recognition FT complex composed of 2 uvrA and 2 uvrB subunits scans DNA FT for abnormalities. When the presence of a lesion has been FT verified by uvrB the uvrA molecules dissociate (By FT similarity). InterPro: Excinuclease ABC A subunit" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1K1" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR004602" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K1K1" FT /protein_id="CAL92706.1" FT /translation="MSEPKDSIRIRGARQNNLRNLSLDLPLNRLTVVTGVSGSGKSSLV FT FDTLYAEGQRRYVETFSPYARQFLDRMDKPQVDRIEGVPPAIAIDQTNPVRTSRSTVGT FT MTELADHFKLLYARAAHLHCRQCGEPVRRDTPASIAADLAQRAAATGDPRLVVCFPVTV FT PKNFSEAEVTALLNAQGYTRIQQRIEAADGDLLQVVQDRFRLSNVEPARLAEALEAALQ FT RGHGRLAVYASGDAVPGGEAVWRYSSDLHCAPCDIHYAEPTPALFSFNSPIGACDTCRG FT FGRVIGVDFGLVIPDESKTLAEGAVKPWQTQSFRECQDDLAKMAKKHGVAMDVPFRDLP FT EEHRRWVLEGDDKWKSWDSSWPRYFYGVRHFFEWLETKAYKMHIRVLLSRYRSYTECPA FT CHGARLKPEALLWRLPTAEGGLPIHSLFNLPVDKVRALIAALELPGLADEATELVLGEI FT RSRLDYLADVGLGYLTLDRQSRTLSGGEVQRINLTTALGTSLVNTLFVLDEPSIGLHPR FT DIGRILGVMTRLRDAGNTLVVVEHDPQLIVAADELLEIGPGPGERGGAIVARGTPAELA FT ANPDSITGPWLAGRKTITVARPPLPVDTATPRLVLHGAREHNLKSLTVGFPLQRLVCLT FT GVSGSGKSTLIQDVLHPALAKHFGEATESAANPAGAFERLTGTETLRGVVMVDQTPIGK FT SSRSNPVSYVGAWDPIRNLFAALPEARQRGYTPGTFSFNSGNGRCPTCTGSGFEHVEMQ FT FLSDVWLRCPDCEGKRYRPEVLELSWHGRSVADVLDMTVREALLFFIDQPKVLAALAPL FT ADVGLDYLRLGQPVPTLSGGEAQRLKLAGHLAEAAQKKPARGRSADEAAPGLLFLFDEP FT TTGLHFEDVATLLGAFGKLLEAGHSLVVIEHNLDVIAAADWIIDLGPEGGDGGGEIVAE FT GPPAAVQQHPASHTGLALRDYAAALAETRRAATPAALAAAEPRAAYRPVAAPAIEIRHA FT REHNLKNVSLQIPRDQFTVITGLSGSGKSTLAFDIVFGEGQRRYLESLNAYARQFVQPA FT SRPDVDGLFGIPPTVAIEQRTSRGGRKSTVATLTEIHPFLRLLYVKLGTQYCPTCDVPV FT TPQSFEAIVAQLMRDYRGASIEVLAPLVVNRKGLYTDLAKWARGKGYAQLRVDGDYLPT FT AKWPRLDRYKEHNIELPVGMVVVEPDNEAALRQQVGEALEHGKGVLKVIELGKLGATPV FT TFSTLRACPSCGTGFPEPDPRLFSYNAKHGWCPGCYGTGLKVAGKVEDPDALDLGDSEE FT TIAGDEVCPSCEGARLNPVARAVRFRERGLHQLAALAVDKAADFFAALELAPREADIAR FT DLVAEIRGRLDFLHHVGLGYLALDRAAPTLSGGEAQRIRLAAQLGSNLRGVCYILDEPT FT IGLHPRDNHLLLGTLEALRDRGNTLLVVEHDEDTIRRADHVIDLGPGAGVRGGQVVAEG FT RLPDLIAAPASATGACLRAPLQHPLRPRRAVPAGHPAIHVEGAHLHNLRDIAVRIPLAR FT LTVVTGVSGSGKSSLARDVIHANLRGLLGDPDAVRARRRGQAQPAESAHALAGCRSISG FT WQQVGRVLEVDQTPIGKTPRSCPATYVGFWDAIRKLFADTFDARTHGWNASRFSFNTGA FT GRCPVCDGAGQTTVEMNFLPDVKTPCEACDGARFNPETLSVRWRGKTVAEVLAMPVDEA FT VAFFAAHPAIAHPLQLLQDVGLGYLTLGQPSPTLSGGEAQRIKLVTELAKVRKRPGDAD FT DTDGLPLPADKHSLYVLDEPTVGLHMADVDKLIRVLHRLTDAGHTVLVIEHDLDVMAEA FT DWLIDLGPEGGDGGGAVVAEGPPEVAIATAASHTGRHLREFLASRAAAAEPNPA" FT CDS 105090..105788 FT /transl_table=11 FT /locus_tag="azo0089" FT /product="conserved hypothetical hydrogenase cytochrome FT b-type subunit" FT /function="Cytochrome b" FT /note="Conserved hypothetical hydrogenase cytochrome b-type FT subunit. Homology to C. vinosum of 56% (trembl|Q46471). FT Involved in electron transfer from hydrogen to oxygen. FT probable signal peptide probable 4 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1K2" FT /db_xref="InterPro:IPR016174" FT /db_xref="UniProtKB/TrEMBL:A1K1K2" FT /protein_id="CAL92707.1" FT /translation="MNKKLIRVWDLPTRLFHWLLLALVVAAFVTGMIGGNFIVWHGWLG FT IAISGLLAFRLTWGLVGSTYARFAHFVPGPQRILAYLRGHWRGVGHNPLGALSVLALLG FT VLAFQVGSGLVANDDIAFSGPLAPLVSEEVGAWLTGLHRQNIWVILALVGLHVGAIVFY FT VRAKKDNLVKPMITGMKEVADGGVKSAEGGGVIPFVIALAVAAAVVWVTAGGLVPPPPP FT PAPAEAAPAW" FT CDS complement(105850..106314) FT /transl_table=11 FT /gene="cycA1" FT /locus_tag="azo0090" FT /product="probable cytochrome c'" FT /function="Cytochrome c556" FT /note="Probable cytochrome c'. Homology to cycA of C. FT vinosum of 61% (sprot|CYCP_CHRVI). CYTOCHROME C IS THE MOST FT WIDELY OCCURRING BACTERIAL C-TYPE CYTOCHROME. CYTOCHROMES C FT ARE HIGH-SPIN PROTEINS AND THE HEME HAS NO SIXTH LIGAND. FT THEIR EXACT FUNCTION IS NOT KNOWN. Pfam: Cytochrome c. FT signal peptide no TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K1K3" FT /db_xref="InterPro:IPR002321" FT /db_xref="InterPro:IPR010980" FT /db_xref="InterPro:IPR012127" FT /db_xref="InterPro:IPR015984" FT /db_xref="UniProtKB/TrEMBL:A1K1K3" FT /protein_id="CAL92708.1" FT /translation="MKKIIARIAFGMAAFALASAASAQVKPEDQIKYRKAGYSYMMSWN FT MGKIKANLEGSYNKDQVAAAANAIAGIANSGMGALYGPGTEKAVGGQTTRVKPAMFTDK FT EGVTKVAVDFNKAANNLAKVAADGDAAAVKVAFGEVGKTCKACHDQYREE" FT CDS 106574..108199 FT /transl_table=11 FT /locus_tag="azo0091" FT /product="probable methyl-accepting chemotaxis protein" FT /function="Methyl-accepting chemotaxis protein" FT /note="Methyl-accepting chemotaxis protein," FT /note="Specificity unclear" FT /db_xref="GOA:A1K1K4" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004089" FT /db_xref="UniProtKB/TrEMBL:A1K1K4" FT /protein_id="CAL92709.1" FT /translation="MGRLANTPIWLRLTGAIWLMLVLAWGSMIAWETRANRDIAIEQAK FT DFARSVNEMTMAGLTGMMITGTVAQRDVFLDQIKELSAVRDLEVIRGEAVSKLFGPGAG FT AASEPPDAVEREVLAGGEPVMRVENDAQNGEHLRVVIAARASHNYLGKDCILCHQVAEG FT TPLGAVSMRISLDKVNAAVTSFRNQSIVFAVLVSLPLLAVVFLFIRRFVIRPLDHLGAG FT MAEIAQGEGDLTRRLARDGDDEIGRTAEVFNRMLATLAGLVRQVGESASQVTGSAASLA FT SGAARVAESSHRQNDRSLSAAGAVEALTVDIARIAESTERVRERSRESLARSLEGQHSL FT AQLIGEVGHVEGAVQHMATAVDAFMQSTSAITRMTQEVREIAEQTNLLALNAAIEAARA FT GEQGRGFAVVADEVRKLAEKSAHSAGGIDAITREIGQQSDSVNQAIARGLEHLASSRRA FT ADVVSGVLDAANAAVSEVGEGLDHIAATTAEQRRSSESVTASIEAIAGMARDNNAAIEE FT TVAAARELEQLAARLQDSVSRFRV" FT CDS complement(108207..109646) FT /transl_table=11 FT /gene="mucD1" FT /locus_tag="azo0092" FT /product="probable serine protease MucD" FT /function="Trypsin-like serine proteases typically FT periplasmic contain C-terminal PDZ domain" FT /EC_number="3.4.21.-" FT /note="Probable serine protease. Homology to mucD of P. FT aeruginosa of 55% (AAC43718). Pfam: Trypsin; PDZ domain FT (also known as DHR or GLGF) signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1K5" FT /db_xref="InterPro:IPR001254" FT /db_xref="InterPro:IPR001478" FT /db_xref="InterPro:IPR001940" FT /db_xref="InterPro:IPR009003" FT /db_xref="InterPro:IPR011782" FT /db_xref="UniProtKB/TrEMBL:A1K1K5" FT /protein_id="CAL92710.1" FT /translation="MRHPLAVTALALSLAGWIPAASLSSSAHAALFGDSSPASNRYGLP FT DFGDLVEQVGPAVVNISVVQQQAGGDGGLANDPFYDFLRRFGVPTPEMPGQGAPRISRG FT IGSGFIVSADGYVLTNAHVVGESGAEVTVTLVDKREFKARVVGTDKRTDVAVIKIDARN FT LPTVKIGDAERSRVGEWVIAVGSPFGFDHSVTAGIISAKARRLPDENYVPFLQTDVAIN FT PGNSGGPLFNLGGEVIGINSQIYSRSGGFMGISFAIPIDVAMKVKDQLVTHGRVQRGRL FT GIAIQGVDKELAQSFGLPDARGALVANVEPDSAADKAGVKAGDVVLAVDGTRINDSADL FT PRIIGDKRPGTRVRLEVWRDGRSREVSATLDELGAETAAAAPARPGRGESTGGKLGLTA FT RPLSSQEAAQLGINGGLVVEAASGPAAKAGLERGDIVLAINNQPVTTVAQFRQLAEKAG FT NRFALLVQRGSARIFVPVRLD" FT CDS complement(109778..111763) FT /transl_table=11 FT /gene="irgA1" FT /locus_tag="azo0093" FT /product="putative TonB-dependent receptor" FT /function="Outer membrane receptor for ferrienterochelin FT and colicins" FT /note="23% TonB_boxC. Pfam:PF00593; TonB_dep_Rec; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1K6" FT /db_xref="InterPro:IPR000531" FT /db_xref="InterPro:IPR012910" FT /db_xref="UniProtKB/TrEMBL:A1K1K6" FT /protein_id="CAL92711.1" FT /translation="MSAHAEEGYFETLPVVLSVSRLPQAMEDTPGAVTVIDSELIAATG FT YRDLARLFRLVPGMQVGQERANHHWVTYHGLGSDYPNQMQVLVDGRSVYSPYFFGGADW FT GSLPIALEDIDRIEVVRGSDSAAYGSNAFLGVVNILTRHTGAETGNSVSLRGGTNGIAD FT ATGRAVLHDGAMGLRVTAQHIEDRGMADLHDSQRIDVLNLRADLRVSAVDEVTVTAGMS FT SGARSAGYEGTQFDVVAPRTARHEDGAVHLKWRRTLSPDDEWSLSWYRNREQSREDWLL FT DSHKNLRPEVAYLRNLPRLVVTVDNDRDSLRDNIEFSQRLRPLDDLRLLWGTEWRRDWL FT RAPMLFYGGDSHSQQEWRLFGNAEWRMAPRWLWNIGAMAEQIEGDRLRLAPRVFLNWQP FT SPTQTWRAGYSRAWRQPTLFERSADIRVVHPQLGLIMLDHLPNPDIRPQRIDAWEVGFL FT GQLPQQGSFDLRLFHERIEDFIVRRAVDPAELPDNDIQRAAGATRWVNSGDGVRLVGLE FT YQLRTRPWSGGQLVLSHSLIRAHSDDDAVRRSVAPYTASLTWLQRYGPWQSTLSLLRMG FT ASDSGSGYVPGYRYKVPAYTTLDWSIARTLQVGPNPVELRLTGINLLGKHQELVLRPLQ FT SMPGYGDDRPANELDRQLHLSVRVGF" FT CDS 111975..112913 FT /transl_table=11 FT /gene="oxyR" FT /locus_tag="azo0094" FT /product="putative oxyR" FT /function="Transcriptional regulator" FT /note="oxyR, Hydrogen peroxide-inducible genes activator. FT BELONGS TO THE LYSR FAMILY OF TRANSCRIPTIONAL REGULATORS FT REQUIRED FOR THE INDUCTION OF A REGULON OF HYDROGEN FT PEROXIDE INDUCIBLE GENES SUCH AS CATALASE FT GLUTATHIONE-REDUCTASE ETC. (BY SIMILARITY). mreB: cell FT shape determining protein M 51% HTH_LysR. IPR005119; FT LysR_subst. IPR009058; Wing_hlx_DNA_bnd. PF00126; HTH_1; 1. FT PF03466; LysR_substrate; 1. HTH reporting nucleic acid FT binding motif" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1K7" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1K7" FT /protein_id="CAL92712.1" FT /translation="MTLTDLRYLVALAHERHFGRAAEKCHVSQPTLSVAIKKVEDELGI FT ALFERSASEVKITETGRRIVAQAEKVLVEASQIHEIAAAGKDPLAGPLRVGVIYTIGPY FT LLPRLIPRVHQLAPRMPLIIQENYTTRLAEALKRGELDVIIISLPFEEAGIVAQPVYDE FT PFRVLLPAAHPWTALDSIDPEHLAEDQLLLLGSGNCFREQVLEVCPHCRNVGGLQRTLE FT GSSLETIRHMVATGLGVTVLPSSAADELTIQNPLVAVRPFTAPEPSRRVALAWRVTYPR FT SGAIDILRTAILESELPGVRPIGRVPAVEAA" FT CDS complement(112981..115554) FT /transl_table=11 FT /locus_tag="azo0095" FT /product="DNA topoisomerase III" FT /function="Topoisomerase IA" FT /EC_number="5.99.1.2" FT /note="DNA topoisomerase I (EC 5.99.1.2) (Omega-protein) FT (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE FT REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE FT CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY FT PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR FT EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON FT EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR FT MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE FT PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE FT A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: FT Prokaryotic DNA topoisomerase I" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1K8" FT /db_xref="InterPro:IPR000380" FT /db_xref="InterPro:IPR003601" FT /db_xref="InterPro:IPR003602" FT /db_xref="InterPro:IPR005738" FT /db_xref="InterPro:IPR006171" FT /db_xref="InterPro:IPR013497" FT /db_xref="InterPro:IPR013824" FT /db_xref="InterPro:IPR013825" FT /db_xref="InterPro:IPR023405" FT /db_xref="InterPro:IPR023406" FT /db_xref="UniProtKB/TrEMBL:A1K1K8" FT /protein_id="CAL92713.1" FT /translation="MSKQLIIAEKPSVAQDIARALGGFTKEKDYFESDDYVLSSAVGHL FT LELAVPEEFEVKRGKWTFAHLPVIPPHFALKPIEKTDDRLKLLTRLIKRKDVTGLINAC FT DAGREGELIFNFIAQHAGTNKPMQRLWLQSMTPAAIRDGFAHLRAARDVEGLRNAAICR FT AESDWLIGINGTRAMTAFNSKTGGFHLTTVGRVQTPTLAIVVEREDKIRKFKPRDYWEL FT EATFGCAAGEYTGRWLDENFRKPEGDEHANAHRLWDKARAEAIRAKCEGKPGVVTEEAK FT PSTQLSPLLFDLTSLQREANGRFGFSARVTLQLAQALYEKHKVLTYPRTDARALPEDYL FT GTVKDVMAGLPDTYAPFANEIAKQGWVRPNKRIFNNAKISDHFAIIPTGTLPKSLSEAE FT HKIYDLVTRRFLSVFYPAAEYQITTRITRVEGEAFKTEGKVLVNAGWLAVYGKEAANED FT GEGKDAGKDSGRQLVAVKPGETVSTDDILVKALQTKPPARFNEATLLSAMEGAGKMVDD FT EELRAAMAERGLGTPATRAQIIEGLIAEQYIHREGRELIPSAKAFSLITLLTGLGVNAL FT TSPELTGGWEYKLSRMERGELSREAFMHEIAEMAREVVERAKRYESDTVPGDFVTLKTP FT CPKCGGTVKENYKKFACQACDWSTWKIVAGRQFEIDEIETLLRDGKVGPLLGFRNKMGR FT LFNAEIKLNDDKQPEFDFGQPKEGEEGGEAVDFSGQQSIGACPKCGANVFEHGLAYVCE FT KSVGPGKNCDFRSGKIILQQPIEREQMAKLLTDGKTDLLKGFVSARTRRKFSAFLVRGK FT DGKVGFEFEAKTPKAGAKSTPAKAAANEETGKPAPRKRAGGKTAG" FT CDS complement(115666..116133) FT /transl_table=11 FT /locus_tag="azo0096" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Protein smg homolog, 45% identity (65% similarity) FT to SwissProt;P30853 43% identity to SwissProt;Q8X8F6,E.coli FT smg protein. Has PF04361(IPR007456):Protein of unknown FT function (DUF494);Members of this family of uncharacterised FT proteins are often named Smg. No signal peptide or TMH FT reported present." FT /db_xref="InterPro:IPR007456" FT /db_xref="UniProtKB/Swiss-Prot:A1K1K9" FT /protein_id="CAL92714.1" FT /translation="MFDILVYLFESYIHANACPASDQLARKLSAAGFEDEEINEALDWL FT AGLRRVAAETHPCVAPSRSAVRLYSDYECTRLSAACRGFLTFLEGAGVLDAVSRELIVE FT RAVALSNFTITLGRLKVIVLMVLWQREQPVDTLIIDELLSSDDDEGAPLLH" FT CDS complement(116194..117312) FT /transl_table=11 FT /gene="drpA" FT /locus_tag="azo0097" FT /product="putative DNA processing protein DrpA" FT /function="Protein involved in DNA uptake" FT /note="Putative DNA processing protein DrpA (Smf protein). FT Homology to drpA of H. influcenzae The SMF family (DNA FT processing chain A, dprA) are a group of bacterial FT proteins. In Helicobacter pylori, dprA is required for FT natural chromosomal and plasmid transformation InterPro: FT SMF family Tigerfam: dprA: DNA processing protein FT DprA,putative Pfam SMF family no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1L0" FT /db_xref="InterPro:IPR003488" FT /db_xref="UniProtKB/TrEMBL:A1K1L0" FT /protein_id="CAL92715.1" FT /translation="MPPGKDLAGWLRLALAPGLGPERQRRLLAAFGLPEAVFQSSRSAI FT ASVIGNEAADRLLAPPDGKAIDAALAWADEPGNHILTLADADYPPALLEISDPPALLYL FT KGEPALLQRPALAVVGARSATANGEANAAAFARALGEAGLVIVSGLAAGIDAAAHRGAL FT AASGGAGTVAVIGTGPDRIYPASNAELARQIAQAGAILSEFPLGAPALRHHFPRRNRLI FT AGLSLGVLVVEAAVGSGSLITARLATETGREVFAIPGSIHSPLARGCHRLIRDGAKLVE FT TAEDVLEELRGRFSPAQHAPSTAAAGPDSAPPPPADPAAALVLALIGHEPVDIELLVQR FT SGLTVDALYAILLPMELDGRIGRCAGSRFQRL" FT CDS complement(117316..118503) FT /transl_table=11 FT /locus_tag="azo0098" FT /product="conserved hypothetical membrane protein" FT /note="Conseved hypothetical membrane protein. Homology to FT RSO2271 of R. solanacearum of 36% (trembl|Q8Y3B1(SRS)). FT Pfam: Lysin motif (SM00257) This domain is about 40 FT residues long and is found in a variety of enzymes involved FT in bacterial cell wall degradation. This domain may have a FT general peptidoglycan binding function. No signal peptide 1 FT TMH" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1L1" FT /db_xref="InterPro:IPR002482" FT /db_xref="InterPro:IPR018392" FT /db_xref="UniProtKB/TrEMBL:A1K1L1" FT /protein_id="CAL92716.1" FT /translation="MQNFKRFDMHAHVLCRAGFRRRWGGLRSPCFDPWRQSGVPGRREP FT SRTYRKRAMIRIIFPLLVSIATLFAGAAAAQGVQLADDAPDSYTVVKGDTLWGISGRFL FT KQPWRWPEVWRFNRDQIRNPHLIYPGQVILLDRSGPWLTVGRRVGSRDEKLFPQVYSES FT GTQPVPSIPLHVIDPFLTRPLIVDGARIANSATIVATETSRVYTGTGDTVFAKNVREGV FT DSWQIYRPARALHDPVTQELLGYEAEYLGSARVTERGNPTTLEILNANEEIGVGDLMVP FT SEPPSVFSYAPHAPEQAVEGRVVSIYRGVTETGRLHVVALGAGAQQGVERGHVLALYRN FT RGVAEYKDDQGRESFQLPEKRYGLVFVFRVFDRISYGLIMETDGQVSIGDSIRKP" FT CDS 118530..119033 FT /transl_table=11 FT /gene="def1" FT /locus_tag="azo0099" FT /product="probable peptide deformylase" FT /function="N-formylmethionyl-tRNA deformylase" FT /EC_number="3.5.1.88" FT /note="Probable peptide deformylase (EC 3.5.1.88). Homology FT to def of E. coli of 54% (sprot|DEF_ECOLI(SRS)). Removes FT the formyl group from the N-terminal Met of newly FT synthesized proteins. Requires at least a dipeptide for an FT efficient rate of reaction. N-terminal L-methionine is a FT prerequisite for activity but the enzyme has broad FT specificity at other positions Interpro: Formylmethionine FT deformylase (IPR000181) Pfam: Polypeptide deformylase FT Tigrfam: pept_deformyl: polypeptide deformylase no signal FT peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1L2" FT /db_xref="InterPro:IPR000181" FT /db_xref="InterPro:IPR023635" FT /db_xref="UniProtKB/TrEMBL:A1K1L2" FT /protein_id="CAL92717.1" FT /translation="MALLPILRYPDPRLHRRAAPVDTVDDDVRKLIDDMAETMYEAPGI FT GLAATQVDVHRRVVVIDISEDKSGLMALINPQILERDGEQVCEEGCLSVPGVYEKVTRA FT ERVTVRALDRNGHPFEVAAEGLLAVCIQHEIDHLDGKVFVEYLSPLKLGRIKSKLAKKA FT RITA" FT CDS 119079..120044 FT /transl_table=11 FT /gene="fmt" FT /locus_tag="azo0100" FT /product="Fmt protein" FT /function="Methionyl-tRNA formyltransferase" FT /EC_number="2.1.2.9" FT /note="Methionyl-tRNA formyltransferase (EC 2.1.2.9). FT Modify the free amino group of the aminoacyl moiety of FT methionyl-tRNA(fMet). The formyl group appears to play a FT dual role in the initiator identity of FT N-formylmethionyl-tRNA by: (I) promoting its recognition by FT IF2 and (II) impairing its binding to EFTu-GTP (By FT similarity). InterPro: Methionyl-tRNA formyltransferase FT fmt: methionyl-tRNA formyltransferase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1L3" FT /db_xref="InterPro:IPR001555" FT /db_xref="InterPro:IPR002376" FT /db_xref="InterPro:IPR005793" FT /db_xref="InterPro:IPR005794" FT /db_xref="InterPro:IPR011034" FT /db_xref="InterPro:IPR015518" FT /db_xref="UniProtKB/TrEMBL:A1K1L3" FT /protein_id="CAL92718.1" FT /translation="MSLPLRVAFAGTPEFAASALAAILDAGYSVPLVLTQPDRPAGRGM FT KLTPSPVKQLALARGLDVDQPEKLRTDEQRQRLAACEPDVLVVAAYGLILPAAVLQLPR FT YGCINIHASLLPRWRGAAPIHRAVEAGDAETGITIMQMDEGLDTGDMLLRRAIPIRPDD FT TTGTLHDKLAALGAECIVEALAALPGGTLSRTPQPAAGVTYANKIHRDEAAIDWTRPAA FT DIERAVRAFNPFPVAVGSLRDTVIKVWAAEVVAVPAPDAAPGTVLAADAEGVVVACGAQ FT ALRLRELQRPGSRRFAAGEFLRGFPVCAGERFAVGGAQAG" FT CDS 120104..120946 FT /transl_table=11 FT /gene="htpX" FT /locus_tag="azo0101" FT /product="putative protease HtpX" FT /function="Zn-dependent protease with chaperone function" FT /EC_number="3.4.24.-" FT /note="Putative protease HtpX Homolog to htpX of E. coli of FT 30% (AAA62779) InterPro: Peptidase family M48 (IPR001915) FT Pfam: Peptidase family M48 signal peptide TMHs3" FT /note="Family membership" FT /db_xref="GOA:A1K1L4" FT /db_xref="InterPro:IPR001915" FT /db_xref="InterPro:IPR022919" FT /db_xref="UniProtKB/TrEMBL:A1K1L4" FT /protein_id="CAL92719.1" FT /translation="MFGNWIKTSILMAGIVALFGAVGGVIGGKQGMLLALVLGGAMNLW FT AYWFSDKMVLKMYNAREVDEATSPYLYNMVRGLAQRAGLPMPKVYIIDEDQPNAFATGR FT NPEHAAVAATTGIMRMLSERELRGVMAHELAHVKNRDILISTISATVAGAISSLAQFGM FT FFGGSRDGEDRPNPVVSIIVMILAPIAGMLIQMAISRTREFGADRGGAEISGDPQALAS FT ALAKIDAYARGIPMHTAEAHPETAQMMIMNPLSGGSLRGLFSTHPSTEERIARLRAMG" FT CDS 120960..121487 FT /transl_table=11 FT /gene="helX" FT /locus_tag="azo0102" FT /product="putative thiol:disulphide oxidoreductase" FT /function="Thiol-disulfide isomerase and thioredoxins" FT /EC_number="1.8.4.7" FT /note="Putative thiol:disulfide oxidoreductase. Homology to FT helX of R. casulata of 35% Periplasmic protein FT thiol:disulphide oxidoreductase is involved in the FT biogenesis of c-type cytochromes as well as in disulphide FT bond formation in some periplasmic proteins. Tigrfam: dsbE: FT periplasmic protein thiol:disulfide signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1L5" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR013740" FT /db_xref="InterPro:IPR017937" FT /db_xref="UniProtKB/TrEMBL:A1K1L5" FT /protein_id="CAL92720.1" FT /translation="MTSRRLLRRFFCALAVCLAPASAFAVDLEPLATLPPAPAALQAEL FT ARVQGRAVLINFWASWCEPCRDEMPALVELDEQEPGIALITVAVADRAADSRRFLDDYL FT LDNVVLINDPEQLIARAWGARLLPTTIMLDAAHRPRFRVRGEADWRAPELRARLRALTA FT SESTPIPKGKTP" FT CDS 121484..122596 FT /transl_table=11 FT /locus_tag="azo0103" FT /product="conserved hypothetical secreted protein" FT /function="Transglutaminase-like enzymes putative cysteine FT proteases" FT /note="Conserved hypothetical secreted protein. Homology to FT SMa0025 of S. meliloti of 46% pir|D95263(SRS). Pfam: FT Transglutaminase_like Superfamily signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR002931" FT /db_xref="InterPro:IPR019546" FT /db_xref="UniProtKB/TrEMBL:A1K1L6" FT /protein_id="CAL92721.1" FT /translation="MKRRDFLKTSALAAGLALPAWARAADTAAPLFAPSPAAGWREFEV FT VTRIEPVQAAGVVRAWLPLPYTEETDWFRPLGNAWQGNAGLARVVRDPRYGAAMLYAEW FT AADAGVPELEITSRFATRDRAVDFSRPAARPLALSAAEHALYTGATELLPTDGIVRDTA FT LQITAGAKTDEDKARAIYEWVVDNTFRNPKTRGCGIGDIKAMLETGNLSGKCADLNALY FT VGLARAAGIPARDVYGVRVADSRFGYKSLGKSGNISKAQHCRAEVFLARFGWVPVDPAD FT VRKVVLEEPPGNLALDDAKVRAARKQLFGAWEMNWLAYNVAHDLELPGSGGAPVPFLMY FT PQGESAQGRFDSLDPDSFRYTLTAREVVRA" FT CDS 122689..123570 FT /transl_table=11 FT /locus_tag="azo0104" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT ebA582 of Azoacrus sp EbN1 (trembl:Q5P8D6). No domains FT predicted. SignalP reporting signal peptid. no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR004010" FT /db_xref="InterPro:IPR006311" FT /db_xref="UniProtKB/TrEMBL:A1K1L7" FT /protein_id="CAL92722.1" FT /translation="MPVSRRRVLGLATALCAAASLQSSVLRAATPEPARLSERWDEKRA FT ARLLDRAVKHIEAKGEAGVADFSRQGPFVDRDLYVYALGSDGRFLASGGSSAALIGQNV FT AATTDAAGKPFFREMLDTAASRGEGRIEYRWLNPADQREEPKVTLFRKVGGIIVAVGFY FT TPRATPAQARALLDQAAAALARDSGAALGEFQQVGGRFIQDDLYVFVVDMGDGRFLAHG FT ATPALVGRDARELRDPKGKALITDMINVARKKGEGELDYAWQNPVTAKLESKHTYFRVV FT DGKLLGVGYYTR" FT CDS 123626..124126 FT /transl_table=11 FT /gene="tpx" FT /locus_tag="azo0105" FT /product="probable thiol peroxidase" FT /function="Peroxiredoxin" FT /EC_number="1.11.1.-" FT /note="Probable thiol peroxidase. Homology to E. coli of FT 62% (sprot:TPX_ECOLI) Has antioxidant activity. Could FT remove peroxides or H(2)O(2) (By similarity). Pfam: FT AhpC/TSA family no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1L8" FT /db_xref="InterPro:IPR002065" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR013740" FT /db_xref="InterPro:IPR018219" FT /db_xref="UniProtKB/TrEMBL:A1K1L8" FT /protein_id="CAL92723.1" FT /translation="MATVTLGGNPISIAGRFPQVGESAPAFALTTPELADVGLDTWAGK FT RKVLNIVPSLDTPTCATSTRRFNAEAGALANTVVLVISGDLPFAAKRFCAAEGLDNVKT FT LSTFRNPGFARDYGVAISSGPLAGLTARAVVVVDENDKVIHAELVSEIKNEPDYAAALA FT VLK" FT CDS 124218..125105 FT /transl_table=11 FT /locus_tag="azo0106" FT /product="conserved hypothetical membrane protein" FT /function="Permeases of the drug/metabolite transporter FT (DMT) superfamily" FT /note="Conserved hypothetical membrane protein. Homology to FT an orf of R. palustris (tremblnew|CAE28417). Tigrfam: 2A78: FT Carboxylate/Amino Acid/Amine Tranporter InterPro: Integral FT membrane protein DUF6 Pfam: Integral membrane protein DUF6 FT no signal peptide probable 10 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1L9" FT /db_xref="InterPro:IPR000620" FT /db_xref="UniProtKB/TrEMBL:A1K1L9" FT /protein_id="CAL92724.1" FT /translation="MQPARIPPRTLLALVLLTLFWGVNWPVMKFSLREITPLYFRALTV FT SGGLLLLIAWFRLRGVSLRVPRREWGRVMLLALPNIAGWYCFSIFGVQALASGRAAILG FT FTMPIWTVLLGVLFFRERMNPRLWLATACAAAAVLLLLWHELGQLSGRPLGMAWMLAAA FT ASWALGTLLLKRLAPAVSTEALTVGMLVCALPVLWALAVLKEPVPTLQFSLPMWVAVVY FT GVVIACAAAQVLWFSIARSLPPVASALSVMMIPVIGLASAMPITGERPHPQDLAAAVLI FT MLALSAALLPRRAG" FT CDS complement(125118..125834) FT /transl_table=11 FT /locus_tag="azo0107" FT /product="conserved hypothetical membrane protein" FT /function="uncharacterized conserved protein" FT /note="conserved hypothetical membrane proteins, 42% FT identity (59% similarity) to TrEMBL;Q73PF0 Has FT PF02592;Uncharacterized ACR, YhhQ family FT COG1738;IPR003744:This is a family of uncharacterized FT proteins. Conserved regions of hydrophobicity suggest that FT all members of the family may be integral membrane FT proteins. no signal peptide. 4 TMH." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR003744" FT /db_xref="UniProtKB/TrEMBL:A1K1M0" FT /protein_id="CAL92725.1" FT /translation="MNPTPAAPRQYRYYEFVMAAFVAVYLCSNLIGPAKAAQIELPLIG FT AVTFGAGVLFFPISYIFGDVLTEVYGYARARRVIWAGFGAMIFASLMAWVVVKLPPAPG FT WQNQAAYEIAYGSTWRIVAASLTAFFCGEFVNSFVLAKMKVWTEGRHLWARTIGSTVVG FT EGVDSLLFYPLAFWNSGLIPNELLPAVMVGQFVSKVMVEVVFTPLTYRIVAFLKRAERE FT DYYDRDTDFTPFSIRA" FT CDS 126088..127293 FT /transl_table=11 FT /locus_tag="azo0108" FT /product="conserved hypothetical secreted protein" FT /function="Beta-galactosidase/beta-glucuronidase" FT /note="Conserved hypothetical secreted protein. Homology to FT XCC0740 of Xanthomonas campestris of 33% FT (trembl|Q8PCI6(SRS) Pfam: Glycosyl hydrolases family 2,TIM FT barrel domain This family contains FT beta-galactosidase,beta-mannosidase and beta-glucuronidase FT activities. No TMHs Signal peptide: present." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1M1" FT /db_xref="InterPro:IPR006103" FT /db_xref="InterPro:IPR013781" FT /db_xref="InterPro:IPR017853" FT /db_xref="UniProtKB/TrEMBL:A1K1M1" FT /protein_id="CAL92726.1" FT /translation="MERGGLRRLALLGWLAVSAAALPAAGAQWQGAAFEGDRAALERLA FT RAGARVIRVYRESDAWVLDAAQQLGLKVVMGLWVGHPRHGVRLEDETVLRAHEAALRDF FT VTRHRDHPALLAWGVGNEVETGTADHLAVWRRIDRLAGVVKAADPSHPTLMVVADTGMA FT QLRQLADCCAHVDMLGINVYAGAVFDLPQRLAEAGIAKPVVVAELGPLGQWQAGRKPWG FT APVELTSSQKAAFYRDALAFLRQQPQIAGVFPFLWGAKQEQTATWHGLLLADGSATAMS FT DALAAAWGRPETHAAPVIRGIGIAADEFAPGQEISAGVDAIAPDGAPLVTDWAVFAEAT FT DLRKGGDVETAPPRVAVQLRHADAASVRFVAPQAPGAYRLFLTVRDGRGKVATANLPFL FT VR" FT CDS 127357..127812 FT /transl_table=11 FT /gene="yihZ" FT /locus_tag="azo0109" FT /product="D-tyrosyl-tRNA(Tyr) deacylase" FT /function="D-Tyr-tRNAtyr deacylase" FT /EC_number="3.1.-.-" FT /note="D-tyrosyl-tRNA(Tyr) deacylase (EC 3.1.-.-). FT Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free FT tRNA(Tyr). Could be a defense mechanism against a harmful FT effect of D-tyrosine." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1M2" FT /db_xref="InterPro:IPR003732" FT /db_xref="InterPro:IPR023509" FT /db_xref="UniProtKB/Swiss-Prot:A1K1M2" FT /protein_id="CAL92727.1" FT /translation="MMALLQRVTRARVTVDGATTGEIGTGLLALVCAEQGDTEAEADKL FT LAKLLKLRVFADEGGRMNRSLQEVGGGLLVVSQFTLAADTSGGNRPSFANAAPADTGRA FT LYEHFVARARAQHGEVATGRFGAMMQVELVNDGPVTIPLRIPPASAA" FT CDS complement(127825..128703) FT /transl_table=11 FT /locus_tag="azo0110" FT /product="probable pirin-related protein" FT /function="Pirin-related protein" FT /note="Pirin-like protein. TREMBL:Q8P799: 52% identity,65% FT similarity. InterPro: DUF209 his region is found the FT C-terminal half of the Pirin protein. The function of Pirin FT is unknown but the gene coding for this protein is known to FT be expressed in all tissues in the human body although it FT is expressed most strongly in the liver and heart. Pirin is FT known to be a nuclear protein, exclusively localised within FT the nucleoplasma and predominantly concentrated within FT dot-like subnuclear structures. A tomato homologue of human FT Pirin has been found to be induced during programmed cell FT death. Human Pirin interacts with Bcl-3 and NFI and hence FT is probably involved in the regulation of DNA transcription FT and replication. It appears to be an Fe(II)-containing FT member of the Cupin superfamil InterPro:IPR007113; FT Cupin_sup. IPR008778; Pirin_C. IPR003829; Pirin_N. Pfam FT PF02678; Pirin; 1. PF05726; Pirin_C molyb_syn: molybdenum FT cofactor synthesis Absence of transmembrane helices (TMHMM FT predicted)" FT /note="Function unclear" FT /db_xref="InterPro:IPR003829" FT /db_xref="InterPro:IPR008778" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR012093" FT /db_xref="InterPro:IPR014710" FT /db_xref="UniProtKB/TrEMBL:A1K1M3" FT /protein_id="CAL92728.1" FT /translation="MPELLIEPRRADLGHGLVVQRILPYARRRMVGPFIFLDHAGPVRL FT PPELARLADVRPHPHIGLATVSYLLGGEITHRDSLGMEQPIRPGEVNWMTAGRGIVHSE FT RFDSPAAFAGTGLELLQSWVALPAEHEETAPAFDHYPAALLPTATEGGLWLRVIAGKAF FT GLASPVRTLSPMFYLHVKLTAGSAVALPGDYSERAAYVVDGRIEIDGTAYGAGRMLVFG FT QAEAPTLRALDDATVMLLGGEPVGERHIWWNFVSSRKDRIEQAKADWRAGRIPLPPNDN FT AEFIPLPETVA" FT CDS 128838..129824 FT /transl_table=11 FT /gene="adhA" FT /locus_tag="azo0111" FT /product="putative alcohol dehydrogenase" FT /function="Zn-dependent alcohol dehydrogenases" FT /EC_number="1.1.1.1" FT /note="Putative Alcohol dehydrogenase. Homology to adh-HT FT of B. stearothermophilus (sprot|ADH3_BACST) THERMOSTABLE FT AND THERMOPHILIC NAD(+)-DEPENDENT ALCOHOL DEHYDROGENASE. FT BEARS MAINLY AN ETHANOL-DEHYDROGENASE ACTIVITY. CATALYTIC FT ACTIVITY:An alcohol + NAD(+) = an aldehyde or ketone + FT NADH. COFACTOR: Binds 2 zinc ions per subunit (By FT similarity). Pfam: Zinc-binding dehydrogenase Tirgfam: tdh: FT L-threonine 3-dehydrogenase no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1M4" FT /db_xref="InterPro:IPR002085" FT /db_xref="InterPro:IPR002328" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR013154" FT /db_xref="InterPro:IPR014187" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K1M4" FT /protein_id="CAL92729.1" FT /translation="MRAMVLDTPGQPLRPAVLPQPTPGPGQVLLKVEACGVCRTDLHLV FT DGELPEPRLPVVPGHEIVGRVVATGPGVTALRIGQRAGVPWLGWTCGECSYCRGGHENL FT CDAARFTGYTLDGGYAEYTVADQRYCFPLPDPLPAVELAPLLCAGLIGYRALAMAGDAE FT RIGIYGFGAAAHILAQVLVHQGRAFYAFTRPGDLAGQGFACRLGAAWAGGSDEAPDQAL FT DAALIFAPAGPLVPAALRAVRKGGTVVCAGIHMSDIPAFPYDILWGERVLRSVANLTRA FT DGERFLRIVADNPVRSHVQVYRLDQANEALDALRLGRIEGAAVLVPE" FT CDS complement(129841..130737) FT /transl_table=11 FT /gene="gstR1" FT /locus_tag="azo0112" FT /product="putative transcriptional regulator" FT /function="Transcriptional regulator" FT /note="Putative transcriptional regulator. Homology to gstR FT of R. leguminosarum of 37% (tremble:Q52827). Has PF00126, FT HTH_1,Bacterial regulatory helix-turn-helix protein, lysR FT family.IPR000847, HTH_LysR; Numerous bacterial FT transcription regulatory proteins bind DNA via a FT helix-turn-helix (HTH) motif. These proteins are very FT diverse, but for convenience may be grouped into FT subfamilies on the basis of sequence similarity. One such FT family, the lysR family, groups together a range of FT proteins, including ampR, catM, catR, cynR, cysB, FT gltC,iciA, ilvY, irgB, lysR, metR, mkaC, mleR, nahR, FT nhaR,nodD, nolR, oxyR, pssR, rbcR, syrM, tcbR, tfdS and FT trpI. The majority of these proteins appear to be FT transcription activators and most are known to negatively FT regulate their own expression. All possess a potential HTH FT DNA-binding motif towards their N-termini. Has PF03466, FT LysR substrate binding domain;IPR005119, LysR_subst; The FT structure of this domain is known and is" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1M5" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1M5" FT /protein_id="CAL92730.1" FT /translation="MDKLKAMQIAVAIADSGSLTAAADSLDISLPVVVRTLAALEAGLG FT VRLFNRSTRRLSLTDEGRDYLARCRQILADIHDAEAALASDAVVPSGRVVVTAPVMFGQ FT QHVAPALTRFVQHYGQMRVELRLHDRVVNLLEEHIDVAVRIGAIEDQSLVAHALGTLRR FT IVVAAPAYLAARGTPQHPRELAAHECIVFNGNSAGWWRFIDDGHEFGMTVDGRLTYNHV FT APALDACRAGMGLGTFIAYQIADDLHAGRLLPVLEAFELPPRPVHVAFPHARLLPTRTR FT VLVDWLRRDLGEQLAAL" FT CDS 130842..131489 FT /transl_table=11 FT /gene="gstA" FT /locus_tag="azo0113" FT /product="probable glutathione transferase" FT /EC_number="2.5.1.18" FT /note="Probabe glutathione transferase. Homology to gstA of FT R. leguminosarum of 58% (sprot:GSTA_RHILE) Conjugation of FT reduced glutathione to a variety of targets. Pfam: PF02798, FT GST_N, Glutathione S-transferase, N-terminal domain; FT PF00043, GST_C, Glutathione S-transferase, C-terminal FT domain Interpro: IPR004045, GST_Nterm; IPR004046,GST_Cterm; FT no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1M6" FT /db_xref="InterPro:IPR004045" FT /db_xref="InterPro:IPR004046" FT /db_xref="InterPro:IPR010987" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR017933" FT /db_xref="UniProtKB/TrEMBL:A1K1M6" FT /protein_id="CAL92731.1" FT /translation="MTRSIPQGELVLYGLPLSGHCHRVALFLSLLRLPYRYENVDLAGG FT AHRRPDFLALNPFGQIPVLKDGEQVIADSNAILVYLARRYGGGEEIEWLPDEPVAAAEV FT QRWFSAAAGLLAFGPARARLKHVFGAPIDYDAAVELANRLLPVMEAELARRPYLAADAP FT TLADIALYSYTAHAPEGGISLQPYPHIRAWLARVEALPGFVGMPRSALPAGA" FT CDS 131492..132490 FT /transl_table=11 FT /locus_tag="azo0114" FT /product="conserved hypothetical protein" FT /function="predicted flavin-nucleotide-binding protein FT structurally related to pyridoxine 5-phosphate oxidase" FT /note="Conserved hypothetical protein. Homology to bp2124 FT of B. pertussis of 48% (trembl|Q7VWS5). Pfam: Pyridoxamine FT 5-phosphate oxidase no signal peptide no TMHs" FT /db_xref="GOA:A1K1M7" FT /db_xref="InterPro:IPR009002" FT /db_xref="InterPro:IPR011576" FT /db_xref="InterPro:IPR012349" FT /db_xref="UniProtKB/TrEMBL:A1K1M7" FT /protein_id="CAL92732.1" FT /translation="MAPVEPVAGTAAFHAGERLLQERVGKAAQMAEIGARVIRDYMPEQ FT HRSFFAQLPFVVLGAADGEGRPCATLLTGPPGFVSSPDSHTLRIDALPGAGDPLIGAIR FT VGATVALLGLEPPTRRRNRMNGRVVAADTAGFSVAVRESFGNCPKYIQARSAEFVAGAR FT ASAPPQTLEPADDSLRRVVAAADTLFIATAHPPGGDDPAARYGADVSHRGGKPGFVRWD FT AAADGTVTLTLPDFAGNNFFNTFGNIVLDPRVGLVFVDIAGAAEDGVADIFHVAGHAEI FT VEDAAAVAAFAGALRLLRVRVDAVLRRPKALPLRWGAEVEFSPFLEGTGVW" FT CDS complement(132910..133359) FT /transl_table=11 FT /locus_tag="azo0115" FT /product="conserved hypothetical protein" FT /function="Acyl dehydratase" FT /note="MaoC protein (Phenylacetic acid degradation protein FT paaZ). Entry name :- TREMBL:Q8XXS0 Prim. accession # Q8XXS0 FT InterPro:-IPR002539; MaoC_dehydratas. Pfam:-PF01575; FT MaoC_dehydratas; 1. Identities = 77/145 (53%) Number of FT predicted TMHs: 0" FT /db_xref="GOA:A1K1M8" FT /db_xref="InterPro:IPR002539" FT /db_xref="UniProtKB/TrEMBL:A1K1M8" FT /protein_id="CAL92733.1" FT /translation="MDTRYLDDLQPGERFCTGGVTLTEAEIIDFAWRYDPQPFHLDTGA FT AEQSPYGGLIASGFQSLALCFRLFIQTGVLAQSSLGSPGIDELRWLAPVRPGDTLHCEV FT EVLETRPSSSKPDRGIARLRYAALNQRGETVMTFVIAHLLRRRMG" FT CDS complement(133377..134873) FT /transl_table=11 FT /gene="amn" FT /locus_tag="azo0116" FT /product="AMP nucleosidase" FT /EC_number="3.2.2.4" FT /note="AMP nucleosidase InterPro: Purine and other FT phosphorylases family 1" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1M9" FT /db_xref="InterPro:IPR000845" FT /db_xref="InterPro:IPR011271" FT /db_xref="InterPro:IPR018017" FT /db_xref="InterPro:IPR018953" FT /db_xref="UniProtKB/TrEMBL:A1K1M9" FT /protein_id="CAL92734.1" FT /translation="MSPDAPYFAPERFDDAAAALARVATIYDASVNHLRTTLQRFVAGE FT DIGRHVRACYPFVRVRTGTVARADSRLSYGFVAGPGTYETTLTRPDLFADYYLEQFRLL FT LQNHGVALEIGTGTQPIPLHFSVGAHDHIEGELGLARREQLRDLFDLPDLNAMDDGIAN FT GTHEPRPGEAHPLALFTAPRVDYSLHRLRHYTGTVPEHFQNFVLFTNYQFYIDEFIKLG FT HALMAEGGSHGYEAFVEPGNVVTRPADQPPRPGDELGSAPPRLPQMPAYHLVRGDRAGI FT TMVNIGVGPANAKTITDHIAVLRPHAWIMLGHCAGLRNTQQLGDYVLAHGYVREDHVLD FT EELPLWVPIPPLAEVQLALEAAVEDVTRLSGYELKRLMRTGTVATTDNRNWELLPSHGM FT ASSPERRFSQSRAVALDMESATIAANGFRFRVPYGTLLCVSDKPLHGEIKLPGMANHFY FT RERVDQHLRIGIRALERLRDQGVDRLHSRKLRSFAEVAFQ" FT CDS 135086..135853 FT /transl_table=11 FT /gene="braF" FT /locus_tag="azo0117" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems ATPase component" FT /note="ATP-binding cassette (ABC) transporters are FT multidomain membrane proteins, responsible for the FT controlled efflux and influx of substances (allocrites) FT across cellular membranes. ATP-binding protein is for FT coupling the energy of ATP hydrolysis to conformational FT changes in the transmembrane domains. Similar to FT trembl|Q8XU49 (72%) and to sprot|BRAF_PSEAE (40%). Pfam: FT ABC transporter Smart: AAA ATPases" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1N0" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A1K1N0" FT /protein_id="CAL92735.1" FT /translation="MSEFILETTGLTKEFKGFVAVSGVDLKVQRGHIHALIGPNGAGKT FT TVFNLLTKFLPPTAGTIRFEGEDITREAPAVTARRGLIRSFQISATFPKLTVLENVRIG FT LQRKLGTGFHFWRSEKSLNVLNDRAMALLESVDLGKFADTITGEMPYGRKRALEIATTL FT ALEPTMMLLDEPTQGMGHEDIERVVALIRKVAENRTILMVEHNLSVVANLCDRITVLTR FT GSILAEGSYEEVSKNPKVLEAYVGSDDMADAHH" FT CDS 135870..136592 FT /transl_table=11 FT /locus_tag="azo0118" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems ATPase component" FT /note="ATP-binding cassette (ABC) transporters are FT multidomain membrane proteins, responsible for the FT controlled efflux and influx of substances (allocrites) FT across cellular membranes. ATP-binding protein is for FT coupling the energy of ATP hydrolysis to conformational FT changes in the transmembrane domains. Similar to FT trembl|Q7W5F6 (63%) and to trembl|Q8U8G7 (59%). Pfam FT (PF00005): ABC transporter Smart (SM00382): ATPase FT superfamily" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1N1" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K1N1" FT /protein_id="CAL92736.1" FT /translation="MTSAFESHAEMLRISDLHAFYGESHILHGIDLQVARGECVTLLGR FT NGSGRSTTLKSILGLVGRRSGSIMVNGNEVIAEPTHRMARHGVGYVPEERAIFASLTAE FT ENLLLPPQVSSGGMSVDEIYGMFPNLLERRNSPGTKLSGGEQQMLAMARVLRTGAKLLL FT LDEITEGLAPVIVKKLGEVITELKSRGFTIVLVEQNFRFAAPLADRHYVLEHGEIIATI FT QKDELPGRMDWLHQTLGV" FT CDS 136627..137841 FT /transl_table=11 FT /locus_tag="azo0119" FT /product="probable ABC transporter substrate binding FT protein" FT /function="ABC-type branched-chain amino acid transport FT systems periplasmic component" FT /note="ABC transporter substrate binding proteins count to FT the family of extracellular ligand binding proteins. It is FT a component of the high affinity amino acid transport FT system. Similar to trembl|Q8XU51 (58%) and to FT tremblnew|CAE27314 (45%). Pfam (PF01094): Receptor family FT ligand binding region SignalP reporting Signal peptide." FT /note="Specificity unclear" FT /db_xref="UniProtKB/TrEMBL:A1K1N2" FT /protein_id="CAL92737.1" FT /translation="MHTKKLLTAACTAALAMLATGAHAQFSGNTVKIGVLTDMSGTYSD FT LAGQGAVVATQMAIEDFVAKEKPGFKVEMVSADHQNKADIASNKAREWFEREGVDTATE FT LVTTSTALAVMKVAKEMNKVVLMNGPGSTPITNEQCNDVSVHYTYDTYALANGTAKAVT FT QQGGKNWFFLTADYAFGQALEKDSSAVVTANGGKVVGSVRHPFPASDFSSFLLQAQASN FT AQIIGLANAGADTTNAIKQAAEFGITPKQQLAGLLMFISDVHSLGLKNAQGMFLTTGFY FT WDLNDETRAWSKRFFDKQKRMPTMVQAGQYSSVMHYLKAVKAAGTDDTTKVMAQMKKTP FT INDFFAKNGQIREDGRMVHDMYLVQVKKPEESKYPWDYYHVKQVIPGAEAFQPLSLSRC FT PLVKK" FT CDS 137898..138782 FT /transl_table=11 FT /locus_tag="azo0120" FT /product="ABC transporter permease protein" FT /function="Branched-chain amino acid ABC-type transport FT system permease components" FT /note="Branched-chain amino acid transport system typically FT composed of a periplasmic substrate-binding protein, one or FT two reciprocally homologous integral inner-membrane FT proteins and one or two peripheral membrane ATP-binding FT proteins that couple energy to the active transport FT system.The integral inner-membrane proteins translocate the FT substrate across the membrane. Similar to trembl|Q92LQ5 FT (71%) and to trembl|Q8XU52 (69%). Pfam (PF02653): FT Binding-system dependent bacterial transporters (araH, FT livH/limM families) TMHMM reporting eight Tmhelix." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1N3" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:A1K1N3" FT /protein_id="CAL92738.1" FT /translation="MEIFGVPSALFGSQLLIGLINGSFYAILSLGLAIIFGLLNIINFA FT HGAQYMMGAFVAWIALTKFGVNYWVALLLSPILIGALGVVLERTMLRKLYKLDHLYGLL FT LTFGLALIFEGIFRDQYGISGQAYEVPDALKGGVNLGFMFMPIYRGWVVVAALAVCFGT FT WFMIEKTKLGAYLRAGTENPQIVQALGINVPLLITFTYGYGVALAAFAGVLAAPIYQVS FT PQMGANLIIVVFAVVVIGGMGSIMGSIVTGLGLGLIEGLTRVFYPEASAVVVFFIMVIV FT LLVRPAGLFGKAA" FT CDS 138807..139763 FT /transl_table=11 FT /gene="livM1" FT /locus_tag="azo0121" FT /product="putative branched-chain amino acid transport FT permease" FT /function="ABC-type branched-chain amino acid transport FT system permease component" FT /note="Putative branched-chain amino acid transport FT permease. Homology to livM of S. typhimurium of 25%. Part FT of the binding-protein-dependent transport system for FT branched-chain amino acids. Probably responsible for the FT translocation of the substrates across the membrane. Pfam: FT branch-chain amino acid transport system probable signal FT peptide probable 6 TMHs" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1N4" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:A1K1N4" FT /protein_id="CAL92739.1" FT /translation="MSYNDKSLFDRATPVLFGALFIIGLVAPFAVYPTFLMKILCFGLF FT ACAFNLLLGFAGLLSFGHAAFLGSAGYVCGMLVRDLGVTPEVGIIGGTLAAGVLGWVFG FT VLAIRRSGIYFAMITLALSQMVFFFALQWKATGGEDGLQGVPRGHLFGLIDLSNNLAMY FT YLVFAVFCAGFFIIYRAIHSPFGQILKAIRENEPRAISLGYDVSKYKLLAFVLSAALAG FT LAGATKTLVFQLASLTDVHWHMSGEVVLMTLLGGLGTILGPLVGASVIVSLQSELADKV FT GSWVTVIMGVIFVLCVLLFRRGIVGELQALIRRSGIN" FT CDS complement(139919..141091) FT /transl_table=11 FT /locus_tag="azo0122" FT /product="probable Fe-S cluster redox enzyme" FT /function="predicted Fe-S-cluster redox enzyme" FT /note="Region start changed from 140962 to 141091 (129 FT bases)" FT /db_xref="GOA:A1K1N5" FT /db_xref="InterPro:IPR004383" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR023404" FT /db_xref="UniProtKB/Swiss-Prot:A1K1N5" FT /protein_id="CAL92740.1" FT /translation="MEDQDRVGEQAENGRGFHPAIVAASAAQRHSARPPVRATIHPLMR FT IDDLTQRLRALGAKPAHEQRVLRAWVQRSSMDNRRQAAKDFLPLALREALPALTAELEG FT LARLRSQHPGEDGSARLLVELADGQTVESVLLLRDGLCVSTQLGCAVGCVFCMTGREGL FT LRQLGSAEIVAQVVLARSLRPVKKVVFMGMGEPAHNLDNVLEAIDLLGTAGGIGHKNLV FT FSTVGDYRVFERLPRQRVKPALALSLHTTRADLRAQLLPRAPQIAPQELVELGERYARS FT TGYPIQYQWTLIEGVNDSPEEMDGIVRLLRGKYALMNLIPYNSVPELEFRRPGREAAVA FT LAAYLHRHGVLAKLRQSAGQDVEGGCGQLRARVVKMDRRPRTARATPPTA" FT CDS 141038..141463 FT /transl_table=11 FT /locus_tag="azo0123" FT /product="putative threonine efflux protein" FT /db_xref="InterPro:IPR021218" FT /db_xref="UniProtKB/TrEMBL:A1K1N6" FT /protein_id="CAL92741.1" FT /translation="MESAAVFRLLANAVLVLHAGFVLFVVAGLVLILVGGALDWRWVRD FT VRLRVLHLAAIGVVVAESWLGVVCPLTTLELWLRRLGGQTFYEGDFVAFWLRRLLFFDA FT PGWVFVLAYTGFAALVLLAWWRYPPRRPRQPAQDDGN" FT CDS 141533..141742 FT /transl_table=11 FT /locus_tag="azo0124" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. no homology to the FT data bank. no domains predicted signal peptide no TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K1N7" FT /protein_id="CAL92742.1" FT /translation="MNTSTLLRLAVVACAPALLTACSTQSWYEGARVHAENECRRQPGS FT AAEECMARVNTQRYEDYERARKAQ" FT CDS 141717..142061 FT /transl_table=11 FT /locus_tag="azo0125" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein," FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007077" FT /db_xref="UniProtKB/TrEMBL:A1K1N8" FT /protein_id="CAL92743.1" FT /translation="MSARARRSSGAAAQGLAALPNLGVRSASMLDAAGIHSEAELRALG FT AVAAYVRVKRSGARPGLNLLWALEGALSGTPWQVVAREHRTSLLLALEDEDRGPSAGVP FT GKIDENRSGE" FT CDS 142061..142369 FT /transl_table=11 FT /locus_tag="azo0126" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein with 74% FT similarity(57% identity)to Conserved hypothetical protein FT [Sinorhizobium meliloti]. No Signal peptide reported to be FT present. No TMH reported to be present. Has PF07045,Protein FT of unknown function (DUF1330)This family consists of FT several hypothetical bacterial proteins of around 90 FT residues in length. The function of this family is unknown. FT TIGRFAM:acolac_sm: acetolactate synthase,small s" FT /note="Family membership" FT /db_xref="InterPro:IPR010753" FT /db_xref="InterPro:IPR011008" FT /db_xref="UniProtKB/TrEMBL:A1K1N9" FT /protein_id="CAL92744.1" FT /translation="MKGYWIVRVDVADSERFMNYAQLAGPALKLYGARFLARVGPHTVV FT EGAARARNTVVEFPSYQAALDCWHSPEYQAARALRLGAAEVDIVVIEGFEGTQPGER" FT CDS 142468..142659 FT /transl_table=11 FT /locus_tag="azo0127" FT /product="Hypothetical protein" FT /note="Hypothetical protein, 40% identity to TrEMBL;Q73S36 FT Weak Homology with most protein hits in the database. No FT Domains/Features/Motifs predicted present." FT /db_xref="UniProtKB/TrEMBL:A1K1P0" FT /protein_id="CAL92745.1" FT /translation="MDQTLALEQAGRRYHLSIEFDTPVPSPELRDIEVDLSGVLPSSRR FT PPLPVIRFVPGQWKEGYT" FT CDS complement(142690..143106) FT /transl_table=11 FT /locus_tag="azo0128" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein, 50% FT identity (62% similarity) to TrEMBL;Q7NQ67. No domains FT predicted TMHMM2 reporting 1 TMH's present. No signal FT peptide reported present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR012427" FT /db_xref="UniProtKB/TrEMBL:A1K1P1" FT /protein_id="CAL92746.1" FT /translation="MFSEAEEWVRMGVEWLRLLVETIGAAIIAVGIVVALHGLARHWLH FT HCRDEFNPVRLAFARYLAMALEFQLAADILSTAVAPSWEQLGKLATVAVIRTGLNFFLM FT REIRDEHRGTAEDAGAEHPRPGRPPPGTEKSASA" FT CDS 143294..144907 FT /transl_table=11 FT /gene="tap" FT /locus_tag="azo0129" FT /product="putative dipeptide chemoreceptor" FT /function="Methyl-accepting chemotaxis protein" FT /note="The Tap (taxis toward peptides) receptor and the FT periplasmic dipeptide-binding protein (DBP) of Escherichia FT coli together mediate chemotactic responses to dipeptides. FT Similar trembl|Q7P0E0 (32%) and to SWISSPROT:MCPC_SALTY FT (23%). Pfam(PF00015): Bacterial chemotaxis sensory FT transducer Pfam (PF00672):HAMP domain TMHMM reporting two FT TMH. SignalP reporting Signalpeptid." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1P2" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004089" FT /db_xref="InterPro:IPR004090" FT /db_xref="InterPro:IPR024478" FT /db_xref="UniProtKB/TrEMBL:A1K1P2" FT /protein_id="CAL92747.1" FT /translation="MSIARRIALLLAILIGALVALGTMGVVQMSRVNEGLVYQNEKILP FT KLDLIAATQRRAITYRLLVLRHVLTTDARAMEAAEAPLRQLASEIDADLRKYESMTDSD FT EDRRLLRADREALTAYAAVAERSLAHSRANRNEEASALANGEAAERGNALIAALDAHAR FT YNRELNEAFATGAEETFRSSRALTVALVVLALAAGGGFGFLAYRRIVGALLAMSAAVEG FT VSSTLDFSRRVPADGKDEVAQTGRAFNALLERVQQSLRKMSTHAGEVSAAGSQLASSAR FT QVSIGSSAQSEAAAAMAAAVEQMTVSINHVADRAGEARRLAVLAGDEARGGAEVIGLTL FT ADIRRIDVSVRQAAERVQQLDEDSARVSAVVTVIKEVADQTNLLALNAAIEAARAGEQG FT RGFAVVADEVRKLAERTAQSTQEISSTMEAMQAGARNATGGMSAAVELVGVGVAHAQQA FT EASVRQIEDGARRTVDIVAEISDAIREQSVASSSIAQQVERVAQMTDENSAAAASTSDT FT AVGLEGLAQEMQGEVARYRV" FT CDS 145152..146765 FT /transl_table=11 FT /gene="nahY" FT /locus_tag="azo0130" FT /product="putative aromatic hydrocarbon chemotaxis FT transducer" FT /function="Methyl-accepting chemotaxis protein" FT /note="The ability of bacteria to recognize and swim toward FT aromatic hydrocarbons is possibly an important prelude to FT their degradation. In Pseudomonas putida G7,NahY is the FT receptor required for the chemotaxis to naphthalene. FT Similar to trembl|Q7NU44 (38%) and to trembl|Q7NY58 (33%). FT Smart: HAMP domain Pfam (PF00015): Methyl-accepting FT chemotaxis protein (MCP) signalling domain SignalP FT reporting Signal Peptide." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1P3" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004089" FT /db_xref="InterPro:IPR004090" FT /db_xref="InterPro:IPR024478" FT /db_xref="UniProtKB/TrEMBL:A1K1P3" FT /protein_id="CAL92748.1" FT /translation="MTIAKRIALLLALFTLALLTVGATGVLQVRSLNQGLLYQTSNILP FT SLARIGDLQLQVMRFRSIVLSHVLATEAKEMAEIEVELGKVRQGIEEGLVKYQTLVSDE FT EDGRRLAAVSAALRGYLTLADHEIELSRQNRNEEARRMIATEGAKHSAELIGALERLAE FT YNRELAERFEHEAERSFRNGLVLSVGMTLVAIAGGALLGFATYRRVVGSLVAMSGAVQD FT VSTTLDFSRRVPVEGRDEVAQTARAFNALLERVQQSLRQMSQHASSVFAAGTSLAASAQ FT QVSAGSSEQSEAAGAMAAAVEEMTVSVNHVADRASEASELAASAGRDAHAGAEVIGKTL FT ADIRRIDASVRQAAERVQQLDADSARVSAVVAVIKDVADQTNLLALNAAIEAARAGEQG FT RGFAVVADEVRKLAERTAQSTQEISSTMEAMQSGARNAVSGMTEAVEQVARGVGHAQQA FT EESIRQIEAGSRRTVERVAEISDAIREQSEASSNIARQVERVAQMTDENSAAAASTSDT FT AAALNGLARDMQSEVSRYRV" FT CDS 146889..147092 FT /transl_table=11 FT /gene="dmpI" FT /locus_tag="azo0131" FT /product="probable 4-oxalocrotonate tautomerase" FT /function="uncharacterized protein 4-oxalocrotonate FT tautomerase homolog" FT /EC_number="5.3.2.2" FT /note="Probable tautomerase lin2709 (EC 5.3.2.2). FT TREMBL:Q7UE84: 67% identity, 86% similarity FT InterPro:IPR004370; Taut. ProDom: PD404143 InterPro: FT 4-oxalocrotonate tautomerase taut: 4-oxalocrotonate FT tautomerase No signal peptide no TMH's" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1P4" FT /db_xref="InterPro:IPR004370" FT /db_xref="InterPro:IPR014347" FT /db_xref="InterPro:IPR018191" FT /db_xref="UniProtKB/TrEMBL:A1K1P4" FT /protein_id="CAL92749.1" FT /translation="MPYVNIQVTAGVTRAQKAQLVREVTDALVRVLGKKPEHTHVVIQE FT IDEENWGYAGMLTDDWRRQQGS" FT CDS 147273..148154 FT /transl_table=11 FT /locus_tag="azo0132" FT /product="transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="Transcriptional regulator, LysR family," FT /note="Specificity unclear" FT /db_xref="GOA:A1K1P5" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1P5" FT /protein_id="CAL92750.1" FT /translation="MRLPPLHALVAFEAAARAGSFLAAAAELHLTPSAVSHRIKALEDW FT LGTALFERRQRLVVLTEAGRDYLAQIQPALADIETASAAMQAPHSRVLRLSVAPAIGAK FT WFVGQLAAYREVDPGLEFVLSTASTMAPVAAGKADVGLCYGEPPWPGLEAYELRRETVF FT PVCNPALAARLGDPPAAAALAALPLLRHPLLAWRPWFAAVGLDRAEPAEGPLFEDAMMM FT LEAASAGVGVALTVELLARPYLASGALQRPFAVAVPGKAFHAVLRADAYGRPWVRRFVR FT WLQGRARRDTAA" FT CDS 148401..149321 FT /transl_table=11 FT /gene="ilvE1" FT /locus_tag="azo0133" FT /product="branched-chain-amino-acid transaminase" FT /function="Branched-chain amino acid FT aminotransferase/4-amino-4-deoxychorismate lyase" FT /EC_number="2.6.1.42" FT /note="Branched-chain amino acid aminotransferase (EC FT 2.6.1.42) (BCAT). Acts on leucine isoleucine and valine (By FT similarity). InterPro: Aminotransferases class-IV" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1P6" FT /db_xref="InterPro:IPR001544" FT /db_xref="InterPro:IPR005785" FT /db_xref="UniProtKB/TrEMBL:A1K1P6" FT /protein_id="CAL92751.1" FT /translation="MSMEDRDGWIWMDGQWLPWRDAKVHALTHTLHYGLGCFEGIRAYP FT TAHGPAVFRLDDHIERLFDSAHILGLAMPCTPAEVRAACLEAVRRNGLDGGYIRPLVFL FT GAEKVGVDPAGAATHVMVAAWQWGAYLGAQALERGIRVKVASFARHHVNVQMCRAKSVS FT TYTNSILACREARAEGYDEALLLDTDGFVAEGPGENVFVVKRGVIYEPEITSALDGITR FT RTLQTLASEAGYEIRARRITRDELYIADEVFFTGTAAEITPVVEVDRRRVGSGRPGPVT FT QALQRRFFACVRGEDPAHADWLAPA" FT CDS complement(149318..150751) FT /transl_table=11 FT /gene="ydaM" FT /locus_tag="azo0134" FT /product="putative response regulator" FT /function="Response regulator containing a CheY-like FT receiver domain and a GGDEF domain" FT /note="Hypothetical response regulator, TREMBL: FT trembl|Q7MSI2 (24% Wolinella succinogenes, hypothetical FT protein ws0414) InterPro: IPR001610 PAC. IPR000014 PAS. FT IPR001789 Response_reg. IPR000160 GGDEF. Pfam: PF00990 FT GGDEF domain. PF00072 Response_reg. PF00785 PAC. PF00989 FT PAS. TIGRFAM: TIGR00254 putative diguanylate cyclase FT (GGDEF) domain. TIGR00229 PAS domain S-box." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1P7" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR013655" FT /db_xref="UniProtKB/TrEMBL:A1K1P7" FT /protein_id="CAL92752.1" FT /translation="MSGRYAIVCIDDEETILESLSMELAGRFPGVDLELLQDNADAEGL FT IGSLLAAGVEVPVVVCDYIMPGRRGDAVLAAVHRLAPAARTIMLTGQSNLEGVTHAINH FT ANLYRYIAKPWNKEDLALTLQGALESYIQEATIQRQNQALVALNDGLERKVAERTEALR FT AANANLTEANRKIGEYLEIIDRQVLICRINRAGLVTYASEAFCRRSGYTRADLIGLNYW FT HALYSATTETLMREILARIEAGAGWEGEILHQCRNGEYYWARETIAPDVGEHGAVIGFT FT SIRQDITDKKAVEALSVTDPLTGLANRRQFQQVLEGEIARASRGARALAFCLVDVDHFK FT AYNDHYGHAAGDKVLQRLGRLLTDTFRRSTDFTFRIGGEEFALLFPVRDSAEAATTAAE FT LVALVEAQAIVHAFGSPGPHLTISMGVRVISPREQPLDVDRIFQEADALLYQAKHEGRN FT RYVLGGEAVAAAPASSGDA" FT CDS complement(150748..151149) FT /transl_table=11 FT /locus_tag="azo0135" FT /product="putative response regulator" FT /function="FOG: CheY-like receiver" FT /note="Putative response regulator," FT /db_xref="GOA:A1K1P8" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="UniProtKB/TrEMBL:A1K1P8" FT /protein_id="CAL92753.1" FT /translation="MTDGVILCVDDEETILTALEMQLDELFDARFIVELAQGAAEAYEV FT LESYEAGELPLLVIISDWQMPQIKGDEFLIEAHRRFPHVVKIMLSGHADPAAVDNAREH FT ADLYCFLSKPWDKDELRNAILDGIRDKRP" FT CDS complement(151184..153406) FT /transl_table=11 FT /locus_tag="azo0136" FT /product="putative hybrid sensor and regulator protein" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.3.-" FT /note="Putative hybrid sensor and regulator protein," FT /db_xref="GOA:A1K1P9" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="UniProtKB/TrEMBL:A1K1P9" FT /protein_id="CAL92754.1" FT /translation="MSRLKSIGAELGLLFLVVALAPIVTAYYVANDIFGEAIRQEKREA FT LTAIADAAHGRIESYVRTLISDTTTLAKSPKVGELLSALEHLPGPSPATAEFLRAYREE FT KGYYDVMLVDHLGNIRLSLSQPEVVGQSIQGELLRGSALARTIDAANTLLQTEVSNFAH FT FPPSKGHAAFLAAPVFAGGVIIGNAVLQIDNRELDGIINRFGGLGESGEVLVGTIENAQ FT LLITAPPRHDATLRNRQVDAARFAPLRAALEGSQGTGGYTDYRGHDTLAVWRYLPSLNW FT GMLVKIDTAELYAPIRRFEAISLMVMVASVLLVLFGVALSNRLVSRPLVRFAQTVKALD FT EESLPAAVNIDARHEIRDLVTAFNTLIGSVRSHQHQLEARVSERTAELATANAGLARAN FT LDLQESNAELAVTLDELQRTHRQLVESEKLATLGQLIAGIAHEINTPLGSIASSIDTII FT AGGQQQTAFLALYAGLGEDHRALVCSLLNVAATGSSLSLKEKRALKKDYETRLAEHPAV FT DARKAAELLSHLPPLDLERYLPLLTHPEAGAILDQVKHAMNLHRASHNIKLASEKARKV FT VFALKNFARFGDHGSKTPTRLRDSIDTVLTLYHNQIKQAVDLRAELPDLPPIPAYADEL FT GQVWMNLIHNALQAMDYCGRLDITLEQDAERAVVRISDTGCGIPEEIRERIFQPFFTTK FT PAGEGSGLGLDIVRKILDKHGGSIRVESAVGRGSTFEVTLPATETA" FT CDS complement(153403..154701) FT /transl_table=11 FT /gene="amiC1" FT /locus_tag="azo0137" FT /product="putative aliphatic amidase expression-regulating FT protein" FT /function="ABC-type branched-chain amino acid transport FT systems periplasmic component" FT /note="Aliphatic amidase expression-regulating protein,AmiC FT regulates the expression of the inducible aliphatic amidase FT activity in Pseudomonas aeruginosa. Similar to FT sprot|AMIC_PSEAE (31%) and to trembl|P74390 (50%).Pfam FT (PF01094): Receptor family ligand binding region SignalP FT reporting Signal peptide." FT /note="Specificity unclear" FT /db_xref="InterPro:IPR017777" FT /db_xref="UniProtKB/TrEMBL:A1K1Q0" FT /protein_id="CAL92755.1" FT /translation="MKSRILAAVAVLLVAGIAAAVAIWPSAGPARAGQVQPIRVGVLHS FT LSGTMAISERSVAAATRLAIDHINAAGGVLGRPLEAVVRDGASDWSTFAREADALIARE FT KVEVVFGCWTSASRKTVKPVFERHDHLLFYPVQYEGLESSPNIVYTGAAPNQQIIPAVK FT WALDNIGRRFFLVGSDYVFPHSANAIMKDQIRSLRGEVVGEHYVLLGSSAVEAAVEAIA FT ATRPDVILNTLNGDSNVAFFKALRAYGITPQVIPTISFSIAEAELQAMGSADFAGDYAA FT WNYFQSLPGEANADFVAAYKARYGEQEVVTDPMEAAWIGVHLWARAVESAGSADPRAVR FT LALQGKSMAAPEGAVSIDPHSQHLWKSVRIGRILPGGQFEVVWSTPKPVRPLPYPGYRP FT PHEWDAFLGRLNERWNGHWANPGATPSTVEARS" FT CDS 154860..155846 FT /transl_table=11 FT /locus_tag="azo0138" FT /product="conserved hypothetical protein" FT /function="Sphingosine kinase and enzymes related to FT eukaryotic diacylglycerol kinase" FT /note="Conserved hypothetical protein.Similarity to FT b.subtilis bmru and to synechocystis pcc 6803 sll0036. FT Identities = 29/85 (34%) Entry name SWISSPROT:YEGS_ECOLI FT Prim. accession # P76407 InterPro IPR005218; FT Cons_hypoth147. IPR001206; DAGKc. Pfam PF00781; DAGKc; 1. FT Prediction: Non-secretory protein Signal peptide FT probability: 0.00 Number of predicted TMHs: 0" FT /db_xref="GOA:A1K1Q1" FT /db_xref="InterPro:IPR001206" FT /db_xref="UniProtKB/TrEMBL:A1K1Q1" FT /protein_id="CAL92756.1" FT /translation="MNADAKPALPADSVQSVAEGAIDGPLLIVLNPGSGAQDADDARRR FT IAAVLDAAGRAHEFIAVEDPAQLGGIAADCALRAAASGGAVVAAGGDGTINAVAHAVLE FT AGCRFGVLPMGTFNYFGRTHHIPEDLEAAARVLVEGELRPVQVGEVNGRIFLVNASVGM FT YPQLLEERETAKRQFGRSRAVAFVSALYTLLRNHRVLRLWLRCDDATGRVETPTLFVGN FT NRLQLEQIGMAEAACVDAGALAVIGLRPVSPLGMLALALRGTLGRLGDADNVFSFPCAA FT LFVSAGGGRRPPRVKVATDGEVLWMRLPLQFRVAPARLQLLCPPPAP" FT CDS 155860..156708 FT /transl_table=11 FT /gene="cpdA" FT /locus_tag="azo0139" FT /product="probable phosphodiesterase" FT /function="predicted phosphohydrolases" FT /EC_number="3.1.4.17" FT /note="Serine/threonine (S/T) phosphatases catalyse the FT dephosphorylation of phosphoserine and phosphothreonine FT residues. In mammalian tissues four different types of PP FT have been identified and are known as PP1, PP2A, PP2B and FT PP2C. Except for PP2C, these enzymes are evolutionary FT related. The catalytic regions of the proteins are well FT conserved TREMBL:Q7VZQ9: 41% identity, 50% similarity FT InterPro:IPR004843; M-ppestrase. Pfam:PF00149; Metallophos FT InterPro: Serine/threonine specific protein phosphatase No FT transmembrane helices sbcd: exonuclease SbcD" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1Q2" FT /db_xref="InterPro:IPR024654" FT /db_xref="UniProtKB/TrEMBL:A1K1Q2" FT /protein_id="CAL92757.1" FT /translation="MAALLHLSDPHFGTERAPVVEALLHCVARQTIDVAVISGDITQRA FT RRHQFDAARAFVERLRAGLNGAPVLVLPGNHDIPLYALQRRLLRPFAGFRRVFGPQLEA FT CHEDDSLQLQLVNTVSRWRHTDGVVRADQVERVARRLEAARPGQLRVIVTHQPAAVVRP FT QDASDLLRGRERALRRWAAAGADLLLGGHIHLPYVQPLALPGPDGAPRPLWVVQAGTAL FT SHRIRHEAGNSFNLIRHGAGASACVVERWDYDEAEHRFACRAQTPLALECGPAEATTRA FT S" FT CDS complement(156692..157861) FT /transl_table=11 FT /locus_tag="azo0140" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to an orf FT of Ralstonia eutropha of 61% (ZP_00167955). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="InterPro:IPR013702" FT /db_xref="InterPro:IPR019494" FT /db_xref="UniProtKB/TrEMBL:A1K1Q3" FT /protein_id="CAL92758.1" FT /translation="MTAPTFLAAHAAAPQWRRALDVCLARLEHGARNAGRPLGDYTLGW FT CYFTDAYTAAAEPLLAELQRRVPGASWVGTAGSGVAASGVEYIDQPALVLMLAPLPRSA FT FRVFSGRQPLHPERDGFPAHAALVHADGNTPDLQELLPELAARTATGYLFGGLSSASRH FT LQLADAVLSGGLSGVAFSDEVGLISRVTQGCQPIGPLRTATRVDDNVLLTLDGLPALAC FT VLQDLGLANDIPVAEMADALSGTLVGLRAPGEAQPGAPGRFGADTVVRHIVGVDPRARV FT LVVADEVAAGSRLAFCHRNPDAAMADLHRIAGEIRDELATRGQRAAGAVYASCIGRGGP FT HFGRPNAELAAIREVLGDMPLAGFFAGGEIARDRLYGYTGVLTVFTMPA" FT CDS 158045..159949 FT /transl_table=11 FT /gene="gidA" FT /locus_tag="azo0141" FT /product="glucose inhibited division protein A" FT /function="NAD/FAD-utilizing enzyme apparently involved in FT cell division" FT /note="Glucose inhibited division protein A." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1Q4" FT /db_xref="InterPro:IPR002218" FT /db_xref="InterPro:IPR004416" FT /db_xref="InterPro:IPR020595" FT /db_xref="UniProtKB/Swiss-Prot:A1K1Q4" FT /protein_id="CAL92759.1" FT /translation="MLYPTRFDVIVVGGGHAGTEAALAAARMGCRTLLLSHNIETLGQM FT SCNPSIGGIGKGHLVKEVDALGGAMAAATDEGGIQFRILNASKGPAVRATRAQADRVLY FT KAAIRKRLENQPNLWLFQQAVDDLTVAGDRVTGVVTQIGLRFEAPAVVLTAGTFLNGLI FT HVGLEHYSAGRAGDPPAISLGQRLKELALPQGRLKTGTPPRLDARSIDFSVMTVQPGDD FT PVPVFSFLGSAAQHPAQLPCWMTHTNTRTHDVIRANLDRSPMYSGVIEGVGPRYCPSIE FT DKIHRFADKDSHNIFLEPEGLTTHEIYPNGISTSLPFDVQLEIVRSIRGLENAHILRPG FT YAIEYDYFDPRNLKSSLETKSIGGLFFAGQINGTTGYEEAAAQGLLAGANAALQVQGRE FT AWCPRRDEAYLGVLVDDLITRGVSEPYRMFTSRAEYRLQLREDNADLRLTEKGRELGLV FT DDVRWAAFCAKREAIERETARLKTSLARPDLIPVADQERVLGKTLEREARYFELLRRPE FT TTYASLMSLPGAPEQPETDPQVVEQLEIAAKYQGYIDRQQDEVAKQLQAESTRLPADLD FT YAEVRGLSKEVQQKLNLHKPETIGQAGRIQGITPAAISLLLVWLKRRDLAARSERRSA" FT CDS 159946..160584 FT /transl_table=11 FT /gene="gidB" FT /locus_tag="azo0142" FT /product="probable methyltransferase GidB" FT /function="predicted S-adenosylmethionine-dependent FT methyltransferase involved in bacterial cell division" FT /EC_number="2.1.-.-" FT /note="Probable methyltransferase GidB. Homology to gidB of FT E. coli of 47% (sprot|GIDB_ECOLI) Probable FT S-adenosyl-L-methionine dependent methyltransferase FT specific for a sterol and/or lipid substrate (By FT similarity). InterPro: Glucose inhibited division protein FT (IPR003682) Pfam: Glucose inhibited division protein FT Tigrfam: gidB: glucose-inhibited division protein no signal FT peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1Q5" FT /db_xref="InterPro:IPR003682" FT /db_xref="UniProtKB/Swiss-Prot:A1K1Q5" FT /protein_id="CAL92760.1" FT /translation="MSVLTPYAGRLADGIAALGLDIPTATQARLIAFGELLLKWNKVYN FT LTAIRAPQEVITHHLLDSLAVLPYLSAVTRLADIGSGGGLPGIPLAIVRPELSVISVET FT VNKKASFQQQAKIELGLGNFQPLNARVENLKPEQPCDGVISRAFSSLKDFVELSGHLVG FT DGGALYAMKGVRPDDEVAALPAGWTVRATHPLAVPGLDAERHLLVIARG" FT CDS 160716..161486 FT /transl_table=11 FT /gene="parA1" FT /locus_tag="azo0143" FT /product="ParA family protein" FT /function="ATPases involved in chromosome partitioning" FT /note="putative chromosome partitioning protein" FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR002586" FT /db_xref="UniProtKB/TrEMBL:A1K1Q6" FT /protein_id="CAL92761.1" FT /translation="MARIFCVANQKGGVGKTTTCVNLAAALHQCGQRTLLVDLDPQGNA FT TMGSGVDKRSLEQSVYHLLVGLTGLAEARVTSPTGGYDVLPANRDLAGAEVELVSLENR FT ENRLREALQQFDADYDFVLIDCPPSLSMLTLNGLCAAHGVIIPMQCEYYALEGLSDLVN FT TIKKVHANLNRDLKIIGLLRVMFDPRVTLQQQVSAQLEGHFGDKVFSAIVPRNVRLAEA FT PSHGMPGVVFDKAAKGAQAYMAFAGEMIERAKAF" FT CDS 161496..161789 FT /transl_table=11 FT /locus_tag="azo0144" FT /product="probable nucleotidyltransferase" FT /function="predicted nucleotidyltransferases" FT /EC_number="2.7.7.-" FT /note="Hypothetical protein MJ0435. trembl:Q8DGT1:51% FT identity, 64% similarity InterPro: IPR002934; NTP_transf. FT Pfam: PF01909; NTP_transf_2 No signal peptide (Signal P FT predicted) No transmembrane helices (TMHMM predicted). FT hstdl_phs_rel: histidinol phosphatase-r" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1Q7" FT /db_xref="InterPro:IPR002934" FT /db_xref="UniProtKB/TrEMBL:A1K1Q7" FT /protein_id="CAL92762.1" FT /translation="MGRLFEQLIARREEVLACLARHRASNPRVFGSVARGEEGADSDID FT LLVDLPRDISSFEVVRLNQELDDMLAHRVDLVIEDELHPALRVRVLAEARTL" FT CDS 161786..162148 FT /transl_table=11 FT /locus_tag="azo0145" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical secreted protein. Homology to FT TLL2231 of Thermosynechococcus elongatus of 34% FT (tremble:Q8DGT2). Signal peptide present. No TMH reported FT present. Has (IPR008201)PF01934 Protein of unknown function FT DUF86;The function of members of this family is unknown." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR008201" FT /db_xref="UniProtKB/TrEMBL:A1K1Q8" FT /protein_id="CAL92763.1" FT /translation="MTRERDALLLVGDMLAALAEIESFAQVGEAAFMADLRTQRAIERS FT FEILGEAASQLSTELRARYAEVPWRVVIDHRNRLIHGYASIEPARVWQTIVRDLPGLRA FT SLEQAQTLIRGEQPGD" FT CDS 162150..163013 FT /transl_table=11 FT /gene="parB" FT /locus_tag="azo0146" FT /product="probable chromosome partitioning protein ParB" FT /note="Probable chromosome partitioning protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1Q9" FT /db_xref="InterPro:IPR003115" FT /db_xref="InterPro:IPR004437" FT /db_xref="UniProtKB/TrEMBL:A1K1Q9" FT /protein_id="CAL92764.1" FT /translation="MTPPKLKGLGRGLDALLAANRDDEAEKGELQTLATAALQPGKYQP FT RTRMDPGSLEELAASIKAQGVMQPVLVRPLPQLNGAPRYEIIAGERRWRASQIAGLAEL FT PCLVREIPDEAALAMSLIENIQREDLNPLEEAGGIQRLIDEFAMTHQQAADAVGRSRPA FT ASNLLRLLNLARPVQELLMAGDIDMGHARALLPLDGASQIQLANLVAARQLSVRETERL FT VQHTLNPRQKKAAAAPDRDLVRLEEEIADAIGATVKIKANKKGAGEVTIRFGSLDQLDG FT LLGRLR" FT CDS complement(163114..165879) FT /transl_table=11 FT /locus_tag="azo0147" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT RS05051 of Ralstonia solanacearum of 45% FT (trembl|Q8Y1A4(SRS)). TMHMM2 reporting the presence of 26 FT TMH's. Signal P reporting Signal Peptide present. Coils2 FT program reporting presence of Coiled coil." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR014600" FT /db_xref="InterPro:IPR019286" FT /db_xref="UniProtKB/TrEMBL:A1K1R0" FT /protein_id="CAL92765.1" FT /translation="MAMVIWIAAGALVGLIGGPAGILAGAVLGGLVAQLRKDGQQTASR FT QDQRIAALEREVATLSRRVAAITAPPASAGAAPAGPVEEPAPLHLDLDLPPLQTASADV FT AAPAGSPPADDALVPAKAGPALPPRSPSVAPLDADAPDLDALYLRCRDWLLGGNTLVRV FT GILVLFFGLAFLARYAVEHDLLPPALRLAGIGGGGLALAALGWRLRRRRPGYALTLQGG FT GVAVLYLTVFAAFRLYALLPAGAAFALMLLIVAAAAWFAVRQDAPALAVIGTAGGFAAP FT ILASTGGGTHVELFTYYALLNTGVLALAWWRAWRSLNLTGFLFTFAIGLAWGAADYHPW FT HFATTEPFLVLFFLMYVAAAVAYAWKRAPALGDPVDGTLVFGVPVVGFGLQAALVHGMP FT DALAWSAAAVGVFYLVLAAALHRLRKPALELLVASFTALGIAFLTLAIPLAFDGRWSAA FT AWALEGAALWWVGLRQQRRLAAACGLLLQAGAGLLFAADLAQHPGLRDLAVLNSAFLGT FT TMIAGAGFVSAWLAARETRWPAWLQAVGHALLAWAWLWWLGGGWAEIDAQVFTGTRPAA FT HLLLFAASGAVAVGLAARLRWADLQSAVALPAAGMLLAIAQVMNYGVPPSGHGGWLAWP FT AALALHAFALYRADAHPARGLLGWTHAAGVWLLALAAAQEVGQRVATLGWGNGWETPAF FT ALPPVLVLALLTRMASGARWPFATWRPAYLVAGAVPLAIGLVLWSLVVLPLADGSTRPY FT GYVPLANPLDLTVIAALGTIAGWLRRARPQLEARFGPLQPLQAGLALVAFIAANGSLLR FT AVHHATGLPWELPRLLAADTTQTALSLMWAVLGLGLMLLANRRASRPTWVAGAALMAAV FT VAKLFLVDMAASGTLTRIVSFIGAGLLLLVVGYFSPLPPKQTVPAERAPE" FT CDS complement(165901..167784) FT /transl_table=11 FT /locus_tag="azo0148" FT /product="putative acyltransferase family protein" FT /function="bifunctional protein" FT /EC_number="2.3.1.-" FT /note="Similar to the Aas bifunctional protein [includes: FT 2-acylglycerophosphoethanolamine acyltransferase FT (2-acyl-gpe acyltransferase); acyl-acyl carrier protein FT synthetase (acyl-acp synthetase)].Plays a role in FT lysophospholipid acylation. 25% Acyltransferase.IPR000873; FT AMP-bind. Pfam:PF01553; Acyltransferase; 1.PF00501; FT AMP-binding; 1. TMhelix:10" FT /note="Function unclear" FT /db_xref="GOA:A1K1R1" FT /db_xref="InterPro:IPR002123" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="UniProtKB/TrEMBL:A1K1R1" FT /protein_id="CAL92766.1" FT /translation="MSQQFELMKQRRFLPFFLTQFLGAFNDNVYKNALVVLLTFQAARY FT TTLAPGVLVNLCAGLFILPFFLFSATAGQIADKYEKSRLIRFTKLLEIGVMLLGCIAFA FT AESLVLMLATLFLMGAQSTLFGPVKYAILPQHLRENELVGGNALVESGTFVAILIGTLA FT GGVMVSMPDGTLWVSAAIVTLALAGYLSSRGIPTAPAAAPELRINWNPVTETWRNLAFT FT RGNRSVFLAVLGISWFWFYGAVFLSQFPAYAKDVLGGDEHAVVLLLAVFSVGIGIGSLL FT CERLSTGHIEIGLVPFGSLGLSLFALDLWWASPAAVVPGTPAAPLSALLAQPANWRVVA FT DLVAIGIFGGFYIVPLYALIQSRSEPGHRSRIIAGNNILNAAFMVVAAGMGAALLAAGL FT DVTALFLVTALLNAVVAIYIYTLVPEFLLRFLVWLLVHSVYRLQVRGVQHIPEQGAAVL FT VCNHVSFVDALVIMAASRRPIRFVMHHQIFRLPLLRFVFREGRAIPIASAREDPAMMER FT AFDEIARALEAGELIAIFPEGHITEDGDISPFRPGIRRILERTPVPVVPLALRGLWGSF FT FSRKDGRPMSRPLRRGLFSRIELVAGEPLAAAAASPEALQGRVAELRADWR" FT CDS complement(167781..169031) FT /transl_table=11 FT /gene="uxuA" FT /locus_tag="azo0149" FT /product="putative mannonate dehydratase" FT /function="predicted metal-dependent hydrolase of the FT TIM-barrel fold" FT /EC_number="4.2.1.8" FT /note="tremblnew|AAR36422:35% identity, 46% similarity FT EMBL:AE017218; AAR36422.1; TIGR:GSU3030; This FT Fe2+-requiring enzyme plays a role in D-glucuronate FT catabolism in Escherichia coli. Mannonate dehydratase FT converts D-mannonate to 2-dehydro-3-deoxy-D-gluconate. An FT apparent equivalog is found in a glucuronate utilization FT operon in Bacillus stearothermophilus T-6. FT Interpro:IPR004628;Man_dehyd SignalP predicted signal FT peptide present. No. of transmembrane helices: 1 (TMHMM FT predicted) pyrC_dimer: dihydroorotase homodimeric" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1R2" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR006992" FT /db_xref="UniProtKB/TrEMBL:A1K1R2" FT /protein_id="CAL92767.1" FT /translation="MSRPTCNTRRRLLLAAGGVALAGTAAGFAAARPLLMNECRAQLPA FT DPAVQALLTAAWADLDPARVWDVHVHLAGTGDSGRGIELSERMQTPLRPFDYAQRLFYL FT NAGCAHRAPGQVDESYIARLQNLCADAPAGFKLMLFAFDRAYDEHGRVLPLEGSMYIPN FT DYASEVARRAPERFEWVCSIHPWRTNAVAQLQAAAEQGARAVKWLPPAMGIDPASPRCD FT AFYDALARLDLPLLTHVGEEKAVHGPGLPEWGNPLRLRRALERGVRVIAAHCGSLGSDV FT DTDRASRPRVPTFDLFARLMDDEAHASRLLGDVSAITLINRDPEVIRTIVERREWHERL FT LFGSDYPLPGIVPLIPLAKLVRERLLDAGAVPALDALRHHNPILFDFALKRQLASRGRR FT LPASVFETRRHFDRSVA" FT CDS complement(169028..171166) FT /transl_table=11 FT /gene="aas" FT /locus_tag="azo0150" FT /product="bifunctional Aas protein" FT /function="Acyl-CoA synthetases (AMP-forming)/AMP-acid FT ligases II" FT /EC_number="6.2.1.20" FT /note="AAS bifunctional protein [Includes: FT 2-acylglycerophosphoethanolamine acyltransferase FT (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein FT synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN FT LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE FT 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE FT PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS FT TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY FT TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE FT A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% FT identity). Pfam (PF00501): AMP-binding enzyme. Pfam FT (PF01553): Acyltransferase. TIGRFAM (TIGR00530): FT 1-acyl-sn-glycerol-3-phosphate acyltransferases. SignalP FT reporting signal peptide." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1R3" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR002123" FT /db_xref="InterPro:IPR020845" FT /db_xref="UniProtKB/TrEMBL:A1K1R3" FT /protein_id="CAL92768.1" FT /translation="MPVIRFVLRLLLGTLFSVRVRGDNASLSARRLLIVANHESFLDGL FT LLGLFLPADPVFVVHTGVTRRFWFRLALRLVDHLAVDPTNPMAMKRVIRLLEEGRPVVI FT FPEGRITVTGSLMKVYEGPAFVAAKTGATIVPVRLDGAARSYFSRVAGRHPRRMLPRIT FT LSIQPPTRIEMPEAPTAKARRQKAGEAMRRLMQEMLFASRPSQTLFDALLDTAALHGRQ FT RAVVEDVKQVEYSYGDLIKMSLALGRLGSRLGGPGERIGVLLPNLAPTLGLVFGLNAFG FT RTPAMLNYTAGTEGLQAACTAACLRTVITSRAFLEQARLTERVTALEGVRIVYLEDLRA FT TLGLADKLWLMLWALHFPRLATCRQQPGDPAVVLFTSGSEGKPKGVVLSHQALLANVAQ FT IRAVVDISPDDKILNALPLFHSFGLTAGSLLPVLSGADVFLYPSPLHYRVIPELAYDRG FT CTVLLGTSTFLGNYARFAHPYDFFRLRYVIAGAEKLSEAVRTSWFEKFGIRIFEGYGAT FT ETAPVLAVNTPMAYRSGTVGQLLPGLHAKLLAVPGIDRGGILHVSGPNLMSGYLRVEQP FT GVLQPPSSAAGEGWYETGDVVDIDDDGFLRIVGRVKRFAKVAGEMVSLESVEKLAVQTA FT SEFAHAASTQPDPARGESIVLFSTDPALTRERLQAAARDGGWPEIAVPRRIVPVDALPL FT LGTGKIDYVTLKRWAEAA" FT CDS complement(171247..171558) FT /transl_table=11 FT /gene="smtB" FT /locus_tag="azo0151" FT /product="putative transcriptional repressor" FT /function="predicted transcriptional regulators" FT /note="Putative transcriptional repressor," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1R4" FT /db_xref="InterPro:IPR001845" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1R4" FT /protein_id="CAL92769.1" FT /translation="MNPDYSREIPQPWRQMSRVFTALGDEHRQRILLTFERDERLNVSQ FT IAGVSTLSRPAVSHHLKILREAGVLSSEKVGKEIYFWVNTSFLTETFDNVRDYLASRL" FT CDS 171735..172085 FT /transl_table=11 FT /locus_tag="azo0152" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT BB4612 of Bordetella bronchiseptica of 37% FT (trembl|Q7WEM2(SRS)). No domains predicted. signal peptide FT 3 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR005598" FT /db_xref="UniProtKB/TrEMBL:A1K1R5" FT /protein_id="CAL92770.1" FT /translation="MTSPMLRSVLLQLGAGLVATAIAAVFFGPRGAISAAYGALACIVP FT AAMFALRLGALARRSGATVTAFVVGEFVKIASIVGLLVLFPALYPGVHWGALLIGLILA FT LKANLFAFLVRN" FT CDS 172088..172936 FT /transl_table=11 FT /gene="atpB" FT /locus_tag="azo0153" FT /product="probable ATP synthase A chain" FT /function="F0F1-type ATP synthase subunit a" FT /EC_number="3.6.3.14" FT /note="Probable ATP synthase A chain (Protein 6). Homology FT to atpB of E. coli of 47% (sprot|ATP6_ECOLI). Key component FT of the F-type ATPases (EC 3.6.3.14). The ATPase has 2 FT components, CF(1) - the catalytic core - and CF(0) -the FT membrane proton channel. CF(1) has five subunits: alpha, FT beta, gamma, delta, epsilon. CF(0) has three main subunits: FT a, b and c. Subunit A might be component of the proton FT channel; it may play a direct role in the translocation of FT protons across the membrane. InterPro: ATP synthase A FT subunit (IPR000568) Pfam: ATP synthase A chain no signal FT peptide probable 6 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1R6" FT /db_xref="InterPro:IPR000568" FT /db_xref="InterPro:IPR023011" FT /db_xref="UniProtKB/Swiss-Prot:A1K1R6" FT /protein_id="CAL92771.1" FT /translation="MATEHAPTASEYVVHHLTHLNSTGHAQTSIVDFSVINVDSMFYSV FT LLGLLTVFLLWLAARKATAGVPGRFQGFVELLVEMVADQAKGIIHSAESRKFVAPLALT FT VFVWIFLMNAMDMLPVDLLPRIWEGVYASAGGDPHHAYMRVVPTADLSATLGMSCGVLL FT LCLYYNVKIKGVSGWVHELFTAPFGSHPLLYPINFAMQIIEFVAKTVSHGMRLFGNMYA FT GELIFILIALLGSTATVFGFVGHIVAGSIWAIFHILIITLQAFIFMMLTLVYIGQAHEG FT H" FT CDS 172992..173237 FT /transl_table=11 FT /gene="atpE" FT /locus_tag="azo0154" FT /product="probable ATP synthase C chain" FT /function="F0F1-type ATP synthase subunit FT c/Archaeal/vacuolar-type H+-ATPase subunit K" FT /note="ATP synthase C chain. Homology to atpE of E. coli of FT 48% (sprot|ATPL_ECOLI). Key component of the F-type ATPases FT (EC 3.6.3.14). The ATPase has 2 components, CF(1) - the FT catalytic core - and CF(0) - the membrane proton channel. FT CF(1) has five subunits: alpha, beta, gamma,delta, epsilon. FT CF(0) has three main subunits: a, b and c. Pfam: ATP FT synthase subunit C probable signal peptide probable 1 TMH" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1R7" FT /db_xref="InterPro:IPR000454" FT /db_xref="InterPro:IPR002379" FT /db_xref="InterPro:IPR005953" FT /db_xref="InterPro:IPR020537" FT /db_xref="UniProtKB/Swiss-Prot:A1K1R7" FT /protein_id="CAL92772.1" FT /translation="MENVLGFVALAAGLIIGLGAIGACIGIGIMGSKYLEASARQPELM FT NALQTKMFLLAGLIDAAFLIGVGIAMMFAFANPFQL" FT CDS 173279..173752 FT /transl_table=11 FT /gene="atpF" FT /locus_tag="azo0155" FT /product="probable ATP synthase B chain" FT /function="F0F1-type ATP synthase subunit b" FT /note="Probable ATP synthase B chain. Homology to atpF of FT E. coli of 43% (sprot|ATPF_ECOLI) Key component of the FT F-type ATPases (EC 3.6.3.14). The ATPase has 2 FT components,CF(1) - the catalytic core - and CF(0) - the FT membrane proton channel. CF(1) has five subunits: alpha, FT beta,gamma, delta, epsilon. CF(0) has three main subunits: FT a, b and c. Pfam: ATP synthase B/B' CF(0) no signal peptide FT 1 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1R8" FT /db_xref="InterPro:IPR002146" FT /db_xref="InterPro:IPR005864" FT /db_xref="UniProtKB/Swiss-Prot:A1K1R8" FT /protein_id="CAL92773.1" FT /translation="MNLNATLIAQLVVFFILAWFTMKFVWPPIVKALDERAKKIADGLA FT AADKAKADLALAEKKVVEELRKARESAGDVRASAEKQASQLVDEARAEASRIIAQAREA FT AEAEAGAAAQRAKEALRDQVAHLAVAGAEKILRREINAQVHAELLANLKQELQ" FT CDS 173756..174289 FT /transl_table=11 FT /gene="atpH" FT /locus_tag="azo0156" FT /product="putative ATP synthase delta chain" FT /function="F0F1-type ATP synthase delta subunit FT (mitochondrial oligomycin sensitivity protein)" FT /note="putive ATP synthase delta chain. Homology to atpH of FT E. coli of 32% (sprot|ATPD_ECOLI). Key component of the FT F-type ATPases (EC 3.6.3.14). The ATPase has 2 FT components,CF(1) - the catalytic core - and CF(0) - the FT membrane proton channel. CF(1) has five subunits: alpha, FT beta,gamma, delta, epsilon. CF(0) has three main subunits: FT a, b and c. Subunit delta seems to be part of the stalk FT that links CF(0) to CF(1). It either transmits FT conformational changes from CF(0) into CF(1) or is FT implicated in proton conduction. InterPro: ATP synthase FT delta (OSCP) subunit (IPR000711) Pfam: ATP synthase delta FT (OSCP) subunit no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1R9" FT /db_xref="InterPro:IPR000711" FT /db_xref="UniProtKB/Swiss-Prot:A1K1R9" FT /protein_id="CAL92774.1" FT /translation="MAENVTIARPYADAAFELARGAGALGPWSEALDRLAAVAADSSMR FT ACINDPKLSADQLNTLVQEVGGNLTAEQQNFVRVLVDNERLQVLPEIRDLFVALKNEHE FT GVLEAEIASAFPLDDAALAALKADLEARFQARLNVTVSIDPELIGGVRIAVGDEVIDAS FT VRGKLANMAAALKN" FT CDS 174303..175841 FT /transl_table=11 FT /gene="atpA" FT /locus_tag="azo0157" FT /product="ATP synthase alpha chain" FT /function="F0F1-type ATP synthase alpha subunit" FT /note="ATP synthase alpha chain. Homology to atpA of E. FT coli of 70% (sprot|ATPA_ECOLI). Key component of the F-type FT ATPases (EC 3.6.3.14). The ATPase has 2 components,CF(1) - FT the catalytic core - and CF(0) - the membrane proton FT channel. CF(1) has five subunits: alpha, beta,gamma, delta, FT epsilon. CF(0) has three main subunits: a, b and c. FT Produces ATP from ADP in the presence of a proton gradient FT across the membrane. The alpha chain is a regulatory FT subunit. Pfam: ATP syntahse alpha/beta family,beta barrel FT domain; ATP synthase alpha/beta chain, C terminal domain; FT ATP synthase alpha/beta chain, nucleotide binding domain no FT signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1S0" FT /db_xref="InterPro:IPR000194" FT /db_xref="InterPro:IPR000793" FT /db_xref="InterPro:IPR004100" FT /db_xref="InterPro:IPR005294" FT /db_xref="InterPro:IPR018118" FT /db_xref="InterPro:IPR020003" FT /db_xref="InterPro:IPR023366" FT /db_xref="UniProtKB/Swiss-Prot:A1K1S0" FT /protein_id="CAL92775.1" FT /translation="MQLNPSEISDLIKSRIQNLQLAATSRNEGTVVSVTDGITRIHGLT FT DVMQGEMLEFPGNTFGLALNLERDSVGAVVLGEYEHITEGDTVKATGRILEVPVGPELI FT GRVVNALGQPIDGKGPINAKLTDKIEKVAPGVIARQSVSQPVQTGLKSVDSMVPIGRGQ FT RELIIGDRQTGKTAVAVDAIINQKGQNMFCVYVAIGQKASTIANVVRKLEENGAMEYTI FT VVAATASESAAMQYLSAYAGCTMGEYFRDRGQDALIVYDDLTKQAWAYRQVSLLLRRPP FT GREAYPGDVFYLHSRLLERAARVNADYVEKFTNGEVKGKTGSLTALPVIETQAGDVSAF FT VPTNVISITDGQIFLETDLFNAGIRPAINAGISVSRVGGAAQTKVVKKLSGGIRTDLAQ FT YRELAAFAQFASDLDDATRKQLERGRRVTELMKQPQYAPLSVAEMAITLYAVNNGYFDD FT VEVARVLAFESGLQQFVKAKAPELVAKITDTKELDADGEKTLVAAIAEFKKSWA" FT CDS 175863..176732 FT /transl_table=11 FT /gene="atpG" FT /locus_tag="azo0158" FT /product="probable ATP synthase gamma chain" FT /function="F0F1-type ATP synthase gamma subunit" FT /note="Probable ATP synthase gamma chain. Homology to atpG FT of E. coli of 58% (sprot|ATPG_ECOLI) Key component of the FT F-type ATPases (EC 3.6.3.14). The ATPase has 2 FT components,CF(1) - the catalytic core - and CF(0) - the FT membrane proton channel. CF(1) has five subunits: alpha, FT beta,gamma, delta, epsilon. CF(0) has three main subunits: FT a, b and c. PRODUCES ATP FROM ADP IN THE PRESENCE OF A FT PROTON GRADIENT ACROSS THE MEMBRANE. THE GAMMA CHAIN IS FT BELIEVED TO BE IMPORTANT IN REGULATING ATPASE ACTIVITY AND FT THE FLOW OF PROTONS THROUGH THE CF(0) COMPLEX. InterPro: FT ATP synthase gamma subunit(IPR000131) Pfam: ATP synthase no FT TMHs no signal peptide" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1S1" FT /db_xref="InterPro:IPR000131" FT /db_xref="InterPro:IPR023632" FT /db_xref="InterPro:IPR023633" FT /db_xref="UniProtKB/Swiss-Prot:A1K1S1" FT /protein_id="CAL92776.1" FT /translation="MASGKEIRTKIKSVQNTRKITKAMEMVAASKMRKAQDRMRAARPY FT ADKIRRLAANLSQANVTDYKHPFLVRKDQVKRVGLILVTTDKGLCGGLNTNVQRVAVNA FT MKEWEAAGATEIRACCIGNKGFGFMQRIGAKVVSHVTQLGDTPHLEKLIGPVKVMLDAF FT QNGELDAVYVAYTRFINTMKQEPQLEQLLPLTGEKLGTPDNSWDYLYEPDPQVVIDELL FT VRYVEALVYQAVAENMASEQSARMVAMKAASDNAKNVIGELQLVYNKTRQAAITKELSE FT IVGGAAAV" FT CDS 176757..178157 FT /transl_table=11 FT /gene="atpD" FT /locus_tag="azo0159" FT /product="ATP synthase beta chain" FT /function="F0F1-type ATP synthase beta subunit" FT /note="ATP synthase beta chain. Key component of the F-type FT ATPases (EC 3.6.3.14). The ATPase has 2 components,CF(1) - FT the catalytic core - and CF(0) - the membrane proton FT channel. CF(1) has five subunits: alpha, beta,gamma, delta, FT epsilon. CF(0) has three main subunits: a, b and c. FT Produces ATP from ADP in the presence of a proton gradient FT across the membrane. The beta chain is the catalytic FT subunit. InterPro: ATP synthase alpha and beta subunit FT central region(IPR000194); ATP synthase alpha and beta FT subunit, N-terminal (IPR004100); ATP synthase alpha and FT beta subunit, C-terminal (IPR000793); AAA ATPase FT superfamily (IPR003593) Pfam: ATP synthase alph/beta FT family, beta-berrel domain; ATP synthase alph/beta FT family,nucleotid binding domain; ATP synthase alpha/beta FT chain, C terminal domain no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1S2" FT /db_xref="InterPro:IPR000194" FT /db_xref="InterPro:IPR000793" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR004100" FT /db_xref="InterPro:IPR005722" FT /db_xref="InterPro:IPR018118" FT /db_xref="InterPro:IPR020003" FT /db_xref="InterPro:IPR024034" FT /db_xref="UniProtKB/Swiss-Prot:A1K1S2" FT /protein_id="CAL92777.1" FT /translation="MSNGTIVQCIGAVVDIQFPRDSMPKVYDALKLEDAADSFAEAGLT FT FEVQQQLGDGVVRTIALGSSDGLRRGMKVSNTGKPISVPVGHGTLGRIMDVLGRPIDEA FT GPVETDELRAIHQKAPKFDELSPSVELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTV FT NMMELINNIAKQHSGLSVFAGVGERTREGNDFYHEMKDSNVLDKVAMVFGQMNEPPGNR FT LRVALTGLTMAERFRDEGRDILFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEM FT GRLQERITSTKVGSITSIQAVYVPADDLTDPSPATTFLHLDSTVVLSRDIAALGIYPAV FT DPLDSTSRQLDPLVVGEEHYSVARAVQQTLQKYKELRDIIAILGMDELSPDDKLAVARA FT RKIQRFLSQPFHVAEVFTGSPGKYVSLKDTIAGFKAIVNGEYDHLPEQAFYMVGGIEEV FT LEKAKKLQ" FT CDS 178210..178635 FT /transl_table=11 FT /gene="atpC" FT /locus_tag="azo0160" FT /product="probable ATP synthase epsilon chain" FT /function="F0F1-type ATP synthase epsilon subunit FT (mitochondrial delta subunit)" FT /note="Probable ATP synthase epsilon chain. Key component FT of the F-type ATPases (EC 3.6.3.14). The ATPase has 2 FT components, CF(1) - the catalytic core - and CF(0) - the FT membrane proton channel. CF(1) has five subunits: FT alpha,beta, gamma, delta, epsilon. CF(0) has three main FT subunits: a, b and c. InterPro: ATP synthase Delta/Epsilon FT chain (IPR001469) Pfam: ATP synthase, Dleta/Epsilon chain FT no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1S3" FT /db_xref="InterPro:IPR001469" FT /db_xref="InterPro:IPR020546" FT /db_xref="InterPro:IPR020547" FT /db_xref="UniProtKB/Swiss-Prot:A1K1S3" FT /protein_id="CAL92778.1" FT /translation="MAMTVHVDIVSAEEQIFSGLAEFVALPGEAGELGILPGHMPLMTR FT IKPGAVRVKVQNQAEEEVVFVAGGLLEVQPGLVTVLADTAIRGKDLDEAKALEAKRKAE FT EALANQSSQLDYAKAQAELAEAIAQIAAIQRLKKGIH" FT CDS complement(178705..179283) FT /transl_table=11 FT /locus_tag="azo0161" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to rsc0460 FT of R. solanacearum of 39% (trembl|Q8Y276(SRS) Pfam: DUF1243 FT This family consists of a number of hypothetical bacterial FT proteins of around 200 residues in length. The function of FT this family is unknown. no signal peptide no TMHs" FT /db_xref="GOA:A1K1S4" FT /db_xref="InterPro:IPR003033" FT /db_xref="UniProtKB/TrEMBL:A1K1S4" FT /protein_id="CAL92779.1" FT /translation="MIEQAVLATINHLLAQSGWARTRLVPHAGRTAHLDLAPVHVGFSV FT ANDGYLAQWAHEGEQPDVRLRVAATELLPDLVARGPAGVMQRVHLEGNAEFADALGFVF FT RNLRWDAEEDLSRVVGDILAHRAVTTARALVAGQQRAAANAAANVAEFLTAEERLLLGR FT PALGGFTAEIVDIRDQLGRLDKRITKLGG" FT CDS complement(179327..180064) FT /transl_table=11 FT /gene="ubiE1" FT /locus_tag="azo0162" FT /product="ubiquinone/menaquinone biosynthesis FT methyltransferase" FT /function="Methylase involved in ubiquinone/menaquinone FT biosynthesis" FT /EC_number="2.1.1.-" FT /note="Ubiquinone/menaquinone biosynthesis FT methyltransferase ubiE (EC 2.1.1.-). Methyltransferase FT required for the conversion of dimethylmenaquinone (DMKH2) FT to menaquinone (MKH2) and the conversion of FT 2-polyprenyl-6-methoxy-14-benzoquinol (DDMQH2) to FT 2-polyprenyl-3-methyl-6-methoxy-14-benzoquinol (DMQH2) (By FT similarity). InterPro: ubiE/COQ5 methyltransferase FT hemK_rel_arch: methylase putative" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1S5" FT /db_xref="InterPro:IPR004033" FT /db_xref="InterPro:IPR023576" FT /db_xref="UniProtKB/TrEMBL:A1K1S5" FT /protein_id="CAL92780.1" FT /translation="MNDKTTHFGFETVAENQKQRRVAEVFSSVASRYDVMNDLMSFGLH FT RLWKAFTIQVSGVRSGDRVLDVAGGTADLSLAFARKVGPTGQVWLTDINHAMLSRGRDR FT VLDHGFALPVAQCNAERLPFPDDWFDCVTVAFGLRNMTHKDVALAEMRRVLRPGGRLLV FT LEFSKVWKPLAPLYDLYSFKLLPWMGDKVAKDADSYRYLAESIRMHPGQDELRDMMEQA FT GLARVDYFNLSAGVVALHRGYKT" FT CDS complement(180072..180494) FT /transl_table=11 FT /locus_tag="azo0163" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to rs04443 FT of R. solanacearum of 69% (trembl|Q8Y279). Pfam: FT PF06155,Protein of unknown function (DUF971) Interpro: FT IPR010376; This family consists of several short bacterial FT proteins and one sequence (Q8RZ62) from Oryza sativa. The FT function of this family is unknown. No Signal Peptide. No FT TMH present." FT /db_xref="InterPro:IPR010376" FT /db_xref="UniProtKB/TrEMBL:A1K1S6" FT /protein_id="CAL92781.1" FT /translation="MAGLDKDTPLPTDITLHRQSRVLEIGFEDGRSFRLPFEFLRVYSP FT SAEVRGHGPGQETLQQGKRDVDITGLEPVGNYAIKPVFSDGHDSGLYSWDYLYELGLQH FT DELWQQYLDRLAAAGGSREAGAVPPAAPKSGCGHHH" FT CDS 180644..181354 FT /transl_table=11 FT /gene="phoB" FT /locus_tag="azo0164" FT /product="phosphate regulon transcriptional regulatory FT protein" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="Phosphate regulon transcriptional regulatory FT protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1S7" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011879" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K1S7" FT /protein_id="CAL92782.1" FT /translation="MPANILLVEDEPAIQELIAANLSRAGHHVVRAADAEAAQRLVRDA FT LPDLVLLDWMLPGMSGIDFARRLRAEERTREIPIIMLTARGEEQDKVAGLETGADDYIT FT KPFSPRELVARIKAVLRRRAPQATEDAVELGGLRLDPATHRVTAGERALSLGPTEFRLL FT HFLMTHAERVHSRAQLLDQVWGDHVFVEERTVDVHIRRLRCALEPSAHDALIQTVRGSG FT YRFSAQVDVTSATR" FT CDS 181446..182717 FT /transl_table=11 FT /gene="phoR" FT /locus_tag="azo0165" FT /product="phosphate regulon sensor protein" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.13.1" FT /note="Phosphate regulon sensor protein, 3 Signal P FT reporting signal peptide TMHMM reporting 1 transmembrane FT helices. MEMBER OF THE TWO-COMPONENT REGULATORY SYSTEM FT PHOR/PHOB INVOLVED IN THE PHOSPHATE REGULON GENES FT EXPRESSION. PHOR MAY FUNCTION AS A MEMBRANE-ASSOCIATED FT PROTEIN KINASE THAT PHOSPHORYLATES PHOB IN RESPONSE TO FT ENVIRONMENTAL SIGNALS." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1S8" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="InterPro:IPR014310" FT /db_xref="InterPro:IPR021766" FT /db_xref="UniProtKB/TrEMBL:A1K1S8" FT /protein_id="CAL92783.1" FT /translation="MAGLAALVGGSLAALLAALVGLLAAGWYHLVNLYRLVQWTREPVG FT TPLPRAAGTWGKVFADMSRRSRLAYDMRERLAATLDRFRDASQAMPDGVMYLAESDTIE FT WMNLKAEQHFGLDHTRDIGAPVTNLVRQPAFVQYLHGGHYEESLVLPSTRPGGLTLQVQ FT VIPFGDGQKMVLSRDISQLERLETMRQDFVANVSHELRTPLTVVGGFLETLIDGAGDFE FT PDDVQRYLRLALEQSNRMRHLIEDLLTLSALETGAPAPAEERVGVATLVRDVYAEAEAL FT SSGRHQLSLVLDTDAVLLGSHKELRSAFANLCSNAVRYTPDGGRIEVGWRQDDAGGEFW FT VRDDGIGIDAQHIPRLTERFYRVDRGRSRETGGTGLGLAIVKHILTRHQAELHVVSTPG FT AGSRFSVRFPRARLMQPKAAALRS" FT CDS complement(182683..184287) FT /transl_table=11 FT /locus_tag="azo0166" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ebA3023 FT of Azoarcus sp. EbN1 of 61% (trembl:Q5P4D4). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K1S9" FT /protein_id="CAL92784.1" FT /translation="MDYRNAAECLNLLHRLHASNVDETHAALSTVVFGMLDALPPPNQH FT LEVLEAARPMIARVQAEMSRRYTAQPLPPDSLENEILLRVVTLWRNLARSYARIVRHDA FT RDGTLDDQRALLFQRRMHYAGQGVVEYFRAHRAVPAGQWAEAHECFAAAEEADLAQIRV FT ADSLNEVWKAQSTLEAYVAVLLVDLANPFGRTERELAWICRWAQRFAPYCALGTPESQK FT PTLYGVDLGADHGLRPLGLLPASPRLRRFDGSTLAGQIRAVLAQFKQGLKPASLGLGED FT CTVEAGNRLLLSLYRPWGLASAGRRFPRRGSRGQVELTGDWLAIGFHVDGKVFTQPRTY FT GVASSLNSDMNLLTFGERAPQADDPARREALRQHEAEQLGFVCEQWEILDQSVGGFRLQ FT QRPRAERLEHHQLVGVRPQDGDRFLLGHVSWLMYRADGLLEAGVHVLPGVPSLVAARPV FT SLHSGRSPFHQAFLLPATPALKTGPSLVLPSRWYHPSAVIEIHVEGKSSQVRLEQLVLR FT GANFDQVSFEALPPSVA" FT CDS complement(184317..184733) FT /transl_table=11 FT /locus_tag="azo0167" FT /product="conserved hypothetical protein" FT /note="55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad FT (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a FT hydrophobic amino acid) was identified as being highly FT conserved in a variety of organisms." FT /db_xref="GOA:A1K1T0" FT /db_xref="InterPro:IPR001310" FT /db_xref="InterPro:IPR011146" FT /db_xref="InterPro:IPR011151" FT /db_xref="UniProtKB/TrEMBL:A1K1T0" FT /protein_id="CAL92785.1" FT /translation="MQVDCPLCQIDRAKLVWQDERCSVIRVDDAAHPGFCRVVWRDHVA FT EMTDLAAADRRHLMDVVFATEAALRQLMQPAKINLASFGNMVPHLHWHVIPRFADDRHF FT PESVWGPAQREGVAHPGPDTAVLARAVQAALDAR" FT CDS complement(184801..185625) FT /transl_table=11 FT /locus_tag="azo0168" FT /product="conserved hypothetical glutamine FT amidotransferases class-II (Gn-AT),YafJ-type" FT /function="COG: Predicted glutamine amidotransferase" FT /note="Conserved hypothetical glutamine amidotransferases FT class-II (Gn-AT), YafJ-type. Homology to ebA3026 of FT Azoarcus sp. EbN1 of 75% (gnl|keqq|eba:ebA3026(KEGG)). FT Pfam: Glutamine amidotransferases class-II. YafJ is a FT glutamine amidotransferase-like protein of unknown function FT found in prokaryotes, eukaryotes and archaea. YafJ has an FT Ntn hydrolase" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1T1" FT /db_xref="InterPro:IPR000583" FT /db_xref="InterPro:IPR017932" FT /db_xref="UniProtKB/TrEMBL:A1K1T1" FT /protein_id="CAL92786.1" FT /translation="MCQLLGMNCNVPTDICFSFTGFRARGGLTDHHRDGWGIAFFEGKG FT VRLFLDPCASADSAVAELVRQYPIRSLNVIAHIRKATQGEIRLENTHPFQRELWGRYWI FT FAHNGNLLNYAPALSGRFQPVGGTDSETAFCHILDELARRFGDRPPPAPALHACLAELA FT TAIGRHGEFNFLLSDGERLFAHCSSRLAYVLRQAPFALAHLADEDLAVDFSEVTTPNDR FT VAVIATIPLTDNETWHRMPSGTLMSFRHGVPDELGMLPTVAAPPCATPIRSA" FT CDS complement(185689..186207) FT /transl_table=11 FT /locus_tag="azo0169" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT bll7463 of B. japonicum of 30% (tremble:Q89DH6). No domains FT predicted. No TMHs. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR022061" FT /db_xref="UniProtKB/TrEMBL:A1K1T2" FT /protein_id="CAL92787.1" FT /translation="MQRRLSILAGALAALVAASTLAEPPADMPRRKPGLWEMKTTLVEL FT GGLTQMLQMCVGPNTDDILYQRGGKQGGCEQQTWRREGERSTFSAVCRIEGSLANLRGS FT FTGDFTTRYSGELYSTYNPPLQGMASMTMRQDSRWLGECQPGQKPGDIVRQGVGGIDLD FT AMMKGMQRR" FT CDS complement(186300..187760) FT /transl_table=11 FT /gene="gatB" FT /locus_tag="azo0170" FT /product="glutamyl-tRNA(GLN) amidotransferase subunit B" FT /function="Asp-tRNAAsn/Glu-tRNAGln amidotransferase B FT subunit (PET112 homolog)" FT /EC_number="6.3.5.-" FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase FT subunit B (EC 6.3.5.-) (Asp/Glu-ADT subunit B). Allows the FT formation of correctly charged Asn-tRNA(Asn) or FT Gln-tRNA(Gln) through the transamidation of misacylated FT Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack FT either or both of asparaginyl-tRNA or glutaminyl-tRNA FT synthetases. The reaction takes place in the presence of FT glutamine and ATP through an activated FT phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1T3" FT /db_xref="InterPro:IPR003789" FT /db_xref="InterPro:IPR004413" FT /db_xref="InterPro:IPR006075" FT /db_xref="InterPro:IPR017958" FT /db_xref="InterPro:IPR017959" FT /db_xref="InterPro:IPR018027" FT /db_xref="InterPro:IPR023168" FT /db_xref="UniProtKB/Swiss-Prot:A1K1T3" FT /protein_id="CAL92788.1" FT /translation="MSRSDWEVVIGLEVHAQLNTASKIFSGASTAFGAEPNVQASAVDI FT ALPGVLPVLNRGAVERAIRFGLAIGATVAPTSVFARKNYFYPDLPKGYQISQFELPVVQ FT GGTITIRVGEGENAYEKTVNLTRAHLEEDAGKSLHEDFHGMSGIDLNRAGTPLLEIVSE FT PDMRSSAEAVAYARTLHALVRWIDICDGNMQEGSFRCDANVSVRKKGAEKFGTRREIKN FT LNSFRFLQQAIDYEVQWQIDTIEDGGTIQQATVLFDPDTGETRMMRSKEDAHDYRYFPD FT PDLLPLVISPEWKARVQGEMPELPEAMKARFIEQLGLSAYDATTLTASKEVATYYQATV FT DAAGAALAKPCANWVMGDLAARLNKAELDIAVSPVSPAQLAGLVARIADNTISNAIAKK FT VFEALWNGEGASADEIIDKQGLKQVTDSGAIEAMIDEVLAANQKSVEEFRAGKDKAFNA FT LVGQVMKASKGKASPAQVNELLKKKLAG" FT CDS complement(187818..188330) FT /transl_table=11 FT /locus_tag="azo0171" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT an orf of Dechloromonas aromatica of 41% FT (gi|46141061|ref|ZP_00152875.2|(NBCI ENTREZ)). No domains FT predicted. Signal P reporting signal peptide present. NO FT TMH present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K1T4" FT /protein_id="CAL92789.1" FT /translation="MARFALRLAGRIAAAEFALWLAACATPPAGTEPATRQEAEEMEEA FT PTAARGRLKPMPIRPLTVQADCTFRDEAGYAASTRLDVSASQVRGFAANVEVPRRGSCH FT FDLADFRQVPAETHVELRARDGCTVRMWEQGDQVTVAFTQCANRCSKGTFEYVWPILVD FT RPSGQCN" FT CDS complement(188336..189799) FT /transl_table=11 FT /gene="gatA" FT /locus_tag="azo0172" FT /product="glutamyl-tRNA(GLN) amidotransferase subunit A" FT /function="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A FT subunit and related amidases" FT /EC_number="6.3.5.-" FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A (EC FT 6.3.5.-) (Glu-ADT subunit A). Furnishes a means for FT formation of correctly charged Gln-tRNA(Gln) through the FT transamidation of misacylated Glu- tRNA(Gln) in organisms FT which lack glutaminyl-tRNA synthetase. The reaction takes FT place in the presence of glutamine and ATP through an FT activated gamma-phospho-Glu-tRNA(Gln) (By similarity). FT InterPro: Glutamyl-tRNA(Gln) amidotransferase A subunit FT gatA: glutamyl-tRNA(Gln) amidotransferase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1T5" FT /db_xref="InterPro:IPR000120" FT /db_xref="InterPro:IPR004412" FT /db_xref="InterPro:IPR020556" FT /db_xref="InterPro:IPR023631" FT /db_xref="UniProtKB/Swiss-Prot:A1K1T5" FT /protein_id="CAL92790.1" FT /translation="MINASVSELRRALDTRQVSSVELATLFLDRIAERNPALNAFITID FT REGALAAARAADARIAAGTAGPLTGIPLAHKDLFCTEGVLTTCGSKMLADFVSPYDAHV FT VSRLKDAGAVSLGKTNMDEFAMGSSNESSHYGAVRNPWDTTRIPGGSSGGSAAAVAARL FT VPLATGSDTGGSVRQPASHTGVTGIKPTYGVVSRYGMIAYASSLDQGGAFGASAEDCAL FT LLTAMAGFDPRDSTCLDRPAEDYAAALAPTAGGKPLAGLRIGLPREFFAEGMADDVRAA FT VDAALDQYRALGAVTVEVSLPNAKLAVPAYYVIAPAEASSNLSRFDGVRYGHRAAEYGD FT LNDMYCKSRAEGFGAEVKRRILVGTYVLSHGYYDAYYLQAQKLRRLIAQDFQAAFAQCD FT VIAGPTSPTTAWAIGEKADDPVQMYLSDIYTIAVNLAGLPGLSHPCGFGAGRLPVGLQL FT IGNYFGESRLLATAHQYQQASDWHLQRPE" FT CDS complement(189852..190139) FT /transl_table=11 FT /gene="gatC" FT /locus_tag="azo0173" FT /product="glutamyl-tRNA(GLN) amidotransferase subunit C" FT /function="Asp-tRNAAsn/Glu-tRNAGln amidotransferase C FT subunit" FT /EC_number="6.3.5.-" FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C (EC FT 6.3.5.-) (Glu-ADT subunit C). Allows the formation of FT correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through FT the transamidation of misacylated Asp- tRNA(Asn) or FT Glu-tRNA(Gln) in organisms which lack either or both of FT asparaginyl-tRNA or glutaminyl-tRNA synthetases. The FT reaction takes place in the presence of glutamine and ATP FT through an activated phospho-Asp-tRNA(Asn) or FT phospho-Glu-tRNA(Gln)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1T6" FT /db_xref="InterPro:IPR003837" FT /db_xref="UniProtKB/Swiss-Prot:A1K1T6" FT /protein_id="CAL92791.1" FT /translation="MSLSNEQVGRIARLARLAISEGEIDAVRAKLDGIFGLIEQMQAVD FT TAGVEPMSHPQELATRLRDDVVTETDRRSAFQSVAPQTEAGLYLVPKVIE" FT CDS 190256..191299 FT /transl_table=11 FT /gene="mreB" FT /locus_tag="azo0174" FT /product="rod shape-determining protein MreB" FT /function="Actin-like ATPase involved in cell FT morphogenesis" FT /note="Rod shape-determining protein mreB. INVOLVED IN FT FORMATION OF THE ROD SHAPE OF THE CELL. MAY ACT AS A FT NEGATIVE REGULATOR OF FTSI. InterPro: Cell shape FT determining protein MreB/Mrl mreB: cell shape determining FT protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1T7" FT /db_xref="InterPro:IPR001023" FT /db_xref="InterPro:IPR004753" FT /db_xref="UniProtKB/TrEMBL:A1K1T7" FT /protein_id="CAL92792.1" FT /translation="MFGFLRSYFSNDLAIDLGTANTLIYVRGKGIVLDEPSVVAIRTEG FT GPNAKRTIQAVGHAAKQMLGKTPGNITAIRPMKDGVIADFVVTEQMIKQFIKKVHDSRL FT LSPSPRIIICVPCGSTQVERRAIRDAALAAGASQVYLIEEPMAAAIGAGLPVSDATGSM FT VVDIGGGTTEVGVISLGGMVYAGSVRVGGDKFDDAIVNYIRRNYGMLIGDTTAENIKKN FT IGSAFPGSEVREMEVKGRNLAEGIPRSFTISSNEILEALTEPLNQIVSAVKIALEQTPP FT ELGADIADRGMVLTGGGALLRDLDRLLMEETGLPVIVAEEPLTCVARGCGLALDKMDKL FT GSIFTSD" FT CDS 191345..192262 FT /transl_table=11 FT /gene="mreC" FT /locus_tag="azo0175" FT /product="rod shape-determining protein" FT /function="Cell shape-determining protein" FT /note="Rod shape-determining protein mreC. Involved in FT formation of the rod shape of the cell. May also contribute FT to regulation of formation of penicillin-binding proteins." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1T8" FT /db_xref="InterPro:IPR007221" FT /db_xref="UniProtKB/TrEMBL:A1K1T8" FT /protein_id="CAL92793.1" FT /translation="MSLAGHQPPPIFRRGLAPLARLFLLVSVCLAMLVADLRFRYLEVF FT RQGLSVVTYPLQMAAATPADFVRNASRYFATLIEVQLENADLRRQQLGAAERLLRYEQL FT EQEYKQLRGLMQMAERVQVKSVAAEILYNAPDPFARKVILDRGAQQGVEAGLAVVDSDG FT VIGQVTRVYPIQSEVTLLTDRNQAIPVRVLRNGLRGVLFGTGQGRIELRFVIAGADIQV FT GDMLVTSGLDGVFLPGLPVAEVLSVDREAEAFARIVCKPVAGVERSSQVLVLGRAEPPP FT PIPVDPAPAPPAEGRRARRGDGGH" FT CDS 192266..192787 FT /transl_table=11 FT /gene="mreD" FT /locus_tag="azo0176" FT /product="rod shape-determining protein" FT /function="Cell shape-determining protein" FT /note="Rod shape-determining protein mreD. Involved in FT formation of the rod shape of the cell. May also contribute FT to regulation of formation of penicillin-binding proteins." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1T9" FT /db_xref="InterPro:IPR007227" FT /db_xref="UniProtKB/TrEMBL:A1K1T9" FT /protein_id="CAL92794.1" FT /translation="MQPTNRSSRILLPVRLGFIYFSLMVALALAYVPTGRFPGVPDWVA FT LVLAFWCIREPLRIGMGAGFLFGVLVDIGQGAAMGQHALAYVVLAYLATGLARRVMWFP FT PLLQALHVLPMLLASQMLMVAVRLIAGAEFPGWAYFLSSFTAVALWVPLNYLLLLPQYQ FT PVDRDDNRPI" FT CDS 192797..194686 FT /transl_table=11 FT /gene="pbpA" FT /locus_tag="azo0177" FT /product="penicillin-binding protein" FT /function="Cell division protein FtsI/penicillin-binding FT protein 2" FT /note="Penicillin-binding protein 2 (PBP-2). CELL WALL FT FORMATION; PBP2 IS RESPONSIBLE FOR THE DETERMINATION OF THE FT ROD SHAPE OF THE CELL. ITS SYNTHESIZE CROSS- LINKED FT PEPTIDOGLYCAN FROM THE LIPID INTERMEDIATES. InterPro: FT Penicillin binding protein transpeptidase domain" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1U0" FT /db_xref="InterPro:IPR001460" FT /db_xref="InterPro:IPR005311" FT /db_xref="InterPro:IPR012338" FT /db_xref="InterPro:IPR017790" FT /db_xref="UniProtKB/TrEMBL:A1K1U0" FT /protein_id="CAL92795.1" FT /translation="MTEFRTPAQEKSRFRNRVVVAALFILACFALLAMRFYYLQVTRHA FT YFHTRAEDNRIALLPVVPNRGTITDRNGVVLARNYAAYTLEITPSKAGDLEATIDGLAE FT VVTIEPRDRRRFRKVLEESRNFESVPIRTRLTDEEVARFTAQRYRFPGVEVQARLFRDY FT PEGEVASHVIGYIGRINDRDVERIEERGQTANYRGSEYIGKAGLEQSYEAELHGQTGFE FT QVEVNAGGRAVRRLSRTAAMVGNNLELTLDIELQKIAENAFGNRRGALVAIEPGTGGVL FT ALVSKPTFDPNLFVEGISAQDWKQLNDSPDHPLLNRAIFSAYPPGSTFKPFMALGALTT FT GKRTPGYVMADPGYFVSGGHRFMDDKVGGHGMVDLHKSIVVSCNTFYYQLANDMGIDGI FT ADFMRPLGFGSRTGIDVPGEAEGVLPSPAWKKKRFRRPEQQRWFGGETISVGIGQGYNA FT YTPLQLANALATVVSDGKVFRPHIVRHVVDARDNRRVIEPEPLRQLNFKPEHLALVRRA FT MVDVNKSGTGARAFAGAPYEVGGKTGTAQVFSLKGAKYVEGRVSERLRDHSWFIAYAPA FT DNPKIALAVLVENGGFGAQSAAPIARQVIDYHLLGKRPNQPAGEDADAPESTE" FT CDS 194683..195819 FT /transl_table=11 FT /gene="rodA" FT /locus_tag="azo0178" FT /product="rod shape-determining protein" FT /function="Bacterial cell division membrane protein" FT /note="Rod shape-determining protein rodA. THIS IS ONE OF FT THE PROTEINS RESPONSIBLE FOR THE ROD SHAPE OF THE CELL. IT FT IS REQUIRED FOR THE EXPRESSION OF THE ENZYMATIC ACTIVITY OF FT PBP2 WHICH IS THOUGHT TO SYNTHESIZE PEPTIDOGLYCAN IN THE FT STEP OF INITIATION OF CELL ELONGATION." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1U1" FT /db_xref="InterPro:IPR001182" FT /db_xref="InterPro:IPR011923" FT /db_xref="InterPro:IPR018365" FT /db_xref="UniProtKB/TrEMBL:A1K1U1" FT /protein_id="CAL92796.1" FT /translation="MSDHRFNPLLLLRAVLRPIDPVLMLVLMMLLGYAFVLMASASPDR FT LDSQLVNTTVALLAMWVAAWLPSQRLLSFALPLYALGVVLLVAVELFGEVSKGAQRWLH FT VGVTRIQPSELMKIAMPLMLAWYFQQREAKIGLREFIVAGLLLVVPVGLILIQPDLGTS FT LLVTAAGFYVIFFAGLSWKLIVPVGLVGIIGIGSIVAFGDTLCQPDVDWFGLREYQKQR FT VCTLLDPTRDPLGKGFHIIQSTIAIGSGGVVGKGWMDGTQTHLAFLPERHTDFIFAVLA FT EEFGLVGTLVLLVTYLALLARSFQIATQAPTLATKLLGGAMAMIFFTYAFVNMGMVSGI FT LPVVGVPLPFISYGGTALVTLCLGVGILMGIRRGRPAS" FT CDS 195800..196840 FT /transl_table=11 FT /gene="rlpA" FT /locus_tag="azo0179" FT /product="lipoprotein" FT /function="Members of this family are quite diverse, and if FT catalytic this family may contain several different FT functions" FT /note="RlpA-like protein precursor." FT /note="Function unclear" FT /db_xref="InterPro:IPR007730" FT /db_xref="InterPro:IPR009009" FT /db_xref="InterPro:IPR012997" FT /db_xref="UniProtKB/TrEMBL:A1K1U2" FT /protein_id="CAL92797.1" FT /translation="MAVPRPDLPAVMMMKSVPAAFTLRARPLTLVVASCCAAWLAGCST FT APVQESSAPGARPSPPPPVASPAPAPAKRGGAYYKDDGPGDNPPDNLDAVPDAQPRLEP FT LHRFANRPYNVFGQDYVPATRLAPFRERGLASWYGRRFHGGNTSSGEPYDMYAMTAAHP FT TLPIPSYARVTNVATGRSVVVRINDRGPFHKGRIMDLSYTAAYRLGYVNGGSAEVEVEQ FT ILPDEVPMEAMSPPVPPLPGRRVPPALAAAAPDPAPATAAPASPSAGAVAFFLQLGAFA FT SRDNAEGFRATVQRDLAAFAQRVDLLAEGGRFRLHAGPYASENEARVAAERIAATLKLK FT PFVVAR" FT CDS 196966..198096 FT /transl_table=11 FT /gene="dacC" FT /locus_tag="azo0180" FT /product="probable D-alanyl-D-alanine carboxypeptidase" FT /function="D-alanyl-D-alanine carboxypeptidase" FT /EC_number="3.4.16.4" FT /note="Probable D-alanyl-D-alanine carboxypeptidase. FT Homology to dacD of E. coli of 41% (sprot|DACD_ECOLI) FT Removes C-terminal D-alanyl residues from sugar-peptide FT cell wall precursors. Pfam: D-alanyl-D-alanine FT carboxypeptidase signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1U3" FT /db_xref="InterPro:IPR001967" FT /db_xref="InterPro:IPR012338" FT /db_xref="InterPro:IPR012907" FT /db_xref="InterPro:IPR015956" FT /db_xref="InterPro:IPR018044" FT /db_xref="UniProtKB/TrEMBL:A1K1U3" FT /protein_id="CAL92798.1" FT /translation="MRFVFALLLSLFSLLAAAQSIPAPALAAKAWVLVDHNTGQVLAAN FT DPDARIEPASLTKLMTAYLTFSALKAGTIALDQPVPVSERAWRQEGSRMFIEPQKPVTV FT QELIRGVIVQSGNDACVALAELIAGTEEAFAAMMNREAQRLGMSNTHFTNSTGLPDPQL FT YTTAKDLALLASAIIRDFPDYYASLYSLKEYRYNNITQPNRNRLLWMDSTVDGMKTGHT FT SSAGYCLISSALRGPRRLVSVVLGAESDTVRAQESLKLLNFGFQFFDTVKLYSADQALS FT QFRVWKGQANEVAAGFTSDFVISLPKGQADKITATLESRQPVLAPLQKGQEIGTLKLSL FT DGKPLGEYPVVALQDVPVAGFFGRLWDALVLWIKSL" FT CDS 198136..198993 FT /transl_table=11 FT /gene="daaA" FT /locus_tag="azo0181" FT /product="D-alanine transaminase" FT /function="Branched-chain amino acid FT aminotransferase/4-amino-4-deoxychorismate lyase" FT /EC_number="2.6.1.21" FT /note="D-alanine aminotransferase (EC 2.6.1.21) FT (D-aspartate aminotransferase) (D-amino acid FT aminotransferase) (D-amino acid transaminase) (DAAT). Acts FT on the D-isomers of alanine Leucine aspartate glutamate FT aminobutyrate norvaline and asparagine (By similarity). FT InterPro: Aminotransferases class-IV" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1U4" FT /db_xref="InterPro:IPR001544" FT /db_xref="UniProtKB/TrEMBL:A1K1U4" FT /protein_id="CAL92799.1" FT /translation="MNLCYLDGRYLPLDEARVSPMDRGFLFGDGAYEVVPVYSRRPFRL FT AEHLGRLARTLAAMRLPNPHSDEEWADRVTTLVAGNPWEDQSIYLQVTRGADAVRNHAF FT PKDVRPTVFMLSEPLLTPAPELLASGVAAVSAADFRWLRCDLKSVSLLANCLLRQYGFD FT QGCAETVLFRDGFLTEGSASNIFVVRDGRLLAPPKSHLMLAGITYDVVLELAAAHGLPL FT EVREILDAEVRSADELWMTSSTKEVLAITRLDGRPVGSGAPGPLGRQMYAWYQEFKNTV FT MRSG" FT CDS 198986..199267 FT /transl_table=11 FT /locus_tag="azo0182" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical protein. Homology to RSC0326 FT of Ralstonia solanacearum of 53% (tremble:Q8Y2K9) Has FT PF04359;Protein of unknown function (DUF493);This family FT includes several proteins of uncharacterised function. FT InterPro;IPR007454 No Signal Peptdie or TMH present." FT /db_xref="InterPro:IPR007454" FT /db_xref="UniProtKB/TrEMBL:A1K1U5" FT /protein_id="CAL92800.1" FT /translation="MADQTPQPRQTLLEFPCDFPIKIMGARVDGFAQAVIEVVLRHAPD FT FDPAGAEMRPSSKGNYLAVTCTFRAISQQQVDALYMELTSHPMVKVVL" FT CDS 199264..199947 FT /transl_table=11 FT /gene="lipB" FT /locus_tag="azo0183" FT /product="LipB protein" FT /function="Lipoate-protein ligase B" FT /note="Lipoate-protein ligase B (EC 6.-.-.-) (Lipoate FT biosynthesis protein B). Involved in the attachment of FT lipoyl groups to proteins by creating an amide linkage that FT joins the free carboxyl group of lipoic acid to the FT epsilon-amino group of a specific lysine residue in FT lipoylated proteins (By similarity). InterPro: FT Lipoate-protein ligase B lipB: lipoate-protein ligase B" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1U6" FT /db_xref="InterPro:IPR000544" FT /db_xref="InterPro:IPR004143" FT /db_xref="InterPro:IPR020605" FT /db_xref="UniProtKB/Swiss-Prot:A1K1U6" FT /protein_id="CAL92801.1" FT /translation="MTAAAVLAGHEGPAAAVSVPLLVKRLGRVDYAPAWEAMQHFTASR FT GEDTADEIWLLEHPPVYTLGQAGRPEHLLRNDAGIPLVKIDRGGQITYHGPGQLVAYLL FT LDLRRRHLKVRELVALMEQAVIDCLAEYGLHAERKDGAPGVYIDGAKIAALGLRVRNGC FT SYHGLALNVDADLAPFGWINPCGYEGLQTIRLKDFGVGDDVAAVGERLLQHLLRLLPPG FT VVPSR" FT CDS 199989..200936 FT /transl_table=11 FT /gene="lipA" FT /locus_tag="azo0184" FT /product="lipoic acid synthetase" FT /function="Lipoate synthase" FT /note="Lipoic acid synthetase (Lip-syn) . Synthesis of FT alpha-(+)-lipoic acid. It may be involved in the sulfur FT insertion chemistry in lipoate biosynthesis (By FT similarity). InterPro: Lipoate synthase lipA: lipoic acid FT synthetase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1U7" FT /db_xref="InterPro:IPR003698" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/Swiss-Prot:A1K1U7" FT /protein_id="CAL92802.1" FT /translation="MDNPARKQRGAEKTARIPIKIVPAERLKKPDWIRIRLGAGAEAER FT FNEIKQTLREHKLHTVCEEASCPNIHECFGKGTATFMIMGDICTRRCPFCDVGHGRPEP FT LNPNEPTDLARTIAAMRLNYVVITSVDRDDLRDGGAQHFVDCIRETRAASPSTTIEVLV FT PDFRGRMEIALEIFNQAPPDVMNHNMETVPRLYKQARPGADYAYSLRLLKEFKAGHPDV FT LTKSGLMVGLGETDDEILDVMRDLRAHDVDMLTIGQYLQPSGGHLPVLRYVHPDTFKMF FT ETEALRMGFRNAACGPMVRSSYWADQQAHGAGVV" FT CDS 201005..201682 FT /transl_table=11 FT /locus_tag="azo0185" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT PP1518 of P. putida of 54% (trembl|Q88MQ2(SRS) No domains FT predicted Signal P reporting signal peptide present. No TMH FT reported present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K1U8" FT /protein_id="CAL92803.1" FT /translation="MKFLQKTLILFALCSSAWAASLVDLSDAEVGGGLKEALTQGAGHA FT VEVLGRKDGFLSNPKVKIPLPGVLKQAEPLLRMSGRGEDLDQLVTSMNRAAEAAVPGAK FT NLLVGAVKQMSVADAKKILTGGDDSVTRYFRDKTEAQLTRMFLPTVKQNTDKLALAGQY FT NALVGQAAGLGLVKSEDAQIENYVTRKALDGLYLMIAEEERAIRKDPVGAVGGLAKKVF FT GAL" FT CDS 201756..203750 FT /transl_table=11 FT /gene="rep" FT /locus_tag="azo0186" FT /product="ATP-dependent DNA helicase" FT /function="Superfamily I DNA and RNA helicases" FT /EC_number="3.6.1.-" FT /note="ATP-dependent DNA helicase rep (EC 3.6.1.-). REP FT HELICASE IS A SINGLE-STRANDED DNA-DEPENDENT ATPASE INVOLVED FT IN DNA REPLICATION; IT CAN INITIATE UNWINDING AT A NICK IN FT THE DNA. IT BINDS TO THE SINGLE-STRANDED DNA AND ACTS IN A FT PROGRESSIVE FASHION ALONG THE DNA IN THE 3 TO 5 DIRECTION FT (BY SIMILARITY). InterPro: UvrD/REP helicase." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1U9" FT /db_xref="InterPro:IPR000212" FT /db_xref="InterPro:IPR013986" FT /db_xref="InterPro:IPR014016" FT /db_xref="InterPro:IPR014017" FT /db_xref="UniProtKB/TrEMBL:A1K1U9" FT /protein_id="CAL92804.1" FT /translation="MSALLNPPQREAIHYLNGPCLVLAGAGSGKTRVITHKIAHLINEC FT GLSPTNVGAITFTNKAAKEMQERVAHLMGGRAPGGLTVCTFHALGVRIIRQEALHCGLK FT PQFSILDASDAVQIVADVAGDQDKGIAKQMQWQISSWKNAMISPAEAAQLADNELSAAA FT AKAFADYERTLRAYQAVDFDDLISLPVRLFEENDEVRERWQNRLRYLLVDEYQDTNRAQ FT YRLLRQLAGVRGAFTAVGDDDQAIYAWRGADVENLKLLQRDYPKLRVIKLEQNYRSSRR FT ILEAANVLIANNEKLFDKRLWSEHGPGEQIAVTSCRDADHEAEWVAMKISAHKFENRTR FT FKDYAILYRGNHQARIIEQQLRNQRIPYVMSGGQSFFEKPEIKDLIAYLRLLMNEDDDL FT AFIRAITMPRRGIGPSTIEALGHYAGGRHISLFAASFEEGVALHLGARQLEAVQQFTAF FT INRIQHRARREPAAQVLEDLLAAIRYEAWLFEHFDSREAESKWSNVRDFVGWLGRKGEE FT DGKNLIELTQTIALISMLDKEDADFDGVQLATLHASKGLEFPHVFLVGVEEGLLPHQSS FT IDEDKVEEERRLMYVGITRAQRSLNITWCERRKAGKEFRPCEISRFIAEMGGDLNIGDR FT KRNAPVSREEGRARLANLKAMFERRDEGS" FT CDS complement(203837..204298) FT /transl_table=11 FT /locus_tag="azo0187" FT /product="conserved hypothetical cytochrome c5" FT /function="Cytochrome c5" FT /note="Conserved hypothetical cytochrome c5. Homology to FT vc0168 of V. cloreae of 38% (tremble: Q9KVH8). This basic FT c-type monoheme cytochrome has an unusally low redox FT potential compaired with mitochaondrial cytochrome C. It is FT reactive with cytochrome c oxidase but not with reductase. FT Pfam: Cytrochrome C probable signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1V0" FT /db_xref="InterPro:IPR002323" FT /db_xref="InterPro:IPR003088" FT /db_xref="InterPro:IPR009056" FT /db_xref="UniProtKB/TrEMBL:A1K1V0" FT /protein_id="CAL92805.1" FT /translation="MSEHRASRRAQRPLRPALSLAMAAAIVLAGCGKDNGKVDPEVTAS FT LIQPVAKVELKVVTVAPGSRTGEQIYKSICSSCHDAGMLGAPKTGDSGAWGPRLAQGFD FT GLTKSAIAGKNAMPPRGGGSDLTDTEVKRAVAFLANKAGAGYTEPPVAQ" FT tRNA 204448..204524 FT /gene="tRNA-Arg" FT /locus_tag="azo_tRNA_0001" FT /product="transfer RNA-Arg" FT /anticodon=(pos:204482..204484,aa:Arg) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT rRNA 204806..206339 FT /locus_tag="azo_rrn1" FT tRNA 206413..206489 FT /gene="tRNA-Ile" FT /locus_tag="azo_tRNA_0002" FT /product="transfer RNA-Ile" FT /anticodon=(pos:206447..206449,aa:Ile) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA 206517..206592 FT /gene="tRNA-Ala" FT /locus_tag="azo_tRNA_0003" FT /product="transfer RNA-Ala" FT /anticodon=(pos:206550..206552,aa:Ala) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT rRNA 206857..209743 FT /locus_tag="azo_rrn2" FT CDS complement(210014..210739) FT /transl_table=11 FT /gene="yueD" FT /locus_tag="azo0189" FT /product="putative benzil reductase" FT /note="Putative benzil reductase. Homology to yueD of B. FT cereus of 32% (trembl|Q8RJ14). Belongs to the short-chain FT dehydrogenases/reductases (SDR) family. Transform benzil to FT (S)-benzion. Interpro: short-chain dehydrogenase/reductase FT SDR (IPR002198) Pfam: short chain dehydrogenase (PF00106) FT no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1V1" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K1V1" FT /protein_id="CAL92806.1" FT /translation="MKAIVTGHSRGLGEALAIGLLERGLEVLGVSRHSHAEMAARFPRF FT SESRVDLADVAAVCRFIESPVFQAFGNAREPVILINNAAMLQPVGRSGSLAAAEIQQAV FT NVNVLGPLLLTNAVVQCADPDLSRRILHISSGAARTAYSGWSIYGATKAALDHHARCVS FT EEGRAHVRICSVAPGVLDTRMQADVRQLETGQFPARERFISLKDSGQLVPPAEAAAKLL FT AFLFAPAFGDTPTADVRTF" FT CDS 210838..211857 FT /transl_table=11 FT /locus_tag="azo0190" FT /product="conserved hypothetical protein" FT /function="Nucleoid-associated protein" FT /note="Conserved hypothetical protein. Homology to an orf FT of R. oxalatica of 31% (trembl|Q84ES1). Pfam: 37-kD FT nucleoid-associaed bacterial protein The Escherichia coli FT nucleoid contains DNA in a condensed but functional form. FT Analysis of proteins released from isolated spermidine FT nucleoids after treatment with DNase I reveals significant FT amounts of two proteins not previously detected in FT wild-type Escherichia coli. Partial amino-terminal FT sequencing has identified them as the products of rdgC and FT yejK. no signal peptide no TMHs" FT /db_xref="GOA:A1K1V2" FT /db_xref="InterPro:IPR007358" FT /db_xref="UniProtKB/TrEMBL:A1K1V2" FT /protein_id="CAL92807.1" FT /translation="MSTDQIITQLLIHRLVKAGDAAARIVQRDRLNSPDAAAIGLVTQL FT ISTFTQRSGKCHGTFEDDEEEFPVARLLREFSGDDERGFIDLGAHLSDHLRNCADLVGL FT DNGGAFLLARVREQAVDWLWIALVPETVTTAVDKDLNLHEHTHLDVHATQAVARIDLTG FT WRRGDERCVAFLSGRGPAAQCFRRFLGCKDVVVALQETRKLVQALTDFADSERLDPPVR FT DEMMERAHRYLDDLGEAGAPVELDALASELWPSAPARLGTTLQTPARALAPAFVPNRRA FT LKPLVRLSASADQWRVEFERAGLRSGAVSYDVVSDTLVLSNLPPYLKQMLIDDGDASS" FT CDS 211933..212409 FT /transl_table=11 FT /locus_tag="azo0191" FT /product="conserved hypothetical protein" FT /function="Acyl dehydratase" FT /note="Entry name TREMBL:Q988L8 Prim. accession # Q988L8 FT InterPro IPR002539; MaoC_dehydratas. Identities = 63/131 FT (48%) Pfam PF01575; MaoC_dehydratas; 1. Number of predicted FT TMHs: 0 Probable MaoC protein (Phenylacetic acid FT degradation protein paaZ)." FT /db_xref="GOA:A1K1V3" FT /db_xref="InterPro:IPR002539" FT /db_xref="UniProtKB/TrEMBL:A1K1V3" FT /protein_id="CAL92808.1" FT /translation="MTETPPQRGAPLYLDDLQVGLRFGSGTHPIDAQQITAFADSFDPQ FT PFHLDHEAAQDSLFGGLAASGWHTAAITMRLLVEGGLPIAGGIIGAGAEVTWPRPTRPG FT DVLQVDSEVLEITPSRSKPDRGIVTLRSETRNQRGEILQVLTSRLVVPRRPLNG" FT CDS 212402..213313 FT /transl_table=11 FT /gene="apbA1" FT /locus_tag="azo0192" FT /product="2-dehydropantoate 2-reductase" FT /function="Ketopantoate reductase" FT /EC_number="1.1.1.169" FT /note="Catalyzes the NADPH-dependent reduction of FT ketopantoate into pantoic acid (By similarity). apbA_panE: FT 2-dehydropantoate 2-reductase" FT /note="Function unclear" FT /db_xref="GOA:A1K1V4" FT /db_xref="InterPro:IPR003710" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR013332" FT /db_xref="InterPro:IPR013752" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K1V4" FT /protein_id="CAL92809.1" FT /translation="MDSSRQREAFSTDVLQAAPYPVAIIGAGALGLSLASRLIRSGPVA FT LVASNADAAQRLRAGVRVGAVVERFDGFAAPRLPRADWVVVVVKAGGTRDALRSALAMR FT PRGVLSLQNGLLDLEPAGTGTCVAQGVTTMGAFRTDEGVMPVSDGETLMPQGFEPLAAL FT FQQAGLPARIEVAMQAARLAKLLVNVVLNPLTAVFRVRTGELLAAPYMNHVEALVAEAW FT PVLRAAGLMLEFDEARAKVWSVVRSTADNRTSMLQDVLAGRRTEREAITGAFLRLADGN FT GAAVPTHRALHTLLGQIDADRC" FT CDS complement(213319..213780) FT /transl_table=11 FT /gene="trxC1" FT /locus_tag="azo0193" FT /product="probable protein-disulfide reductase" FT /function="Thiol-disulfide isomerase and thioredoxins" FT /EC_number="1.8.1.8" FT /note="Probable protein-disulfide reductase. Homology with FT trxC of E. coli of 45% (AAB88587). Participates in various FT redox reactions through the reversible oxidation of the FT active center dithiol to a disulfide. InterPro: Thioredoxin FT Tigrfam: redox_disulf_1: redox-active disulfide Pfam: FT Thioredoxin no TMHs no signal peptide" FT /note="Family membership" FT /db_xref="GOA:A1K1V5" FT /db_xref="InterPro:IPR005746" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR013766" FT /db_xref="InterPro:IPR017937" FT /db_xref="UniProtKB/TrEMBL:A1K1V5" FT /protein_id="CAL92810.1" FT /translation="MHAEEAHMNPSIHLVCPHCDAVNRLPAERMAEHPACGQCHRPLFI FT GEPLALDGARFERHLTRNDLPVLIDFWAPWCGPCRMMAPAFAAAAAQLEPQLRLAKVNT FT EAEPALAQRFGIRSVPTIALFQGGREVTRQAGAMNTEQLVRWVRGQLGR" FT CDS 213935..214333 FT /transl_table=11 FT /gene="hvrA1" FT /locus_tag="azo0194" FT /product="putative trans-acting regulatory protein HvrA" FT /note="Putative trans-acting regulatory protein. Homology FT to hvrA of R. capsulatus of 27% (sprot|HVRA_RHOCA). The FT histone-like nucleoid-structuring (H-NS) protein belongs to FT a family of bacterial proteins that play a role in the FT formation of nucleoid structure and affect gene expression FT under certain conditions (e.g. light). Interpro: Histone FT -like nucleotide-structuring protein H-Ns (IPR001801) Pfam: FT H-NS histone family no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1V6" FT /db_xref="InterPro:IPR001801" FT /db_xref="UniProtKB/TrEMBL:A1K1V6" FT /protein_id="CAL92811.1" FT /translation="MEIDLKSYTLPQLRALREQTARAIDRLQRSQRETLLRRLSALARA FT EGLTLAELAEDAAAMKGAERPRKHPRTTPRQPLPVKYRHPSNRALAWSGRGRQPHWVAA FT WLANGGSMDALATAAEKLAPRIPRGISG" FT CDS 214378..214626 FT /transl_table=11 FT /locus_tag="azo0195" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT CV3728 of Chromobacterium violaceum of 57% (tremble:Q7NRQ2) FT No domains predicted. No TMHs signal peptide present" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR011690" FT /db_xref="UniProtKB/TrEMBL:A1K1V7" FT /protein_id="CAL92812.1" FT /translation="MNKIIVAALISTFALSAHAEGPTCNASAAEKKLVGAAKTSFLKKC FT EKDAAASCEAAAAEKKLAGAAKGSFTKKCVKDAVGAP" FT CDS complement(214688..215722) FT /transl_table=11 FT /locus_tag="azo0196" FT /product="consrved hypothetical transcription factor" FT /function="predicted transcriptional regulator" FT /note="Conserved hypothetical transcription factor," FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR013196" FT /db_xref="UniProtKB/TrEMBL:A1K1V8" FT /protein_id="CAL92813.1" FT /translation="MSQTERLYQIVRMLEDARQPVPLARFLETLEISRASFKRDLDYLR FT DRLGAPIVWRRGSAGDPEGYVLEGERGEAGKRFGIHGMWFNPSEIHALLMMQQLATAME FT PGLLAGQVDGLMTRIGLMLGSANDDPAEVGRRVRILHSANRRATPAAFDTVAQATMKRR FT RLALRYYTRSRNAESDRVVSPQQLLHYRENWYLLGYCHQARALRLFALDAIRSASVRPG FT SAREVGERRLKEATGAAFGIFAGAPRERAELRFSAEVAPWVASEIWHPAQTSAPQTDGS FT LLLGVPYADSRELVMEILRYGADVEVLAPPALRAAVADRLRRAAAQYEGADATSGPDTT FT QPRD" FT CDS 215834..216118 FT /transl_table=11 FT /locus_tag="azo0197" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. Signal peptide. 1 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K1V9" FT /protein_id="CAL92814.1" FT /translation="MKSSRPVLPPPDDVLANRRRLVFSLALLSLPLAFQFAEAAIVPVP FT EAMRIVLAFSVWATLVVLELSAGALVWALCRALRRLRQGGMPAWRAYPR" FT CDS complement(216106..217965) FT /transl_table=11 FT /gene="pabB" FT /locus_tag="azo0198" FT /product="para-aminobenzoate synthase component I / FT 4-amino-4-deoxycho" FT /function="Anthranilate/para-aminobenzoate synthases FT component I" FT /EC_number="4.1.3.-" FT /note="Para-aminobenzoate synthase component I (EC 4.1.3.-) FT (ADC synthase). CATALYZES THE BIOSYNTHESIS OF FT 4-AMINO-4-DEOXYCHORISMATE (ADC) FROM CHORISMATE AND FT GLUTAMINE. InterPro: Anthranilate synthase component I and FT chorismate binding enzyme pabB: para-aminobenzoate synthase FT component I" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1W0" FT /db_xref="InterPro:IPR001544" FT /db_xref="InterPro:IPR005801" FT /db_xref="InterPro:IPR015890" FT /db_xref="InterPro:IPR019999" FT /db_xref="UniProtKB/TrEMBL:A1K1W0" FT /protein_id="CAL92815.1" FT /translation="MESFALLDDSQAAVETPASRLYTGFCGEIRCTDPDRLEADWVRVE FT TELAAGRHAVIVADYEWGVRLAGVTTAKPGGMLRVLLYATLQRLDGAGVAHWLAQQEGR FT DEPDAAGVAEWQASLERPAFDAAIEAIHAAIRAGETYQINFSYRLGGRAYGSPLALYRR FT LRAAQPVPFGALIRLPAPTGDGDGDGGYLLSCSPELFLRHRDGVLEARPMKGTAARRGD FT PAADAQAAGDLAADPKNRAENLMIVDLLRNDLGRIAETGSVQVPALFAVEPYATVLQMT FT STVSARLAARHAFPAVLRALFPCGSITGAPKHRSMRLIDTLEDRPRGTYTGAVGWMDAP FT RAGHRCGDFCLSVAIRTLAVGAERDGRRTAELGVGAGIVIDSRAADEYAECQLKARFVT FT ALDPGFQLIETMRAGPAGSGGAPGIPLLARHLARLAASAAALGFRYDDAQVRAALARHL FT ATLADGMHRVRLLLHKDGRIDVSGGPLPALPPGPVRVLLADAPIDGRDYLLRHKTTRRA FT SYDAAIRAAEAAGAFDTLFFNHAGALTEGGRSNVFVRMDGQWLTPPVEAGVLPGVMRAA FT LLDDPAWQAHEAALTRADLARAEAVVLCNALRGVLHVRFDQRG" FT CDS 218051..219196 FT /transl_table=11 FT /gene="sbcD" FT /locus_tag="azo0199" FT /product="exonuclease SbcD, putative" FT /function="DNA repair exonuclease" FT /EC_number="3.1.11.-" FT /note="Exonuclease sbcD homolog. Probably involved in FT genetic recombination. InterPro: DNA repair exonuclease. FT sbcd: exonuclease SbcD." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1W1" FT /db_xref="InterPro:IPR004593" FT /db_xref="InterPro:IPR024654" FT /db_xref="UniProtKB/TrEMBL:A1K1W1" FT /protein_id="CAL92816.1" FT /translation="MRFLHTADWHLGRVYHGVSLLEDQAHVLRDFVRLAGETRPDAILI FT AGDVYDRSVPPADAVRLLDETLTELVVGLAIPVVLIAGNHDGPDRLAFGASLLGRAGLT FT VRGPVDASVAPVRLRDAHGEVAIYPLPYAEPALVRSAFGEEALADHHAALGAQLRAIRA FT AHAAGTRSVVVAHAFVLGGSESESERPLSVGGSGAVGAELFAGFDYVALGHLHRPQQAG FT GEHIHYSGSLLKYSFAEAGHAKSVNLVEMDAAGRCTVERVALAPRRDLRIVEGTLADII FT AGAAADPGRDDYLLARLSDSGALLDAMGKLRTAYPNALAIERPLHAGDGPGRAAADHRR FT IRIEDLFASFYAETAGRPLEAEAIATVQRIVGAIEQEARHA" FT CDS 219193..222264 FT /transl_table=11 FT /gene="sbcC" FT /locus_tag="azo0200" FT /product="exonuclease SbcC, putative" FT /function="ATPase involved in DNA repair" FT /EC_number="3.1.11.-" FT /note="Nuclease sbcCD subunit C. SbcCD cleaves DNA hairpin FT structures. These structures can inhibit DNA replication FT and are intermediates in certain DNA recombination FT reactions. The complex acts as a 3->5 double strand FT exonuclease that can open hairpins. It also has a 5 FT single-strand endonuclease activity (By similarity). sbcc: FT exonuclease SbcC." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1W2" FT /db_xref="UniProtKB/TrEMBL:A1K1W2" FT /protein_id="CAL92817.1" FT /translation="MKPLKLSLQAFGPFAGREEIDFTLLPEGALFLISGPTGAGKTSIL FT DGITYALYGDTSGGERSAREMRSHHADAALLTEVEFEFALGARRYRVRRVPEQERAAQR FT ATKSGDGLVKVLARAELHRLDDDGVTWLPLAHKTTEVTSELTALLGCQAEQFRQVVLLP FT QGQFRKLLTASSGEREKILETLFGTAAYKRLQDALKQEAQALQKAADETRLRRDTLLQQ FT AAAESVEGLRGQAEALDAELTRLAGEESAARSADTAAQAALQQGRALAAQFAEQHAAGA FT ALAAVEARAGEIAALRLREAAARRALQVVPADEACAGAGRQLALARQRAAEAGERVATA FT AAAMQQARAGLEADKARAPQRDTAQRELLQLEALAAQVEQLAAAERELAARRSQAAAAE FT QALAQARHAAAEAEQGRAALVVRVDQLAPRAAEAEALALRVAQAEQREADAQRLAARRK FT ALAEATAAEAQARQAMDAARAALDAARDAQQALDGLWREAQAAILARHLHDGAPCPVCG FT SAVHPGPATHAGELPSESALREAAARSREAEQGFEARRAAFDRAAQARTAVEAEVGALS FT GALRTAGDDGVQADMLVETAADLRQRLAVARQAGAELTAARDRLQALEQAQRNALAAQE FT QAATAAQSAASALHGAERVVEARREAVPAALRPAGALAAALKTARSALDTLLAASQQAQ FT AAHAGAEAALAAAHAQRDTLAQAETEQAAALEQAQAVFARALAAAAFDDEAGYRAARLA FT AADIDHLAASLRQHDEDAAAARERLARADQAVAGRTPPQLAELETSAQAARAAIDAVLA FT RSADLRGALEKTRHTLALLDELAARNADIEARYRITGELAAVANGDNGRNLTFQRYVLA FT ALLDDVLRAASLRLKAMSRGRYLLQRREEVADARRAAGLDLEVLDDYTGRARPVATLSG FT GEGFMASLSLALGLSDVVQAYAGGVQLDTLFIDEGFGSLDPESLDMAMRTLIDLQRQGR FT MVGVISHVEEMKQQIDVAIEVVQGVRGSRVRVRG" FT CDS complement(222387..223202) FT /transl_table=11 FT /locus_tag="azo0201" FT /product="probable aryl-ester hydrolase" FT /function="predicted hydrolases or acyltransferases FT (alpha/beta hydrolase superfamily)" FT /EC_number="3.1.1.2" FT /note="Arylesterase (EC 3.1.1.2) (Aryl-ester hydrolase) FT pir:C75401:39% identity, 52% similarity:hydrolase-related FT protein - Deinococcus radiodurans . IS A BIFUNCTIONAL FT ENZYME CAPABLE OF BOTH ESTER HYDROLYSIS AND HALOGENATION. FT ACTS ON MANY PHENOLIC ESTERS. Pfam: PF00561: alpha/beta FT hydrolase fold (74-271) InterPro: IPR000073: Alpha/beta FT hydrolase fold IPR000379: Esterase/lipase/thioesterase FT Pfam:Zn binding dehydrogenase mobB: molybdopterin-guanine FT dinucleotid" FT /note="Family membership" FT /db_xref="GOA:A1K1W3" FT /db_xref="InterPro:IPR000073" FT /db_xref="UniProtKB/TrEMBL:A1K1W3" FT /protein_id="CAL92818.1" FT /translation="MSDLNAPSILTHDHSVAHPEGRIFARSWTPAGGAASSEPPIVLLH FT DSLGCVELWRDFPAELSAATGRRVIAYDRLGFGKSDAREGRPAALDFIGEEARRYFPAV FT REQLGLDRFIVFGHSVGGCMAIHCAAEFGADCVALITESAQTFPEDLTLTNIAAAKAQF FT ADEAQLQRLQKYHGDKARWVLEAWTDNWLDPAFAAWTLAPVLPRVSCPVLAIHGQQDEY FT GTTRHPQMIGELSSGPARVEILADTHHVAHREQPAVVLELVAGFVRALV" FT CDS 223457..224176 FT /transl_table=11 FT /locus_tag="azo0202" FT /product="conserved hypothetical protein" FT /function="Ferredoxin" FT /note="Conserved hypothetical protein. Homology only to FT r01975 of S. meliloti of 31% (trembl|Q92P21). no signal FT peptide no TMHs" FT /db_xref="GOA:A1K1W4" FT /db_xref="InterPro:IPR017896" FT /db_xref="UniProtKB/TrEMBL:A1K1W4" FT /protein_id="CAL92819.1" FT /translation="MPPTSDPAAPDFAALDDAGLNLHAVFDFASLPADVRAQLQRDVCT FT PHACRQLILIGNAGRALWAALRASGFSAADPIDAFSVRAVAQWFARQLPGHRYTLLYPG FT EAPVGLQALGRLAGWHHATPFKVGILPGWGSWFGYRVALLADTALPPTPPLQVESPCLS FT CAARPCIAACPAEAMAGGDFALDRCAAHRLQPDSDCAYRCAARDACPVGQDHRYEADHL FT RHTYGASLGALERYLRG" FT CDS 224493..225563 FT /transl_table=11 FT /locus_tag="azo0203" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane-bound metal-dependent FT hydrolases" FT /note="TREMBL:Q82XH5: 33% identity, 44% similarity FT InterPro:IPR007404; DUF457. Pfam: PF04307; DUF457 fnt: FT formate/nitrite transporter Non-secretory protein with FT signal peptide probability of 0.391 TMHMM predicted 4 FT transmembrane helices" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007404" FT /db_xref="UniProtKB/TrEMBL:A1K1W5" FT /protein_id="CAL92820.1" FT /translation="MDTVTHALSGALLGRLFSSGRGGLRPAAAIAAGATAAAFPDIDYL FT LGYVSELTYLRGHRGVTHSVLLLPLWGALLAGLFARLARLRDRRGPDWPAFYGLACAGI FT AIHIAGDLITQFGTMILAPLSDRRFGIGTTFIIDLVFTGIILAGLAASAVFRRSRVPAA FT LALVALAGWVGVGWVGRGEAIEAARAYAVTKRIPVVAIDAAPRPASPFNWTAIVFDGER FT YHYAHLNTRRQHALTVREGDNFIRRFSAPYLPVAQAQWAVKPMFGNGGEGELARAVWNA FT GDFAFYRWFAMFPVLDQVDAATPAGPCASFRDLRFETPGRDGTPFRYGLCGTGNGQGWR FT LFERRDDGGLRWVAGG" FT CDS complement(225594..226691) FT /transl_table=11 FT /gene="bmpA" FT /locus_tag="azo0204" FT /product="probable lipoprotein" FT /function="uncharacterized ABC-type transport system FT periplasmic component/surface lipoprotein" FT /note="Description:abc transporter periplasmic binding FT protein.This is a family of basic membrane lipoproteins FT from Borrelia and various putative lipoproteins from other FT bacteria. All of these proteins are outer membrane proteins FT and are thus antigenic in nature when possessed by the FT pathogenic members of the family Probable CD4+ T FT cell-stimulating antigen precursor. TREMBL: Q8XXD8: 64% FT identity, 79% similarity InterPro:IPR003760; Bmp. Pfam: FT PF02608; Bmp Secretory protein with high signal peptide FT probablity (Signal P predicted). No. of transmembrane FT helices: 1 (TMHMM predicted) prok_nadp_idh: isocitrate FT dehydrogenas" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1W6" FT /db_xref="InterPro:IPR003760" FT /db_xref="InterPro:IPR006311" FT /db_xref="UniProtKB/TrEMBL:A1K1W6" FT /protein_id="CAL92821.1" FT /translation="MSTRRTALKWTAALAAAAALPAPLAAFAADPVKVGFVYVGPVGEA FT GWTYAHDLGRRALEAAFPGQVKTTFIERVPEGADAERVIRSLAQDGHQIIFTTSFGYMD FT ATLKVARQFPKVVFQHATGFKTAANMGTYDVRTYEGAYLAGVLAGKMSKSGNLGVVGSH FT PIPEVIRNINAYTIGARSVNPTATTRVIWVNSWFDPGKERQAALTLIAQGADVLMQNTD FT SPAVLQAAQEKGVYAFGWDSDMTAFGPKAQLAASEIDWGVWYKKVVGEVMAGTFDAKRQ FT VWYGLKEGAIDLGHLAASLPADAKKLVAERRQGILDGKRPVFAGPLRNQAGKEVVAAGQ FT ELADKDKLAMNYYVEGVQGAVPGGK" FT CDS complement(226835..228079) FT /transl_table=11 FT /gene="hipO1" FT /locus_tag="azo0205" FT /product="probable hippurate hydrolase" FT /function="Metal-dependent FT amidase/aminoacylase/carboxypeptidase" FT /EC_number="3.5.1.32" FT /note="Hippurate hydrolase (EC 3.5.1.32) (Benzoylglycine FT amidohydrolase) (Hippuricase). TREMBL:Q7VUP2: 43% identity, FT 57% similarity InterPro; IPR002933; Peptidase_M20. FT InterPro; IPR010168; Pept_M20D_amidh. Pfam; PF01546; FT Peptidase_M20; 1. TIGRFAMs; TIGR01891; amidohydrolases FT TIGR00003: copper-ion-binding protein No signal peptide FT (Signal P predicted) No transmembrane helices present" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1W7" FT /db_xref="InterPro:IPR002933" FT /db_xref="InterPro:IPR011650" FT /db_xref="InterPro:IPR017439" FT /db_xref="UniProtKB/TrEMBL:A1K1W7" FT /protein_id="CAL92822.1" FT /translation="MSAAARPSAGGASSPGEDVAQRQEGSSENIADDALAGLLPALVRL FT RHDLHAHPELGFAEHRTAAVVAAELRAIGLAVHEGIGGTGVVGVLRRGSSGASVGLRAD FT MDALPMDECSGVAYASTHAGAHHGCGHDGHTSMLLGAARLLAARDFDGTVNFIFQPAEE FT GLGGARAMVEDGLFERFPCDAVYALHNWPALPLGTAQTRPGPIMAAADRFDIVIRGRGG FT HAAQPHTTPDAILAAGHLVSQLHAIVSRRIDPVESAVLSITRIESGHTHNVLPAEVKLT FT GTVRSFDPAAQDTIEAALHQIADGVALASGTTIAIDYLRYYPATINHAAEAQVALEAAA FT NAGLQVKTAPAPAFTSEDFAFMLQARPGAYLWLGQGRGGDDKPLHHPAYDFNDAALPHG FT VRWLVAVAERQLQRR" FT CDS complement(228076..228660) FT /transl_table=11 FT /locus_tag="azo0206" FT /product="putative AraC-family transcriptional regulator" FT /function="AraC-type DNA-binding domain-containing FT proteins" FT /note="Putative AraC-family transcriptional regulator," FT /note="Family membership" FT /db_xref="GOA:A1K1W8" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR018060" FT /db_xref="UniProtKB/TrEMBL:A1K1W8" FT /protein_id="CAL92823.1" FT /translation="MRRAPGLHVPAVARTAAVHAQGRAARPCKSTFAVAATGHCSAIVG FT GIAPKLFPMETKPLPTCRGARRPPRGIDNALAYIHRHFDEQLSLEELAEIAGLSVCRFA FT TVFRERMGIPPHRYICILRVRHAQALLRSGMPAANVASEAGFYDQSHLSRHFKNICGMT FT PKQYLREAGPLPEGAYIGALRQPAAFAAHAA" FT CDS 228700..229056 FT /transl_table=11 FT /locus_tag="azo0207" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to bb1472 FT of B. bronchiseptica of 46% (trembl|Q7WMC0). Interpro: FT Protein of unknown function DUF861 (IPR008579). Pfam: FT Cupin_3 (former DUF861) (PFO5899). This family consists of FT several proteins which seem to be specific to plants and FT bacteria. The function of this family is unknown. No signal FT peptide. No TMHs" FT /db_xref="InterPro:IPR008579" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR014710" FT /db_xref="UniProtKB/TrEMBL:A1K1W9" FT /protein_id="CAL92824.1" FT /translation="MGIRIIKQSEDLQGLEAQGPVGRPLGEPVAQMCGVDVALAGAGSN FT DCGIWECTPGRFRRQIDNAEVMHILSGACTFTPEGGEPLQIAAGDTLFFPSHTVGVWEI FT SETLRKVYVVFALR" FT CDS complement(229064..229267) FT /transl_table=11 FT /locus_tag="azo0208" FT /product="Hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Hypothetical protein, 45% identity to TrEMBL;Q7U8P5. FT Weak Homology with hits. No domains,repeats, motifs or FT features predicted Present." FT /note="Function unclear" FT /db_xref="UniProtKB/TrEMBL:A1K1X0" FT /protein_id="CAL92825.1" FT /translation="MLRRGLLDNGYLELPILREHAVSVESLPPIHKDPFDRILVAQATV FT EGILLLTRDALVAQYPGPIQLV" FT CDS complement(229633..230862) FT /transl_table=11 FT /gene="agaE" FT /locus_tag="azo0209" FT /product="probable sarcosine oxidase, beta subunit" FT /function="Glycine/D-amino acid oxidases (deaminating)" FT /EC_number="1.5.3.1" FT /note="Sarcosine oxidase,subunit beta counts to the FAD FT dependent oxidoreductases. Similar to trembl|Q88AX8 (49%) FT and to trembl|Q987J9 (43%). Pfam (PF01266): FAD dependent FT oxidoreductase Pfam (PF01494): FAD binding domain Pfam FT (PF00070): Pyridine nucleotide-disulphide oxidoreductase" FT /note="Function unclear" FT /db_xref="GOA:A1K1X1" FT /db_xref="InterPro:IPR006076" FT /db_xref="UniProtKB/TrEMBL:A1K1X1" FT /protein_id="CAL92826.1" FT /translation="MKPVTAPPIAATSETLRADVIVVGGGLVGASAAFFLRKRGLSVIL FT LERGLVGQQASGTNFGNVRRQGRALAQLPLAARARDIWGQLPALLGEDAEFLDSGHLRV FT CYSEEQAEDFARYAVDAKPYGLNLEVMGAAELRRRYGLFGPEVLAGSLSAVDGHANPRL FT AGPAFGRGARRVGATVLEHTEVLRVEREGGDFLVHTQHPAGGEGPRCRAPQLLVATGAW FT GNRIASAFGEPVPIVAHGPQMGVTEPLPYAIGPAIGVTTRNVTEGMYFRQVKRGNIVFG FT GGPKGPAYADRLRAYVEPTNTLNQLQQLRRLAPALGGLQLIRTWSGIEGYLQDSKPVLG FT PSAKVDGLYYAFGFCGEGFAIGPGIGDSIAELIATGQTATPYPDSHIGRFAVAEAAACA FT RKTRQLDQPA" FT CDS complement(230859..232241) FT /transl_table=11 FT /gene="ooxA" FT /locus_tag="azo0210" FT /product="putative opine oxidase subunit A" FT /function="uncharacterized NAD(FAD)-dependent FT dehydrogenases" FT /note="Putative opine oxidase subunit A. Homology to ooxA FT of A. tumefaciens of 37% (sprot|OOXA_AGRT4). OXIDATIVE FT CLEAVAGE OF OCTOPINE INTO L-ARGININE AND PYRUVATE (BY FT SIMILARITY). InterPro: FAD-dependent pyridine FT nucleotide-disulphide oxidoreductase (IPR001327), FT NAD-bining site (IPR000205) Pfam: Pyridine FT nucleotide-disulphide oxidoreductase no signal peptide no FT TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1X2" FT /db_xref="InterPro:IPR000103" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR017224" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K1X2" FT /protein_id="CAL92827.1" FT /translation="MAAPRVIVVGAGPAGVRASEALVEAGLRPVVVDEGRRDGGQIYRR FT QPPNFSRPYATLYGSEAAKAEALHRAFDALRPHIDYRAETLAWNIANGQLHTVCGKRAE FT ALPFDALIVCSGATDRLLPLPGWNRAGCYSLGAAQIALKAQACAIGSRTVFCGTGPLLY FT LVASQYLKAGARIEAVIDTSPQPALNAIGGLLARPALLLRGLGLIATLHRAGVPLLRGA FT TPLAIDGDDESGVSGITVRDASGRERRFDCDAVALGYHLRAETQLADLARCEFRFDDAS FT RQWLPAIDEDGRASSAGIYLAGDGVRLAGADGAETAGRLAALAALHDLGVAPGIARYIS FT EHKILRATLATMERFRRGLAAAFPWPHAQAAALPDEAVVCRCETITAGELRRTAAELGG FT CELNRAKAFSRVGMGRCQGRYCGHAAAEIVAAATGIPVQQVGRLRGQAPVKPLPLDVEV FT VQ" FT CDS complement(232223..232552) FT /transl_table=11 FT /locus_tag="azo0211" FT /product="conserved hypothetical protein" FT /db_xref="GOA:A1K1X3" FT /db_xref="InterPro:IPR001041" FT /db_xref="UniProtKB/TrEMBL:A1K1X3" FT /protein_id="CAL92828.1" FT /translation="MPASTPPRSPRFVRLAETGRRPVGLRVDGRPATALEGDTLLVAVL FT ANGGRLRQSEFGDGARAGFCLMGACQDCWVRGAQGERWRACSTPVEDGMDILTQPQEAT FT WPRRG" FT CDS complement(232564..233067) FT /transl_table=11 FT /gene="prp" FT /locus_tag="azo0212" FT /product="probable proline dehydrogenase transcriptional FT activator" FT /function="Transcriptional regulators" FT /note="Probable proline dehydrogenase transcriptional FT activator. Similar to sprot|PUTR_AGRTU (31% Agrobacterium FT tumefaciens, proline dehydrogenase transcriptional FT activator prp or putR) InterPro: IPR000485 HTH_AsnC_lrp. FT Pfam: PF01037 AsnC family. HTH reporting nucleic acid FT binding motif." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1X4" FT /db_xref="InterPro:IPR000485" FT /db_xref="InterPro:IPR011008" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR019885" FT /db_xref="InterPro:IPR019887" FT /db_xref="InterPro:IPR019888" FT /db_xref="UniProtKB/TrEMBL:A1K1X4" FT /protein_id="CAL92829.1" FT /translation="MTITTAMPKLDRLDLRILCQLQRNGRITNVDLADAVGLSPSPCLI FT RVKRLEQAGYIAGYGAQVKLDKLGEMLTVFTEVTLADHRREDFMRFESAIRNIDEILEC FT HLVSGGYDYLLKFMTQGVNHYQSIIEGLLERSIGIEKYFSYIVIKSPFIKNYYPIERVV FT DTSK" FT CDS complement(233142..234524) FT /transl_table=11 FT /locus_tag="azo0213" FT /product="aminotransferase, class III" FT /function="Adenosylmethionine-8-amino-7-oxononanoate FT aminotransferase" FT /note="Adenosylmethionine-8-amino-7-oxononanoate FT aminotransferase (EC 2.6.1.62) (78-diamino-pelargonic acid FT aminotransferase) (DAPA aminotransferase). bioA: FT adenosylmethionine--8-amino-7-oxononanoate FT aminotransferase" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1X5" FT /db_xref="InterPro:IPR005814" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:A1K1X5" FT /protein_id="CAL92830.1" FT /translation="MTTDALLDLDRKHLIHPVAAWRGHEQRGTTVLASGHDGVWLRDIH FT GKEVLDAFAGLWCVNIGYGHESVVQAAAEQMRKLPYATGYFGFGSEPAIRLAAKLAEIA FT PKSLRHTYLTLGGSEAVDAAIRLITHYYNATGRPQKKHFIAIERGYHGSSSVGSGLTAL FT PAFHRGFDVPLPNQHYIASPYPYRSPVGDDPQAVIAASVAALRAKVAELGADNVAAFFC FT EPVQGSGGVIVPPKGWLKAMREASRELGILFVVDEVITGFGRTGPMFACLAEDVEPDLM FT TMAKGLTSGYVPMGALMISDEVYNGIADGAAPNVLVGHGATYSGHPVSAAVALEVIRLY FT EEGGILAHAQAMEPGFAAGLGEMLDHPLVGDVRHRGLLGAVELVADKASKRAFDPALGL FT ADRLFRSGYQNGLIFRSFGDHILGFAPALCFTEDNFAQLFARLKRTLDEVLDAPDVRRA FT LA" FT CDS complement(235059..235934) FT /transl_table=11 FT /locus_tag="azo0214" FT /product="conserved hypothetical acetyltransferase" FT /function="Histone acetyltransferase HPA2 and related FT acetyltransferases" FT /EC_number="2.3.1.-" FT /note="Conserved hypothetical acetyltransferase. Homology FT to putative acetaltransferase (GNAT family) of P. syringae FT of 42% (trembl|Q88AY8). Pfam: Acetyltransferase (GNAT) FT family no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1X6" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:A1K1X6" FT /protein_id="CAL92831.1" FT /translation="MIGEIALRETSADGVTLRPLEAADLDAAHGLSVAVRWPHRLEDWR FT FVAALGQGLVAVRDGEVVGTALGWHWDNSQAIFGMVIVAPQVQGRRIGQRLMQGLLDSA FT GQRAVMLHATAEGRGLYERLGFVRHGEIRQHQGQARQAPLLMPGAGERLRPLGRGDSDR FT LVELDAQASGMPRGAAIRALLDTAETVVLDRDGEAVGFAVLRRFGRGHAIGPVVAPSLA FT SAKALIAHWSNLCAGKFLRIDVEAGGGLIEWLEEIGLRRVGMVAIMSRGEIPRRGPETG FT LYAILSQALG" FT CDS 236153..237637 FT /transl_table=11 FT /gene="aldH" FT /locus_tag="azo0215" FT /product="putative aldehyde dehydrogenase (NAD+)" FT /function="NAD-dependent aldehyde dehydrogenases" FT /EC_number="1.2.1.3" FT /note="Putative aldehyde dehydrogenase (NAD+) (EC 1.2.1.3). FT Homology to adlH of E. coli of 35% (sprot|DHAL_ECOLI). FT Aldehyde dehydrogenases (EC: 1.2.1.3 and EC: 1.2.1.5) are FT enzymes which oxidize a wide variety of aliphatic and FT aromatic aldehydes using NADP as a cofactor. InterPro: FT Aldehyde dehydrogenase family (IPR002086) Pfam: Aldehyde FT dehydrogenase family no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1X7" FT /db_xref="InterPro:IPR015590" FT /db_xref="InterPro:IPR016160" FT /db_xref="InterPro:IPR016161" FT /db_xref="InterPro:IPR016162" FT /db_xref="InterPro:IPR016163" FT /db_xref="UniProtKB/TrEMBL:A1K1X7" FT /protein_id="CAL92832.1" FT /translation="MPIFDPDQIQVPVGHFIGGRLQTPAGAALEVQRPSDGKVYAALPV FT ADEALVDIAAENAWTAWKESDWARCAPRDRARVLRRWADLVEAEAPRLGVLEALGSTRP FT VRDAIAWDVPFTAEGLRFFAEYADKLGGEVAATRHDHLGMVIAEPYGLIGAITPWNFPL FT VMVSWKVGAALAAGNAVLLKPSELTPFSALRLAELAIQAGVPAGIFNIVQGDGRTTGEA FT ITRHPRVSKMTFTGSTRTGAAIMSACALHGPKPVTLELGGKSPQLVFDDVRDLDKLAAT FT IAGAITGNAGQVCVAGSRLIVQRRVAGALVERIRAIFTGHRPGATWDEDATLPPIISAQ FT QAARIAAIVERAQAAGGRVKCGGRIVDGGYGGAYYLPTLIDGVDTANPAVSEEIFGPVL FT TVQTFDDEEEGFALASHDSYGLAAGVHTSDVGRAMRAVRRIEAGTVWVNRYGRSADFVI FT PTGGYHQSGIGKDLGRQAVEANLRFKSVLMDIGSPQ" FT CDS 237835..238500 FT /transl_table=11 FT /gene="hadL" FT /locus_tag="azo0216" FT /product="probable haloalkanoic acid dehalogenase" FT /function="predicted hydrolase (HAD superfamily)" FT /EC_number="3.8.1.2" FT /note="Probable 2-haloalkanoic acid dehalogenase (EC FT 3.8.1.2) (L-2-haloacid dehalogenase) (Halocarboxylic acid FT halidohydrolase). TREMBL:Q92Y68: 68% identity, 82% FT similarity These proteins catalyze the hydrolytic FT dehalogenation of small L-2-haloalkanoic acids to yield the FT corresponding D-2-hydroxyalkanoic acids [1]. They belong to FT the Haloacid Dehalogenase (HAD) superfamily of FT aspartate-nucleophile hydrolases InterPro:IPR006328; FT HAD_II. IPR006388; HAD_SF_IA_v2. IPR005834; Hydrolase. Pfam FT PF00702; Hydrolase rpiB_lacA_lacB: sugar-phosphate isomer FT No signal peptide No transmembrane helices" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1X8" FT /db_xref="InterPro:IPR006328" FT /db_xref="InterPro:IPR006388" FT /db_xref="InterPro:IPR006439" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:A1K1X8" FT /protein_id="CAL92833.1" FT /translation="MTFRPKYITFDCYGTLIRFRMGDTARAMYADRLPPEQLERFVHDF FT NAYRLDEVMGDWKPYVDILKSALERTCKRHGVKYLEEEGQKYYDLVPTWGPNPDVPEPL FT AVIAKEIPLVILSNAANEQIMTNVEKLGAPFHAVYTAEQARAYKPRLQAFEYMLDQLGC FT GPEDILHVSSSLRYDLMSADDLGIKNKVFVNRGHDPACAAYNYTEIKDIGGLPALVGL" FT CDS 238541..239833 FT /transl_table=11 FT /gene="ordL" FT /locus_tag="azo0217" FT /product="FAD dependent oxidoreductase family protein" FT /function="Glycine/D-amino acid oxidases (deaminating)" FT /note="This family includes various FAD dependent FT oxidoreductases: Glycerol-3-phosphate FT dehydrogenase,Sarcosine oxidase beta subunit, D-alanine FT oxidase, D-aspartate oxidase. Similar to trembl|Q88AY5 FT (61%) and to sprot|ORDL_ECOLI (32%). Pfam (PF01266): FT D-amino acid oxidase ProSite (PS50205): NAD binding site" FT /note="Family membership" FT /db_xref="GOA:A1K1X9" FT /db_xref="InterPro:IPR006076" FT /db_xref="UniProtKB/TrEMBL:A1K1X9" FT /protein_id="CAL92834.1" FT /translation="MKLESYWTDSAPAFAGADTPLPKRADVAIVGGGFTGLSAALACAK FT RGASVVVLEAGALAGEASGRNGGHVNNGLAVDYAALADKVGRDQARAWYHAYDAAVDSV FT ARVVEEEGIACDFARNGKLKLAARPAHFEALARGFEQLKNEVDPDVELVDAAAVRDELA FT SERYCGGILIKKSAQMHMGRFAVGLAEAAQRHGARIHTNTTVTRLERRRSEGVYAHRVH FT TSAGSFDAAQVLVASGATRHGGFGSFGWLRRRIVPVGSFIVVTAPLGAERAAALLPRRR FT TYTTTENIHNYFRLTPDNRLVFGGRARFAISSPQSDLKSGHILQAALVRTFPQLADVGI FT DYCWGGLVDMSRDRLPRAGERDGLFYSLGYSGHGTQMSVHMGGIMAEVMAGNAAANPWR FT DLPWPAIPGHFGPPWFLPAVGLYYRLKDTLV" FT CDS 239850..241457 FT /transl_table=11 FT /gene="dppA" FT /locus_tag="azo0218" FT /product="putative dipeptide transport system, FT periplasmic-binding protein" FT /function="ABC-type dipeptide transport system periplasmic FT component" FT /note="Part of the ABC transporter complex dppABCD involved FT in dipeptide import. Similar to the dipeptide FT periplasmic-binding protein dppA in E.coli. FT DIPEPTIDE-BINDING PROTEIN OF AN OSMOTIC-SHOCKABLE TRANSPORT FT SYSTEM. DPPA IS ALSO REQUIRED FOR PEPTIDE CHEMOTAXIS. FT InterPro: Bacterial extracellular solute-binding protein FT family 5 Signal peptide" FT /note="Specificity unclear" FT /db_xref="GOA:A1K1Y0" FT /db_xref="InterPro:IPR000914" FT /db_xref="InterPro:IPR006311" FT /db_xref="UniProtKB/TrEMBL:A1K1Y0" FT /protein_id="CAL92835.1" FT /translation="MSSSTLTSSLPGVAPATPGLSRRAALGRLLAGGCALPGLGLPGPA FT FASLAAMTAPPPRQGGYLRVAAAAAAITDTLDPARQSNQTDYIRGKMFYNGLTELDAHL FT NPLPALAESFASEDAQEWTFRLRRGVVFHDGKPLTPADVVYSLMRHKDPAVGSKANAIA FT AQIDSVAADGPQAVKVRLKAPNADLPVLMGTFHFHIVADGTTDFRLANGTGPYRCQEFR FT PGVRSIAVRNPNYWKPGRPYVDTIECVGIVDEVARVNALLSGDIDLVSAVNPRSALRIA FT ATPGFTFMTTQSGQYSDLVMRQDRGPGANADFVLALKYLMDRELMMKVIAQGHAMVGND FT QPIDPTHTFYAPGLPQRAYDPERARFHLRKAGMEGARLPIVASPAATYSVEIALVLQHA FT AARAGLNLEVKRMPVDGYWSNHWMKHPLSFGNINPRASADAVFTQFYQSSSAWNATGWK FT NPRFDQLLVAARSELDEHRRRALYADMQALVHDECGSGIPLFIASIDGLSSRVKGLSQI FT PLGGLMGYSFAENVWLEG" FT CDS 241462..242418 FT /transl_table=11 FT /gene="dppB" FT /locus_tag="azo0219" FT /product="putative dipeptide transport system, permease FT protein" FT /function="ABC-type dipeptide/oligopeptide/nickel transport FT systems permease components" FT /note="Part of the ABC transporter complex dppABCD involved FT in dipeptide import. Probably responsible for the FT translocation of the substrate across the membrane. Similar FT to the dipeptide permease protein, DppB in E.coli." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1Y1" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:A1K1Y1" FT /protein_id="CAL92836.1" FT /translation="MNALVLRLIAARIGLALVSLLLVSAVVFAITALLPGDAAEEKLGL FT EATAETLAALRHEMGLDRPALVRYGDWLAGMAGGDPGRSVVSGAPVGQLIASRLPNSLL FT LAGLTAAISVPLALALGIAAAMWRGSRFDRAVSMGAVAVVSVPEFLIATLAVLLFAVQL FT RWLPALAYTGPDADLAELARAYALPVFSLCCVIISQMLRMTRAAVVDQLRAPYIEMVRL FT KGASPLRMVLRHALPNALGPIANAVALSLSYLLGGVIIVETIFNYPGVAKLMVDGVTQR FT DMPLVQTCAMLFCAAYLLLVTVADVLGIVSNPKLRHR" FT CDS 242415..243290 FT /transl_table=11 FT /gene="dppC" FT /locus_tag="azo0220" FT /product="ABC transporter, permease protein" FT /function="ABC-type dipeptide/oligopeptide/nickel transport FT systems permease components" FT /note="Part of the ABC transporter complex dppABCD involved FT in dipeptide import. Probably responsible for the FT translocation of the substrate across the membrane. Similar FT to the dipeptide permease protein, DppC in E.coli." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1Y2" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:A1K1Y2" FT /protein_id="CAL92837.1" FT /translation="MSDQPMPASSAPAPALPAEPPRRRLPRLPLPGLLGLAVILFWLAT FT ALFGPWLLAPEANEPGVDVVFGRLSAAHPLGTDYLGRDMLARLVLGAGYTVGVAIVATL FT LASAGGTALALLAAVRGGWTDGALSRLMDTLISIPSKLFALIMVAAFGSSVTLLALTAA FT LIYVPGVFRIARSLAVNINAMDYVAVARSRGEGDLYIMRHEILPNMLGPMLADLGLRFV FT YVVLLLAGLSFLGLGVQPPEADWGSLVRENLGGLPEGAPAVIVPALAIASLTIAVNLFI FT DNLPGRANRE" FT CDS 243283..245109 FT /transl_table=11 FT /gene="dppD" FT /locus_tag="azo0221" FT /product="putative dipeptide transport system, ATP-binding FT protein" FT /function="ATPase components of various ABC-type transport FT systems contain duplicated ATPase" FT /note="Part of the ABC transporter complex dppABCD involved FT in dipeptide import. Similar to the dipeptide transport FT membrane protein, DppD in E.coli Probably responsible for FT energy coupling to the transport system." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1Y3" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR013563" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K1Y3" FT /protein_id="CAL92838.1" FT /translation="MNDRADKEIAMRADKPGAAVAVRGLRIAAGGKPIVHGLDFDIAPG FT EVLALIGESGSGKTTTALALMGYARQGCEIVGGTVRVGDDIEVLGLDAAGRRKLRGRTV FT AYIAQSAAASFNPSRTIMDQVVEPALIHGLMPRAEAERRAVALFRELALPKPETIGARY FT PHQVSGGQLQRLMAAMALITDPALVILDEPTTALDVTTQIEVLRAFRRVVRERGTSAVY FT VTHDLAVVAQMADRILVLRHGAARELGDTRQVIEAPADDYTRSLLAAAHPAAREGGAVA FT AAGSTPLLEVRNLAAGYGARGADGMPAVPILADIDLTLHRGQAIGVIGESGSGKTTLAR FT VVAGLVGPARGEVLLDGAPLPATLAGRSREQLRRIQIVFQIADTALNPAHTVERILARP FT LQLYHGLSGAALQARIARLLDLVQLPAAVAGRLPGGLSGGQKQRINLARALAAEPDIIL FT ADEVTSALDTVVGAAVLDLMAELRRELGLSYLFISHDLNTVRAVCDEVVVLYAGRKVEA FT VPRERFGTSVRHPYFDLLARSVPEMRIGWLDDIARNEVAPVARTPGGCVFIDRCPLRVD FT GLCDSMPPPRQRLAGGSEILCHRSEAELAAAV" FT CDS 245317..246789 FT /transl_table=11 FT /gene="gabD1" FT /locus_tag="azo0222" FT /product="probable succinate-semialdehyde dehydrogenase FT [NAD(P)+]" FT /function="NAD-dependent aldehyde dehydrogenases" FT /EC_number="1.2.1.16" FT /note="Probable succinate-semialdehyde dehydrogenase FT [NAD(P)+]. Homology to gabD of R. eutropha of 68% FT (AAF19796). Catalysis of the reaction: succinate FT semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H + H+. FT Pfam: Aldehyde dehydrogenase family no signal peptide no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1Y4" FT /db_xref="InterPro:IPR010102" FT /db_xref="InterPro:IPR015590" FT /db_xref="InterPro:IPR016160" FT /db_xref="InterPro:IPR016161" FT /db_xref="InterPro:IPR016162" FT /db_xref="InterPro:IPR016163" FT /db_xref="UniProtKB/TrEMBL:A1K1Y4" FT /protein_id="CAL92839.1" FT /translation="MPLTLTRPDLQRQHNFIANAWHDATDGRLLPVSDPATDTVFAHVP FT DSAAADARAAVDAAHAAFPAWRALTGRERAQYLKRWHALILAYQDDLGRLISREQGKPL FT AEGRGEVLYAASYVEWFAEEAARSHGEVIPEPVRGRKMLMVKEPVGVVAAITPWNFPAA FT MIARKIAPALAAGCTVVAKPAEDTPLTSLALVRLAEEAGLPAGVLNMVTASRERAAEVV FT DVWLADSRVRKITFTGSTPVGKHLVRESAATLKRVSMELGGNAPFIVFEDADLDAAVAG FT LMAAKFRNGGQTCVCPNRVFVHDAVHYDFVARLSARVAALKVGPASAPDSQIGPMINAR FT AVDKIAAHVADAVERGACVVTGGERLAALGANYFAPTILVGVDAGMRCTQEETFGPVVP FT VTRFEHEDEVVAAANDTPFGLAAYFYTRDMARAWRVADRLESGIVGINEGALAAEVAPF FT GGIKESGYGREGSRHGLDDYTQMKYLCQGGLG" FT CDS 247001..247369 FT /transl_table=11 FT /locus_tag="azo0223" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT an orf of Polaromonas sp. JS666 of 34% (ZP_00360285) . No FT domains predicted. No TMHs. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K1Y5" FT /protein_id="CAL92840.1" FT /translation="MFRMVHRVIHFLLMLAVLFHAVVAQGGWAAAGSSPKASHAALHWQ FT GAAHHHRGVDGTHIHHDTSPESLKHVNFDCAVHAVALLSAGLADLPRLPDATLFVATVL FT EPPVPFLERLKRPPRSAA" FT CDS 247500..248717 FT /transl_table=11 FT /locus_tag="azo0224" FT /product="hypothetical outer membrane efflux protein" FT /function="Outer membrane protein" FT /note="Hypotethical outer membrane efflux protein. Homology FT to PA2525 of P. aeruginosa of 25%. signal peptide. no TMHs" FT /db_xref="GOA:A1K1Y6" FT /db_xref="InterPro:IPR003423" FT /db_xref="UniProtKB/TrEMBL:A1K1Y6" FT /protein_id="CAL92841.1" FT /translation="MAACAIAGSMICCAALAQTTAPRVGLARALDAAWQRTQAGTEAQV FT ALARAEAEQAAADSLLPEPPALELSHRSDRWHDNKGARENEVGLALPLWLPGQRSARQA FT AAEAGQALARSGEDADRLRLAGEVREAAWALAGLDAEAAVAEAQLRYLRELAADVERRV FT QAGELARTDAIAARAEALAAQAALSEARERRHAAMTRWQTLTGLDAPADPREADTVPDA FT AGDDGLPATHPGLRLAAQAVEHARRGVEVARTDRAAPPELTLSYRREVGESGAAAERSI FT NVGLRVPFGTDARNRPLAAAAQGELAQAQVAELRLRQQLAGDLLVARGALQAAQAQAEA FT ARERAGLLRERAQLIDKAFRAGEAALPELLLAASAATQGEAGRARQDAALGLARARLQQ FT VSGILP" FT CDS 248714..249310 FT /transl_table=11 FT /locus_tag="azo0225" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank no domains predicted signal peptide no TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K1Y7" FT /protein_id="CAL92842.1" FT /translation="MTPISSFPLRRGFAALALAAAGAVFASPGAHGPNGEHLDTPSGAV FT AVSATPRVEAHSEAFELVGKLDHGQFSFFIGRYETNEAVLGATVELEADGLKSIATFRA FT ESGDYLVSDAAMVAALAKPGAHALLFTVETADDSDLLDASLTVADDHAVAHEGGKRGLP FT LAWTAAGVLGLAAVGTVALRRRKSAPNPSARGGRA" FT CDS 249307..250452 FT /transl_table=11 FT /locus_tag="azo0226" FT /product="conserved hypothetical secreted protein" FT /function="Membrane-fusion protein" FT /note="Conserved hypothetical secreted protein. Homology to FT cc1787 of C. crescentus of 30% (trembl|Q9A7D6) no domains FT predicted signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K1Y8" FT /protein_id="CAL92843.1" FT /translation="MNRKSFSLSTLALALAVLGSPLASASPGAHGPNGEHLDAPGAAVI FT ASGLARLPDGSVNVPMAAQRRMGVLTRFSVESEAAATVELAGRVVMDPNAGGRVQPMYA FT GRVEAGPKGLPVAGQAVKRGEVLAYLRYQAEPYAQAEQQAQLAEVRNNRKLAEQRVERL FT QGLEGSIPRKEMDAARAELDTLKAREQRIGAALGAREALLAPVDGVIARADAVAGQVVE FT ARDVLYEIIDPARVLVEATVADPALATGIAEARVVEAPQVAFKLVGAARSLRDGVLPLT FT FRAVPDPKAKVAALPLAVGQPVTVVAALAERTRGFVLPAEAVVRNSANEPIVWIKSGAE FT RYIPQPVQYRALDATRVVVTHGLGADNRVVVQGAPLIAQIR" FT CDS 250466..253597 FT /transl_table=11 FT /gene="czcA1" FT /locus_tag="azo0227" FT /product="putative cation efflux system protein" FT /function="Putative silver efflux pump" FT /note="Cobalt-zinc-cadmium resistance protein CzcA (cation FT efflux system protein CzcA). In A.eutrophus has a low FT cation transport activity for cobalt, it is essential for FT the expression of cobalt, zinc, and cadmium resistance.Czca FT and Czcb together would act in zinc efflux nearly as FT effectively as the complete czc efflux system FT (czcABC).Belongs to the acrb/acrd/acrf family. 41% FT similarity to the A.eutrophus CzcA protein. FT SWISSPROT:CZCA_ALCEU:P13511 InterPro: Heavy metal efflux FT pump CzcA. InterPro:IPR001036; Acrflvin_res.IPR004763: FT CzcA. Pfam:PF00873; ACR_tran; 1. InterPro:TIGR00914:Heavy FT metal efflux pump CzcA InterPro:PF00873:Acriflavin FT resistance protein Signal peptide: present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1Y9" FT /db_xref="InterPro:IPR001036" FT /db_xref="InterPro:IPR004763" FT /db_xref="UniProtKB/TrEMBL:A1K1Y9" FT /protein_id="CAL92844.1" FT /translation="MFNWIVRYSLANRLFVLALALLMMAYGAYTAWKTPVDVFPDLNKP FT VVTVLTEAGGMAPEEVEQLVTFPLETALGGMPGVTRVRSVSGVGLSIVYAEFDWGTDIY FT RNRQLVSERLSLVREQLPTGITPMMGPVSSIMGEVMLIGLPLAADGKVSAMQAREYADF FT VLRPRLLSIAGVSQVIPIGGEVRQLRVEPDTARMAQVGVSLTQVEEALRGFASNAGGGF FT IDLNRREYLIRHLGRGNNVEDLAGLAVAWKDGRPVLLEQVATVRFAPSLKRGDAGYNGG FT PAVIVSVQKQPDADTVKLTGQIEVALAELDHGRPAGLAAPKVLFRQANFIEASIGNVSE FT ALRDGAIMVAIVLFAFLLSARTTLISLVAIPLSLAVTALVFQLLGQSINVMTLGGLAIA FT IGELVDDAVVDVENILRRLKQNRALPNPAPVLEVVAAASVEVRSGIVYATIIVCLVFVP FT LFALPGIEGRLFSPLGIAYIVSILASMLVSMTVTPALSSFLLPRMKRLDHGDSPLVAKL FT KVWDAKLLTWSFPRAKLLIGIAALAVAAAAASVPFFPRAFLPAFNEGSLVLGMVLNPGT FT SLEEANRLGALAETLIREVPEVTQVGRRTGRAELDEHAEGVHAAEIDVDLHPSERGREA FT VMADIRDKLSVLPAQVAIGQPISHRLDHLLSGVRAQVAVKIFGDDIDTLRGLAEQMRQG FT LASVPGLVDLTVEKQVLIPQITVRLDHRKAAQAGLTPGEAVRLLQALTDGAHSAEIVDG FT PRRYDLVLRLADARRSPQDLARTLIDTPAGRLPVSAIATVQETDGPNQVGRENGRRRIV FT VYANTDGSDMGRVIADVRAVIARTPMPAGNFVTLEGQFQAQEQATRLIAGLSLVSLAMI FT FLVLYSRYKSAVLAGVIMANIPLALIGSVVAMWLAGVTLSVASMVGFITLAGIATRNGI FT LKVSHYINLCRFEGETFGDAMIVRGSLERLTPVLMTALVAAFALTPLLLAADAPGKEIL FT HPVAVVIFGGLVSSTLLDTLLTPVIFRLVGEKPTRRLLEGGEEGAVQGLPQEAY" FT CDS 253594..254088 FT /transl_table=11 FT /locus_tag="azo0228" FT /product="Hypothetical protein" FT /note="Hypothetical protein, 32% identity to TrEMBL;Q82T66 FT No Signal Peptide/Features/Domains/TMH detected." FT /db_xref="UniProtKB/TrEMBL:A1K1Z0" FT /protein_id="CAL92845.1" FT /translation="MTATATIPPVRAPARNEIRGPRGAACKVRRTFDGDIPMTALKTLL FT VAVAFGAASLAAAPVLAHGDSAPKHGGIVKSANDLSFELVAEGGDAALYIDDHGSAFDT FT AGASGKLTVLAGSDKTAVELKPAGGNKLLAAGARLPAGAKVVAVITTAQNKTASVRFNL FT P" FT CDS 254346..256517 FT /transl_table=11 FT /gene="fhuA1" FT /locus_tag="azo0229" FT /product="probable ferrichrome-iron TonB-dependent FT receptor" FT /function="Outer membrane receptor proteins mostly Fe FT transport" FT /note="In E.coli this receptor binds the ferrichrome-iron FT ligand. It interacts with the tonB protein, which is FT responsible for energy coupling of the ferrichrome-promoted FT iron transport system. Acts as a receptor for bacteriophage FT T5 as well as T1, phi80 and colicin M. Binding of T5 FT triggers the opening of a high conductance ion channel. Can FT also transport the antibiotic albomycin. Signal peptide." FT /note="Specificity unclear" FT /db_xref="GOA:A1K1Z1" FT /db_xref="InterPro:IPR000531" FT /db_xref="InterPro:IPR010105" FT /db_xref="InterPro:IPR010916" FT /db_xref="InterPro:IPR012910" FT /db_xref="UniProtKB/TrEMBL:A1K1Z1" FT /protein_id="CAL92846.1" FT /translation="MTTRTKRRLRRVLVPAAAALSCASVFAAEPADTQDAADTTPAAAT FT ASASTLDTVSVTGKKQPYRKLTATGATKTDTLLKDLPQSVRVLTEDLLEDAGVTNLAGA FT LDLSSGVSRQSNLGGLWDSYAMRGFTGDPSFGSDYLVNGFNYSRGYNGVRDAANTGSVE FT VLKGPSAALYGRGEPGGTVNITTKKPLFQREGQVDISYGSFDAFRTAIDLTGPISDRMA FT YRLNGAYEKAGSYRDHVSSERSLISPSFLWMLSDDTTLSYELEVSRQKATFDRGVMAIN FT GKLGVLSRKRFLGEPGDGDHDTETVGHQVFLQHYLNDDWQLQGGFSFRESSIKGTSTEV FT RFLRADGENAARQRRTRDNEASDLSARAELLGSFRTGPLKHNVLFGVDAYKFVDERLQY FT RIANAGDINIFEPVYGNVVWGFTPANRNTDTKEEQDSRSLYAQDQIDLTEQWKLLLGVR FT FDDYDQKLTNNRNGIVVKKSLAATSPRVGLVYQPTKQVSLYAQAGKSFRPNGGVSRDFT FT AFDPEEGRSYELGAKWDSADQRITSTVALFHITKENVLSPDPVDPNNFYVTAGEVESKG FT LEFDLSGEIMPTVRLSFAYAYTKTEVTKDNNKLLEGRELANVPLHSANLMLVKSLSLND FT KPATVGVGLNYVGEREGAVAPLVAADDFKLPGYTTVKLTGSYNFDKQTKLMLEVDNLFD FT KEYYTSSYSQAWVYPGSPRAFKATLQHRF" FT CDS 256540..257289 FT /transl_table=11 FT /locus_tag="azo0230" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT RPA1846 of R.palustris of 39% (trembl:Q6N8Q7). No domains FT predicted. No TMHs. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K1Z2" FT /protein_id="CAL92847.1" FT /translation="MNLKPVFRSLAAGLALAAVAGAAHAHQIWFEQAGNSITFRYGELD FT ENLHEVSPGGLDRFRALEARWVKAEGTAPLAMQKLQDGYAVPARTAAGESLLAIDNNYP FT MFDTRRDGKLLRTWWVPATRWVGDFSARKAELPLDFVPTGAKRGDAVEFQLVYKGEPLA FT GEKVKLATPSGWVKYATTDADGKVAFALPWKGNYVLGVYYTDEIEGVRGDEKYQLEGYN FT TSVSFNLAKGLAPLATAERTLPATGKH" FT CDS 257937..259160 FT /transl_table=11 FT /locus_tag="azo0231" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT SO1157 of Shewanella oneidensis of 50% FT (trembl|Q8EHR0(SRS)). No domains predicted. Signal peptide. FT 7 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR012429" FT /db_xref="UniProtKB/TrEMBL:A1K1Z3" FT /protein_id="CAL92848.1" FT /translation="MSSTASLSSTVGFGPAAAAGSMPLAAVRAPRIVSIDILRGLVMLV FT MLLDHVRETLYLHLQVTDPMTIATTPAALFFSRFAAHFCAPAFVFLTGLSAWLYANPPA FT GTPRPVKSFLMKRGFLLLFLEATVITFAWSGDLPPRVIYLQVIWAIGLAMIVLALMSGL FT PRKLLAAIGFVIVFGHNALAGLSFAPDSPLYLPWTLLLHRGPVIAEGALQIKLTYPVLP FT WIGVILLGWVAGPLYAHTVGAARRIKLLLALGLACLGLLLVLRGFNIYGENAPWEYGAT FT TVHTVMSFLNFTKYPPSLDFLLTTLGTAFLLLAAFERADNRVGRFLATFGGAPMFYYIG FT HLLLLLVLYKILLAVFGPNQGTRFGVNPDQFWVVWVSTVALIPVLYFPCRAFARYKRTS FT KRAWVRYF" FT CDS 259217..260059 FT /transl_table=11 FT /gene="exbB1" FT /locus_tag="azo0232" FT /product="putative biopolymer transport protein ExbB" FT /function="Biopolymer transport proteins" FT /note="Putative biopolymer transport protein ExbB. Homology FT to exbB of B. pertussis of 35%. ExbB is part of the FT TonB-dependent transduction complex. The TonB complex uses FT the proton gradient across the inner bacterial membrane to FT transport large molecules across the outer bacterial FT membrane. PFam: MotA/TolQ/ExbB proton channel family FT signals peptide most probable 4 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K1Z4" FT /db_xref="InterPro:IPR002898" FT /db_xref="UniProtKB/TrEMBL:A1K1Z4" FT /protein_id="CAL92849.1" FT /translation="MKLRRFFSSLSLAFAIACGAVSAPAFAQSDPATTASADSASAVAG FT TIDAAPTAKPAAGAAAKVENPYGLEALWAGSDAVAKVVLVLMIIMSAGSWYIIIVKLIE FT QTRMYRQAKAVEGVWKSATIKHGAENLENGSPFRFIAEAGLEATNRHDSLLEHVDLNDW FT VTLSIHRAIEKVQSRMQNGLAFLATVGSTAPFVGLFGTVWGIYHALTAIGIAGQASIDK FT VAGPVGEALIMTAIGLAVAVPAVLGYNWLVRRNKGVMDQVRGFGNELHTVILSSAKRA" FT CDS 260085..260513 FT /transl_table=11 FT /gene="exbD1" FT /locus_tag="azo0233" FT /product="putative biopolymer transport protein ExbD" FT /function="Biopolymer transport protein" FT /note="putative biopolymer transport protein ExbD. ExbD is FT part of the TonB-dependent transduction complex. The TonB FT complex uses the proton grandient across the inner FT bacterial membrane to transport large molecules across the FT outer bacterial membrane. InterPro: Biopolymer transport FT protein ExbD/TolR Pfam: Biopolymer transport protein FT ExbD/TolR no signal peptide probable 1 TMH" FT /note="Family membership" FT /db_xref="GOA:A1K1Z5" FT /db_xref="InterPro:IPR003400" FT /db_xref="UniProtKB/TrEMBL:A1K1Z5" FT /protein_id="CAL92850.1" FT /translation="MAMNVGSADEDDGVMSAINTTPLVDVMLVLLIIFLLTIPVATVSV FT PVELPKETIEARETKPENVILSVDKGGALFWHDVRVANVDALVERLKKVSVQQPQPEVQ FT IRGDLDAAYDGVGRILYACQRAGITKVAFITEPPARGG" FT CDS 260535..260960 FT /transl_table=11 FT /gene="exbD2" FT /locus_tag="azo0234" FT /product="putative biopolymer transport protein ExbD" FT /function="Biopolymer transport protein" FT /note="Putative biopolymer transport protein ExbD. Homology FT to exbD2 of X. campestris of 36% ExbD is part of the FT TonB-dependent transduction complex. The TonB complex uses FT the proton gradient across the inner bacterial membrane to FT transport large molecules across the outer bacterial FT membrane. InterPro: Biopolymer transport protein ExbD/TolR FT Pfam: Biopolymer transport protein ExbD/TolR no signal FT peptide probable 1 TMH" FT /note="Family membership" FT /db_xref="GOA:A1K1Z6" FT /db_xref="InterPro:IPR003400" FT /db_xref="UniProtKB/TrEMBL:A1K1Z6" FT /protein_id="CAL92851.1" FT /translation="MNVGSAGASSEPEVMVDINTTPLIDVMLVLLIMLIITIPIQLHSV FT NLDLPVGTPPASDIKPEIVKIDIDDKSTVYWQGVALADMGELETRLREIAARPVAPDLH FT LRPDKAARYAVVARVLADTKRLGLTKIGVIGSEQFVQ" FT CDS 260989..261636 FT /transl_table=11 FT /locus_tag="azo0235" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT an orf of Rubrivivax gelatinosus of 55% FT (gi|47575633|ref|ZP_00245668.1|(NBCI ENTREZ)). No domains FT predicted. No signal peptide. 1 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K1Z7" FT /db_xref="InterPro:IPR006260" FT /db_xref="UniProtKB/TrEMBL:A1K1Z7" FT /protein_id="CAL92852.1" FT /translation="MDYSFQPKQTSGRYVGIGIVVGLHVVIGWALASGMARKAVEVIKK FT PLEAVVIQEVTLPPPPPPPPPPKIVQPPKQVVAPKVQAPPPPPFVPPPEVAVAPSAAPA FT IEAVHTPPPAPPVIAPPAPPAPPAPVAAKSDIGVACPVQAKPEMPEKAINSGIAGVVRA FT EAVIRGGVVQEVRILSGPRVFHAAVKTAMQQYRCTAPDGTVASQDFDFKVEG" FT CDS complement(261880..262902) FT /transl_table=11 FT /gene="add" FT /locus_tag="azo0236" FT /product="adenosine deaminase" FT /EC_number="3.5.4.4" FT /note="Adenosine deaminase (Adenosine aminohydrolase). FT InterPro: Adenosine and AMP deaminase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1Z8" FT /db_xref="InterPro:IPR001365" FT /db_xref="InterPro:IPR006330" FT /db_xref="UniProtKB/TrEMBL:A1K1Z8" FT /protein_id="CAL92853.1" FT /translation="MDPSRLTDLHAYIRALPKAELHLHIEGTLEPELMFALAARNGVAL FT PWDSVEATRAAYAFSDLQSFLDLYYAGAAALIHEQDFHDLALAYFERAHEDGVVHAELF FT FDPQTHTARGVAFDTVLDGLERACIEAQERWGISSRLILCFLRHLSEEDGFATLEQALP FT HLARIHGVGLDSSEKGHPPAKFARLFARCRELGLHIVAHAGEEGPPAYIEEALDILQVE FT RIDHGVRAAESAALMERLAREQVPLTVCPLSNVKLCVFERLQDHNLKQLLDAGLKVTIN FT SDDPAYFGGYVGQNYQQTAEALGLSRTELKQLAKNSLEASFVPQAVLDPWLLRLAAVPD FT " FT CDS complement(262974..263831) FT /transl_table=11 FT /gene="npd1" FT /locus_tag="azo0237" FT /product="putative NAD-dependent deacetylase" FT /function="NAD-dependent protein deacetylases SIR2 family" FT /note="Putative NAD-dependent deacetylase (EC 3.5.1.-) FT (Regulatory protein SIR2 homolog). Modulates the activities FT of several enzymes which are inactive in their acetylated FT form. Similar to SWISSPROT: sprot|NPD_AERPE (27% Aeropyrum FT pernix, NpdA or aq_2170) Pfam: PF02146 Sir2 family." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K1Z9" FT /db_xref="InterPro:IPR003000" FT /db_xref="UniProtKB/TrEMBL:A1K1Z9" FT /protein_id="CAL92854.1" FT /translation="MTAPPPSTLHAAAQDAAAALAGADALLVTAGAGMGVDSGLPDFRG FT AEGFWRAYPALRQTGLRFEEIADPVHFERDPALAWGFYGHRLALYRRTVPHAGFGLLRE FT LGRALAQGVFVFTSNVDGQFQRAGFDADRIVEVHGSIHHLQCIHGCRDAIWPADAFAPD FT VNEATCRLSNPPPRCPHCGAVARPNILMFGDWGWLEERSAAQQARLADWLDRVQRPLVV FT EIGAGTAIPTVRRVGERAGATLVRINPQADRDPPPGSIALHCGGLAGIRALHAAAAAAG FT LVGA" FT CDS complement(263828..264958) FT /transl_table=11 FT /locus_tag="azo0238" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein no homology to the FT data bank no domains predicted no signal predicted 7 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K200" FT /protein_id="CAL92855.1" FT /translation="MEHALRPALLPTLPQLVLRGVDARHNMPAVIMLAAAGGLFVLSWA FT AASVGSGDQFPLFLIGNLIGLALLLTGYSAAGVMLMDQARGRPPRSVGDTLRAGAVCAL FT RHAVLAFFAAVGLALFALCVAMALLLARIPGLGVLFYLLLFPLASLGSAALFGLGGYAF FT LLLGPALWCGAGVRQAALHVWAVFQHKPRQVLIACTLLTVLTAVLVLAGGAVAAAGTVF FT VGGLSVPMLGEVDDFSGLFATPAQHLASGVTALSWAGVVGAGLVYAAIGAFVAAVMILG FT TSHAWLHLTRDLDLEQAGRAFDDPAFDDAGEERGSLLAAPSAAHALVAAGSILAHAAHT FT AAGLPPPAEGSCHRCGAGPEPGDRFCTACGCLLTRP" FT CDS complement(264970..266250) FT /transl_table=11 FT /locus_tag="azo0239" FT /product="hypothetical membrane protein" FT /note="Hypothetical protein, showing only very low FT similarity to known proteins (SWISSPROT: sprot|FRAH_ANASP; FT >10% Anabaena sp., FraH). Important Domains are: Pfam: FT PF00034 Cytochrome c. SMART: SM00438 ZnF_NFX TMHMM FT reporting 1 transmembrane helices." FT /db_xref="GOA:A1K201" FT /db_xref="InterPro:IPR009056" FT /db_xref="UniProtKB/TrEMBL:A1K201" FT /protein_id="CAL92856.1" FT /translation="MDCPACGHPNRTSAHFCSACGQHLDGPVPPALQVCPSCGRSCRGD FT AHFCPACGFHLAGPLPDMSDIDFSQLDPARAEPGPAAQPFPPMGEPDATVILPPGWTAT FT RPPAPDPAPAPASEARPGADAPAAAGGDEPAAGPTPVPPPPPADSAGRRPLALALGFVL FT VVVAGLAAWWTTTAPHDEPPPPPPVAVDDAAARAERALALAERALAERAQLDTAPAAGS FT AATPDTAAPPPVAEVDTAAANASTQPVAAVAPAAAPRPVRTLYARGCAACHERGANGAP FT RTADPEQWQDLLQGSPHDQSQRVLAGHGGAPAGAGLGLTPVESERLVAHVGELVGQART FT REAAAERSRAAERSARATTAAAERPAAPAAPRQDDWQRSLKSELARCGQLGFFERVACT FT EKARWTYCNNRWNSVPECAVRNHQSAP" FT CDS 266442..267473 FT /transl_table=11 FT /gene="dctP1" FT /locus_tag="azo0240" FT /product="putative C4-dicarboxylate-binding periplasmic FT protein" FT /function="TRAP-type C4-dicarboxylate transport system FT periplasmic component" FT /note="Putative ABC transporter periplasmic binding FT protein, DctP: TRAP dicarboxylate transporter.Binds FT C4-dicarboxylates; part of the binding-protein- dependent FT transport system for uptake of c4-dicarboxylates. 28% FT TRAP_transptDctP. Pfam:PF03480; SBP_bac_7; 1. FT TIGRFAMs:TIGR00787; dctP; 1. Signal peptide:present. FT TMhelix:1" FT /note="Specificity unclear" FT /db_xref="GOA:A1K202" FT /db_xref="InterPro:IPR004682" FT /db_xref="InterPro:IPR018389" FT /db_xref="UniProtKB/TrEMBL:A1K202" FT /protein_id="CAL92857.1" FT /translation="MKKRQFSALLAGLCASFALGLPLPAAAAPYKDEYKLSTVLGEAFP FT WGWGAKRWADLVAEKTQGRIKIKVYPGTSLVSGDQTKEFTALRQGIIDIAVGSTINWSP FT QVKELNLFALPFLMPDHKAIDALTHGRVGKKMFELLAERDVVPLAWGENGFREVSNSKK FT PIRTPDDLKGLKMRVVGSPLFLATFSALGANPTQMSWADAQPAMATGAVDGQENPLGVF FT SAAKLHTVGQKHLTLWGYVADPLIFVVNKNVWNSWTPEDQKAVAEAAQQAAREEIARAR FT AGISAGDDALLKEIAANGVTVTTLTEAEREGFRKATAGVYKEWAGKVGAELVKQAEEDI FT AKR" FT CDS 267570..268058 FT /transl_table=11 FT /gene="dctQ1" FT /locus_tag="azo0241" FT /product="DctQ1 protein" FT /function="TRAP-type C4-dicarboxylate transport system FT small permease component" FT /note="C4-dicarboxylate transport system,permease small FT protein,DctQ. The Dct locus encodes a high-affinity FT transport system for the C4-dicarboxylates FT malate,succinate, and fumarate. 22% DctQ. Pfam:PF04290; FT DctQ; 1. TMHelix:4." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR007387" FT /db_xref="UniProtKB/TrEMBL:A1K203" FT /protein_id="CAL92858.1" FT /translation="MNPDPSADTAAEAPAPLSPEQILCGIAMALIVLISLGNVVARYLT FT SQSFAATEEFSIALLLILSFLGSSTAFAFDRHIRVTFFIERLPSRWRQGAEWLSFVVTA FT ALFGFIAFYAGRLTWDQYRFEETSPALGLPQWWYTVWMPALAVVIVLRLVVTRLGARS" FT CDS 268055..269338 FT /transl_table=11 FT /gene="dctM1" FT /locus_tag="azo0242" FT /product="probable TRAP-type C4-dicarboxylate transport FT system, large permease component" FT /function="TRAP-type C4-dicarboxylate transport system FT large permease component" FT /note="TRAP-type C4-dicarboxylate transport system, large FT permease component, DctM.The Dct locus encodes a FT high-affinity transport system for the C4-dicarboxylates FT malate,succinate, and fumarate. 34% DctM.IPR000252; FT DedA.IPR004681; TRAP_transptDctM. Pfam:PF06808; DctM; FT 1.PF00597; DedA; 1. TIGRFAMs:TIGR00786; dctM; 1. Signal FT peptide: present. TMhelix:11." FT /note="Specificity unclear" FT /db_xref="GOA:A1K204" FT /db_xref="InterPro:IPR004681" FT /db_xref="InterPro:IPR010656" FT /db_xref="UniProtKB/TrEMBL:A1K204" FT /protein_id="CAL92859.1" FT /translation="MTGVVLIGLFLLALVAGLPLAVGLGVASIAVLALAGFDQLAVPTN FT IYAGIAKYPLLAIPMFILAGMIFERSGVALRLVRFVTAMVGEWTGSLAVVAVLVSMLLG FT GISGSGPADAAAVAAVMLPSMVARGYPKGFSAGLIAAAGSTAIVIPPSVAFIVYSVMVP FT AATVPALFAAGLFPGMIAALCLLIPAVLISRKYGFGRDYRAERPPLGKSFVDAIWGLLA FT PVIILGGLRAGIFTPTEAAVVAVAYGIFVGMVVYRTITPKTLFRLLVDAGELSAVVMMI FT IGVASVFAWAGNTLGIFDAAAKALVEMHPGHWGMLLSVNLLLLVAGMFLDAVSIFLILL FT PLLVPIALAMGWDLVWFGVMMTINLAIGQFTPPMALSLMITSRIAGIGIEQTFRWVIWF FT VLAMGAGLAAMVVFPELALWLPRRLGYV" FT CDS complement(269367..270011) FT /transl_table=11 FT /gene="uidR" FT /locus_tag="azo0243" FT /product="putative TetR family transcriptional regulator" FT /function="Transcriptional regulator" FT /note="Putative TetR family transcriptional regulator," FT /note="Family membership" FT /db_xref="GOA:A1K205" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011075" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:A1K205" FT /protein_id="CAL92860.1" FT /translation="MTADRSPVDAPRAEARRAQILDAAVACFRAHGFHGASIAQISKAA FT GMSAGHIYHYFDNKEAIIAAIVEQDLERLLTLTAEMRSARDVLEAMIERAAEGVRDNLD FT PASVGLKLEIVAEASRNPRVAEIVRQADATCRDSLAETLRAMRANCGHRDDEAAIAGLT FT EVLAAMFGGLMIRSVRNPDLEQDTVIRMFQRVIRFIITDALAAPAPGEAPH" FT CDS 270224..271426 FT /transl_table=11 FT /locus_tag="azo0244" FT /product="membrane fusion protein" FT /function="Membrane-fusion protein" FT /note="HlyD family secretion protein. The secretion of a FT number of proteins/molecules require the help of members FT belonging to the ABC transporter family and a membrane FT fusion protein belonging to the HlyD family, TREMBL:Q8XRL2 FT (55% identity); SWISSPROT:P31223 (53% identity). Pfam FT (PF00529): HlyD family secretion protein. SignalP FT predicting signal peptide. TC (8.A.1): The Membrane Fusion FT Protein (MFP) Family." FT /note="Family membership" FT /db_xref="GOA:A1K206" FT /db_xref="InterPro:IPR006143" FT /db_xref="UniProtKB/TrEMBL:A1K206" FT /protein_id="CAL92861.1" FT /translation="MQTPPSLLLKPLAVLVAAALLLTACGGQQAPAGAPPGGGAPTVGV FT VKVQSEAVALTTELPGRTAPYQIAEVRPQVTGIVKKRAFREGSEVKGGELLYQIDPATY FT QAAYDSAKASLARAEANLYTAKLKGERYADLSQINAISKQANDDAVAALKQAEADVAAA FT RAAVDKARIDLEFTRVSAPIPGRIGRSSVTAGALVTANQADPLATVQQLDPIYVDVTQS FT SAELLALRRSLAEGKLQRAGDNAARVQLVMEDGSLYPAEGKLEFSEVSVDTGTGSVVLR FT AVFPNPKNDLLPGMYVRARFAQGVRQDAVLVPHAGVTRDARGNAVVMVVNGDNKVEARQ FT VRAEQALADKWVVSEGLAAGDRVIVEGLQKVRPGADVQVQEVGAAAPQAAAAAPTAAAA FT K" FT CDS 271438..274596 FT /transl_table=11 FT /locus_tag="azo0245" FT /product="RND efflux transporter, permease protein" FT /function="Cation/multidrug efflux pump" FT /note="Members of this family are integral membrane FT proteins. Some are involved in drug resistance. AcrB FT cooperates with a membrane fusion protein, AcrA, and an FT outer membrane channel TolC. The structure shows the AcrB FT forms a homotrimer, TREMBL:Q8E8H2 (65% identity); FT SWISSPROT:P31224 (63% identity). InterPro (IPR001036): FT Acriflavin resistance protein. InterPro (IPR004764): FT Hydrophobe/amphiphile efflux-1 HAE1. TIGRFAM (TIGR00915): FT Hydrophobe/Amphiphile Efflux-1 (HAE1) Family protein. FT TIGRFAM (TIGR00914): Heavy metal efflux pump, CzcA family. FT Pfam (PF00873): AcrB/AcrD/AcrF family. TMHMM reporting 12 FT transmembrane helices. TC (2.A.6.2): The (Largely FT Gram-negative Bacterial) Hydrophobe/Amphiphile Efflux-1 FT (HAE1) Family." FT /note="Specificity unclear" FT /db_xref="GOA:A1K207" FT /db_xref="InterPro:IPR001036" FT /db_xref="InterPro:IPR004764" FT /db_xref="UniProtKB/TrEMBL:A1K207" FT /protein_id="CAL92862.1" FT /translation="MARFFIDRPIFAWVVAIVIMLAGALSILSLPVSQYPAIAPPQIAI FT NATYPGATAKAVEDSVTQVIEQKMTGLDNLLYMNSTSDSYGRVTVTLTFNAGTNPDIAQ FT VQVQNKLQTALPLLPQAVQQQGVQVAKSTRNFLMVLGFVSRDGSQSANDLSDFLASTVQ FT DPLSRVTGVGEVQVFGSQYAMRVWLDPAKLNNYKLMPSDVRSALEAQNTQVSAGQLGGT FT PALPGQGFTASITAQSRLQTAEQFENILLKSSAQGGEVRLRDVARVEVGAQDYGFTARY FT NGKPAAGIGIKLAAGSNALDTAKAVRKAIDGMSRYFPAGVEVVTPYDTTPFVRLSIEEV FT VKTLVEAIVLVFLVMFLFLQNLRATLIPTIAVPVVLLGTFGLMAAFGFSINTLTMFGVV FT LAIGLLVDDAIVVVENVERIMTEEGLSPREATRKSMGQITGALIGIGLVLSAVFVPMAF FT FGGSTGVIYRQFSITIVSAMALSVLVAIVFTPALCATMLKPVEKGHDHSEGGWFSGFFR FT WFNRMFARNTTRYESAVGGILRRSGRFLLIYALIVGVLAFLFLRMPTSFLPEEDQGVMF FT TQVMLPAGATQERTIEVLKKVENHFLEGEKDYAKSIFTVAGFSFAGSGQNMAIGFVHLR FT DWDERKGPAGNVKAVAGRAMAAFSQIREAMVFAFVPPAVLELGTSNGFDVQLQDRSGLG FT HDALIAARNQFLGMAAQDKRLVAVRPNGQEDMQEYVLDIDHAKAGALGVSVSDINATLS FT TAWGGVYVNDFLDRGRIKKVYLQSQAEGRMRPEDLTKWYVRNKAGEMVPLSAFASGHWA FT FGSPRLERYNGQSSVEVLGQGAPGVSSGDAMAAVEEIIAKLPPGIGYEWTGTSYEERRS FT GSQAPALYALSLIVVFLCLAALYESWSVPFAVMLVVPLGVLGAIVAATGRGLSNDVYFQ FT VGLLATIGLSAKNAILIVEFAKEQMEKEGKALIDATLEAVRMRLRPILMTSLAFGLGVL FT PLAVATGAGSGSQNAIGTGVLGGTIFATVLGIFFIPLFYVAIKRIFKDKPAADAAPLAV FT QEAR" FT CDS 274611..276014 FT /transl_table=11 FT /gene="oprM1" FT /locus_tag="azo0246" FT /product="probable outer membrane efflux protein" FT /function="Outer membrane protein" FT /note="Probable outer membrane efflux protein. Homology to FT oprM of P. aeruginosa of 57%. Component of an efflux system FT that confers multidrug or multible antibiotic resistence. FT Pfam: Outer membrane efflux protein signal peptide no TMHS" FT /note="Family membership" FT /db_xref="GOA:A1K208" FT /db_xref="InterPro:IPR003423" FT /db_xref="InterPro:IPR010131" FT /db_xref="UniProtKB/TrEMBL:A1K208" FT /protein_id="CAL92863.1" FT /translation="MPLKTLAVALAAASLGACSTLAPDYERPAAPVAAAWPAEPAQPAA FT GTPSADAVAWRSFFADERLRQVVDLALANNRDLRVSALNIERARALYQIQRAELVPWIG FT VGGGQSAQRLPADLTQRGEPTISRQYSATVGFSSYELDFFGRIRSLRDAALEQYLATED FT ARRSAQISLVAEAANAWLTLAADRERLDLARRTYETQQQSYELTKKSFDFGAVSAIDLR FT QAQTARESARADLAAYTTQVARDINALNLVAGAAVPDELLPTALTDKVSAVGDLPAGLP FT SEVLVSRPDILAAERQLRAAYANIGAARAAFFPSITLTAAAGTASASLEGLFKAGSGTW FT SFAPQINLPIFQGGRLLANLQVAKVDREIAVADYEKAIQSAFREVADALAERANVGEEL FT DARRALVEATAETYRLSEARYRSGVDSYLGLLDAQRTLYSAEQGLISVRLADAANRVAL FT YRVLGGGAQ" FT CDS 276172..276657 FT /transl_table=11 FT /gene="bfr1" FT /locus_tag="azo0247" FT /product="putative bacterioferritin" FT /function="Bacterioferritin (cytochrome b1)" FT /note="Bacterioferritin (BFR) (Cytochrome B-1) (Cytochrome FT B-557). In E. coli is an iron-storage protein consisting of FT 24 identical subunits that pack together to form a highly FT symmetrical, nearly spherical shell surrounding a central FT cavity of about 8 nm diameter.X-ray crystallographic FT studies have revealed a close structural similarity between FT BFR and the ferritins, a family of iron-storage proteins FT found in both eukaryota and prokaryota. Key role in iron FT homeostasis. InterPro: Bacterioferritin. Non-secretory FT protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K209" FT /db_xref="InterPro:IPR002024" FT /db_xref="InterPro:IPR008331" FT /db_xref="InterPro:IPR009040" FT /db_xref="InterPro:IPR009078" FT /db_xref="InterPro:IPR012347" FT /db_xref="UniProtKB/TrEMBL:A1K209" FT /protein_id="CAL92864.1" FT /translation="MKGKTPVISALNALLVDELAARDQYFIHSRMLAEWGLHHAAERIA FT HEMEDETQHASDLICRILFLEGIPAMTPAAITVGADLPDIFAKDLAVEYKVVDNLRAAM FT ALCEAEQDYVTRDILLKMLADTEEDHAHWLEQQLRLISLVGLQNYLQSQMKTGTPGS" FT CDS 276847..277365 FT /transl_table=11 FT /gene="dksA1" FT /locus_tag="azo0248" FT /product="probable dnaK suppressor protein" FT /function="DnaK suppressor protein" FT /note="Probable dnaK suppressor protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K210" FT /db_xref="InterPro:IPR000962" FT /db_xref="InterPro:IPR012784" FT /db_xref="InterPro:IPR020458" FT /db_xref="UniProtKB/TrEMBL:A1K210" FT /protein_id="CAL92865.1" FT /translation="MNARAALPAVFGNFIPAWFHQPAGSKREDFSMNDVLTPLMTEAEL FT RAAPEDDYMSPRQLAFFRALLEKEMKTLLEAAHETTTHLQENAATPDPADRASVEEEHT FT LELRVRDRERKLLKKIEEAIARIDDGSYGWCEETGEPIGIGRLLARPTATLSLEAQERR FT EKLKKMHGG" FT CDS 277409..277567 FT /transl_table=11 FT /locus_tag="azo0249" FT /product="hypothetical protein" FT /note="Hypothetical protein. No homology to the data bank. FT No domains predicted. No signal peptide. No TMHS" FT /db_xref="UniProtKB/TrEMBL:A1K211" FT /protein_id="CAL92866.1" FT /translation="MRCAPARLLPQRLLPGRRIVLNIPARDRRALSLLPSSALSRAVPR FT EPVRRPY" FT CDS complement(277561..278289) FT /transl_table=11 FT /locus_tag="azo0250" FT /product="hypothetical flavodoxin reductase" FT /function="Flavodoxin reductases (ferredoxin-NADPH FT reductases) family 1" FT /note="Hypothetical flavodoxin reductase. Homology to the FT N-terminal part of bb4317 of B. bronchisptica of 40% FT (trembl|Q7WFF6). InterPro: Oxidoreductase FAD and FT NAD(P)-binding domain ((IPR001433); NADH: cytochrome b5 FT reductase (CBR) (IPR001834) Pfam: Oxidorectase FAD-binding FT domain; Oxidoreductase NAD-binding domain no signal peptide FT no TMHs" FT /db_xref="GOA:A1K212" FT /db_xref="InterPro:IPR000951" FT /db_xref="InterPro:IPR001433" FT /db_xref="InterPro:IPR008333" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:A1K212" FT /protein_id="CAL92867.1" FT /translation="MSASMPSRPPPSDRIPVRVRSVRDEARDIRSLEFEAVRGGDLPPW FT PPGAHVLVYPPACPPRAYALCSLPGEAATYRIAVRRDAGTGNTPAQLHALHPGDQLAVS FT APHSSFALDEGAERHLLVAGGIGIAPLLSMFRALERGGAEAELHYFARSEDDAAFLAEL FT EGARARGTLHCHFGLSGGATAARLQDLFATAAQRPGAGAGLAIYTCGPAGLMRAVDVAA FT AANLHAAQLRQQHFGPTLDQ" FT CDS 278417..279895 FT /transl_table=11 FT /locus_tag="azo0251" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein, 38% FT similarity to trEMBL;Q7WDT1,Putative membrane protein FT [BB4906] [Bordetella bronchiseptica (Alcaligenes FT bronchisepticus)]. TMHMM2 predicts 6 TMH's present. No FT signal peptide present." FT /note="Family membership" FT /db_xref="InterPro:IPR021296" FT /db_xref="UniProtKB/TrEMBL:A1K213" FT /protein_id="CAL92868.1" FT /translation="MSVRPPSLSQSPAAPDAVDAAARASFHARWLAEVVRRHEEAHGAL FT PDEAELTAARRAPPRFEDRLLARARLLAAREGWDADLARLARRLRVGAAAALVAAFVVG FT WAAGAAVLGDGGRAVNVVWALGGVLGAHLVGLLVWLGAVAFGLRRGQGGGAWLARAGRA FT AANLLDHGARAGPAAAALFGLLGRGGGLPWAAGLLNHLLWAAALGGAAGSMLLLFATRR FT YGFVWETTILPVGLFVELGSALGRLPAALGFPVPDSTALAAAGVPASAVGDGAAGRGWA FT GWLIGCVLLYGVLPRLLLAGLCAALLRRAVAAVRLDEDQPGHAALRARLLPDSERLGIH FT DADHSGAPPRAPAAPAGGEGALALALELGDDLDWPPPFGAGDIASAADPRCAPRRLDSR FT EQRQAWLAAVRARPPQRLLVAVDARQTPDRGSLGTLVELAACAGCLRVWTLPGSAAGRL FT AQWRTALAERDLATADRAVLTDADAARRWLETGA" FT CDS 279963..281318 FT /transl_table=11 FT /locus_tag="azo0252" FT /product="conserved hypothetical protein" FT /note="conserved hypothetical protein, 54% identity to FT TrEMBL;Q9JYD1 Hypothetical protein NMB1644 [NMB1644] FT [Neisseria meningitidis(serogroup B)]. Has FT PF00009:Elongation factor Tu GTP binding domain:IPR000795 FT ProtSyn_GTPbind: This domain contains a P-loop motif, also FT found in several other families such as Ras, Arf and FT Myosin_head. Elongation factor Tu consists of three FT structural domains, this plus two C-terminal beta barrel FT domains. Elongation factors belong to a family of proteins FT that promote the GTP-dependent binding of aminoacyl tRNA to FT the A site of ribosomes during protein biosynthesis,and FT catalyse the translocation of the synthesised protein chain FT from the A to the P site. The proteins are all relatively FT similar in the vicinity of their C-termini, and are also FT highly" FT /db_xref="GOA:A1K214" FT /db_xref="InterPro:IPR006073" FT /db_xref="InterPro:IPR021871" FT /db_xref="UniProtKB/TrEMBL:A1K214" FT /protein_id="CAL92869.1" FT /translation="MSLLRIAVVGHTNTGKTSLLRTLARDAGFGEVSDRAGSTRHVEGL FT RLFADGEAVIELFDTPGMEDAIALLEHLEGLAGPGERIDGPERVARFLAGAEAAGRYEQ FT EAKVLRQLLASDAGLYVVDARDPVLPKHRDELAILAGCARPLLPVLNFVRAADARPQAW FT REALARLGLHAVVSFDTVAPARDGERLLFEALATLLHGGRGPLARLLAARAREALARQH FT AAQRLGAALLVQLAALRVTVAAEPTAIAAATETLQAAVRAREQACVEALLALYRFRADD FT LSAPALPLVAGRWASDLFNPESLRQLGVRVGGGAAAGAAAGVGVDLLAGGLTLGAAAAL FT GALAGSVLQVAGGYRERLLARVRGQRELTVDDAVLRLLALRLHALVEALEGRGHAALDP FT IRLADPGARRWREAALPAELRRARSHPEWARGEGPGYEAAVQALADAEAAPG" FT CDS complement(281341..282051) FT /transl_table=11 FT /locus_tag="azo0253" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to MCA0921 FT of Methylococcus capsulatus of 54% (trembl:Q60AE3). N FT domains predicted. No TMHs. NO signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K215" FT /protein_id="CAL92870.1" FT /translation="MSSAFRKRLLDAATAPYRPAGHFAWHFARGKLGRDPIFFSLLRHG FT LIPDPATVLDLGCGQGLLSNWITAAARLHDEGRWPADWPPPPRLQGYRGIELMQNDVDR FT ALPALPPGAVVEQGDMRHADYGEANVVFILDCLHYVDIAAQDAVLARVRDTLAPRGRLI FT MRVGDAGAGLPFHLCSWVDRVVTFVRGHRLGTLHCRPVTAWQATLEGLGFRVQTMPMDA FT GTPFANTMLVGSLD" FT CDS complement(282048..282746) FT /transl_table=11 FT /locus_tag="azo0254" FT /product="conserved hypothetical polysaccharide FT deacetylase" FT /note="Conserved polysaccharide deacetylase. Homology to FT rs03397 of R. solanacearum of 62% (trembl|Q8Y2A8). FT Interpro: Polysaccharide deacetylase (IPR002509). Pfam: FT Polysaccharide deacetylase (PF01522). The family of FT polysaccharide deacetylases includes NodB (nodulation FT protein B from Rhizobium) which is a chitooligosaccharide FT deacetylase. It also includes chitin deacetylase from FT yeast, and endoxylanases which hydrolyses glucosidic bonds FT in xylan. No signal peptide. No TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K216" FT /db_xref="InterPro:IPR002509" FT /db_xref="InterPro:IPR011330" FT /db_xref="UniProtKB/TrEMBL:A1K216" FT /protein_id="CAL92871.1" FT /translation="MLAALALNHAALTAAGLWPRSRLLGPNWTRLPAAAAARGEIALTI FT DDGPDPEVTPQVLAQLAAAGARATFFLIGENAARHPQLVADILRAGHEVQNHSQWHRKT FT FSLFGPRRMERDVAAAQHTLTGLGAPLPRFFRAPAGLRNPFLEPVLARHGLTLASWTRR FT AFDTREGEPAAVLARLTRGLGPGDILLLHDGHAARSPGGRAVILEVLPRLLDAVRTAGL FT HPVTLTAALR" FT CDS complement(282948..283649) FT /transl_table=11 FT /locus_tag="azo0255" FT /product="hypothetical protein" FT /note="Hypothetical protein. No good homology to the data FT bank. No domains predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K217" FT /protein_id="CAL92872.1" FT /translation="MSTLQPPPPPPPRARLDQHIVRAGAEPAADVLVLLAGAYDGPADF FT IAAGFADARAARGLALDLVLVESDLAAVCDGSLAHRLQHEVIAPARAAGATRVHTGGIS FT IGALTALMHADACPDEAASLVLLAPYPGNRAISGEIAGAGGLAQWTPAADYPPNDERRG FT WRALQRIAAAGAPPVWLGYGSEDRFARGHALMGAMLPAGAHCRHPGGHDWPTWTALWDH FT ALTWLAPRLHR" FT CDS complement(283646..286057) FT /transl_table=11 FT /locus_tag="azo0256" FT /product="conserved hypothetical membrane protein" FT /function="predicted exporter" FT /note="Conserved hypothetical membrane protein. Homology to FT rsc0429 of R. solanacearum of 52% (trembl|Q8Y2A7). Tigrfam: FT 2A0604s01: protein-export membrane protein signal peptide FT 10 TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K218" FT /db_xref="InterPro:IPR004869" FT /db_xref="UniProtKB/TrEMBL:A1K218" FT /protein_id="CAL92873.1" FT /translation="MSRRPRLAALTIWLAVMAVLALIIARSQFTADMSVFLPRNPTPEQ FT RLLVDQLRDGMVSRLILVGISGGNAETRGRVSQAMAAALHGDARFVSVNNGESGALQEE FT QRWLFDNRYLLSPAVTPARFSTDGLRAALTDTLNLLASPAGMLVKPLVTRDPTGELMQL FT LQRLDPGTQPARDPAHGVWITRDGETALMLALTRAAGSDIDAQEAAMGALQREFETARG FT SAAAATPLRLEMTGPGVFAVESRATIKREVERIAVLGAVLTVGFLLAVYRSLTVLLLGM FT LPVVTGTLAGVAAVSLGFGVVHGLTLGFGTTLIGEAVDYAIYLFVRAGRGPGTAAEDDD FT PDEGRDGFWATIRLGLLTSVAGFAALFASGFPGLAQLGLYSIAGLIAAVLVTRYLLPTL FT LPADFRLRDVRPLGLRLAALANAAGRLPWLVVALAAGAAAVLALRHDGLWNSELLALSP FT VPMRQQELDMRLRTEMGAPDVRYLVVVDGADTETTLRAVEALAPRLDALQADGVIAGWD FT APTRYLPSLATQAARRAALPAREELAARLHAATAGLPLRAERLTPFLDEIDAARQRPPL FT TPESMAGSSLGLAVQAMLIHTEGGVRALLPLRAPEDGTDLIDAGRVRAALAGAGDGSAP FT LFLDLKQESDALYANYLREAIRLALGGVAAVVVLLLVFLRSPRQVLRVVTPLAAAVLVV FT TAGLALAGKQLILLHLVGMLLIVAVGSNYTLFFNRADGRMAAPRTLASLFFANCTTVCA FT FGLLAFSEVPVLQAIGITVGPGAVLALVFSAMLGSRGDARAALPAPACGR" FT CDS complement(286054..286632) FT /transl_table=11 FT /locus_tag="azo0257" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT RS03399 of R. solanacearum of 47% (trembl|Q8Y2A6(SRS)) No FT domains predicted. Signal Peptide present. No TMH FT reported." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K219" FT /protein_id="CAL92874.1" FT /translation="MSRFLSAALLALAFAFTPPPVAAAAWDVPQLMTLLAANGGGRVRF FT TETRHLAMLDAPLVATGELVYVPPARLERHTETPVRETMVLDGDTLSLTREGRNHSLKL FT RDYPEAAALIESIRATLAGDRKALERTYALSLSGSAAQWALDLLPSDPAVTKVVLRIRV FT SGSRGEVRGVEIQQADGDRSVMHIEPPAR" FT CDS complement(286629..287561) FT /transl_table=11 FT /locus_tag="azo0258" FT /product="conserved hypothetical acetyltransferase" FT /function="predicted acyltransferase" FT /EC_number="2.3.1.-" FT /note="Conserved hypothetical acetyltransferase. Homology FT to rsc0431 of R. solanacearum of 61% (trembl|Q8Y2A5) Pfam: FT Bacterial lipid A biosynthesis acetyltransferase no signal FT peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K220" FT /db_xref="InterPro:IPR004960" FT /db_xref="InterPro:IPR014548" FT /db_xref="UniProtKB/TrEMBL:A1K220" FT /protein_id="CAL92875.1" FT /translation="MSVHSTPGQGSTGTEWAQRPERSNMLLLRVMAWISLRLGRPAGRL FT VLHLITTYFVLFTPSARRASRAYLGRALGRPARLADGYRHVHCFASTIHDRLYLLKDRF FT DLFDIRIEGEALIEEVVASGRGALLFGAHLGSFEVIRAVGRHQPDLRIALAMYEDNARR FT INTLLAAINPAARPEVIALGRLDAMLKVRARLAQGALVGVLADRSLESEDRVSLPLLGS FT PAALPAGPFRMAAMLEARVVFMAGLYHGGNRYTIRFLPIADFAGVARDGREAAIAAAMR FT RYADALETCCREAPSNWFNFFDFWGDADR" FT CDS complement(287558..287869) FT /transl_table=11 FT /locus_tag="azo0259" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to xac 4098 FT of X. axonapodis of 36% (trembl|Q8PF87). No domains FT predicted. No signal peptide. No TMHs." FT /db_xref="InterPro:IPR013114" FT /db_xref="UniProtKB/TrEMBL:A1K221" FT /protein_id="CAL92876.1" FT /translation="MSGSRTLAIAADHPAFAGHFPGRPIVPGVVLLDEAVQALEAEFAL FT PPTCWKLASAKFLSPVGPGDVVTLSWQAPAASGAIAFRLACGERAVASGTLAPPDAAR" FT CDS complement(287866..289215) FT /transl_table=11 FT /locus_tag="azo0260" FT /product="conserved hypothetical protein" FT /function="Acyl-coenzyme A synthetases/AMP-(fatty) acid FT ligases" FT /note="Entry name:- TREMBL:Q87EI7 InterPro:- IPR000873; FT AMP-bind. Pfam:- PF00501; AMP-binding; 2. Identity :- 45% FT Prediction: Non-secretory protein Signal peptide FT probability: 0.000 Number of predicted TMHs: 0" FT /db_xref="GOA:A1K222" FT /db_xref="InterPro:IPR000873" FT /db_xref="UniProtKB/TrEMBL:A1K222" FT /protein_id="CAL92877.1" FT /translation="MLPLVTHTSPDAVVARRHGEAITVRHFLADVRKVAAALPAGRHVL FT NACTDRYRFAVGFAAGMVAGKISLLPSTYTPDTLRHLAAFAPDTTVLTDGDVADLPLPA FT MPFPALLDAAAVPAGACDIPCIASEQLVAWVFTSGSTGSPVPHPKTWGRLVVNVQAEGV FT ALGLDPAHPATLVGTVPPQHMYGFESTVLVALQSGAAFDAGRPFYPADIVAALQRAPAP FT AALVTTPFHLRTLLDEGIPVPPAALVVSATAPLPVELAVAAEAAFGAPLLEIYGSTETG FT QIATRRSAQGEAWTLFPGIELAPRDDGHTWASGGHIERAVPMSDVIEQVGARRFLLRGR FT NADLVNIAGKRTSLGYLNQQLLSIPGVRDGAFYLPDDSGGAHIVRLAAFVVAPTLDAAT FT LQAALRERIDAVFLPRPVVWLDALPRNATGKLPRETCAALLAAHAERRAR" FT CDS complement(289232..289885) FT /transl_table=11 FT /locus_tag="azo0261" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT rsc3402 of R. solanacearum of 46% (trembl|Q8Y2A3(SRS)) no FT domains predicted signal peptide 5 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K223" FT /protein_id="CAL92878.1" FT /translation="MTTPLRFGRAALAAVAFAAYLLLAHHTTASGQHPTLGALLAVVPY FT MAAALAMAARARHRGFALALWALGAALLWRQWPVVEARFEWVYLIQHVGTFGLLAIGFG FT RSLGGEPMITRFARLVHGAELALPLVRYTRGATAAWALFFAAMTTASLLLFFGGPLPLW FT SLLVNILTPLLVALMFAAEFLVRRLLLPPGLRTGLVESVRACMHAGRRASPPAA" FT CDS complement(289885..290169) FT /transl_table=11 FT /locus_tag="azo0262" FT /product="hypothetical protein" FT /function="Acyl carrier protein" FT /note="Similar to TREMBL:Q9PFA7 (61% identity); FT TREMBL:Q87AD9 (61% identity); SWISSPROT:Q7VKH6 (34% FT identity)." FT /note="Function unclear" FT /note="ORF1" FT /db_xref="GOA:A1K224" FT /db_xref="InterPro:IPR006163" FT /db_xref="InterPro:IPR009081" FT /db_xref="UniProtKB/TrEMBL:A1K224" FT /protein_id="CAL92879.1" FT /translation="MTHTAPASADAALLAEVAALIVTALNLEVRAEDIEPDAPLYGEGL FT GLDSIDILEVALVVSKRYGFSLRADNEDNLKIFASLRSLGDYIATHRVQ" FT CDS complement(290292..291683) FT /transl_table=11 FT /locus_tag="azo0263" FT /product="probable two-component system histidine kinase" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.13.1" FT /note="Probable sensor protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K225" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="UniProtKB/TrEMBL:A1K225" FT /protein_id="CAL92880.1" FT /translation="MSADALPLPGWSLKRRLLGLLLLVAGGVSALTIVLAYRAAHTEAE FT HAFDAQLVVVAETLMAIAADAGVDYAEHELSEHAYPDTLPVAYQVWGRQDGRVSLLLRS FT ASAPATAMTVHEGLSDGERDGRRWRHYLLRRGDFAVIAGQDHAGRDALARELTLRILLP FT FLLALPLLAAAIWLTVGRALQPVAALAAEVEAMKPDGLNPVGLADPPPQEIAPLLQALN FT RLIGRMAAALAGEQRFTADAAHELRTPLAALRIQAQVAARAGEDSAARERALDQVIAGV FT DRMTHLVDQLLTLARLEPAAAQPAFAPVDLAAVAEAAVAALAPRSAARKQHVECALAPA FT TVSGNAVWLGILARNLIDNALRYAPPGSHIRVRTAREGMRCVLEVSDDGPGLEPGARDS FT LRARFARGVAADGEGCGLGLSIVGRIVELHGGEFRLGDGLPRSAPAGVGLAATVVLAAA FT SPSPR" FT CDS complement(291680..292336) FT /transl_table=11 FT /gene="qseB1" FT /locus_tag="azo0264" FT /product="transcriptional regulatory protein" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="Transcriptional regulatory protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K226" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K226" FT /protein_id="CAL92881.1" FT /translation="MRILLVEDDALLGDGLQAGLRLAGFNADWVRSAEAAETALALEHF FT SAVVLDLGLPGRDGNSLLAALRQRHDDIPVLILTARDAVADKVRGLDLGADDYMVKPVD FT LDELAARLRAALRRAGGRASGVIRHGEVELDPAARRVRRAGAEVALTSREFDLLYVLLS FT RAGTVLTRRMLDEQLYAWDEGAESNTLEVHIHHLRRKLGADLIHTVRGVGYTVPA" FT CDS 292491..292763 FT /transl_table=11 FT /locus_tag="azo0265" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT bd0091 of B. bacteriovorus of 52% FT (tremblnew|CAE77770(SRS)). no domains predicted. signal FT peptide. no TMHs." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K227" FT /protein_id="CAL92882.1" FT /translation="MKTRSAFVVLAACTLSTVALAGPQCTEAPKSQWLPEEAMKQKISA FT AGYTVDKFKVTSGNCYEIYGKDKDGKKVEIYYNPVDGSVAREKRG" FT CDS 292777..293298 FT /transl_table=11 FT /locus_tag="azo0266" FT /product="conserved hypothetical cytochrome b561 family FT protein" FT /function="Cytochrome b" FT /note="Conserved hypothetical cytochrome b561 family FT protein. Homology to rsc2354 of R. solanacearum of 43% FT (trembl|Q8XWW6). Involved in electron transfer from FT hydrogen to oxygene. Pfam: Nickel-dependen hydrogenase FT b-type cytochrome no signal peptide probable 4 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K228" FT /db_xref="InterPro:IPR016174" FT /db_xref="UniProtKB/TrEMBL:A1K228" FT /protein_id="CAL92883.1" FT /translation="MGIERVKVWDLPVRLFHWSLVAAFLTAWLSADDAETLHQGAGYCA FT LGLVAFRVLWGFVGCRHARFVDFVPSPQGLFGYLRAALRGQEPRFRGHNPAAAVMILFL FT LAMIGVIGATGWAMTTDWGWGADWLEEIHEAAAHLTLAAVAVHVAAAIYGSWHHRENLV FT RAMVDGYKRL" FT CDS 293415..294473 FT /transl_table=11 FT /gene="czcB" FT /locus_tag="azo0267" FT /product="putative membrane fusion protein" FT /note="Putative membrane fusion protein. Homology to cnrb FT of A. eutrophus of 30% (pir|F47056). Proteins of the MFP FT family function as auxiliary proteins or FT 'adaptors',connecting a primary porter in the cytoplasmic FT membrane of a Gram-negative bacterium with an outer FT membrane factor protein that serves a porin or channel FT function in the outer membrane. In A. eutrophus is this FT protein involved in cobalt and nickel resistance. No FT domains predicted. No signal peptide No TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K229" FT /db_xref="InterPro:IPR006143" FT /db_xref="UniProtKB/TrEMBL:A1K229" FT /protein_id="CAL92884.1" FT /translation="MSFSVAAPVAAAEAVVLDAARLTAAGIELAPVQAAGAASLAHLPA FT RVVVPSAQQRFVAAPVAGLVAAVLVGSGETVRAGQPLARIASPELLALRRDLTQAGAEQ FT ERARLALQRDQQLHAEGLIPAARLEATRAAAAQAGAALAERRALLGLSGGASEGGGELT FT IVAPIAGVVLAQPAQPGMRVEAAAPLFHIARLDPLALEVDLPPALAAQLKPGLRVRVPA FT GGAEGRVVAVGRAVSGAQTVTVRALLDRGLGALGPGQNVEVEIERGGDAAAGAAPVWAV FT PASALVRLGEDGGGSAVFVRRGDAFVPVPVSVLGEQGGNAVLRGELHADERVAVRGASL FT LKAAAMGIGKGE" FT CDS 294470..297574 FT /transl_table=11 FT /gene="czcA2" FT /locus_tag="azo0268" FT /product="putative cation efflux system protein" FT /function="Putative silver efflux pump" FT /note="Cobalt-zinc-cadmium resistance protein CzcA (cation FT efflux system protein CzcA). In A.eutrophus has a low FT cation transport activity for cobalt, it is essential for FT the expression of cobalt, zinc, and cadmium resistance.Czca FT and Czcb together would act in zinc efflux nearly as FT effectively as the complete czc efflux system FT (czcABC).Belongs to the acrb/acrd/acrf family. 41% FT similarity to the A.eutrophus CzcA protein. FT SWISSPROT:CZCA_ALCEU:P13511 InterPro: Heavy metal efflux FT pump CzcA. InterPro:IPR001036; Acrflvin_res.IPR004763: FT CzcA. Pfam:PF00873; ACR_tran; 1. InterPro:TIGR00914:Heavy FT metal efflux pump CzcA InterPro:PF00873:Acriflavin FT resistance protein Signal peptide: present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K230" FT /db_xref="InterPro:IPR001036" FT /db_xref="InterPro:IPR004763" FT /db_xref="UniProtKB/TrEMBL:A1K230" FT /protein_id="CAL92885.1" FT /translation="MSVLARLVEFSLTQRLLVLVLTALLVGAGAMALRSLPIDAFPDVS FT TTQVKIIVKAPGMTPEEVEARITVPIEQELLGIPAQRMLRAVSKYGITDITVDFDDGTD FT IYWARQQVSERLDAAMSGLPAQASGGLAPITTPLGEMFMFTIEGPLSLEEKRTLLDRVI FT RPQLRTIRGVADVNSLGGHVRSYEVVPNPQLLAARGLGLNLLREAIERNNRNDGAGRLG FT DGEETLIVRAEGAVNEPADLAAVVVATRDGVPVRLGDVAEVRIGSLTRYGAVTRDGAGE FT TVQGLVLGLRGANAQAVIAGVKARLAELAPSLPPGVSIVPFYDRSALVDRAVGTVSKAL FT FEAIALVVVLLLAFLGNLRAALVVALTLPLAALGTFILMRYTGVSANLMSLGGLAIAIG FT MLVDAAVVVVENVETQLAADGVQARLPLLHVVYRAVREVALPVASGIAIIIIVFVPLLT FT LQGLEGKLFVPVALSIVYALASSLVLALTVIPVLASLLLKRGEAHTPWLVRRLDAAYAP FT ALDWALANARTVIAVALLSLALAAAGYAFVGKTFMPTMDEGDLIMQLEKLPSIGLEQTI FT AVDSRVQRTILEQVPEVKSVVARSGSDELGLDPMGLNQTDSFLVLKPVAEWRQPDKAWL FT TDELRRVVAEFPGIDVTFTQPIDMRVSEMLTGVRGDIAIKVFGTDLAALGRAAGEIEAL FT LAAMDGAEDVFTAKNEGVQYLRVEIDHLAAGRLGLSVDDVQSALRSLVEGEQAGAVIEA FT GRRVPILIRADEGVRASASRFADLRLALPGGGAVPLSAVARLERVAGPVKVDRENGSRY FT VTVQSNVRGRDLVGFVEEAQARVAATVKLPAGYRLEWSGQFENQQRAAARLAVVVPVAL FT LLIFLLLFSTFGSVRQAALVLANVPFALVGGVFALLLAGEYLSVPASVGFIALLGIAVL FT NGVVMVTYFNQLIEQGMPLARVVVEGARRRLRPVLMTASIAAFGLVPLLFATGPGSEIQ FT RPLAIVVIGGLISSTLLTLLLLPILFRRFGMDRAPALSAPEALLP" FT CDS 297571..297885 FT /transl_table=11 FT /locus_tag="azo0269" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein.30% identical to FT TrEMBL; Q89MS9. Signal Peptide present." FT /db_xref="InterPro:IPR015867" FT /db_xref="InterPro:IPR021634" FT /db_xref="UniProtKB/TrEMBL:A1K231" FT /protein_id="CAL92886.1" FT /translation="MTATPDTLLTLVAPAALEDKLVDLLLALPGMASGFTTHPASGHGR FT EIALVGANENVRGRGARVCVRLALQSAALQPLLGEVRAALPDANIFYWVTPLLDCGRVS FT " FT CDS 297885..299159 FT /transl_table=11 FT /locus_tag="azo0270" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. Homology to cnfc of FT Ralstonia sp CH34 of 28% (tremblnew|CAB82451(SRS). Pfam: FT outer membrane protein. Interpro: Type I antifreeze protein FT (IPR000104). singal peptide. no TMHs" FT /db_xref="GOA:A1K232" FT /db_xref="InterPro:IPR003423" FT /db_xref="UniProtKB/TrEMBL:A1K232" FT /protein_id="CAL92887.1" FT /translation="MAAFLSRRGAVLAPLAALMLALPARAADYPAELPPLPMLQAAIEA FT APEVRAAEALREGGEAERRQLAAGPYEWTLNADYGRRRTREAGVTARTGEWEVALERPL FT RLPGKAGLDERLGDLKVKAAELGLADARHETARALLAAWYDWLREQAGAGVLRAQAEAA FT AREAAAVTRRAELGDASRLDAMQAEAAAAQAAAAARLGEGRAAAAAAGLRQRYPQLALP FT ARPPLPDPAPPGADLQELVELALEHDHGLLLARSAAARAEAESQRAAAQRRPDPTFGVR FT YGRERDSAEHMVGAYVAIPLGGSYRNATADMARASAAAAAEQANAAERRLAGELRARHE FT MVIATHDHWRLAEDSAARLAAAAERLALAQRLGEAPLAEVLLARRQALEAALQASGARV FT DALAEQASLRLAAHRLWADGEDHGE" FT CDS complement(299301..300887) FT /transl_table=11 FT /locus_tag="azo0271" FT /product="conserved hypothetical protein" FT /function="Fe-S oxidoreductase" FT /note="Conserved hypothetical protein. Homology to FT Daro03000974 of Dechloromonas aromatica of 68% FT (gi|46140980|ref|ZP_00152750.2|(NBCI ENTREZ)). Pfam: FT Elongator protein 3, MiaB family, Radical SAM. This FT superfamily contains MoaA, NifB, PqqE, coproporphyrinogen FT III oxidase, biotin synthase and MiaB families, and FT includes a representative in the eukaryotic elongator FT subunit, Elp-3. Some members of the family are FT methyltransferases; Pfam: B12 binding domain. This domain FT binds to B12 (adenosylcobamide), it is found in several FT enzymes, such as glutamate mutase Q05488, methionine FT synthase Q99707 and methylmalonyl-CoA mutase. no signal FT peptide. no TMHs" FT /db_xref="GOA:A1K233" FT /db_xref="InterPro:IPR006158" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR023404" FT /db_xref="InterPro:IPR023970" FT /db_xref="UniProtKB/TrEMBL:A1K233" FT /protein_id="CAL92888.1" FT /translation="MPGQPDFTLLANRMAPIGILQLASWLEKHGHPTQLHDCMGPYAPA FT SLEANVAQIIATKPELVGFSATTSGFMDAVDMAEQIKQKLPHVKTFFGNVHTSSIGAPL FT LEHFPEIDYLCIGEGEGAILDVANGMAPKDIANIIYRDDAGRAVINERRTRILDLDELP FT FPAYEKLAGFPHGYHLPLFSYEKRWGATMITSRGCPYTCSFCDRTVYERLYKYNSAQYV FT HDHIRHLRDTFGVHHINIYDDLFTAHKKRIHELCELLIAKPLGVDFNCAIRTGHTSDEM FT LALLKRAGALMVSMGIESADPGMMERHKTGVTLEAVKKTVEQIHTAGLRAKGLFIFGLP FT GETPETLKKTSDFILELDLDEMNMTKFSPMYGAPIWDECVSGKEGDFNEDWRLMNCLNF FT VFKPNGFESREQMDALYNWHVRRYYDSKAYRRRFSKRIWQHRWSLWHLLKNAPRVIQAA FT RYFSANKAQIEAAARDFAPHPRQPRGLQPFLSPELQADALAAMSPVKISRKPKPKVEDA FT TAIAAPRIQAA" FT CDS complement(301090..301368) FT /transl_table=11 FT /locus_tag="azo0272" FT /product="hypothetical protein" FT /note="Hypothetical protein. No homology to protein of FT similar size in the data bank. No domains predicted. No FT signal peptide. No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K234" FT /protein_id="CAL92889.1" FT /translation="MNTPSPADPLRKRLRALPPPAAGTALRARLLADADARLPHPAAWW FT QPLWRTGLAAMAVVAVCAFGVNEYLAWQEIQELAELDTLSTATMLLL" FT CDS complement(301346..301972) FT /transl_table=11 FT /gene="sigW" FT /locus_tag="azo0273" FT /product="putative ECF-family RNA polymerase sigma factor" FT /function="DNA-directed RNA polymerase specialized sigma FT subunit sigma24 homolog" FT /note="Putative RNA polymerase sigma factor, Myxococcus FT xanthus carQ; Alcaligenes eutrophus plasmid pMOL28-encoded FT cnrH; Escherichia coli fecI; Pseudomonas syringae hrpL; FT rpoE from Escherichia coli, Salmonella typhimurium and FT Haemophilus influenzae; Streptomyces coelicolor sigE; and FT Bacillus subtilis sigma factors sigV, sigX, sigY and sigZ." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K235" FT /db_xref="InterPro:IPR007627" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR013249" FT /db_xref="InterPro:IPR013324" FT /db_xref="InterPro:IPR013325" FT /db_xref="InterPro:IPR014284" FT /db_xref="UniProtKB/TrEMBL:A1K235" FT /protein_id="CAL92890.1" FT /translation="MSLAALLPASWRADATLLAAALDGDRRAVAALVDRLAPQGHALAW FT RLTGSRAEAEDAVQEAFLRLWRDGGRLEARGQISTWFLTVVRNLCFDRLRRRDDPLDDE FT TRDTLVDDGPTPEDRLLLTAAASELHAALERLPPRQRHALMLWAWQDHDVGQIADALDI FT APNAAHQLLFRARRSLRQAVEAIRAASTHPVSAVKDIGHEYPQPR" FT CDS complement(301969..302409) FT /transl_table=11 FT /locus_tag="azo0274" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT XCC0845 of X. campestris of 30% (trembl|Q8PC89). No domains FT predicted. Signal peptide. No TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR021455" FT /db_xref="UniProtKB/TrEMBL:A1K236" FT /protein_id="CAL92891.1" FT /translation="MTSPLHRLLFAACLLAAWPPAHAAAPAVPELGQWFTLEPAVRRER FT AHQIREQLADASPAERQAFRAALRERLAALPPERRRSVADQLQQEWRELSPQERDAMRA FT ERRAYLRSLSREERRQLLEDRRAMLQRLSPEERQRWQQGLER" FT CDS 302583..302924 FT /transl_table=11 FT /locus_tag="azo0275" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT CC3220 of Caulobacter crescentus of 34% FT (trembl|Q9A3I4(SRS)) No domains predicted. Signal Peptide FT present. NO TMH present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K237" FT /protein_id="CAL92892.1" FT /translation="MYAFRSSLFALIAALVVAPSLVHAETPAERMAQRIDNRQARQEQR FT IDKGVASGALTAREAARMERQQGHVDRVEDRALADGTLSRREAVHMERLQDRTSRHIAV FT QKHDRQVSR" FT CDS 303050..303640 FT /transl_table=11 FT /locus_tag="azo0276" FT /product="Hypothetical protein" FT /note="Putative Hypothetical protein. No Good homologous FT hits in the DB. No domains/features/signal peptide or FT motifs present." FT /db_xref="UniProtKB/TrEMBL:A1K238" FT /protein_id="CAL92893.1" FT /translation="MASVPPGFKPGIANLEKAWGSSPELVGHAQWSGMDAIDLETLQEF FT CRAERKLLIFRAPGGLGRQVRGLGVEILPKPAAMKQKTHGRWIVQDGRLYTSDWDLLSA FT WQRTGNGYSRFELGADSRQTAEFLKRINRQLLFPLQHGANDDYLDEAGNARNRAIGERF FT IAIDETGGIDRCETQVLMKAYYATRGLAPWLYG" FT CDS 303727..304134 FT /transl_table=11 FT /locus_tag="azo0277" FT /product="Hypothetical protein" FT /note="Hypothetical protein. Weak Homology. 39% identity to FT TrEMBL;Q8EWG7. No domains, repeats, motifs or features FT present." FT /db_xref="UniProtKB/TrEMBL:A1K239" FT /protein_id="CAL92894.1" FT /translation="MKAAQLQVSYDLIGPANWKGKYTSNNPYNSPNWTWYKDGNNRLTN FT YPHITLAFNEVWEVAKNGEWVGFHVSYPLSRSGKNARFNYTIRNGVVTFNNMTRKGFTD FT MALAEAEEISRDNWQDIDAFAEAFYRAATNT" FT CDS complement(304110..304865) FT /transl_table=11 FT /locus_tag="azo0278" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. Signal peptide. 1 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K240" FT /protein_id="CAL92895.1" FT /translation="MSLPVLTSARCLRPALMAAALTCTALPAHALVVPGALEAVEGNIN FT NAFPFIPDPLRAQQVYDASAFAGVGGPLLLTGLAFRPDAVDGAPQAWVVPDVRIHLSTT FT SAGPDRLSTTFADNVGSDDTEVLRGALSLSTADLPGPGGTRLFDIVIRFTTPFRYDPAR FT GNLLLDIFSAGGSPVVSYDAHNLAGDAISRVIGDLDTARGIADSSGLVTAFDFVALAVP FT APGTLALLLAAALALPAARRRPQVLVAAR" FT CDS 305070..305825 FT /transl_table=11 FT /locus_tag="azo0279" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to BB1132 FT of B.bronchiseptica of 42% (tremble:Q7WNA8). No domains FT predicted. No Signal peptide or TMH present." FT /db_xref="InterPro:IPR021783" FT /db_xref="UniProtKB/TrEMBL:A1K241" FT /protein_id="CAL92896.1" FT /translation="MAQGLPRTRFNTSALQRALAGLVVEEPGESRQPFAERLGQWLDFK FT DALALFSVLDARPGEAATAAAAASPLGAELARVRSTLAQAIGADGASAPGVGRIAAPLP FT PLDGGPEALADFAPYQRYCLARQRDMQAAIATLRGDARAALARHSAALARLAALDAVLE FT QGLAVRERALLATIPALLAQRFEQLLAAHRAAQPAGTADDPAGWSRPGGWLATFRADLR FT TVLLAELALRLQPVSGLVEALEGAPAAGA" FT CDS 305877..308081 FT /transl_table=11 FT /locus_tag="azo0280" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT rs03062 of R. solanacearum of 48% (tremble:Q8XQ05) no FT domains predicted signal peptide 2 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR008520" FT /db_xref="UniProtKB/TrEMBL:A1K242" FT /protein_id="CAL92897.1" FT /translation="MNRTACAAAFVVGLVVVGWVGYGYLGGSPLALTMTALIAAVYVAG FT ATEMLRFQRATAALQRALADIPPQLADPAAWIATLPPTLRNAVRLRLEGERVALPGPTV FT TPYLIGLLVLLGMLGTFLGMVVTLNGAVVALESTTDLQTIRAALAAPVKGLGVAFGTSV FT AGVAASAMLGLITTLCRRARQQAAHLLDARIATALRPFSRAHQRDEGFKAMQQQARLLP FT ELVDALGTLMAQLERRSGEAEQRLAAEQARFHREAREAYSELAAAVGRSLQASLSESAR FT LAGETIKPVVDTTMAGIARETAALQARVADAVQAQLDGAGARFDSAVTRVTASWTAALE FT QHQRANAAVGAQIEAALGAHAERVDQHSAALLASVAQAHDALRGELATTAARLTDDTAA FT LHARLAAGTERHLDGLATRFDAAVSAVSETWTRALAEHERSGSVLIERLDGALGAFAGR FT FDDRAGALLAEVAERSASLQAALASQEEARLAAQRAALAELAGSLQQRWAEAGADSEAR FT QQRICQTLDDTARALVAETKAQASGTLAEVGALMERAAEAPRAAAEVIGELRKELSASV FT ARDNELLAERSRIMETLRALLDAINHASTEQRSAIDALVASSAAALEQAGTRFGDTVAT FT ESSRMADAAGLLAGGAAEVASLGEAFQLALRLFGESNTQLMESLQRIEGALDKSMARSD FT EQLAYYVAQAREIIDLSIGSQQQIVDDLRRLSAPALAGGV" FT CDS 308084..308728 FT /transl_table=11 FT /locus_tag="azo0281" FT /product="conserved hypothetical outer membrane protein" FT /note="Outer membrane protein A precursor. Homology with FT hypothetical transmembrane protein and probable outer FT membrane protein of 56% as well as with motB (flagellar FT motor protein B) from amino acid 84 of 34%. Pfam: OmpA no FT signal peptide probable 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K243" FT /db_xref="InterPro:IPR006665" FT /db_xref="UniProtKB/TrEMBL:A1K243" FT /protein_id="CAL92898.1" FT /translation="MDEIDGGIEHAAPVWAVFADLMSGLLGAFVLILVGVLGVQMELAS FT SLEAEVQKRRVEEQRREALEKALAVPLASGRVTLANGRIGISGSVLFALNSDELQPDGR FT QLLKSLAPPLAAYLASHDEMLMVSGFTDDRPVRDSNRQFADNWELSAQRALTVTRVLVE FT EGVPSAAVFAAAFGQEQPVASNADADGRARNRRVEMAPVPRSAKAAGADRG" FT CDS 308721..309476 FT /transl_table=11 FT /locus_tag="azo0282" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to RS03060 FT of R.solanacearum of 35% (tremble:Q8XQ03) No domains FT predicted. No signal peptide or TMH present." FT /db_xref="InterPro:IPR021549" FT /db_xref="UniProtKB/TrEMBL:A1K244" FT /protein_id="CAL92899.1" FT /translation="MAEAEATTVAADGASAQTLIEALRARGAARFDAVGFRFLDALAAR FT LAALDGAAKQRLESRLAEAAAALGERMDAAAREAEACCAAAAARFPAAAAALAKDLAAG FT DFTALRRRIAALEAGLAPGPLGELVARLQRPAADAPEAAAEPGGAPAELRSLRRFRRTW FT SRLSTEQQLAEAFAQAPENAGPLNAHFLVLRALTRMRDLAPAYLEQFVSYANTLLWLEQ FT VEAGRAAAQKPGARAERGRKRKPAAGGAS" FT CDS complement(309473..310132) FT /transl_table=11 FT /locus_tag="azo0283" FT /product="hypothetical protein predicted by FT Glimmer/Critica" FT /note="Hypothetical protein predicted by Glimmer/Critica. FT no homology to the data bank. no domains predicted. no FT TMHs. no signal peptide" FT /db_xref="UniProtKB/TrEMBL:A1K245" FT /protein_id="CAL92900.1" FT /translation="MIALAAFYRQHYDAAALSAAARTCCAVPLRRAGAMTELVLTGVHA FT CLDSQPPRPTALIWGSRTGIRHATARVVGDLCISGEAPMPFDFLATQPALAAVPVQQTF FT PCVVNAVYQPWQAEADAHWARMLHLAIAWLQSGRHERVLCAQVEPATEHPQGDWLVLQR FT GDGAAWPEVQVGLADGTHGAGSAALFDWLEAGIGKGFVLRGADALPALRFYRAGAR" FT CDS complement(310129..311193) FT /transl_table=11 FT /locus_tag="azo0284" FT /product="putative Beta-ketoacyl synthase family protein" FT /function="3-oxoacyl-(acyl-carrier-protein) synthase" FT /note="Pfam (PF02801): Beta-ketoacyl synthase, C-terminal FT domain. Pfam (PF00109): Beta-ketoacyl synthase, N-terminal FT domain." FT /note="Function unclear" FT /db_xref="GOA:A1K246" FT /db_xref="InterPro:IPR000794" FT /db_xref="InterPro:IPR014030" FT /db_xref="InterPro:IPR014031" FT /db_xref="InterPro:IPR016038" FT /db_xref="InterPro:IPR016039" FT /db_xref="UniProtKB/TrEMBL:A1K246" FT /protein_id="CAL92901.1" FT /translation="MNPAAPPRRAVHVARLGHCSARGHDAPSAAEALLAGADDTATREL FT LDARHPWFELPLAENGWTARARAAVTAVGAQLTAGMDPARVAALPLFIGSSSLQAGAIE FT AAARAGGCVEMPPDAAAFAADVAAWLGIGSVPWTFSTSCTSGLAALDAAATLIAAGLID FT EALVLGFEFANDTTLAGFAGLGILAATPEADGLVLGEAVGGVLLSATPGAAGWRVAACR FT LGVDGYSPTAPAPDGGVIAKVIAAALADAGLHSADIALLKPHRGQLASTDAAEAAALQR FT VFGAAPPPAVALKRQLGHTLGASGLVELGALLAMLDAPAGRARHGSPRHLLLNLIGFGG FT SIAALVLSRSGGQP" FT CDS complement(311190..311462) FT /transl_table=11 FT /locus_tag="azo0285" FT /product="conserved hypothetical acyl carrier protein" FT /note="Conserved hypothetical acyl carrier protein. FT Homology to psptO5093 of P. syringae of 44% FT (trembl|Q87V48). Interpro: Phosphopanteteine-binding FT (IPR00613). Pfam: Phosphopantetheine attachment site FT (PF00550) Phosphopantetheine (or pantetheine 4' phosphate) FT is the prosthetic group of acyl carrier proteins (ACP) in FT some multienzyme complexes where it serves as a 'swinging FT arm' for the attachment of activated fatty acid and FT amino-acid groups. Tigrfam: acyl_carrier: acyl carrier FT protein. no signal peptide. no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K247" FT /db_xref="InterPro:IPR006163" FT /db_xref="InterPro:IPR009081" FT /db_xref="UniProtKB/TrEMBL:A1K247" FT /protein_id="CAL92902.1" FT /translation="MTALTHELKVLIVDACDKACDPATISDDEILFGPEAPLALDSLDA FT LQVSMALQKKYGVRLTDSKETRRILASVANLAAFLQAHGKTGTSA" FT CDS complement(311480..312718) FT /transl_table=11 FT /locus_tag="azo0286" FT /product="putative ABC transporter permease" FT /function="ABC-type multidrug transport system permease FT component" FT /note="Similar to TREMBL:Q7NFQ1 (27% identity); FT TREMBL:Q97E48 (20% identity); TREMBL:Q8FWI9 (21% identity). FT TMHMM predicting six transmembrane helices. TC (2.A.6.2): FT The (Largely Gram-negative Bacterial) Hydrophobe/Amphiphile FT Efflux-1 (HAE1) Family." FT /note="Specificity unclear" FT /db_xref="UniProtKB/TrEMBL:A1K248" FT /protein_id="CAL92903.1" FT /translation="MAGAPLPLTRLRALWRKETLTLLRDRHALAALFLMPAIFILVMSL FT ALRDAFVPGVQSELAYAVVDLDRSPASQELVERLDRIAVLRAQGVLDNEAAGRGAVADG FT RLAFALVVPAGFGERLAARQGDEGAPPLRVLADPTVPRAVQSGFEQQVAAEAARLRVLT FT LLDGLGRKLMVPELRRQVGIDASPRVISEAVRSDAGAAAPPAVVPSSVQQSVPAWLIFS FT MFFVVVPLSAVFIAERQQGTLQRLATQQVPFGLVLAGKLLPYFVVNQVQAVVMVMVGRW FT LVPLAGGEALTLPAGAASLVALWLMAAAVSVAAVAWALLIASLTRSSEQATIVGGVGNI FT LMGALGGIMVPKFLMPPEMQTLTQLSPMAWALDGFHRVMLLGDGVAGILPQAATLLCFG FT LAALAAAILRTGR" FT CDS complement(312733..313155) FT /transl_table=11 FT /locus_tag="azo0287" FT /product="conserved hypothetical protein" FT /function="predicted nucleic acid-binding protein contains FT PIN domain" FT /note="Probable DNA mismatch repair protein mutS. FT TREMBL:Q92SQ4:42% identity, 55% similarity. FT InterPro:IPR002716; PIN. Pfam: PF01850; PIN Absence of FT signal peptide Absence of transmembrane helices L17: FT ribosomal protein L17" FT /note="Function unclear" FT /db_xref="GOA:A1K249" FT /db_xref="InterPro:IPR002716" FT /db_xref="InterPro:IPR022907" FT /db_xref="UniProtKB/TrEMBL:A1K249" FT /protein_id="CAL92904.1" FT /translation="MIYLDTSVLGAIFFREPGAAALVEQLERVRADGLLISAWTLTEMA FT SVGGIKQRTGSIDAALRQQALSNFQRFASAELRTVEVEPADFRTAAVFIDCPVALRAGD FT AVHLAVTRRSGARIASLDRRLGDAADALGIPRFQLA" FT CDS complement(313152..313379) FT /transl_table=11 FT /locus_tag="azo0288" FT /product="hypothetical protein" FT /note="no significant homologies" FT /db_xref="InterPro:IPR006442" FT /db_xref="UniProtKB/TrEMBL:A1K250" FT /protein_id="CAL92905.1" FT /translation="MKTATIADAKTHLSSLIADIEAGEDVVITRRGRAVARLVAEPAAE FT EFGWAALKSWVAEEATTGLSVADMRERDLL" FT CDS complement(313482..314405) FT /transl_table=11 FT /locus_tag="azo0289" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type multidrug transport system ATPase FT component" FT /note="ATP-binding cassette (ABC) transporters form a large FT family of proteins responsible for translocation of a FT variety of compounds across biological membranes. They are FT composed of two transmembrane domains responsible for FT binding and transport and two nucleotide-binding domains FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the TMDs, TREMBL:Q8R788 (35% FT identity); TREMBL:Q81S77 (37% identity). InterPro FT (IPR003439): ABC transporter. InterPro (IPR003593): AAA FT ATPase. InterPro (IPR001687): ATP/GTP-binding site motif A FT (P-loop). Pfam (PF00005): ABC transporter. TC (3.A.1): The FT ATP-binding Cassette (ABC) Superfamily." FT /note="Family membership" FT /db_xref="GOA:A1K251" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A1K251" FT /protein_id="CAL92906.1" FT /translation="MLRARDLTYRYRPEQPPALDGVSLDVPAGSLFGLLGPNGAGKTTL FT ISLVAGLLAPQGGSLEYDGRPLARARRAQPNAIALVPQDHAFYPTLTVAENLDFFAGVQ FT GLGGALARQRVGAALAFGQLDSYAKRRAGELSGGLKRRLNLAIGLLADPQLLLLDEPTV FT GVDPQSRHFLLDAIRELRTAGKTVIYTSHYMDEVEALCEQVAIVDHGRVLVQGTLAEVL FT RDTEPVLTLQLDRPPPAALAAAWTARHPGLEIDATAVRVPGATAAELPALLAELAAAGC FT TPHSLGYGEQNLEQVFMRLTQRSLRD" FT CDS complement(314413..315417) FT /transl_table=11 FT /locus_tag="azo0290" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT Daro03001929 of Dechloromonas aromatica of 68% FT (gi|53730629|ref|ZP_00348881.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K252" FT /protein_id="CAL92907.1" FT /translation="MADFQHQHASHCESGVMSAIVRHYGLPFSEPMAFGLASALSFAWL FT PFVKLGGLPLVAYRMPPKAIIRGLRKPLALDMRFETFRDPARGMARLDELLAQGKVVGL FT QTSVFWLPYMPEDLRFHFNAHNVLVYGRDAASGDYLLSDPVFEHPVRCAAEDLSRARFA FT RGVLAPKGLLYYPANRPSAPDWGKAIPAAIRKTERIMLKAPLPLIGARGIERAARAVGR FT LPAQDKDGDVRHSKLFIGHLVRMQEEIGTGGAGFRYLYASFLEEGAELAQRPALKEFSG FT RLVEIGDRWREFALAAARMIRDRDPLDPPRLAAMLSERAAEERAFFTDLGRAL" FT CDS complement(315418..315813) FT /transl_table=11 FT /locus_tag="azo0291" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT Daro03001928 of Dechloromonas aromatica of 59% FT (gi|41724574|ref|ZP_00151411.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K253" FT /protein_id="CAL92908.1" FT /translation="MDIDDVPQEGNRSLGGHRKALYARGADGQLALVPSRGWEAEEIVT FT RQAVEELDRLAAEAQERARAGTGSALEYHMYKARMDSLMLAQVTGLWHWRVRRHLRPEV FT FRRLRPALLARYAEALGLDLATLTRIP" FT CDS complement(315826..316980) FT /transl_table=11 FT /gene="darB" FT /locus_tag="azo0292" FT /product="probable 3-oxoacyl-[acyl-carrier-protein] FT synthase" FT /function="3-oxoacyl-[acyl-carrier-protein] synthase III" FT /EC_number="2.3.1.41" FT /note="3-oxoacyl-[acyl-carrier-protein] synthase (EC FT 2.3.1.41) (Beta- ketoacyl-ACP synthase III) (KAS III). FT Catalyzes the condensation reaction of fatty acid synthesis FT by the addition to an acyl acceptor of two carbons from FT malonyl-ACP. Catalyzes the first condensation reaction FT which initiates fatty acid synthesis and may therefore play FT a role in governing the total rate of fatty acid FT production. Possesses both acetoacetyl-ACP synthase and FT acetyl transacylase activities. Its substrate specificity FT determines the biosynthesis of branched- chain and/or FT straight-chain of fatty acids (By similarity). Entry name FT trembl|Q84H29(SRS) Identities = 238/384 (61%) Prediction: FT Non-secretory protein Signal peptide probability: 0.0 FT Number of predicted TMHs: 0 Pfam:- Beta-ketoacyl synthase, FT N-terminal do Accession number:-Pf00109" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K254" FT /db_xref="InterPro:IPR013747" FT /db_xref="InterPro:IPR016038" FT /db_xref="InterPro:IPR016039" FT /db_xref="UniProtKB/TrEMBL:A1K254" FT /protein_id="CAL92909.1" FT /translation="MAEARAVYITATAAFLPNAPVGNDDIEAVLGRIGGRPSRARRLVL FT RNNGIESRHYAIDPASGAATHTNAQLTAAAVRALEAPGFALDTLECLVTGTSLPDQLMP FT NHGVMVHGELGTPACEVVSTAGICLAGMTALKYAWLSVLAGNSRNAVASGSELASAVMR FT AAHFEAENEARVDALETHPEIAFEKDFLRWMLSDGAGAFLLQDAPRPDAPSLRIDWFEL FT SSQAHAQPACMYAGADKDADGSLRGWARFSAAEWGRRSIFAVKQDVRQLNEQVVRQTLE FT IPLASLIARRGLKADAIDWFLPHMSSAYFRQPVADCLARLGCAIPPERWFTNLAQRGNT FT GSASIFIMLDELVRSGRLRRGQRLLCFVPESGRFSSGFLHLTVV" FT CDS complement(316973..317914) FT /transl_table=11 FT /gene="darA" FT /locus_tag="azo0293" FT /product="probable dialkylrecorsinol condensing enzyme" FT /note="Probable dialkylrecorsinol condensing enzyme. FT Homology to darA of P. aurantiaca of 56% FT (trembl|Q84H30(SRS)) no domains predicted no signal peptide FT 1 TMHs" FT /note="Family membership" FT /db_xref="UniProtKB/TrEMBL:A1K255" FT /protein_id="CAL92910.1" FT /translation="MKKVLVVHYSQTGQLADIVGTLLQPLRAAGVAIHEEVLRPAQPHP FT FPWPFFEFLDVFPESVRLDAAPNLPLTVPADADFDLVILAWQVWYLSPSLPVTAFLKSA FT EGRRLLAGKPVVSVVACRNMWMTAHEKLAALLADAGARLVDHVALTDGAHPLATFITTP FT RWMFTGRRDRFLGLPRAGVAGEDVAGAARFGSALAAALAADRERSGEPMLAGLRAAVVN FT PRLVISERAGQRAFKVWSALVRACGRPGQRRRRPALALFALYLVTLIITVVPASLALQT FT LFAPLLRARLERLRAQYEQPSGSADFRLTRNG" FT CDS complement(317928..319742) FT /transl_table=11 FT /locus_tag="azo0294" FT /product="putative penicillin-binding protein" FT /function="Beta-lactamase class C and other penicillin FT binding proteins" FT /note="INVOLVED IN CELL WALL BIOSYNTHESIS AND MAY ALSO ACT FT AS A SENSOR OF EXTERNAL PENICILLINS, TREMBL:Q7UMP8 (30% FT identity); TREMBL:Q988N4 (27% identity)." FT /note="Family membership" FT /db_xref="InterPro:IPR001466" FT /db_xref="InterPro:IPR012338" FT /db_xref="UniProtKB/TrEMBL:A1K256" FT /protein_id="CAL92911.1" FT /translation="MPASPRPAARIAHPVAALARRLLAPAAILLLGACAAIQPPPRPAH FT VGSGDYAYTRDYLRWLIGQEMEENRITGLSIALVDDQRVVWAEGFGKEDAERDVAAGPH FT TRYRMGSIAKVLTATAAMQMAERGEIDIDRPLADYLPGFSVRSRFDDRTPITPRNIMHH FT HSGLPANYLKGMMGGDPPPFTTLVEAVREEYVAYPPEFIFGYSNLAVTLLGAALEQRAG FT LPFADHMAKSLIEPLGMTETRFESNPALRVYDARGQIEALPLRDLPSGGLVSSVADMSR FT FMRMVFAGGRSGNTQLLRPETLHEMLRAQNEHIALDLGFRVGLGWLLSGIEIRNAGLVA FT SHGGTLFDSHSMMVVLPEHKLGVIVASNSGTSQGTVKKIATEALIHALEAKAGIRQPEA FT AAIAQPEVRLAPEQLASYSAWYDSMVGLIRVKPRAGALDADVMGHTLQLRAQPGGQFGL FT RYKLFGLIPVQVGAFDGVRISAAAIGGHEVLVGHFGDDTMLVGEKLAPRPIPRTMLDYV FT GEYEIVGKPPGLAPDRLALRVEDGMLIGECSFSELPGFMLRIALNPISPTEAVISGLGT FT GKGETIRILPGEGRRLLFSGLELRQKTN" FT CDS 320022..320456 FT /transl_table=11 FT /locus_tag="azo0295" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to CV2374 FT of C.violaceum of 31% (tremble:Q7NVG9). No domains FT predicted. No signal peptide or TMH present." FT /db_xref="InterPro:IPR007791" FT /db_xref="UniProtKB/TrEMBL:A1K257" FT /protein_id="CAL92912.1" FT /translation="MTDATPDAAPAAPDPQRLTIARLIALTLIADGDLASRELEALDRH FT RIAELVGVPRDLLIQTVIDHCRTLRAGEAPGTLRVLDLERTERMLDSITDPALRALACR FT AMLVLSKADGRITLPEQTLLRHALTRWGLSLEAIAADAAS" FT CDS complement(320512..321492) FT /transl_table=11 FT /locus_tag="azo0296" FT /product="probable metallo-beta-lactamase superfamily FT protein" FT /function="Zn-dependent hydrolases including glyoxylases" FT /EC_number="3.5.-.-" FT /note="InterPro:IPR001279- Metallo-beta-lactamase FT superfamily,glyoxalase II family, that catalyse the FT hydrolysis of S-D-lactoyl-glutathione to form glutathione FT and D-lactic acid. TREMBL:Q7WEK1-55% Identity. FT Pfam-Presence of phosphoribosyltransferase, tissue factor, FT and GMP reductaseC like domains Signal P predicting signal FT peptide and TMHMM predicting transmembrane helices. ccoP: FT cytochrome c oxidase cbb3-type s" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K258" FT /db_xref="InterPro:IPR001279" FT /db_xref="UniProtKB/TrEMBL:A1K258" FT /protein_id="CAL92913.1" FT /translation="MHLPRARHWILAAAIATAAPLLSLSAAHAEAPQVKTQAPGFYRMA FT LGQFEITALYDGYVDLDPKLLKNASQRDIQRLLAHRFQDGPKMQTAVNAYVINTGSKLV FT LVDAGAAKVFGPSLGYITDNLKAAGYDPAQIDAVLLTHLHGDHANGVVGADGKAVFPKA FT VVYAAQNDADFWLAEGALEKAPESGKPFFQMAQAAVAPYRADNRFKTLQDGDEIVPGIK FT AVAAYGHTPGHSGFLVESGDKRLLIWGDIVHNAAVQFAKPEVAIEFDVDSKQAVRTREA FT VFKRVAREKLLVAGMHLPFPGIGHVRRAEKGSYEWVPVDYSPVRE" FT CDS complement(321614..321958) FT /transl_table=11 FT /locus_tag="azo0297" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein, 66% similarity to FT TrEMBL; Q6NA86. Signal peptide present. No TMH reported FT present." FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR013096" FT /db_xref="InterPro:IPR014710" FT /db_xref="UniProtKB/TrEMBL:A1K259" FT /protein_id="CAL92914.1" FT /translation="MALPPHGTLLGTLPPAGAEERFERLLQTDAACIERIVSNGQASPP FT GFWYDQPDDEWVMLVAGQAELLFDDAGAHTRLALRAGDWVTIPARLRHRVESTSADAVW FT LAVHLRTAPR" FT CDS complement(321964..322572) FT /transl_table=11 FT /gene="paaY" FT /locus_tag="azo0298" FT /product="probable phenyl acetic acid degradation protein" FT /function="Carbonic anhydrases/acetyltransferases FT isoleucine patch superfamily" FT /note="pathway:carnitine metabolism (conversion of FT carnitine to gamma-butyrobetaine). TREMBL:Q9F9V3: 71% FT identity, 83% similarity similarity:belongs to the FT transferase hexapeptide repeat family Carnitine operon FT protein caiE. InterPro:IPR001451; Hexapep_transf. FT Pfam:PF00132; Hexapep InterPro: Bacterial transferase FT hexapeptide repeat TIGR00094: conserved hypothetical FT protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K260" FT /db_xref="InterPro:IPR001451" FT /db_xref="InterPro:IPR011004" FT /db_xref="InterPro:IPR011974" FT /db_xref="UniProtKB/TrEMBL:A1K260" FT /protein_id="CAL92915.1" FT /translation="MPCYEIDGLKPVIHPTAYVHPDAVLIGDVIIGPRCYVAPLASLRG FT DFGRIVMEEGSNIQDSCVMHGFPGTDTVVGVDGHIGHGAILHGCQVGRNALIGMNAVVM FT DNAVIGDSAIVAASAFVKAGMEVPPRTLVAGMPAKVVRELSDQEVSWKMDGTRTYQDLT FT VRSLATLKPCEPLAEMEPGRKRFEMPGVVPLVDAKKNGG" FT CDS complement(322766..324430) FT /transl_table=11 FT /gene="paaZ" FT /locus_tag="azo0299" FT /product="conserved hypothetical dehydrogenase" FT /function="NAD-dependent aldehyde dehydrogenases" FT /EC_number="1.2.1.-" FT /note="Conserved hypothetical dehydrogenase. Homology to FT paaZ of A. evansii of 83% (trembl|Q9F9V2). Pfam: Aldehyde FT dehydrogenase family no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K261" FT /db_xref="InterPro:IPR011975" FT /db_xref="InterPro:IPR015590" FT /db_xref="InterPro:IPR016161" FT /db_xref="InterPro:IPR016162" FT /db_xref="InterPro:IPR016163" FT /db_xref="UniProtKB/TrEMBL:A1K261" FT /protein_id="CAL92916.1" FT /translation="MTHPLYAKHQATLEAALAAIHTRGYWTPYAEMPSPKVYGETAADD FT GKRAFEACLGKDFELDQPGRSGWAASERSPYGIALDVRYPVCEPSALIAAAEAAMPGWR FT KIGAEGRVGVCLEILDRLNKRSFEIAHAVMMTTGQGWMMAFQAGGPHAQDRGLEAVAYA FT WDAMRGVPATTVWEKPQGKNPPLKMQKHYEIVGRGVALVVGCGTFPTWNTYPGLFAALA FT TGNPVIVKPHSNAILPAAMTVKIAREVLAEAGLDPSVVSLAVVEKRSDTQALATHPAVK FT SIDFTGSNVFGQWLIDNARQAQVYAELAGVNNVVIESTDNYKAMLRNLAFTLCLYSGQM FT CTTTQAILVPAGGIDTDQGHKRYDEVAADLGAAIDKFLSDPAVATAVLGAIQSDATLAR FT INEAGQYGDIVLASKKIEHPEFPQAEVRTPVLLACDAAAEKSYMEERFGPIAFVVKVAD FT GAAAVALSERIVREHGALTVGLYSTKAEVIDAMTEATLRAGVALSINLTGGVFVNQSAA FT FSDYHGVGMNPAANASYSDAAFVANRFRVVQRRYHVE" FT CDS 324719..325522 FT /transl_table=11 FT /gene="paaG1" FT /locus_tag="azo0300" FT /product="probable enoyl-CoA hydratase" FT /function="Enoyl-CoA hydratase/carnithine racemase" FT /EC_number="4.2.1.17" FT /note="Probable enoyl-CoA hydratase. Homology to paaG of E. FT coli of 60% (sprot|PAAG_ECOLI(SRS) COULD POSSIBLY OXIDIZES FT FATTY ACIDS USING SPECIFIC COMPONENTS (BY SIMILARITY). FT Activity:- (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA FT + H2O. Interpro: Enoyl-CoA hydratase/isomerase (IPR001753) FT Pfam: Enoyl-CoA hydratase/isomerase no signal peptide no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K262" FT /db_xref="InterPro:IPR001753" FT /db_xref="InterPro:IPR011968" FT /db_xref="InterPro:IPR018376" FT /db_xref="UniProtKB/TrEMBL:A1K262" FT /protein_id="CAL92917.1" FT /translation="MSSFETIRYEVAAGVATLTLNRPDRLNSFNDQMHREVREALAQVQ FT AGRADGSVRVLVIAAAGRGFCAGQDLSDRNVSAGAEAPDLGASIEKNYKPLVTTLRNLD FT LPVIAAVNGVAAGAGANLALACDLVFAARSASFIQSFAKLGLVPDTGGSWILPRLLGPA FT RALGLALLGDKLPAEQAEQWGLIWKCVDDDALQATVQQVAATLANGPTFGYAQTKKAIW FT ASTTNDFDTQLDLERDAMRACGRSHDYREGVAAFMEKRAPQFKGN" FT CDS 325526..327073 FT /transl_table=11 FT /gene="paaH1" FT /locus_tag="azo0301" FT /product="probable 3-hydroxybutyryl-CoA dehydrogenase" FT /function="3-hydroxyacyl-CoA dehydrogenase" FT /EC_number="1.1.1.157" FT /note="Activity:-3-acetoacetyl-CoA + NADPH = FT (S)-3-hydroxybutanoyl-CoA + NADP+ Entry name TREMBL:Q9F9V1 FT InterPro IPR006108; 3HCDH_C. IPR006176; 3HCDH_N. IPR008927; FT 6DGDH_C_like. IPR002110; ANK. IPR000205; NAD_BS. Pfam FT PF00725; 3HCDH; 2. PF02737; 3HCDH_N; 1. Identities = FT 344/510 (67%) Prediction: Signal peptide Signal peptide FT probability: 0.660 Number of predicted TMHs: 1" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K263" FT /db_xref="InterPro:IPR006108" FT /db_xref="InterPro:IPR006176" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR011967" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K263" FT /protein_id="CAL92918.1" FT /translation="MTAADKALDKQVKVLVIGAGAMGSGIAHVAALAGHPVYLYDTRAE FT AIDKGIGGIAKDLAFLVEKGKLAGAERDAVLARISGITQLADAKDAGLAIEAIVENLDI FT KQKLFRELEALLAEDAVLASNTSSLSITAMGAALARPERLVGLHFFNPAPRMKLVEIVS FT GLATPRELAERMHATAKAWGKVPVHAKSTPGFIVNRVARPYYAEAQRVLAECAAEPATL FT DAAMREGCGFPMGPFELMDLIGHDVNFAVTNSVFDAYFGDKRFTPSLLQQELVAAGRLG FT RKSGHGFYSYAAGAARPAPQTEEPHEAEAAITVVGGLGVAAALIGRFEAAGIEVRRTAG FT AGGSDAQGWLEIGGARVALSDGRTATRRAVEEGVPNLVLFDLCLDYATTPRLTLARADQ FT CGHGAWGAAVGTLQRAGLAVSRIDDVAGLVGLRTVAMLANEAADAVLQGIGTAADIDTA FT MRFGTNYPKGPLAWADQLGVAFVARVLANLREHYGEERYRVSPLIQRKTFSGAAFHE" FT CDS 327066..327536 FT /transl_table=11 FT /gene="paaI" FT /locus_tag="azo0302" FT /product="phenylacetic acid degradation protein PaaI" FT /function="uncharacterized protein possibly involved in FT aromatic compounds catabolism" FT /note="Phenylacetic acid aerobic catabolism. Similar to FT TREMBL:Q9F9V0 (74% identity); SWISSPROT:P76084 (48% FT identity). InterPro (IPR003736): Phenylacetic acid FT degradation-related protein. Pfam (DUF157): Uncharacterized FT protein PaaI, COG2050" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K264" FT /db_xref="InterPro:IPR003736" FT /db_xref="InterPro:IPR006683" FT /db_xref="InterPro:IPR011973" FT /db_xref="UniProtKB/TrEMBL:A1K264" FT /protein_id="CAL92919.1" FT /translation="MSEAAYRDVTAGLDPQALAEKVRDGMFERDQAARSLAMEITAVGP FT GRATIAMKVREDMLNGFRICHGGFITTLADTAFAYACNSGNEQTVASGISVDFMAPGKP FT GDVLTAEAQQVFEAGRTGVYDITVTNQQGELIAVMRGKSYRLKGRPVVEIQA" FT CDS 327612..328934 FT /transl_table=11 FT /gene="paaK" FT /locus_tag="azo0303" FT /product="Phenylacetate--CoA ligase." FT /function="Coenzyme F390 synthetase" FT /EC_number="6.2.1.30" FT /note="Phenylacetate-coenzyme A ligase (EC 6.2.1.30) FT (Phenylacetyl-CoA ligase) (PA-CoA ligase). catalyzes the FT activation of phenylacetic acid to phenylacetyl-coA" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K265" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR011880" FT /db_xref="UniProtKB/TrEMBL:A1K265" FT /protein_id="CAL92920.1" FT /translation="MPINSYAPPQLEPIETASIDELRALQLERLKWSVRHAYENVPHYR FT KKFDEKGVHPDDLKSLADLAKFPFTSKYDLRDNYPFGMFAVPMDRIARVHASSGTTGKP FT TVVGYTLKDIDTWATVVARSIRAAGGRPGDMVHVSYGYGLFTGGLGAHYGAEKLGCTVV FT PMSGGQTEKQIQIIQDFKPKIIMVTPSYMLTILDEMERMGIDPKSTSLRIGIFGAEPWT FT PAMRVAMEQRAGIDAVDIYGLSEVMGPGVANECVETKDGPTIWEDHFYPEIIDPNTGEV FT LPDGSEGELVFTSLSKEAMPVIRYRTRDLTRLLPPSARSMRRMAKITGRSDDMLIIRGV FT NVFPTQIEELICKIPKLAPHYLLEVDKQGHMDTLTVKVEINAEAEVGRHPEHKEALARE FT LTHSIKSLIGVSAKVLVGEPFSIERVTVGKAKRVIDRRPKD" FT CDS 328992..329987 FT /transl_table=11 FT /gene="paaA" FT /locus_tag="azo0304" FT /product="phenylacetic acid degradation protein [paaA]" FT /function="uncharacterized conserved protein" FT /note="Phenylacetic acid degradation protein [paaA],86% FT identity(91% similarity) to TrEMBL;Q9F9U9. 72% identity to FT TrEMBL;Q7WGX6, Q8XS77 Has PF05138, Phenylacetic acid FT catabolic protein;IPR007814, PaaA_PaaC; This family FT includes proteins such as PaaA and PaaC that are part of a FT catabolic pathway of phenylacetic acid. These proteins may FT form part of a dioxygenase complex. No Signal Peptide or FT TMH present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K266" FT /db_xref="InterPro:IPR007814" FT /db_xref="InterPro:IPR009078" FT /db_xref="InterPro:IPR011881" FT /db_xref="InterPro:IPR012347" FT /db_xref="UniProtKB/TrEMBL:A1K266" FT /protein_id="CAL92921.1" FT /translation="MYTQALDIPQADAAPLRAVENPAYQAEFDARIDAGDFIEPKDWMP FT EAYRKTLVRQISQHAHSEIVGMLPEGNWITRAPSLKRKAILLAKVQDEGGHGLYLYAAA FT ETLGVSRDELYEALLAGRAKYSSIFNYPTLNWADIGVIGWLVDGAAIMNQIPLCKCSYG FT PYARAMIRVCKEESFHQRQGYDLLLTMMRGTPEQQEMVQDAVNRWWWPSIMMFGPHDSD FT SVHTETTRWGIKRISNDDLRQKFVDATVKQAEVLGVTLPDPALKWNEARGHYDFGAIDW FT DEFRAVVGGHGQCNVDRIAARRKAWEDGAWVREAAVAHAEKQAVRDKAAA" FT CDS 330089..330376 FT /transl_table=11 FT /gene="paaB" FT /locus_tag="azo0305" FT /product="phenylacetic acid degradation protein PaaB" FT /function="uncharacterized enzyme of phenylacetate FT metabolism" FT /note="May be part of a multicomponent oxygenase involved FT in phenylacetyl-coa hydroxylation. Phenylacetic acid FT aerobic catabolism pathway, TREMBL:Q8XS76 (75% identity); FT SWISSPROT:P76078 (61% identity)." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR009359" FT /db_xref="UniProtKB/TrEMBL:A1K267" FT /protein_id="CAL92922.1" FT /translation="MERKEWPLWEVFIRSRNGLDHKHCGSVHAPDARLALQTARDVYTR FT RLEGVSIWVVKASDIVASDPDAKPELFDPAEDKIYRHPTFYQLPEEVNHM" FT CDS 330388..331158 FT /transl_table=11 FT /gene="paaC" FT /locus_tag="azo0306" FT /product="probable phenylacetic acid degradation protein FT PaaC" FT /note="Probable phenylacetic acid degradation protein PaaC. FT Homology to paaI of P. putida of 46% (trembl|O84983). Part FT of a catabolic pathway of phenylacetic acid. These proteins FT forms part of a dioxygenase complex. Interpro: Phenylacetic FT acid catabolic (IPR007814) Pfam: Phenylacetic acid FT catabolic protein (PF05138) no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K268" FT /db_xref="InterPro:IPR007814" FT /db_xref="InterPro:IPR009078" FT /db_xref="InterPro:IPR011882" FT /db_xref="InterPro:IPR012347" FT /db_xref="UniProtKB/TrEMBL:A1K268" FT /protein_id="CAL92923.1" FT /translation="MTQANSANPAHLEYVLRLADNVLILGQRISEWCGHAPVIEEDLAL FT SNMALDLIGQARLLLTHAGRLEGRGRDEDQLAFLRVERDYRNLTLVEVPNQDFGRTVVR FT NMLFGAFQVVLWERLTASADSELAAIAAKSLKEARYHFSHAAEWVVRLGDGTALSHDKV FT QAALDELWPYTNEFFASDETDAAAAAAGIGPASNTLEADWENAVLPVLAQATLVAPART FT PFKTFGKFGRHSEHMGHLLATMQYMQRTYPGAQW" FT CDS 331218..331709 FT /transl_table=11 FT /gene="paaD" FT /locus_tag="azo0307" FT /product="probable phenylacetic acid degradation protein FT PaaD" FT /note="Probable pheylacetic acid degradation protein PaaD. FT Homology to phaH of P. putida of 54% (trembl|Q88HS8) FT Interpro: Protein of unknown function DUF59 (IPR002744) FT Pfam: Domain of unknoen function DUF59 (PF01883). Domain of FT unknown function DUF59;IPR002744; This family includes FT prokaryotic proteins of unknown function. The family also FT includes PhaH O84984 from Pseudomonas putida. PhaH forms a FT complex with PhaF O84982, PhaG O84983 and PhaI O84985,which FT hydroxylates phenylacetic acid to 2-hydroxyphenylacetic FT acid. So members of this family may all be components of FT ring hydroxylating complexes. no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR002744" FT /db_xref="InterPro:IPR011883" FT /db_xref="UniProtKB/TrEMBL:A1K269" FT /protein_id="CAL92924.1" FT /translation="MLTETEAWQALDAVPDPEIPVVSVTELGIIREVRCNDGAVTVVVT FT PTYSGCPATEVIGLAVRDALLAAGAREVAMETQLHPAWTSDWIGEAAREKLRAYGIVPP FT EGRAAPAAVQPIRFMRRTLACPRCGSTDTERLTEFGSTACKATWRCRACLEPFEYFKPI FT " FT CDS 331742..332809 FT /transl_table=11 FT /gene="paaE" FT /locus_tag="azo0308" FT /product="probable phenylacetic acid degradation NADH FT oxidoreductase PaaE" FT /function="Flavodoxin reductases (ferredoxin-NADPH FT reductases) family 1" FT /note="Probable phenylacetic acid degradation NADH FT oxidoreductase paaE. Homology to paaE of E. coli of 50% FT (sprot|PAAE_ECOLI). Probable PART OF A MULTICOMPONENT FT OXYGENASE involved in aerobic degradation of phenylacetic FT acid. InterPro: Oxidoreductase FAD and NAD(P)-binding FT domain(IPR001433); 2Fe-2S Ferredoxin (IPR006057); FT Ferredoxin (IPR001041); NADH: cytochrome b5 reductase (CBR) FT (IPR001834) Pfam: Oxidoreductase FAD-binding domain; FT Oxidoreductase NAD-binding domain; 2Fe-2S iorn-sulfur FT cluster binding domain no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K270" FT /db_xref="InterPro:IPR001041" FT /db_xref="InterPro:IPR001221" FT /db_xref="InterPro:IPR001433" FT /db_xref="InterPro:IPR008333" FT /db_xref="InterPro:IPR011884" FT /db_xref="InterPro:IPR012675" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:A1K270" FT /protein_id="CAL92925.1" FT /translation="MTPRFHPLKVAEVRRETADSVSLRFEVPADLAADYRFVQGQHLNL FT KAVVNGEEVRRSYSICSGVDDGELRVAIRKVDGGRFSSWAVDAVRVGDVFEVMTPEGRF FT STQLDPANAHHYVAFAAGSGITPILSLIKTTLRAEPKSRFTLVYGNRNQNSAMFAEALE FT DLKDRYLTRFALYNVFSREEQEVPLFNGRLDQARVAAFLDTLIPAADIDAAFICGPGGM FT IDEVEAALKGAGVPADRIHLERFGVPASAPRHHVEAGDAPQARITVIVDGLKREMEFRA FT QDPSILDVALRAGLDLPYSCKGGVCCTCRAKVLEGKVRMDKNYTLEQPDIDAGYVLTCQ FT AHPLTERVVISYDDR" FT CDS 332869..333513 FT /transl_table=11 FT /gene="paaR" FT /locus_tag="azo0309" FT /product="putative TetR family transcriptional regulator" FT /function="Transcriptional regulator" FT /note="Putative TetR family transcriptional regulator," FT /note="Family membership" FT /db_xref="GOA:A1K271" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011075" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:A1K271" FT /protein_id="CAL92926.1" FT /translation="MARGKSPTFELQREAILQEAARLFADKGFHNASMAELAAACGVSK FT PLLYHYYRDKEHILFDIADSYMDRLLAIVAGVEAQDLEPQPQLAELVMRFMAEYAHSQS FT QHMVLVQDVKFLQAEQSEQVVGKQRKVVAAFAAAIEAVEPGLKKRKLDKPVAMILFGMI FT NWTFTWLRADGRLTYADMAPVVTAILLNGVKGLLAQLPARGRKPPAEADAA" FT CDS 333560..334762 FT /transl_table=11 FT /gene="paaJ1" FT /locus_tag="azo0310" FT /product="probable beta-ketoadipyl CoA thiolase" FT /function="Acetyl-CoA acetyltransferase" FT /EC_number="2.3.1.16" FT /note="THIOLYTIC CLEAVAGE OF BETA-KETOADIPYL-COA TO FT SUCCINATE AND ACETYL-COA. Entry name:- TREMBL:Q84HH5 FT InterPro:- IPR002155; Thiolase. Pfam:- PF02803; Thiolase_C; FT 1. PF00108; Thiolase_N; 1. Identities = 298/398 (74%) FT Number of predicted TMHs: 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K272" FT /db_xref="InterPro:IPR002155" FT /db_xref="InterPro:IPR012793" FT /db_xref="InterPro:IPR016038" FT /db_xref="InterPro:IPR016039" FT /db_xref="InterPro:IPR020610" FT /db_xref="InterPro:IPR020613" FT /db_xref="InterPro:IPR020615" FT /db_xref="InterPro:IPR020616" FT /db_xref="InterPro:IPR020617" FT /db_xref="UniProtKB/TrEMBL:A1K272" FT /protein_id="CAL92927.1" FT /translation="MTEVFICDGIRTPIGRYGGALSGVRTDDLAALPIKALIARNSGVD FT WAAVDDIYYGCANQAGEDNRDVARMAGLLAGLPIDVPGSTINRLCGSGMDAVGTAARAI FT RTGETQLMIAGGVESMSRAPFVMGKADTAFSRSAKIEDTTIGWRFVNPLMKAKYGIDSM FT PETAENVATDFNINRADQDAFALRSQLRYAAAAERGFYEGELVPVEIAQKKGDPLRVTA FT DEHPRVTTLEALAKLKGVVRPDGTVTAGNASGVNDGSVALLLASEAAAAKHGLKPRARI FT VAMATAGVEPRIMGIGPAPASRKLLALTGLSLDQMDVIELNEAFAAQALAVTRQLGLAD FT DDARVNPNGGAISLGHPLGASGARLVLTALRQLEATGGRYGLCTMCIGVGQGIAMIIER FT V" FT CDS 334888..336033 FT /transl_table=11 FT /locus_tag="azo0311" FT /product="probable ABC transporter substrate binding FT protein" FT /function="ABC-type branched-chain amino acid transport FT systems periplasmic component" FT /note="ABC transporter substrate binding proteins count to FT the family of extracellular ligand binding proteins. It is FT a component of the high affinity amino acid transport FT system. Similar to trembl|Q8XU64 (71%) and to FT sprot|LIVJ_ECOLI (16%). Pfam (PF01094): Receptor family FT ligand binding region SignalP reporting Signal peptide." FT /note="Specificity unclear" FT /db_xref="InterPro:IPR001828" FT /db_xref="UniProtKB/TrEMBL:A1K273" FT /protein_id="CAL92928.1" FT /translation="MKLKHTLLAAIGLAFAAAAHADLNVGVVVSATGPAASLGIPEKNT FT IALMPATIGGEKVNYIVLDDASDTTTAVKNIRKLLSEDKVDVVVGSTITPNSLAMIDVT FT AEAATPMISMAASARIVEPIDDKKRWVFKTPQNDAQMSTAIIEHMTSNGVKTVAFIGFA FT DAYGEGWYEQFKSVAEARKLQIVANERFNRTDTSVTGQVLKVMAAKPDAVLIAGSGTPS FT ALPQKTLKERGYAGKYYQTHGVANNDFLRVCGKDCEGTFLPAGPVLVAAQLPDSNPVKK FT AALEYINKYEAAHGKGSVSTFGAHAWDAGVLLQAAVPVALKKAKPGTKEFRAALRDALE FT GVKETAGAHGIFNMSATDHLGFDQRARVMVQIQNGGWKLVQ" FT CDS 336157..337194 FT /transl_table=11 FT /locus_tag="azo0312" FT /product="ABC transporter permease protein" FT /function="Branched-chain amino acid ABC-type transport FT system permease components" FT /note="Branched-chain amino acid transport system typically FT composed of a periplasmic substrate-binding protein, one or FT two reciprocally homologous integral inner-membrane FT proteins and one or two peripheral membrane ATP-binding FT proteins that couple energy to the active transport FT system.The integral inner-membrane proteins translocate the FT substrate across the membrane. Similar to trembl|Q7W5E8 FT (62%), to sprot|BRAD_PSEAE (25%) and to sprot|LIVH_ECOLI FT (26%). Pfam (PF02653): Branched-chain amino acid transport FT system / permease component TMHMM reporting nine Tmhelix." FT /note="Specificity unclear" FT /db_xref="GOA:A1K274" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:A1K274" FT /protein_id="CAL92929.1" FT /translation="MDFQIALLLGQDGITNGAIYALLALALVLVFAVTRVIFIPQGEFV FT AYGALTLAMLQAGAVPATVWLLAGLGAVAAVLDGRGALQSGNAKKLPGIVGWNLAYPLA FT LAGVLMALPVKELPLAVQVLLALAVVVPMGPYLYRVVYQPIAAAPVLILLIVSVAVHVG FT MVGLGLLFFGAEGQRTPAFSDARFEVGPLLVSGQTIWVIVASIALIAALYQFFERTLYG FT KALRATAINRVGAQLMGISPALAGKLTFVLAAFIGALSGVLIAPITTIYYDTGFLIGLK FT GFVAAIIGGLGSYPIAAIGAVLVGLLEAFSSFWASAYKEVIVFTLIIPVLLWRSLTSHH FT LEEEE" FT CDS 337260..339053 FT /transl_table=11 FT /locus_tag="azo0313" FT /product="ABC transporter ATP-binding/permease protein" FT /function="ABC-type branched-chain amino acid transport FT systems ATPase component" FT /note="ATP-binding cassette (ABC) transporters are FT multidomain membrane proteins, responsible for the FT controlled efflux and influx of substances (allocrites) FT across cellular membranes. The integral inner-membrane FT proteins translocate the substrate across the membrane. FT ATP-binding protein is for coupling the energy of ATP FT hydrolysis to conformational changes in the transmembrane FT domains. Similar to trembl|Q8XRX5 (54%) and to FT trembl|Q8UFI6 (47%). Pfam: ABC transporter Pfam (PF02653): FT Branched-chain amino acid transport system / permease FT component Smart : AAA ATPase SignalP reporting Signal FT peptide. TMHMM reporting nine Tmhelix." FT /note="Specificity unclear" FT /db_xref="GOA:A1K275" FT /db_xref="InterPro:IPR001851" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A1K275" FT /protein_id="CAL92930.1" FT /translation="MLSPRLVLGVFLALLAVAPLVLPPFYVTLLNYIGLYAMVALGLVL FT LTGVGGLTSFGQAAFVGLGAYTTALLCTATELPGWLAWAGGSPWLALVVGLAFTAVVAV FT VLGSLTLKLSGHYLPLGTIAWGISLYFLFGTMESLGGHTGLTGIPPISIFGWVLDQGEE FT IYYLIWVFLLAAVFTTQNLLDSREGRAIRALKGGMVMAEAMGVDTSRSRMIIFVIAALH FT ACASGWLYAHMQRFVNPTPFGLHIGIEYLFMAVVGGAGHVWGALVGAGVITVLKQWLQD FT LLPRLFGQSGNFEVIVFGLMMVIVLQRARDGLWPILTKLVPVKAKRKTLDAAAKELPRR FT ELPGKGELILEAKNVTRKFGGLVANNNMSLEVKAGEILALIGPNGAGKSTMFNQISGVD FT TPTSGEVLFRGKPVAGHDSREIARMGMSRSFQHVKLLPTMSVLENVAIGGHLRGDKGVL FT SAAWRMDREEEARLLAEAARQIERVGLAEHMFDEAGSLALGQQRILEIARALCSDPCLL FT LLDEPAAGLRFKEKEALGELLKKLKAEGMAILLVEHDMDFVMGLVDRVVVMEFGEKIAE FT GLPEDVQKDPKVLEAYLGGVE" FT CDS 339053..339814 FT /transl_table=11 FT /locus_tag="azo0314" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems ATPase component" FT /note="ATP-binding cassette (ABC) transporters are FT multidomain membrane proteins, responsible for the FT controlled efflux and influx of substances (allocrites) FT across cellular membranes. ATP-binding protein is for FT coupling the energy of ATP hydrolysis to conformational FT changes in the transmembrane domains. Similar to FT trembl|Q8XRX4 (68%) and to trembl|Q7WCY5 (63%). Smart: AAA FT ATPases" FT /note="Specificity unclear" FT /db_xref="GOA:A1K276" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K276" FT /protein_id="CAL92931.1" FT /translation="MANETKNKVLEIQDLCVAYGKVEALTNANLTVGEGQIVTVIGPNG FT AGKTTMLSAIMGVLNSKGKVAFDGSIEAVPEVERMVARGMNLVPEKRELFGEMTVEDNL FT TLGAFQRYRMGKRDHGQTMEEVYHLFPRLKERRSQLAGTLSGGERQMLAVGRALMAKPK FT LLMLDEPSLGLAPLIVREIFRIIAELRKRGVSILLVEQNARAALQVADYAYVLETGQIA FT MEGPAAQLKDDPRVIEAYLGLGGKHQEMLAT" FT CDS 340402..340677 FT /transl_table=11 FT /gene="hupB" FT /locus_tag="azo0315" FT /product="DNA-binding protein HU (DNA-binding protein II)" FT /function="Bacterial nucleoid DNA-binding protein" FT /note="DNA-binding protein HU (DNA-binding protein II) FT (HB). Histone-like DNA-binding protein which is capable of FT wrapping DNA to stabilize it and thus to prevent its FT denaturation under extreme environmental conditions. FT InterPro: Bacterial histone-like DNA-binding protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K277" FT /db_xref="InterPro:IPR000119" FT /db_xref="InterPro:IPR010992" FT /db_xref="InterPro:IPR020816" FT /db_xref="InterPro:IPR023630" FT /db_xref="UniProtKB/TrEMBL:A1K277" FT /protein_id="CAL92932.1" FT /translation="MNKGEFVEALADRLDVSRAQADRALSAVLDIISEQLGKGEKVAFT FT GFGSFEVSERAARTGRNPQTGATIDIAASSVPKFTAGATLKAAVNK" FT CDS 341121..342464 FT /transl_table=11 FT /gene="rhlE1" FT /locus_tag="azo0316" FT /product="putative ATP-dependent RNA helicase" FT /function="Superfamily II DNA and RNA helicases" FT /note="ATP-dependent RNA helicase" FT /note="Family membership" FT /db_xref="GOA:A1K278" FT /db_xref="InterPro:IPR000629" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR014001" FT /db_xref="InterPro:IPR014014" FT /db_xref="UniProtKB/TrEMBL:A1K278" FT /protein_id="CAL92933.1" FT /translation="MTFHALGLAEELIAAVEQSGYTTPTPVQEQAIPAAIAGGDLLVSS FT HTGSGKTAAFTLPSLHRLVGRRPAPNSGPRVLVLTPTRELAQQVEEAVKTYGRALRWLN FT TACLVGGAPFFAQVKQLSRPVDVVVATPGRLLDHLNRRKLKLSDVETLVLDEADRMLDM FT GFAEDIEAIVGAIPASRQTLLFSATLDGVVGALANKLTRNPQRIEIASTEAKRGNIEQR FT LMFADDMGHKSRLLEALLGTDGLQQAVVFTATKKSADELSLSLQEKGFSAAALHGDMHQ FT TVRNRTLQRLRQGRIGVLVATDVAARGIDVAGISHVINFDPPRQVEDYVHRIGRTGRAG FT RDGIAITLSGPRETGLIRAIERFTGDRLAVHTIPGLEPAPRRPSAPRPGGPGRRFGSGG FT KPGGGFGGRSEGGYGGRGEGGRGAYGRDGHATRNERSHGDRRDRGPRG" FT CDS complement(342549..343016) FT /transl_table=11 FT /gene="nusB" FT /locus_tag="azo0317" FT /product="putative N utilization substance protein B" FT /function="Transcription termination factor" FT /note="NusB protein (N utilization substance protein B FT homolog) Involved in the transcription termination process FT (By similarity).Belongs to the nusB family 46% 1 TIGR01951 FT nusB; 1" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K279" FT /db_xref="InterPro:IPR006027" FT /db_xref="InterPro:IPR011605" FT /db_xref="UniProtKB/Swiss-Prot:A1K279" FT /protein_id="CAL92934.1" FT /translation="MSSRMARRRARELALQGVYQWLLSGNSPQVVEAHVEAEAADFDKV FT DRELFVMLLRGTLDNVGALQDEFSPFIHRPIEELSPIERAILLLGTHELKHNIETPYRV FT VINEAIELAKAYGGTDGHRFVNGVLDKLAARLRSIEVEAARAKKDAGDGQA" FT CDS complement(343013..343483) FT /transl_table=11 FT /gene="ribH" FT /locus_tag="azo0318" FT /product="riboflavin synthase" FT /function="Riboflavin synthase beta-chain" FT /EC_number="2.5.1.9" FT /note="67-dimethyl-8-ribityllumazine synthase (EC 2.5.1.9) FT (DMRL synthase) (Lumazine synthase) (Riboflavin synthase FT beta chain). Riboflavin synthase is a bifunctional enzyme FT complex catalyzing the formation of riboflavin from FT 5-amino-6-(1-D)- ribityl-amino-24(1H3H)-pyrimidinedione and FT L-34-dihydrohy-2- butanone-4-phosphate via FT 67-dimethyl-8-lumazine. The beta subunit catalyzes the FT condensation of 5-amino-6-(1-D)-ribityl-amino- FT 24(1H3H)-pyrimidinedione with L-34-dihydrohy-2-butanone-4- FT phosphate yielding 67-dimethyl-8-lumazine (By similarity). FT ribH: riboflavin synthase beta subunit" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K280" FT /db_xref="InterPro:IPR002180" FT /db_xref="UniProtKB/Swiss-Prot:A1K280" FT /protein_id="CAL92935.1" FT /translation="MARYDNIAEFESDLNGKGLRVGIVMSRFNQDVCEGLLSACTEELQ FT KLGVSPELIRIATVPGALEIPLVLQKMGQSGKFDALIALGAVIRGETYHFELVSNEMGA FT GITRIGLDTGIPIANGVLTTEDDDQALARMQEKGSDCARAAVEMANLLKVLQ" FT CDS complement(343535..344626) FT /transl_table=11 FT /gene="ribAB" FT /locus_tag="azo0319" FT /product="GTP cyclohydrolase II" FT /function="3,4-dihydroxy-2-butanone 4-phosphate synthase" FT /EC_number="3.5.4.25" FT /note="RibAB; riboflavin biosynthesis bifunctional protein: FT GTP cyclohydrolase II and FT 3,4-dihydroxy-2-butanone-4-phosphate synthase InterPro: FT 3,4-Dihydroxy-2-butanone 4-phosphate synthase ribB: FT 3,4-dihydroxy-2-butanone 4-phosphate synthase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K281" FT /db_xref="InterPro:IPR000422" FT /db_xref="InterPro:IPR000926" FT /db_xref="InterPro:IPR016299" FT /db_xref="InterPro:IPR017945" FT /db_xref="UniProtKB/TrEMBL:A1K281" FT /protein_id="CAL92936.1" FT /translation="MSALSPISEIIADIRAGKMVILVDEEDRENEGDVVLAAEFVTPEA FT INFMVTHCRGLVCLTLTDERCRQLGLEQMVRNNRTPHGTAFTASIEAATGVTTGISAHD FT RSRTVQVAVARHAKPDDIVMPGHIFPLTAQKGGVLIRAGHTEAGCDLAQLAGLEPAAVI FT CEILKDDGTMARLPDLIEFAAQHGLKIGAIRDLIEYRAATEHLVEKVTEKDVDTPHGRF FT RLSAFEDRTSGDIHFALTRGEISPDRETLVRVHEPISVVDFLDPASGKHSFPVNDALAA FT IAKAEAGAIVLLYRPQSGTDLLASLTGTTVERPVKWDPRLFGVGAQILRALGVGRMRLL FT ANPRKIPSMAGFGLEITGFVEKP" FT CDS complement(344623..345237) FT /transl_table=11 FT /gene="ribE" FT /locus_tag="azo0320" FT /product="riboflavin synthase" FT /function="Riboflavin synthase alpha chain" FT /EC_number="2.5.1.9" FT /note="Riboflavin synthase alpha chain (EC 2.5.1.9). FT Riboflavin synthase is a bifunctional enzyme complex FT catalyzing the formation of riboflavin from FT 5-amino-6-(1-D)- ribityl-amino-24(1H3H)-pyrimidinedione and FT L-34-dihydrohy-2- butanone-4-phosphate via FT 67-dimethyl-8-lumazine. The alpha subunit catalyzes the FT dismutation of 67-dimethyl-8-lumazine to riboflavin and FT 5-amino-6-(1-D)-ribityl-amino-24(1H3H)- pyrimidinedione. FT ribE: riboflavin synthase alpha subunit" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K282" FT /db_xref="InterPro:IPR001783" FT /db_xref="InterPro:IPR017938" FT /db_xref="InterPro:IPR023366" FT /db_xref="UniProtKB/TrEMBL:A1K282" FT /protein_id="CAL92937.1" FT /translation="MFSGIVAACGRIERIEPLADGLRLTVDTAGLDLADVQIGDSIANS FT GVCLTVIERDGPRVRFDVSRETLNCTVGLDVEGGEVNLEKALQLSDRLGGHLVTGHVDG FT VGEVLKFAPIGESHELVIRAPGAIAGYIAKKGSVTVNGVSLTVNRVEGPDFSINLIPHT FT VAVTNLKHLKAGSRVNLEIDLIARYVERMLAWREEESKDKP" FT CDS complement(345296..347116) FT /transl_table=11 FT /gene="cutA2" FT /locus_tag="azo0321" FT /product="putative protein disulfide-isomerase" FT /function="Thiol:disulfide interchange protein" FT /EC_number="5.3.4.1" FT /note="Putative Protein disulfide-isomerase (EC 5.3.4.1). FT Homology to dsbD of E. coli of 37% (sprot|DSBD_ECOLI). FT Required to facilitate the formation of correct disulfide FT bonds in some periplasmic proteins and for the assembly of FT the periplasmic c-type cytochromes. Acts by transferring FT electrons from cytoplasmic thioredoxin to the periplasm. FT This transfer involves a cascade of disulfide bond FT formation and reduction steps (By similarity). Pfam: FT Cytochrom C biogenesis protein transporter signal peptide FT probable 8 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K283" FT /db_xref="InterPro:IPR003834" FT /db_xref="InterPro:IPR005746" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR013766" FT /db_xref="InterPro:IPR017937" FT /db_xref="InterPro:IPR022910" FT /db_xref="UniProtKB/TrEMBL:A1K283" FT /protein_id="CAL92938.1" FT /translation="MIHRLFALLAILACLLAHPARASEPIEPEKAFAMQARALDAQTVE FT VVFEIAKDYYLYGSKFRFSAQPAGVTLGEVQRPPGKLKHDEFFGEVETYRGTLRMLVPV FT AAPAGVDAIELTVSSQGCWDGGVCYPPLPQQARVALVAASPAAGASLLDGALARGDVLA FT SDAVAPPAAVSLDESGRIAGLLRDASVPLVLASFFGFGLLLAFTPCHFPMIPILSGIIV FT GGGGQHLSRTRTFALSLAYVLGMAVTYALAGVGAGLSGTLLVAALQNVWVLSAFALVFV FT ALALSMFGFYELQLPSALQSRIADTASHNKGGHLGGVAAMGALSALIVGPCLAAPLAGA FT LLYIARSGDAALGGGALFAMGLGLGAPLLAVGMATRSVLPKVGPWMDGVKKAFGVILLG FT VAIWLLMPVLPPLAGMLAWAALLLFSGIFLHALDPLPPHAHGWQRFWKGVGVVLAIGGA FT AMLVGALAGSRDPLQPLAVLRAEASPAAETVRFERVGSLAELESRLAAAERPVMLDFYA FT DWCVSCKEMERYTFPDPQVAQRLAQMTLLKADVTANSEEHKALLKRFGLFGPPGIIFFD FT GAGRERTDLRVVGFQKPEAFAGVLDSALRR" FT CDS complement(347169..347492) FT /transl_table=11 FT /gene="cutA1" FT /locus_tag="azo0322" FT /product="periplasmic divalent cation tolerance protein" FT /function="uncharacterized protein involved in tolerance to FT divalent cations" FT /note="Periplasmic divalent cation tolerance protein .36% FT similarity to E.coli CutA1 protein involved in copper FT tolerance. InterPro:IPR004323; CutA1. Pfam:PF03091; CutA1; FT 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K284" FT /db_xref="InterPro:IPR004323" FT /db_xref="InterPro:IPR011322" FT /db_xref="UniProtKB/TrEMBL:A1K284" FT /protein_id="CAL92939.1" FT /translation="MSEILLVLTTLPDADSAAALGARLVEERLAACVNILAPCASVYRW FT QGRVETATEVPLLIKTSAARYAALETAILAEHPYELPEIVAVPVQRGLPGYLDWVSTET FT APG" FT CDS complement(347536..348780) FT /transl_table=11 FT /gene="naoA" FT /locus_tag="azo0323" FT /product="2-nitropropane dioxygenase." FT /function="Dioxygenases related to 2-nitropropane FT dioxygenase" FT /EC_number="1.13.11.32" FT /note="TREMBL:Q7MBF3: 80% identity, 89% similarity FT InterPro:IPR004136; 2nprop_dioxygen. IPR003009; FMN_enzyme. FT Pfam: PF03060; NPD tim: triosephosphate isomerase FT Non-secretory protein with no signal peptide. TMHMM FT predicted no transmembrane helices." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K285" FT /db_xref="InterPro:IPR004136" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:A1K285" FT /protein_id="CAL92940.1" FT /translation="MKRVDDFRLRLGSKELVPIMVGGMGVDISTAELSLEAARLGGIGH FT ISDAMVPTVSDRRFNTKYVKNKLQQYKFNVANPDKSVVQFDLGLLAEATALHVGKTMEA FT KRGDGLVFINCMEKLTMNGPKETLRVRLQAAMDAGIDGITLAAGLHLGSFALIQDHPRF FT NDVKLGIIVSSLRALQLFLKKNGRTGRLPDYVVVEGPLAGGHLGFGMDWAKYDLATIVA FT EIRDWLHAEQLDIPLIPAGGIFTGSDAVRFLEMGAGAVQVATRFTVTQECGLPEDVQQE FT YFKAGEDDIEVNQISPTGYPMRMLKNSPAIGDGIRPNCEAYGYLLDASGNCQYIDAYNR FT EVAAHPEARKVKVWDKTCLCTHMRNFECWTCGQYTYRLKDTTRRNEDGTYRVLSAEHVF FT HDYQFSTDDRIALPD" FT CDS 348990..349301 FT /transl_table=11 FT /locus_tag="azo0324" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to GSU0176 FT of G.sulfurreducens of 42% (tremble:Q74GR9) No domains FT predicted. No signal peptide or TMH reported present." FT /db_xref="InterPro:IPR018961" FT /db_xref="UniProtKB/TrEMBL:A1K286" FT /protein_id="CAL92941.1" FT /translation="MSLSVFDILAEQRIADALRRGEFDHLPGAGRPLVFDDEPLLSPEQ FT RMANHILKNAGVTPPEIGLRREIAALRARLETLDGEARARARRELGQLVLRLAELQRR" FT CDS 349421..350749 FT /transl_table=11 FT /locus_tag="azo0325" FT /product="putative flavocytochrome protein" FT /function="predicted ferric reductase" FT /EC_number="1.14.-.-" FT /note="Putative flavocytochrome protein. 48% FT FAD_binding_6.IPR001433; Oxred_FAD/NAD(P). Pfam:PF00970; FT FAD_binding_6; 1.PF00175; NAD_binding_1; 1. TMhelix: 6. FT Siganl peptide: present." FT /note="Function unclear" FT /db_xref="GOA:A1K287" FT /db_xref="InterPro:IPR000951" FT /db_xref="InterPro:IPR001433" FT /db_xref="InterPro:IPR008333" FT /db_xref="InterPro:IPR013130" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:A1K287" FT /protein_id="CAL92942.1" FT /translation="MKNIKLAFLVPPVVLTLLWLAADPVLWGEIRFFPLRAALMNYTGI FT LGIAAMSVGVMLAARPAWADARLGGLDKGYRLHKWLGIAGLVIATLHWALAKLPKWMVG FT WGWLERPLRGPRAEQSVAIFRFFQEQRGLAETVGEWAFHAALVLIALALIKRFPYRRFV FT RTHHLLAVVYLALVFHAVVLMKFSYWSEPLGPLMALLMAGGTLAALASLFRRVGRSRQV FT SGEIEELVRHPDNGVLRVGVRLRGRWPGHQAGQFAFVSFDATEGPHPFTICSAWTGDGR FT LVFMIKGLGDYTARLPDTLKVGDPVRVEGPYGRFDFAGARPRQVWVAGGIGITPFVARL FT QALAGQHDGRPVDLFYSTAAPDEGFIARLRQHAERAGVALHVQVTPIQGRLDAGRIRAE FT VPAWKEADFWFCGPAAFGNTLRAELTAGGLGAGDFHQELFEMR" FT CDS 350997..351800 FT /transl_table=11 FT /locus_tag="azo0326" FT /product="conserved hypothetical protein" FT /note="conserved hypothetical protein. Homology to cv0811 FT of C. violaceum of 43% (trembl|Q7NPT0(SRS) no domains FT predicted no signal peptide no TMHs" FT /db_xref="InterPro:IPR021390" FT /db_xref="UniProtKB/TrEMBL:A1K288" FT /protein_id="CAL92943.1" FT /translation="MSSAAESPATYADRPLFEPVATLLAAFPAGLPDHAGLQHLFEQAA FT PEAVSGGGRPIRFVLPDDSRPAYEVRIHASGEVPTRAGDWHDFFNALAWCVWPRTKAAC FT NALHLQEIAAREVSGAQGRGPRRDALTQFDECGVVVVSADADIPALLADHQWEAVFWQR FT RARLQASTRFLVFGHGSWDQLRRPFFGLCAKAIHRVVEPDWLQLPPAAQQAEVDAWLAA FT HLASLPTLTPRAFSPLPLLGIPGVTPDSEHAGYYRDTRQFRPRRR" FT CDS complement(351835..352428) FT /transl_table=11 FT /locus_tag="azo0327" FT /product="putative TetR family transcriptional regulator" FT /function="Transcriptional regulator" FT /note="Putative TetR family transcriptional regulator," FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K289" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011075" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:A1K289" FT /protein_id="CAL92944.1" FT /translation="MRVSREQAAENRERVVQEASRLFREHGFDGIGVAELMKQAGLTHG FT AFYGQFGSKDALMAEASARALADSLSYWKRRVAAAGEDGLTSIVNKYLSPAHRDHPGRG FT CAFAALGAEAHRRNPAVRQAMSAGLLPLVDELARLLPDSPGADRRQQALAAFSAMVGAL FT VLARAVDDAALSEEILRATAASITAGATPAQPER" FT CDS 352603..353745 FT /transl_table=11 FT /gene="livK1" FT /locus_tag="azo0328" FT /product="putative leucine-specific binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems periplasmic component" FT /note="In enteric bacteria such as E. coli and Salmonella FT typhimurium, periplasmic binding proteins are found to FT participate in the transport of amino acids, sugars and FT ions. Leucine-specific binding protein are coded by livK FT and livJ. Similar to sprot|LIVK_SALTY (23%) and to FT trembl|Q8XUX2 (46%). Pfam (PF01094): Receptor family ligand FT binding region SignalP reporting Signal peptide." FT /note="Specificity unclear" FT /db_xref="GOA:A1K290" FT /db_xref="InterPro:IPR000709" FT /db_xref="InterPro:IPR001828" FT /db_xref="UniProtKB/TrEMBL:A1K290" FT /protein_id="CAL92945.1" FT /translation="MPSLLRPFRLAAGLLALLVPLAPSGAAAQTRELVIGQVAPFSGPQ FT AVTGKAIHAGIRLYFDQVNAQGGVKGARLRLVTRDDAQKPEQTVALARELIQQEAPVAL FT IGTVGTTNVDALIADGVLVRAGLPLVGAVSGASSAIGGRNVFVTKASYHDEVNRLFTSL FT SGLGMKRVGLVYQDDALGQDVIAGADAAAPRAGISLIARAGYERNTVKVEQAVEAMLKA FT NPQVVFLGATTAAAIEFVRQYRARGGDATLYGLSIIDTRQLVAQLGPAGARGFAFSVVL FT PLEGQQTIEVNREYLRLRAASTDPDLSGRSIEGFIAAKALVHALRSAEGAPGGGAVLKS FT LQAMRKVDLGGYMLDFGQPGRPGSSYVDFAMLGDGGRVVH" FT CDS complement(353800..354273) FT /transl_table=11 FT /locus_tag="azo0329" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to SCO5300 FT of Streptomyces coelicolor of 46% (tremble:Q9XAE9). No FT domains predicted. No TMHs. No signal peptide." FT /db_xref="InterPro:IPR011008" FT /db_xref="InterPro:IPR021708" FT /db_xref="UniProtKB/TrEMBL:A1K291" FT /protein_id="CAL92946.1" FT /translation="MQLAELNVARLLAPIDSPQLAGFVNQLDEINALAEASPGFVWRFD FT GDARLGTTSVPDDPLLLINLSVWQDVDALFAFTYQSLHKRPLGGRRDWFERPTEAHLVM FT WWVEDGHRPGVDEALARLALLRRDGPGPRAFDFRCRFAADGRECAAKPGTVTA" FT CDS complement(354344..355339) FT /transl_table=11 FT /gene="blaA" FT /locus_tag="azo0330" FT /product="probable transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="HTH-type transcriptional regulator blaA FT (Beta-lactamase regulatory protein blaA). Positive FT regulator of the expression of the gene (blab) for FT beta-lactamase. Similar to SWISSPROT: sprot|BLAA_PROVU (32% FT Proteus vulgaris, HTH-type transcriptional regulator BlaA) FT InterPro: IPR000847 HTH_LysR. IPR009058 Winged helix FT DNA-binding. Pfam: PF00126 Bacterial regulatory FT helix-turn-helix protein, lysR family. HTH reporting FT nucleic acid binding motif." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K292" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K292" FT /protein_id="CAL92947.1" FT /translation="MEAPGKLPPLPALRSFEAAARLLSFSRAADELHVTHGAVSHQIRA FT LEAQLGLALFARDTRGLRLTPAGEALLQATNGALRGIADAVAGLRRHLRPDRLSVSVMP FT SFAGRWLAPRLAAFLDANPGCELNVLSSDAITDFARDGTDLAIRWGFGGYSGVHSELLM FT DDVMFPVVSPHFAGGVPRTPAGLAGLPLLRSVGEDWLPWFRAAGLDWPEPSRGLVLSDS FT GLLVQAAIDGQGVALARRSLAMRAVREGRLLKPFDIEVPLLYGPGQGKPPSLGLAPDGT FT PKRWRFWLVWPLTPAPTPLLQRFVAWLHAEVAAELDAAAATPASSALTGL" FT CDS 355556..356023 FT /transl_table=11 FT /locus_tag="azo0331" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein, 41% similarity to FT TrEMBL;Q88JC7. Has IPR005544 DUF_HHE:PF03794;Domain of FT Unknown function:This domain normally occurs as tandem FT repeats and is found in bacteria, yeast and plants. It FT contains two fully conserved histidines and one glutamate FT residue. Members of the family include DnrN, NorA and ScdA, FT which have been implicated in NO response and cell wall FT physiology. Has no Signal peptide or TMH reported present." FT /db_xref="InterPro:IPR012312" FT /db_xref="UniProtKB/TrEMBL:A1K293" FT /protein_id="CAL92948.1" FT /translation="MNKSSLPTGLKDVLGALLEDHREAKKLFKDFEKAKSSEEKEEIAR FT TVCEALTLHTQLEEEFFYPAVRELESDSIKALLDEAEVEHASAKELIQQIEGIGADDAL FT FEAKVTVLGEYVSHHIREEEEELFPKLVEEKVDLREVGAAMEEKRNELVAH" FT CDS complement(356048..357376) FT /transl_table=11 FT /locus_tag="azo0332" FT /product="putative esterase" FT /function="predicted esterase of the alpha-beta hydrolase FT superfamily" FT /note="Hypothetical protein yqhO. This family consists of FT various patatin glycoproteins from the total soluble FT protein in potato tubers.Patatin is a storage protein but FT it also has the enzymatic activity of lipid acyl hydrolase, FT catalysing the cleavage of fatty acids from membrane lipids FT SPROT:P54513: 23% identity, 33% similarity SubtiList: FT BG11703; yqhO. InterPro:IPR002641; Patatin. Pfam:PF01734; FT Patatin No signal peptide TMHMM predicted 2 transmembrane FT helices mobB: molybdopterin-guanine dinucleot" FT /note="Family membership" FT /db_xref="GOA:A1K294" FT /db_xref="InterPro:IPR002641" FT /db_xref="InterPro:IPR016035" FT /db_xref="UniProtKB/TrEMBL:A1K294" FT /protein_id="CAL92949.1" FT /translation="MNAADFHRAADAALAAMTAEGLDRRRYSDTLDGEGYQYVDLVMEG FT GGVLGVALLGYIHVLEKAGLRFVGLGGASAGSITALALAALDVPAAAKSDRLIEIVANM FT PMADFIDGKDDDDEDAADFIDTLLKRPGLAKLAWKGMQILDNLDEMIGLNRGDRFHRWL FT TEDVLRAHGIHTTAQLRARMATTPAGWHLREDSPQRESQLRGEARLAPLDPAADYLCVV FT AADVATETKVEFPCMAALYWDEPDQVNPADYVRCSMSIPVFFKPVTRPIRIRDAAHEAL FT WRDLAGMGDDDLKPTRFPPPRAVFVDGGVLSNFPIDVFHRPNKVPARPTFGVKLQWDER FT SHDVNKLAKLITQTFNSARHCLDYEFIRRNPDFKQLVACIDTADHDWLKFEMPDEAKLD FT LFRRGAEAAVGFLRRFDWARYKETRAHLAAAYTTAQQPQIVHL" FT CDS 357462..358568 FT /transl_table=11 FT /locus_tag="azo0333" FT /product="putative esterase" FT /function="predicted esterase of the alpha-beta hydrolase FT superfamily" FT /note="Hypothetical protein Rv1063c/MT1093/Mb1092c. FT TREMBL:Q89EP5: 29% identity, 42% similarity FT InterPro:IPR002641; Patatin. Pfam:PF01734; Patatin 2A0108: FT nitrate transporter Absence of signal peptide No. of TMH's: FT 2 (TMHMM predicted)." FT /note="Family membership" FT /db_xref="GOA:A1K295" FT /db_xref="InterPro:IPR002641" FT /db_xref="InterPro:IPR016035" FT /db_xref="InterPro:IPR021095" FT /db_xref="UniProtKB/TrEMBL:A1K295" FT /protein_id="CAL92950.1" FT /translation="MEVMNHTEPLPVALILGGGLALGAYQAGVLAALETSREVRIVAVT FT GASIGAINGALLAGNRPAERVNRLRGFWDRVTTDLAPGWLEPAGRTGPFRHARNWVNTL FT GTHLAGARGLYRPRIFFDSGPSAVPSFYDSSLAAATLAQLVDFDVLNGGAVRYCAVATD FT VETAAAVPFDTAAGVRIGIPHLLASSALMPSFAPVAIDGRLYADGGLAANAPLELFLSS FT ARVGPLPPLCILIDLFAPQSPPPRTLEAAMARGSDLKFAAQTRLRLEAIERERSLEAAL FT ALPAADAADEGPAGAAPGTELIYLSYRPLAHDAGSEKQYDFSRPTLADRWQRGEDDAAE FT VLRMVAAVAPAAGAQPGLRIHRCGAWVR" FT CDS complement(358579..359157) FT /transl_table=11 FT /locus_tag="azo0334" FT /product="conserved hypothetical secreted protein" FT /function="predicted outer membrane protein" FT /note="Conserved hypothetical secreted protein. Homology to FT BPP2140 of Bordetella parapertussis 0f 44% FT (trembl|Q7W8J3(SRS)) No domains predicted. Signal peptide FT present. No TMH present. 6PTHBS: 6-pyruvoyl FT tetrahydrobiopterin" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR012347" FT /db_xref="UniProtKB/TrEMBL:A1K296" FT /protein_id="CAL92951.1" FT /translation="MSATRLTRHALVACAALFATGALAQSSYPPAPTGDKSSERRMENR FT LASEDRDFLENASQAGQVEIEGSRLAEEKATSAEVKTFAKQMIEDHTKAHRELVTLATR FT KGFTLPDEGSIMQRTELTALKAVSGETFDKMYASRIGVNAHEKTLELFREAASKAKDPE FT IKAYAAKYVPALEKHLGMARTLRDRVGKE" FT CDS 359461..360240 FT /transl_table=11 FT /locus_tag="azo0335" FT /product="EAL-domain containing protein" FT /function="FOG: EAL domain" FT /note="EAL-domain containing protein, ):This domain is FT found in diverse bacterial signaling proteins. It is called FT EAL after its conserved residues. The EAL domain is a good FT candidate for a diguanylate phosphodiesterase function [1]. FT The domain contains many conserved acidic residues that FT could participate in metal binding and might form the FT phosphodiesterase active site." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR001633" FT /db_xref="UniProtKB/TrEMBL:A1K297" FT /protein_id="CAL92952.1" FT /translation="MSDHPPCAGCSGQPLAFGFSYAYQPIVDLAARQIFAHEALVRGPA FT GEGAGTVLAQVNADNRYRFDQACRVRAIETAARLGMQSRLSINFLPNAIQRPDLCIRST FT LEAARLHGFPLERIIFESVEGERIADARWLAEVFREWQHHGFLTAIDDFGAGYAGLNLL FT ADFQPDLVKLDMGLVRAVHRHPARQAIVRGVARICEELDIPVVAEGVEELDEARCLSDA FT GIRLMQGFLFCRPLFEGVGEAATLAWPALAPQAGGRQ" FT CDS 360237..361499 FT /transl_table=11 FT /locus_tag="azo0336" FT /product="PAS/PAC/GGDEF-domain containing protein" FT /function="FOG: PAS/PAC domain" FT /note="PAS/PAC/GGDEF-domain containing protein, suggesting FT involvement into signalling processes. Similarity to FT SWISSPROT: sprot|YDAM_ECOLI (24% Escherichia coli, hyp. FT protein) / TREMBL: trembl|Q887F0 (59% Pseudomonas syringae, FT hyp. protein) Pfam: PF00990 GGDEF domain. This domain is FT found linked to a wide range of non-homologous domains in a FT variety of bacteria. The function of this domain is FT unknown, however it has been shown to be homologous to the FT adenylyl cyclase catalytic domain. This prediction FT correlates with the functional information available on two FT GGDEF-containing proteins, namely diguanylate cyclase and FT phosphodiesterase A of Acetobacter xylinum, both of which FT regulate the turnover of cyclic diguanosine monophosphate. FT TIGRFAM:TIGR00254 putative diguanylate cyclase (GGDEF) FT domain. TIGR00229 PAS domain S-box." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K298" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR013767" FT /db_xref="UniProtKB/TrEMBL:A1K298" FT /protein_id="CAL92953.1" FT /translation="MSSQREKLLEAAVAQSFNAVVITDARLDGGGPHIVYVNRAFCEMT FT GYAAEDLIGQSPRILQGPDTDPEVIDRLRTALRSGSFFEGATVNYRRDGSAYDVEWNIS FT PVRDDGGELSHFVSVQHNISDKMWMRRERDLLAQALNVASDPIIVTDRGGAIVFVNQAF FT ERLTGYPADEMLGRTPAVLRSGAHDAAFYSGLYAALARGRPFRATFTNRRKDGSLFHAE FT QSIAPLCDGEGEVTHFVSVSKDLTERIERERALQEIASRDPLTGLYNRRAGEQALELQV FT QAAHAEGTALSLIIGDIDHFKSINDRHGHPAGDRVLAGVGEALRGAVRSRDLAVRWGGE FT EFVVLVPECGAARALELAERLRSSVAGLQFPAVGRVTMSLGLATLVAGETAAGLVMRAD FT RALYRAKHGGRDRVETAAALD" FT CDS complement(361535..362107) FT /transl_table=11 FT /locus_tag="azo0337" FT /product="Hypothetical protein" FT /note="Probable hypothetical Protein. Extremely weak FT homology with hits in the PDB. No Motif/Features/TMH/ or FT Signal peptide present." FT /db_xref="UniProtKB/TrEMBL:A1K299" FT /protein_id="CAL92954.1" FT /translation="MRATSNPPGLEHQGYEFFPPYDETGATVISWEIQVQTAQDFHEAC FT PRDDEACQWRDPLEASGDFRPTMQTVVRINTLNVALRERLLRLTNDMSNLAIAEMGMRK FT STDAGGAEMAAGPEPLSEDSAQRLMALTRAWFDIIGMAQASMGTLTGYMPRTADRTAAS FT ADYADRPLVERRQNVRHIDFADRRRAG" FT CDS 362400..363443 FT /transl_table=11 FT /gene="pstS1" FT /locus_tag="azo0338" FT /product="putative phosphate-binding periplasmic protein" FT /function="ABC-type phosphate transport system periplasmic FT component" FT /note="38% Peri-phosph.IPR006059; SBP_bac_1. Pfam:PF01547; FT SBP_bac_1; 1. TIGRFAMs:TIGR00975; 3a0107s03; 1. Signal FT peptide present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2A0" FT /db_xref="InterPro:IPR005673" FT /db_xref="InterPro:IPR024370" FT /db_xref="UniProtKB/TrEMBL:A1K2A0" FT /protein_id="CAL92955.1" FT /translation="MAIRFLLLLSLAWSACVAAAPDVLRGAGSSAAQPVYAAWAAAYAA FT THGTVLEYDPAGSGAGIKKLLAAEVDFGASDLVPDAAALQGRDIVVVPTAVTGAVPVIN FT LPGLRGALRLDGATLAEIFAGRIRRWDDAAIRRLNPGLTLPERAIERVVRSDSSGTTWN FT FADYLAKLSPRWRAEFGVAARFDWGEGVIAAKGSGGVAEAVARTPGAIGYVDYNYVVRH FT GLQAVTLQNRDGAFVQAGTDGFAAALSASPWPRSGDFTATLTDQPGARSWPITMGTFIL FT VPRHGGGDGVRRALAFFTWAYLHGDELIRSSHFVRLPDRVQAKAFRSLAAVTDANGTPI FT GFGGLAR" FT CDS complement(363495..363989) FT /transl_table=11 FT /locus_tag="azo0339" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT an orf of Acinetobacter sp. (strain ADP1) of 43% FT (tremble:Q6F6W4). no domains predicted. signal peptide. 1 FT TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR013229" FT /db_xref="UniProtKB/TrEMBL:A1K2A1" FT /protein_id="CAL92956.1" FT /translation="MKKPFLAIAALSLAGCATIIGSTTQPVTIKTEPEGAQISVSNRAG FT EKIHSGSTPVTVTLNRGAGYFKAETYTVRIAKEGYEPREVVLEGHVNGWYFGNIIFGGV FT ILGMLIVDPLSGAMFTLSPDKVDEALQKTGVTGSKDDGSLTVVLIENVPEEVLRTARRV FT N" FT CDS complement(364232..364546) FT /transl_table=11 FT /locus_tag="azo0340" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. No homology FT to the data bank No domains predicted No signal peptide 2 FT TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K2A2" FT /protein_id="CAL92957.1" FT /translation="MLAGDPLLLRARDAGHGRDQDDCIESPYAVTFPFRPRMLEVLLIL FT AQALLEFLFHTVLYGAGWLMLRALTLGRYPPPRPIEHNHDLVALLPLVTVLVTIAFAYA FT " FT CDS 364615..365061 FT /transl_table=11 FT /locus_tag="azo0341" FT /product="putative cytochrome c'" FT /function="Cytochrome c556" FT /note="Putative cytochrome c'. Homology to cytochrome c of FT R. gelatineosus (sprot|CYCP_RHOGE). CYTOCHROME C IS THE FT MOST WIDELY OCCURRING BACTERIAL C-TYPE CYTOCHROME. FT CYTOCHROMES C ARE HIGH-SPIN PROTEINS AND THE HEME HAS NO FT SIXTH LIGAND. THEIR EXACT FUNCTION IS NOT KNOWN. InterPro: FT Cytochrome c class II (IPR002321) Pfam: Cytochrome C FT probable signal peptide no TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K2A3" FT /db_xref="InterPro:IPR002321" FT /db_xref="InterPro:IPR010980" FT /db_xref="InterPro:IPR012127" FT /db_xref="UniProtKB/TrEMBL:A1K2A3" FT /protein_id="CAL92958.1" FT /translation="MPRPLLPALLILLTLAGCGPVEDTRPGQPVKQRQEAFKSILRSFE FT PMGVMLRDNKYQADKFASLAGELVAKRDAPWSHFGPDTNYPPTKAKAAVWSDGETFERE FT RLAFVAATDALFAAAQTRDQAQAKAAYEKVYGSCKSCHDRFKEK" FT CDS complement(365077..365901) FT /transl_table=11 FT /gene="nhoA" FT /locus_tag="azo0342" FT /product="N-hydroxyarylamine O-acetyltransferase" FT /function="Arylamine N-acetyltransferase" FT /EC_number="2.3.1.118" FT /note="Belongs to the arylamine n-acetyltransferase family. FT Arylamine N-acetyltransferase is a cytosolic enzyme of FT approximately 30kDa. It facilitates the transfer of an FT acetyl group from Acetyl Coenzyme A on to a wide range of FT arylamine, N-hydroxyarylamines and hydrazines. Similar to FT TREMBL:Q98D42 (47% identity); TREMBL:Q8FHI6 (39% identity); FT SWISSPROT:P77567 (39% identity). InterPro (IPR001447): FT N-acetyltransferase Pfam (PF00797): N-acetyltransferase." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2A4" FT /db_xref="InterPro:IPR001447" FT /db_xref="UniProtKB/TrEMBL:A1K2A4" FT /protein_id="CAL92959.1" FT /translation="MTPPLDLDAYLARIGGLAAAPDTTLTTLNALIAQHVAAIPFENLS FT PLLGEPVDISPAAVQAKLVAGGRGGYCYEHNRLFADVLRHLGFTVHELGARVVWNQPPG FT AITPRSHMLLEVDTADGPRLVDVGFGGLTLTSALRLQADIEQITPHEPFRLLRDGDDWT FT LQARLGEAWKPLYRFDRVRHHACDYIAPNYFLATHPDSVFTANLMLARAGRNQRWTLFN FT RDYAEYHGDGRIVRRTLADMAELTEVLQRAFGIPPALCATAQPRLARLFDAG" FT CDS 366042..366704 FT /transl_table=11 FT /gene="parA2" FT /locus_tag="azo0343" FT /product="probable ParA family protein" FT /function="ATPases involved in chromosome partitioning" FT /note="Sporulation initiation inhibitor protein soj. FT INHIBITS THE INITIATION OF SPORULATION SPO0J ANTAGONIZES FT THIS INHIBITION. SOJ ULTIMATELY INHIBITS THE ACTIVATION FT (PHOSPHORYLATION) OF SPO0A. IT IS NOT REQUIRED FOR FT CHROMOSOME PARTITIONING. InterPro: ParA family ATPase" FT /note="Function unclear" FT /db_xref="InterPro:IPR002586" FT /db_xref="UniProtKB/TrEMBL:A1K2A5" FT /protein_id="CAL92960.1" FT /translation="MGGTRIVALLSQKGGSGKTTVAMQLAAGLALAGYRVVVADLDPQE FT SASRWADAAAPEAPFPAPVMRLRGSAEDMRQALRAAANRADFVVFDCPPSIDHPHTGSA FT LALCDLALVPVVPSPTDLWATRGMEKLILNQMATRAPLRAALLPNRVMRTALAADVLEV FT LGDFSLPVLDAALTQRSAYAQSAVQGASVYELGRSAQPAQAEVDRLVAAVLNQFEES" FT CDS 366705..367574 FT /transl_table=11 FT /locus_tag="azo0344" FT /product="Hypothetical protein" FT /note="Probable Hypothetical Protein. No FT domains,features,motifs, or signal peptide present." FT /db_xref="UniProtKB/TrEMBL:A1K2A6" FT /protein_id="CAL92961.1" FT /translation="MASTKTQSALRAALKQEDAALTERLPAAGAPAKPKAAKAAAVKPV FT VAEQGKLADALIVPPAEGDGAAKAKPAAAAGPAKPAATKKQAAPVAGKTKAKSTAAKGS FT AASKAAAAPAPVAETAAGSPAGAAKAKAKAAPVKTRPAAAAAAPAVEPAVTPAPAAAKK FT AKAIRNGGAAVSKAAAAPAAELAVAPEAAAKTKAKVEKAEKAEKAEKTDKADKVEKVVR FT DSFSLPASEHRRIKSVREQLGKSGRLVSKSEVLRVALVALGERSADELAALFDALPPVV FT KGKRSKKH" FT CDS complement(367763..369865) FT /transl_table=11 FT /locus_tag="azo0345" FT /product="ATP-dependent DNA helicase" FT /function="Superfamily I DNA and RNA helicases" FT /EC_number="3.6.1.-" FT /note="ATP-dependent DNA helicase pcrA (EC 3.6.1.-). FT InterPro: UvrD/REP helicase" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2A7" FT /db_xref="InterPro:IPR000212" FT /db_xref="InterPro:IPR014016" FT /db_xref="InterPro:IPR014017" FT /db_xref="UniProtKB/TrEMBL:A1K2A7" FT /protein_id="CAL92962.1" FT /translation="MNSPAPAACAPAPAYLDRLNAAQREAVEYGVRGNAGRDIPGPLLV FT IAGAGSGKTNTLAHRVAHLIANGADPGRILLLTFSRRAADEMGRRVQRILAQVAVDTPW FT LAQATLQWSGTFHGIGARLLREYAGRIGLDPAFTIHDREDSADLMNLARHEAGLSTRNK FT RFPLKGTCLAIYSAAVNTRAPLAEVLQTTFPWCAEWEAELKTLFRAYVQAKQAQQVLDY FT DDLLLYWAHMVAEPALGAEIGGLFQHVLVDEYQDTNHLQAEILLAMKPDGRGLTVVGDD FT AQSIYAFRGATIRNILDFPARFEPPAHRVTLEQNYRSTRPILDAANAVIAQAAERYSKD FT LWSLRESTARPQLVSVRDDADQSAFVVERVLARREQGIKLKQQAVLFRAASHSARLEME FT LTRRNIPFVKFGGLKFLEAAHVKDMLAVLRWVENLRDRVSGFRVVQLLVGIGPKTAGKV FT LDHVVAAPEGCELLAEQPVPEAARADWQAFSTLIEHLRRPDAPWPASFELACRWYEGQM FT PRLYDDAVVRQGDIQQLGRIAATYPSRQRFLTELTLDPPSATSDEAGVPLLDEDYLILS FT TMHSAKGQEWNSVSVLNVVDGCVPSDIATRSSAEIEEERRLLYVAMTRAKDHLELLVPQ FT RFYVSQQQGMGDRHVYAGRTRFIPNRLLPQFEQVSWPEPPPEFRGTPQSRQAALDLAAK FT MRGMWD" FT CDS 369965..371605 FT /transl_table=11 FT /locus_tag="azo0346" FT /product="putative Na+/H+ antiporter" FT /function="NhaP-type Na+/H+ and K+/H+ antiporters" FT /note="42% Na_H_porter.IPR004705; NaHantiport_bac.Bacterial FT Na+/H+ antiporter Pfam:PF00999; Na_H_Exchanger; 1. FT TIGRFAMs:TIGR00831; a_cpa1; 1. Signal peptide present FT TMHelix: 12" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2A8" FT /db_xref="InterPro:IPR004705" FT /db_xref="InterPro:IPR004709" FT /db_xref="InterPro:IPR006153" FT /db_xref="InterPro:IPR018421" FT /db_xref="InterPro:IPR018422" FT /db_xref="UniProtKB/TrEMBL:A1K2A8" FT /protein_id="CAL92963.1" FT /translation="MQSIEVVLAMLLAVVASGYLVRVVPVSLPLPLVQIALGAGIAAIS FT GHGVRLDPEIFFLLFLPPLLFLDGWRIPKVGLFRDKGTILELAFGLVVFTVLGAGLLIH FT WMIPAMPLAVAFALAAIVSPTDPVAVSSIAARVPIPKRLMHILEGESLLNDASGLVCFR FT FAVAAVMTGGFSLAAASLTFLWVAFAGLAVGVIVTWVISLAQRWLSRHLGEEAGSPILV FT NLLIPFGAYLVAEHLDASGILAAVAAGVTMSYVELSGRALATTRVQRAAVWDTVQFSLN FT GIMFVLLGEQLPGIVQRAAAAVEDSGHVSRWWLLVYALAISAILAALRFAWVWVSLRVT FT LFKAREAGEPLQRPDWRIVAAVSLAGVRGAITLAGVLTLPLLLPDGRDFPARDLVIFLA FT AAVILVSLLLASLGLPRLLRGLALPDEPAERREEDRARREAAAAAIAAIEKARHALSEP FT GAADADLYTNAAVRVMANYQRRLADSAMPGSVAADRLRAADRAEMALWLAALQAEREAI FT FRLARDYELSDETSRKLVRQIDLMEARYR" FT CDS 371653..372096 FT /transl_table=11 FT /locus_tag="azo0347" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. Signal P reporting Signal FT Peptide present. No TMH reported Present." FT /db_xref="UniProtKB/TrEMBL:A1K2A9" FT /protein_id="CAL92964.1" FT /translation="MSPSRSAVLLILLLAAPAASAEVYQWVDQQGRVHYGDRPAPGVPA FT ARREELSVPEPTQADRDAAAERAERARARLQSLPPSPPPEPTGTEGDRSAPQAEAEDDS FT CAAQHRRYRASQACFAPYVTVTGAVKPEAFQYCENLPQPQCEE" FT CDS 372236..373684 FT /transl_table=11 FT /locus_tag="azo0348" FT /product="4-hydroxybenzoate octaprenyltransferase" FT /function="4-hydroxybenzoate polyprenyltransferase and FT related prenyltransferases" FT /EC_number="2.5.1.-" FT /note="Prenyltransferase family protein. InterPro: UbiA FT prenyltransferase" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2B0" FT /db_xref="InterPro:IPR000537" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:A1K2B0" FT /protein_id="CAL92965.1" FT /translation="MENNTLVPLVVDLDGTLTPTDTLVESGIRLIKQSPLRALGALAAL FT TKGKAALKDAIAAEVDLPVERLPYREPLLDYLREQKAAGRKLVLATAAHCSIADKVAGH FT LGLFEQVLATRPGRNLKGSAKLAAIRSEVGTDFVYAGDCRADLPIWKAARAAVLVAVPP FT SVADEVRRTTPVERDFAPDAAGPKVWARAFRVHQWLKNLLLFVPLFTAFSFFDLTKVGV FT LAAAFVAFSLAASATYVVNDLWDLDNDRVHPRKRARPFASARIPILQGLGAAAAALAVA FT LGVAWAISPPFLLMLLAYLVLTSAYSWVLKEYVLIDVLMLSLLYTLRIIAGSVASGIVI FT SSWLLAFSVFLFLSLALVKRCSELVSLEQSGGAATRGRDYRVTDLVVLWQLGVGAALSA FT VVVFGLFITAPDTVARYGTPHLLWAVAMALTYWLARLWIKTSRGEMHDDPVVYAIKDRG FT SRVTVSAMVGVMAAAHYFRLEWIE" FT CDS 373681..374046 FT /transl_table=11 FT /locus_tag="azo0349" FT /product="putative Small Multi-Drug resistant family FT protein" FT /note="Putative Small Multi-Drug resistant(SMR)family FT protein, 30% identical to TrEMBL;Q8XZS2. Has PF00893,Small FT Multidrug Resistance protein;IPR000390, Smr:This family is FT the Small Multidrug Resistance (SMR) family. Several FT members have been shown to export a range of toxins, FT including ethidium bromide and quaternary ammonium FT compounds, through coupling with proton influx." FT /db_xref="GOA:A1K2B1" FT /db_xref="InterPro:IPR000620" FT /db_xref="UniProtKB/TrEMBL:A1K2B1" FT /protein_id="CAL92966.1" FT /translation="MRTAIVALLSIALSVTAQFSLKAGMASEGVRRALAEPHSLQTLLT FT VLTDKFVFGGFMLYGLGAVIWLDVLSRWDVSKAYPLVGLGFVLTLGVGLALGEQVNAQR FT FAGVALICAGVFLVGRS" FT CDS complement(374102..375397) FT /transl_table=11 FT /locus_tag="azo0350" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein. Homology to FT gll2146 of G. violaceus of 44% (trembl|Q7NIN7(SRS)) no FT domains predicted signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K2B2" FT /protein_id="CAL92967.1" FT /translation="MPAAPTRIALALALAAAAAAAHADTSTLVGWARLPAATFSDGPTS FT GQFAAANPYGSNLPPYVAQQPVQGFSGVLRGPGHSIRVIADNGFGAQTNSADTLLRAYA FT LVPDFKTARGGSGTVSAADWKTGRPLAAFTEASRITLHDPDNLLGNRIQADYTHYYNNP FT ANPEVAPAIRAGRLLTGADFDIESVREDQFGRLWFGDEFGPYLIQTDADGKVLRREVAL FT PGVFAPQNPAVTSGAVTANLGSSGGFEGMAINKRGDRLYTLLEKTVTGDAAKTLRINEF FT DIRKGAYTGVNYRYRLEADGTAIGDMTAIDDERFIVIERNGCTATSACAPFKKLFLADV FT SGVANGGEVVKTELVNLMDVADPDDLNGDGQTRFSFPYTTIEDVLILDANSLLVINDNN FT FPYGGGRELASDDTEFLKIRLPRPIRNPTTAK" FT CDS complement(375522..376307) FT /transl_table=11 FT /gene="nodJ" FT /locus_tag="azo0351" FT /product="ABC transporter permease NodJ" FT /function="ABC-type multidrug transport system permease FT component" FT /note="Forms with NodI a membrane transport complex FT involved in the nodulation process. it probably exports a FT modified beta-1,4-linked n-acetylglucosamine FT oligosaccharide. Belongs to the ABC-2 integral membrane FT protein family, TREMBL:Q7WHD1 (49% identity); FT SWISSPROT:O52619 (49% identity). InterPro (IPR000412): ABC FT transporter, family 2. Pfam (PF01061): ABC-2 type FT transporter. TMHMM reporting six transmembrane helices. TC FT (3.A.1.102): The Lipooligosaccharide Exporter (LOSE) FT Family." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2B3" FT /db_xref="InterPro:IPR000412" FT /db_xref="InterPro:IPR005981" FT /db_xref="InterPro:IPR013525" FT /db_xref="InterPro:IPR013526" FT /db_xref="UniProtKB/TrEMBL:A1K2B3" FT /protein_id="CAL92968.1" FT /translation="MTPNPWRPPALSRRFIPVWQRNFLVWRKLALPSVLGNLADPVIYL FT FGLGFGIGLLVPEVGGVSYISFLAAGMVCYSTMNSATFEVLYSSFSRMHVQRTWDAILN FT APVALDDVVFAELVWAASKALLSGAAILLVTTLFGLVEVRYALWVLPLIFLVGLTFAAL FT GLIMTALAPSYDFFMYYFTLFVTPMMLVSGVFFPADQLPPLLHAATRALPLTHAVEIAR FT PLLLGRVPEGVGLHLAVLAGYAVVAFWVALALTRRRLQK" FT CDS complement(376345..376629) FT /transl_table=11 FT /locus_tag="azo0352" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to mvpT of FT E. carotovora of 44% (trembl:Q6D393) No domains predicted. FT No TMHs No signal peptide" FT /db_xref="UniProtKB/TrEMBL:A1K2B4" FT /protein_id="CAL92969.1" FT /translation="MERSFIFKSKHGQTVGLPPRVELPKSVKQVDIVALGQARLIVPSG FT GAWDSWFESEGVSDDFMDTREQPSGQYRGSFRTHQPYARYQDDVLGLAP" FT CDS complement(376663..376758) FT /transl_table=11 FT /locus_tag="azo0353" FT /product="hypothetical protein predicted by FT Glimmer/Critica" FT /note="Hypothetical protein predicted by Glimmer/Critica. FT No homology to the data bank. No domains predicted. No FT signal peptide No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K2B5" FT /protein_id="CAL92970.1" FT /translation="MRLMVRPTVLEAEQTSPDREQLDELENSLDP" FT CDS 377176..378156 FT /transl_table=11 FT /locus_tag="azo0354" FT /product="putative methylase" FT /function="Site-specific DNA methylase" FT /EC_number="2.1.1.37" FT /note="Region start changed from 377491 to 377176 (315 FT bases)" FT /db_xref="GOA:A1K2B6" FT /db_xref="InterPro:IPR001525" FT /db_xref="UniProtKB/TrEMBL:A1K2B6" FT /protein_id="CAL92971.1" FT /translation="MPTFVDLFCGAGFGARGAVRGGGVPLLGLDAWNLATETYKANFPQ FT ADTITEKIEDVVPKTLGRKYRPDVLLTSPECTSHSIARGAKPGLETSRETAIGIVPWVE FT AMEPRWVIVENVNRMKKWDRHDELVQTIEGLGYAVSDLLLNSADFGSAQARKRMFLVCD FT RKGTTVGREDLLGLVSTPRKTAYDIIDWEADYPATLLRKPGRAPATLERAERAIAELGV FT GVPFLIVYYGSDYAGGWQTLDVPLRTVTTVDRFGLVTWKGDTPYLRMLQPAELLLAMGG FT ATEHVLPHGNRRDKVKLCGNGVCSDVMTAIFQWISLNQAKQQDAA" FT CDS complement(378157..379323) FT /transl_table=11 FT /locus_tag="azo0355" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to lpg1234 FT of L.pneumophila of 42% (gnl|keqq|lpn:lpg1234(KEGG)). Has FT PF04471, Restriction endonuclease;IPR007560, Mrr_cat; FT Prokaryotic family found in type II restriction enzymes FT containing the hallmark (D/E)-(D/E)XK active site. Presence FT of catalytic residues implicates this region in the FT enzymatic cleavage of DNA. No TMHs. No signal peptide." FT /db_xref="GOA:A1K2B7" FT /db_xref="UniProtKB/TrEMBL:A1K2B7" FT /protein_id="CAL92972.1" FT /translation="MTFFTGETLGQVDLIVDAVYAGYKTERGGMADPLVPLVGVSRQGG FT FRYRGTRERPTLLVLTSNLAEPEWPDQLDETTGTFIYYGDNRHPGRLLHDTPRFGNQLL FT RQIFDWAHLGQRHLVPPILVFTTEATGRTFRFRGLAVPGSPALAATEDLVALWKTTEGQ FT RFQNYKAVFTILDEAVIPRAWVHAVGRGETSGLAPVAWNAWLSAGGIRPLMAPRSLLVR FT SKAEQLPATPEDQALIEVIRQRYKENPFGFEACAGALTRLLLPDVARLDLTRPWRDGGR FT DGIGRLRIGQSPAAIEVDFALEAKCYGANNAVGVKEVSRLISRIKHREFGVLVTTSYVD FT RQAYQEVTDDGHPVILTTAQDIVGLLRSAGVRTPTQVDAWLDGITASV" FT CDS complement(379320..379709) FT /transl_table=11 FT /gene="vsr" FT /locus_tag="azo0356" FT /product="putative hypothetical very short patch repair FT endonuclease" FT /EC_number="3.1.-.-" FT /note="Putative hypothetical very short patch repair FT endonuclease. Homology to vrs of E. coli of 29% FT (sprot|VSR_ECOLI) All proteins in this family for which FT functions are known are G:T mismatch endonucleases that FT function in a specialized mismatch repair process used FT usually to repair G:T mismatches in specific sections of FT the genome. Interpro: DNA mismatch endonuclease vsr FT (IPR004603) Pfam: DNA mismatch endonuclease Vsr Tigrfam: FT vsr: DNA mismatch endonuclease no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2B8" FT /db_xref="InterPro:IPR004603" FT /db_xref="InterPro:IPR007569" FT /db_xref="InterPro:IPR011335" FT /db_xref="UniProtKB/TrEMBL:A1K2B8" FT /protein_id="CAL92973.1" FT /translation="MMSRIKGRDTGPELSLRRNIWALGLRYRLQYRIGRTRPDMVFVRA FT RLAVFVDGCFWHGCPQHSTMPKNNRDFWERKLRRNRERDAENTHSLEAEGWRVLRLWEH FT EIQASPADCARRIAVMLGKAEESKA" FT CDS complement(379781..380920) FT /transl_table=11 FT /locus_tag="azo0357" FT /product="hypothetical protein" FT /db_xref="InterPro:IPR011006" FT /db_xref="UniProtKB/TrEMBL:A1K2B9" FT /inference="nucleotide motif:Gismo" FT /protein_id="CAL92974.1" FT /translation="MDWRVLVVDDKAADDVAETIGGNKTVPKPDSISCEKCADFFQAVE FT LLKNQRFDLVILDLKDDGAPEQETLAGERVFEEIKKCRFVPVVFHTGFPHKVGDQTSPY FT VRVVTRADWENLRSTIKEVLDTKLPRLIRHIEEEQRRFMWESAERIWADDLHKDNPTDL FT VYLLARRLANSLSGDVVRSFFGSDGTEGAPKSEMVHAVELYIFPPISQHFLFGDIFEKK FT TSGKSEYFVSLTPSCDHAQRKAEFLLFARCADLSDSEEWKKVQGFLEAKTAPSKSAVND FT LKELMKDNNPRPRLQDRYKYLPGTSFIPDLLVDLQNTLTIDREKLVSGEAGLERIASLD FT SPFSEYLQAKMIRYFGRVGTPSLDTDLTFERFKSRTMKT" FT CDS complement(380934..383189) FT /transl_table=11 FT /locus_tag="azo0358" FT /product="putative two-component sensor kinase" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.3.-" FT /note="Region start changed from 382943 to 383189 (246 FT bases)" FT /db_xref="GOA:A1K2C0" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="UniProtKB/TrEMBL:A1K2C0" FT /protein_id="CAL92975.1" FT /translation="MSNGRNSYESALRPRARIMKTLGSELISNDAVAVIELVKNAYDAE FT ASRVLIKFVGPLQPKQGCIEIFDDGAGMSLDVVRGAWMEPATPGKRQKTSSGSKGRRVL FT GEKGIGRFAAMRLASELELITRARGADQEVYGIFDWTQFEDEQKYLDEVLILTEVRKPE FT VIRSDVGLDAIWPKHEVPVECPPSEQGTLLRMNNLAQAWDAERFRLIQRGLSRLISPFK FT ENKDFSVFLQAPEAFSEFSSEITPPVVLNYPHYTVSGMVDPQGKCDLMLEVKATGEVRS FT VTGGFVREGKDGLQYLENEAYSKLKQTTENQLENDKTEWEKKLPTCGPLQIELRIWDRD FT DLGNVIQQTRSNLQNIRADLDAFAGINIYRDGFRVLPYGEPNNDWLRLDIRRVQNPTKR FT LSNNQIVGHISITADQNNGLKDQSNREGLDENQSYSDLREIMKSILSKIEDLRKRSKGT FT GEGGNKDKQTLNLFAPLDLSPIRQHLESVSPKDEVAKELINNVERAFNTKVESLKAVVA FT KYHALATLGQLIDVLLHDGRLPLAKIRKESLLAQEDIVEGLLTGEDLLNKLAGRLRIIH FT GQSDVLATVFRRVEPFGGRKRGRPKQLYLEKIIEDAFGVCASQIADLQIATSLSTGQTL FT VRVDEAEIQEVIVNLLQNSLYWLQFVDTAVRRIDVSVSRTAQDHVEIIFSDTGPGIPDE FT NRARIFEPYFSTKKDGVGLGLAIVGEIIMDYYGGKLELLDSSGASGAVFRITLTKRV" FT CDS complement(383349..384059) FT /transl_table=11 FT /locus_tag="azo0359" FT /product="conserved hypothetical membrane protein." FT /note="Conserved hypothetical membrane protein. Homology to FT MS2110 of M.succiniciproducens of 40% FT (gi|52426165|ref|YP_089302.1|(NBCI ENTREZ)). No domains FT predicted. No signal peptide. 1 TMHs" FT /note="Family membership" FT /db_xref="InterPro:IPR011528" FT /db_xref="UniProtKB/TrEMBL:A1K2C1" FT /protein_id="CAL92976.1" FT /translation="MTEILGAAYNGMLLLFLLAVVGALLRSPLVKGWFGEAQSALAQEL FT LLDKAIYTAINDITLPTTNGTTQIDHVVVSRYGIFVIETKNMKGWIYGTEKGATWTQNL FT YGRKYRFQNPLHQNYRHVRALAEFLKLDDSHFHSVVMFWGNATLKNPLPPNVMTHGYVS FT YIKGKQRVLFSDEEVAAIITAIQTGRLPRTWATRTAHVESLKARHANTGSRNGYVRTYP FT PTQSAAANQIVGNE" FT CDS complement(384192..385178) FT /transl_table=11 FT /gene="nodI" FT /locus_tag="azo0360" FT /product="ABC transporter ATP-binding protein NodI" FT /function="ABC-type multidrug transport system ATPase FT component" FT /note="Nod factor export ATP-binding protein. Part of the FT ABC transporter complex nodIJ (TC 3.A.1.102.1) involved in FT the export of LCO (lipo-chitin oligosaccharide) and a FT modified beta-14-linked N- acetylglucosamine FT oligosaccharide. Responsible for energy coupling to the FT transport system, TREMBL:Q7W9D3 (58% identity); FT SWISSPROT:O52618 (53% identity). InterPro (IPR003439): ABC FT transporter. InterPro (IPR001687): ATP/GTP-binding site FT motif A (P-loop). InterPro (IPR003593): AAA ATPase. Pfam FT (PF00005): ABC transporter. TC (3.A.1.102) The FT Lipooligosaccharide Exporter (LOSE) Family." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2C2" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR015851" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K2C2" FT /protein_id="CAL92977.1" FT /translation="MSAALPVGSDTSGEVRPSPLIIRGLVKRYGDNEVVRGIDLELAAG FT ECFTLLGPNGAGKTTTLRCALGLTAPTAGDIRLCGEPVPARAREARMRVGIVPQIDNLD FT PDFTCTENLLVYGRYFGIKDADIRARIPELLAFAGLENKADARIQSLSGGMKRRLTLAR FT ALVNRPELLVLDEPTTGLDPQARHLIWDRLKQLIRNGTTVLLTTHFMDEAERLSDHLAI FT LDAGRLLTAGSPRDVIAQHIEPQVVEVFGEWGNAGNGTAGAPAWAAQHAAALSDRFEIS FT GETAFCYVRDPAPLLAHLAAQPGLRYLHRPANLEDVFLKLTGRELRD" FT CDS complement(385249..385866) FT /transl_table=11 FT /locus_tag="azo0361" FT /product="conserved hypothetical glutathione S-transferase" FT /EC_number="2.5.1.18" FT /note="Conserved hypothetical glutathione S-transferase FT protein. Homology to cv3306 of C. violaceum of 50% FT (trembl|Q7NSW3). Conjugation of reduced glutathione to a FT variety of targets. Pfam: Glutathione S-transferase, FT N-terminal domain; Glutathione S-transferase, C-terminal FT domain. no signal peptide. no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2C3" FT /db_xref="InterPro:IPR004045" FT /db_xref="InterPro:IPR004046" FT /db_xref="InterPro:IPR010987" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR017933" FT /db_xref="UniProtKB/TrEMBL:A1K2C3" FT /protein_id="CAL92978.1" FT /translation="MTMKLLASLTSPYARKIRIALAEKNIPFELVVDSPWEAATRVPDV FT NPLGKVPALVLDDGEVFFDSPVIAGYIETLGHAPALLPAGGIERVRVRQSEALVDGILD FT AAVTAYLEGRRPEAQQSAPNLDRQYDKIQRSLDLLEERLAGRNWLDGDSMQLGDIALGV FT ALGYLDLRLGYLEWRAGRPVLEAFAQRMFARPSFAATVPPAG" FT CDS complement(385891..386562) FT /transl_table=11 FT /locus_tag="azo0362" FT /product="conserved hypothetical protein" FT /function="predicted hydrolase of the alpha/beta FT superfamily" FT /note="Conserved hypothetical protein. Homology to rsc0328 FT of R. solanacearum of 59% (trembl|Q8Y2K7). Pfam: Prolyl FT oligopeptidas family no signal peptide no TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K2C4" FT /protein_id="CAL92979.1" FT /translation="MTNRPLATESALLRGGAGAIEVLIDAPEHVRGIALICHPHPLYGG FT ANTNKVAHTLARTFRDLGYAAVRPNFRGVGKSEGTHDLGNGETEDMLSVIAWMQSRWGQ FT LPLALGGFSFGGFVQTRVANRLAEGVAPPRQIVLVGMAAGTAADGARHYETPELAKNVP FT ALIIHGEADDTVPLDNVFDWARPQELPVIVIPGADHFFHARLHLIRDLMLRNVPPAGQA FT A" FT CDS complement(386572..386892) FT /transl_table=11 FT /gene="fer21" FT /locus_tag="azo0363" FT /product="putative ferredoxin 2Fe-2S protein" FT /function="Ferredoxin" FT /note="Putative ferredoxin 2fe-2s protein. Homology to fer2 FT of C. pasteruianum of 35% (sprot|FER2_CLOPA). Ferredoxins FT are iron-sulfur proteins that transfer electrons in a wide FT variety of metabolic reactions. no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2C5" FT /db_xref="InterPro:IPR002023" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:A1K2C5" FT /protein_id="CAL92980.1" FT /translation="MSYFKHHVFFCCNQRQGGETSCNDHGASAMQVYAKERTAELGLKG FT KGSVRINKAGCLGRCDDGPVLVVYPDNVWYTYVDKDDIDEIINEHLAHGRIVERLRLAD FT PA" FT CDS complement(386915..388000) FT /transl_table=11 FT /locus_tag="azo0364" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothtical membrane protein. Homology to FT rc03284 of R. solanacearum of 35% (trembl|Q8Y2L8(SRS) Has a FT weak hit to PF04892(IPR006976;vanZ)in Smart:This family FT contains several examples of the VanZ protein, but also FT contains examples of phosphotransbutyrylases. VanZ confers FT low-level resistance to the glycopeptide antibiotic FT teicoplanin (Te). Analysis of cytoplasmic peptidoglycan FT precursors, accumulated in the presence of FT ramoplanin,showed that VanZ-mediated Te resistance does not FT involve incorporation of a substituent of D-alanine into FT the peptidoglycan precursors . no signal peptide 10 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR006976" FT /db_xref="UniProtKB/TrEMBL:A1K2C6" FT /protein_id="CAL92981.1" FT /translation="MPPRPASSLPRNLALAYAVLVIYACLHPFAGWKASGLPLFDFLVA FT PWPKYFQPIDAVLNMLGYLPLGFVTVAALPRGWPRWRWVVVAALLGAGLSFGLETVQNL FT LPSRVSSNVDLGANAAGALAGALLGARWAHPLFDHRGGLHRWRAERIVGGHTGDAGLIL FT LGLWLLAQLTPDGLLFGSGDLRGLLGLPAPLLFSPERFIGFETGLIAASVLALGLLARC FT MMRVPRPWPVVVLFLLGLGAKSIATSTFFVPGEPLAWLTPGAARGLALGSVLLALALLL FT PRVLQHALAGSALLAATALINLMPENPYLFLGRRLLNQGNFLNFHGLTQLVASLWPFAA FT LAYLSALGLWRGEHLAGERRL" FT CDS 388715..389227 FT /transl_table=11 FT /locus_tag="azo0365" FT /product="Conserved Hypothetical protein" FT /note="Conserved Hypothetical protein, Q82Y48,Rhodanese FT type protein. Has SMART SM00450 Rhodanese Homology FT Domain(RHOD)starting at position 47-153aa;Rhodanese, a FT sulfurtransferase involved in cyanide detoxification (see FT IPR001307) shares evolutionary relationship with a large FT family of proteins. No Signal peptide or TMH reported FT Present." FT /note="Family membership" FT /db_xref="InterPro:IPR001763" FT /db_xref="UniProtKB/TrEMBL:A1K2C7" FT /protein_id="CAL92982.1" FT /translation="MSEASIEAPDVASAPRSIADAVPTAPAVLEAARRRAREEGLPYAG FT SLAPVDAWALVEAGAALLVDVRSAEERRFVGHVPDSLHVAWMTGLSLSRNPRFVRELEG FT KAGKGRVVLLLCRSGKRSAAAAEAAAKAGFTHVFNVLEGFEGDLDDRQRRGAFNGWRHA FT GLPWIQD" FT CDS 389292..390254 FT /transl_table=11 FT /gene="srpH" FT /locus_tag="azo0366" FT /product="probable serine O-acetyltransferase" FT /function="Serine acetyltransferase" FT /EC_number="2.3.1.30" FT /note="Probable serine O-acetyltransferase plasmid (EC FT 2.3.1.30) (SAT). Homology to srpH of Synechococcus of 55% FT (sprot|SRPH_SYNP7) no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2C8" FT /db_xref="InterPro:IPR001451" FT /db_xref="InterPro:IPR011004" FT /db_xref="UniProtKB/TrEMBL:A1K2C8" FT /protein_id="CAL92983.1" FT /translation="MSASTGAVEAAYEDVGGWGVSQVVAELRAARERWRAAQQRNREFA FT VREFPSRDALRQIAADLCGVLFPMRLGPPELHQEGEDYYVGHTLDSTLNALFHQVRLEL FT GYLARHRGIEADIDADAARIVKRFAGGLPALRTLLDSDVEAAYTGDPAARSVDEVLLCY FT PGTLAIIHHRLAHSLHALGARLVARIIAEIAHSATGIDIHPGAQIGSGFFIDHGTGVVI FT GETTVIGNRVRLYQAVTLGARRFAVDENGALEKGAARHPVLEDDVVVYAGATILGRVTI FT GRGSSIGGNVWLTRSVPPGSHVSQASLQHESAAQRVAAS" FT CDS 390251..390484 FT /transl_table=11 FT /locus_tag="azo0367" FT /product="SgrAlc control protein" FT /function="predicted transcriptional regulators" FT /note="SgrAlc control protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2C9" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:A1K2C9" FT /protein_id="CAL92984.1" FT /translation="MSPASVIASFGAAVRQFRERHGWSQELLAERADLNRSYLGEVERG FT TVVPSLATAVKLAAALDIPLSNLLSHCENGRS" FT CDS 390602..391528 FT /transl_table=11 FT /gene="mmpI" FT /locus_tag="azo0368" FT /product="probable immunodominant 35kDa protein" FT /note="Probable immunodominant 35 kDa protein. Homology to FT mmpI of Mycobacterium avium of 69% FT (gi|2498566|sp|Q48899|MMP1_MYCAV(SwissProt (ExPASy)). No FT domains predicted. No signal peptide. No TMHs.," FT /note="High confidence in function and specificity" FT /db_xref="UniProtKB/TrEMBL:A1K2D0" FT /protein_id="CAL92985.1" FT /translation="MSTLPEPTALGDAAARQLANATKTTAQLSTISPRWLTHLLQWLPV FT EAGIYRLNTVKNPRDVRVACSQRDESELPQTFVDYDEAPREYFLNAVTTILDVHTRVSD FT LYSSPHDQIKEQLRLTIETIKERQESELINNPDYGLLANVADEQIISTLTGAPTPDDLD FT ELLTKVWKEPAFFLTHPLAIAAFGRECTRRGVPPPTVSLFGAQFLTWRGIPLIPSDKVP FT VDGGKTKILLLRVGEKRQGVVGLFQPGLVGEQSPGLSVRFMGINRNAIASYLISLYCSL FT AVLVPDALAVLDDVEVGKYHDYPDTYK" FT CDS 391503..393335 FT /transl_table=11 FT /gene="csdB" FT /locus_tag="azo0369" FT /product="probable cysteine desulphurase" FT /function="Selenocysteine lyase" FT /EC_number="4.4.1.15" FT /note="Cysteine desulphurases required for the mobilization FT of sulphur from cysteine. They are present in all FT organisms, where they are involved in iron-sulphur (Fe-S) FT cluster biosynthesis. Similar to sprot|CSD1_MYCLE (54%), to FT trembl|Q82WT8 (55%) and to tremblnew|BAB21542 (34%). Pfam FT (PF00266): Aminotransferase class-V Pfam (PF01041): FT DegT/DnrJ/EryC1/StrS aminotransferase family" FT /note="Function unclear" FT /db_xref="GOA:A1K2D1" FT /db_xref="InterPro:IPR000192" FT /db_xref="InterPro:IPR010970" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:A1K2D1" FT /protein_id="CAL92986.1" FT /translation="MTIPTPTSKGAEGLSGAPLPDLPDEATLGALASAFFRALPGAALP FT PADPVRAQVASAPELSLAQGGSRLAPAPVASDPVDPVGGAGAFVVPQAYAAALPQVAPP FT QVPAGVAEGLPLAVPGSPYYFIGEASPYLQSGAAPALPENRVVARSFGLPGEGELKALL FT AEIAAGRPLADAPAADPGGRFYFIDAAKVPAAEPGARAPFDVNAVRRDFPILQERVNGK FT PLVWFDNAATTHKPQAVIDRLAHFYAHENSNIHRGAHELAARATDAYEAARQKVQRFLG FT AGSADEIIFVRGATEAINLVAKTWGVQNIGEGDEIVVSLLEHHANIVPWQQLAAQVGAK FT IRVIPVDDNGQLKLDELQKLLNPRTRLVSVTQVSNALGTVTPIKQVIDMAHAAGARVLV FT DGAQSVSHMRVNVQALDADFFVFSGHKIFGPTGIGVVYGKAALLEQMPPWQGGGNMIAD FT VTFERTLFQPAPNKFEAGTGNIADAVGLGAALDYVERIGLENIARYEHDLLVYATRGLS FT SIAGVRLIGTAADKASVASFVLAGYSTEEVGRALNEEGIAVRSGHHCAQPILRRFGVET FT TVRPSLAFYNTCEEIDRMLAVVRRLARGKGRVGA" FT CDS 393595..394170 FT /transl_table=11 FT /locus_tag="azo0370" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT NE2493 of Nitrosomonas europaea of 67% FT (trembl|Q82S65(SRS)). Has PF01169, Uncharacterized protein FT family UPF0016;IPR001727; This family contains integral FT membrane proteins of unknown function. Most members of the FT family contain two copies of a region that contains an EXGD FT motif. No signal peptide. 5 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2D2" FT /db_xref="InterPro:IPR001727" FT /db_xref="UniProtKB/TrEMBL:A1K2D2" FT /protein_id="CAL92987.1" FT /translation="MEAFLVSTSIVALAEIGDKTQLLAFILAAKFRKPWPIVLGILVAT FT LANHAGAGALGSFVTSLVSPEVMRWVLGLSFIGMAIWTLIPDKFEEDDATFARFGVFGT FT TLIAFFLAEMGDKTQVATVALAAQYQALVAVVMGTTLGMMIANVPAVLLGDRIANRIPV FT KLVHGIAAAIFAVLGLATLLGAGEGLGL" FT CDS 394317..395381 FT /transl_table=11 FT /locus_tag="azo0371" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. No TMHs. Signal peptide FT present." FT /db_xref="UniProtKB/TrEMBL:A1K2D3" FT /protein_id="CAL92988.1" FT /translation="MPFPLISWRTIVLRPLRHVLWAGLIGLIGEAAAAPCDPLVGEFLM FT EFGKEEIQLRIERSDGRYFVRLDDGRGQWREQLEALQEVPLDELKGLVPDVECGLGGGG FT GVFVKTAVGGARLADNPAEKGHEVGYALTGFLMVIPQGFSISVFDLFPLADHTGAAEPR FT VEPSPERAVAGVMRCPGDRAPDLTQASYDALPKYMKDNIQEGQPLERRTERMCGQRLVR FT SIDSRYAKGAYAKIHGESLQELRSLLEAGQVPRDDKGVSQWWELGKVLLTYHGDGKPSE FT DPLAATSSAIFLNLIVPHLTQESLKARPVRLRALGQIVTTLAGRSDADAREALARMKAA FT GLPVHAQAAAGERG" FT CDS complement(395413..395931) FT /transl_table=11 FT /locus_tag="azo0372" FT /product="conserved hypothetical protein" FT /function="Putative lipid carrier protein" FT /note="Entry name SWISSPROT:YHBT_ECOLI Prim. accession # FT P45474 InterPro IPR003033; SCP2. Pfam PF02036; SCP2; 1. FT Prediction: Non-secretory protein Signal peptide FT probability: 0.001 Number of predicted TMHs: 0 Identities = FT 46/107 (42%)" FT /db_xref="GOA:A1K2D4" FT /db_xref="InterPro:IPR003033" FT /db_xref="UniProtKB/TrEMBL:A1K2D4" FT /protein_id="CAL92989.1" FT /translation="MHFPALPALPLTELLPHSLRQRVAQQFEQRLAGLRIPAFTVPAPL FT ARIAARLPQQIPTQALVTALNLALGRILPRDQLEALSGRGLRIRVTDAGLTLDFTLGDK FT GFRRAAGSSTPDLIISASTRDFLALALREEDADTLFFSRRLLMEGDTELGLLVKNTLDA FT VDWSALRPV" FT CDS complement(395946..396842) FT /transl_table=11 FT /locus_tag="azo0373" FT /product="conserved hypothetical peptidase" FT /function="Collagenase and related proteases" FT /EC_number="3.4.-.-" FT /note="Conserved hypothetical peptidase. Homology to FT Rsp0969 of R. solanacearum of 51% (trembl|Q8XR90). Pfam: FT Peptidas family U32 no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2D5" FT /db_xref="InterPro:IPR001539" FT /db_xref="UniProtKB/TrEMBL:A1K2D5" FT /protein_id="CAL92990.1" FT /translation="MKLSLGPLLYYWPRQSVLDFYAEIADSPVDIVHLGETVCSRRHEL FT RLDDWIEVAAVLADAGKEAVLSSQSLIESESDLKTLRRVVGQQRFRVEANDMAAVRLLA FT EAGRRDWIAGPTLNVFNPHTLGLLVEAGASRWVVAPEMSGAALAEVRSTLPAPIETEIF FT AYGRLPLAHSARCFTARHYNLQKDGCEFRCLGIADGLVLRTREGEPFLTLNGVQTQSAK FT VHTLLGDLPALAGRAEVLRISPQGAHTRGIIEHFRATLDGRQTPAEALAASSAHMPAAP FT CNGFWHGRPGVEQFVPA" FT CDS complement(396857..397870) FT /transl_table=11 FT /locus_tag="azo0374" FT /product="conserved hypothetical peptidase" FT /function="Collagenase and related proteases" FT /EC_number="3.4.-.-" FT /note="Conserved hypothetical peptidase. Homology to cv4084 FT of C. violaceum of 64% (trembl|Q7NQQ39. Pfam: Peptidas FT family U32 no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2D6" FT /db_xref="InterPro:IPR001539" FT /db_xref="UniProtKB/TrEMBL:A1K2D6" FT /protein_id="CAL92991.1" FT /translation="MTSSQRIELVCPAGSLPALKTAIDHGADCVYLGFKDATNARNFTG FT LNFDPAQMREGIAYAHARRRKVLLALNTYPQTANWAGWTAAVDRAAEFGIDAVILADPG FT LMAYAAKTHPQLRLHLSVQGSATSYEAINFYHERFGIQRAVLPRVLSMAQVEQVVGRTP FT VEIEVFGFGGLCVMVEGRCALSAYATGESPNCNGACSPGKHVRWEQTPQGMETRLNGIL FT IDRFGEHERAGYPTLCKGRFEVNDETYYAIEEPTSLNTLEMLPELARVGVAAIKIEGRQ FT RSPAYVAQVTKVWRAALDRVVADPAGFHALPAWMAELNKVSEGQSHTLGAYYRPWK" FT CDS complement(398061..399524) FT /transl_table=11 FT /locus_tag="azo0375" FT /product="probABLE SODIUM/SOLUTE SYMPORTER TRANSMEMBRANE FT protein" FT /function="Na+/proline symporter" FT /note="TREMBL:Q8Y273: 59% identity, 72% similarity FT Osmoregulated proline transporter (Sodium/proline FT symporter). CATALYZES THE SODIUM-DEPENDENT UPTAKE OF FT EXTRACELLULAR PROLINE. InterPro: Sodium:solute symporter FT family InterPro:IPR001734; Na/solut_symport. Pfam:PF00474; FT SSF; TMHMM predicted transmembrane helices sss: SSS sodium FT solute transporter sup" FT /note="Function unclear" FT /db_xref="GOA:A1K2D7" FT /db_xref="InterPro:IPR001734" FT /db_xref="InterPro:IPR018212" FT /db_xref="UniProtKB/TrEMBL:A1K2D7" FT /protein_id="CAL92992.1" FT /translation="MLIGFVTAYLVLSIAIGLYAATRVKNSTDYVAAGRNLPLYIVTAT FT VFATWFGSETVLGISATFIDEGLRGLWSDPFGASLCLILAGLFFARPLYRMNLLTLGDY FT YRTRYGRTVEVLCSLAIVVSYLGWVSAQISALGLVFNILSEGSISAETGMLVGAGIVLA FT YTLFGGMWSVALTDFMQMAIIIVGLAYIAWLVGDMAGGVGAVVAHANEAGKLNFLPAFD FT AKDIIAFTAGILTMGFGSIPQQDVFQRFNAARNERIAVQGTLLGGSGYFLFAFIPLFIA FT YSATLIDPALVANYQESDSQQILPQLILEHTPLFAQVLFFGALLSAIMSTASGTLLAPS FT VTFSENILRSTFRGMNDRQFLVMTRVVVVLFALLVTWYAIHTDESIHGMVENAYKVTLA FT TAFVPLAFGLYWKRASTQGALVSIVAGLAVWVLLEIVAPEADVPPHFAGMLAGVVGMVV FT GSLAPQTLVRQSHGHSAHLNIGAHPQSRN" FT CDS complement(399721..401841) FT /transl_table=11 FT /locus_tag="azo0376" FT /product="conserved hypothetical protein" FT /function="Ornithine/acetylornithine aminotransferase" FT /note="Conserved hypothetical protein. Homology to ebA3609 FT of Azoarcus sp. EbN1 of 62% (gnl|keqq|eba:ebA3609(KEGG)). FT InterPro: Aminotransferase class-III (IPR005814), Arginase FT family (IPR00594). Pfam: Aminotransferase FT class-III,Arginase family. Tigrfam: argD: acetylornithine FT and succinylornithine aminotransferase, FT GABAtrnsam:4-aminobutyrate aminotransferase. no signal FT peptide. no TMHs" FT /db_xref="GOA:A1K2D8" FT /db_xref="InterPro:IPR005814" FT /db_xref="InterPro:IPR006035" FT /db_xref="InterPro:IPR010164" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="InterPro:IPR020855" FT /db_xref="InterPro:IPR023696" FT /db_xref="UniProtKB/TrEMBL:A1K2D8" FT /protein_id="CAL92993.1" FT /translation="MNVPTPLPSGPHDRVHIVGAAFALGAPHGGSADGPEALRHAMLPE FT RLRTTGITGTWLEPLRPLRTPPPDAPMEERLAAVGEYCARLAEQIAGLPEDGFPLVLGG FT DHAVAIGTWRGVARRQGGAPGLIWIDAHLDSHTDQSTWSGNIHGMPLAALLGEGAPALT FT AIPGPRLDPARVCIIGARDWEPAERERLDRLGVRVFDIAEVRERGLPTVFCEALTIARS FT GHGRDGGFGVTLDLDALDPLAVPAVTCPTPDGIDPQQLVDVFHTLRSCGDFVGLEIVEY FT RPDLDPDGHSAALTARLVAAALGPATYWLREKERRFGATNYAPMPVVFHRGEGVWLWDV FT EGTRYLDMMSAYSAVSFGHANPRLLRALQDQAQLLTLTSRSFSNDRLPLLLERLCSLLG FT FERALPVNTGLEAVETALKAARKWAYIVKGVPPDRAEIIACEGNFHGRSITIVGLSSKE FT QYRDGFGPFPPGLRRVPFGDPTALEAAITPHTAAFLVEPIQGEGGIIVPPPGYLAHCAE FT ICRRHNVLLIADEVQTGLGRTGRLLACDHDGVRPDGLILGKALGGGLLPVSAFLADREV FT MDVFRPGDHGSTFGGNPLGAAVALEVLDLLAETRPWEAAERLGRRLRAELEAAELPCVR FT EVRGRGLLIGVALDPVKAPAQLVAELLLARGIATRDTNGNVIRLAPPLTIDEGTLDRAA FT AIIIDTLNPLGR" FT CDS complement(401938..403467) FT /transl_table=11 FT /locus_tag="azo0377" FT /product="probable ubiquinone biosynthesis protein" FT /function="predicted unusual protein kinase" FT /note="Probable ubiquinone biosynthesis protein ubiB. FT Required probably indirectly for the hydroxylation of FT 2-octaprenylphenol to 2-octaprenyl-6-hydroxy-phenol the FT fourth step in ubiquinone biosynthesis (By similarity). FT TREMBL:Q82TL7:65% identity InterPro:IPR004147; ABC1. FT IPR010232; UbiB. Pfam:PF03109; met_pdase_II: methionine FT aminopeptida" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2D9" FT /db_xref="InterPro:IPR004147" FT /db_xref="InterPro:IPR010232" FT /db_xref="InterPro:IPR011009" FT /db_xref="UniProtKB/TrEMBL:A1K2D9" FT /protein_id="CAL92994.1" FT /translation="MRLLRLAKIITVSLRFGLDRMILDADASGRLGRIWHRVFFWRRFS FT EPRAVRLRKALESLGPIFVKFGQMLSTRRDLLPPDLADELALLQDRVPPFPTEQALAVL FT EGFYGRPVDAVFRDFERTPVASASVAQVHFARLPDGTEVAVKILRPGIERVIAHDLALM FT EVGAMLLDKAWPEGRRLKPREVVAEFSKYLRDELDLMREAANCSQLRRNFKDSPLLLVP FT EVYWDWCGRSVMVMERMHGVPISQTAAVTAQGTDLKALSRAGVEIFFTQVFRDGFFHAD FT MHPGNIFVHADGRYIALDFGIMGTLNEVDKNYLAQNFLAFFKRDYKRVAMAHIEAGWVP FT AKTRVDEFEAAIRTVCEPIFDKPLKDISFGKTLLRLFQTARRFEMEVQPQLVLLQKTLL FT NIEGLGRQLDPELDLWKTAKPFLERWMNEQMGWRALVRGIKEEAPAWAGTLPQLPRLVH FT HNLVESSHHHVVHQAALASLAVTQRRQGRLLALLVIAAAALVALELHRLLG" FT CDS complement(403712..405787) FT /transl_table=11 FT /locus_tag="azo0378" FT /product="putative TonB-dependent receptor" FT /note="Putative TonB-dependent receptor. Homology to FT bpp0186 ao B. parapertussis of 54% (trembl|Q7W206) The TonB FT protein interacts with outer membrane receptor proteins FT that carry out high-affinity binding and energy-dependent FT uptake of specific substrates into the periplasmic space. FT These substrates are either poorly permeable through the FT porin channels or are encountered at very low FT concentrations. In the absence of TonB these receptors bind FT their substrates but do not carry out active transport. FT Interpro: TonB-dependent receptor (IPR000531) Pfam: FT TonB-dependent receptor (PF00593) signal Peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2E0" FT /db_xref="InterPro:IPR000531" FT /db_xref="InterPro:IPR012910" FT /db_xref="UniProtKB/TrEMBL:A1K2E0" FT /protein_id="CAL92995.1" FT /translation="MLPRLSPLSLALLCALGTAHAAAQSAAPNDPTAAPPVQLEAVTVS FT ASGLDVDSGAMSTPATVLGGDELVRRRAATLGETLATEPGIHATEFGAGASRPVIRGMD FT GARVRLLSDGAEIMDASTISPDHAVAAEPLLSERIEVLRGPSALAYGGGAVGGVVNVLD FT RRIPTAIPERGVEGSVELRGNTAAREAAGAFEVTAGAGNIAIHAEGLKRDARDYRVGDG FT WAGGRRVDGSYNETETGSLGLSWIGERGYLGVAWTRQRNEYGLPGHAHDLEDCHTHGNS FT LHCGGHDGDDEDDHDHADEGGGVPYVKLDSERWDLRGEYREPFAGISRLRVRASHTRYR FT HDEIEDGAVSTRFRNNASEGRVELQHAPLGGWRGVFGLQTTRRDFSAIGEEAYVPPTLT FT RRHGAFLIEEYPTGDWRFEAGLRHEWQQVEVDADARDRSHRGNSLSLGAVWNFAPDYAL FT GLSLARAQRLPTAEELYADGLHMATRTIERGNADLKAETSHNIDLSLKKLAGATTFNLS FT VFHNRVNDFIYAHTLDALEGMQLIEYAQRDAIFTGVEGQVRQQLDRVFGLTLFGDYVRA FT RLAGGDGDRDRDLPRIPAHRVGLRLDARQGAWQGELEVYRVGRQRQVAEFESSTPGYNM FT VNLGASYAGRIASVPYLFYVKAANLTDELAYSHTSFIKDAAPLMGRNLTMGVKVTF" FT CDS complement(405969..406301) FT /transl_table=11 FT /locus_tag="azo0379" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. signal peptide. No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K2E1" FT /protein_id="CAL92996.1" FT /translation="MRTPLLRAVLALVLVLAQTGALTHLLGHAAEVPQARSASTRIASD FT DRAPVDAFGVCLQCLALGGLDLPLGAGSAALDPGRPGVAHATHALPLPPSSAPALPRCR FT APPALA" FT CDS 406538..408301 FT /transl_table=11 FT /gene="argS" FT /locus_tag="azo0380" FT /product="putative arginine-tRNA ligase" FT /function="Arginyl-tRNA synthetase" FT /EC_number="6.1.1.19" FT /note="Putative arginine-tRNA ligase (EC 6.1.1.19). FT Homology to argS of E. coli of 25% (sprot:SYR_ECOLI) FT CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP + FT diphosphate + L-arginyl-tRNA(Arg). InterPro: Arginyl-tRNA FT synthetase (IPR001278); Aminoacyl-transfer RNA synthetase FT class-I (IPR001412) Tigrfam: argS: arginyl-tRNA synthetase FT Pfam: tRNA synthetases class I no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2E2" FT /db_xref="InterPro:IPR001278" FT /db_xref="InterPro:IPR001412" FT /db_xref="InterPro:IPR005148" FT /db_xref="InterPro:IPR008909" FT /db_xref="InterPro:IPR009080" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR015945" FT /db_xref="UniProtKB/Swiss-Prot:A1K2E2" FT /protein_id="CAL92997.1" FT /translation="MSADPKVLLTDLIKTALKSVAPEHADTAILLERPKQASHGDFATN FT VALQLAKPLKRNPRELAALLLAELPASNLVAKTEVAGAGFINFTLAAAAKTAVVGEVLA FT KGADFGRGAKKNVKVQVEFVSANPTGPLHVGHGRGAAYGASLSDVLCFAGYDVTREYYV FT NDAGRQMDILALSTWLRYLALFGIDVPFPPNAYQGDYVIDMARGLRDAHQGRYAGVTLA FT QVLEGTPGLPVAERKDDEAKQQRELHLDGLIANAKRLLGEDYPFVHGFALNEQLGDGRD FT DLQEFGVHFDKWFSEKSLFDTGLVERAVAELEKRGHIYVQDGAKWFRSTDFGDEKDRVV FT QRENGLYTYFASDIAYHLNKYERGFDRIIDIWGADHHGYIPRVKGAIAALGLPPEKLEV FT ALVQFAVLYRDGQKTSMSTRSGEFVTLRELRREVGNDACRFFYVLRKSDQHLDFDLDLA FT KSQSNENPVYYIQYAHARVCSVLNQWGGEPAELQAADLGKLENERELALCARLAGFPEV FT VQGAAADYAPHQIAFYLKDLAADFHSWYNAERMLVDDEAVKLARLALAAAVRSVLRGGL FT AVLGVSAPESM" FT CDS 408318..408902 FT /transl_table=11 FT /locus_tag="azo0381" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT CV3999 of C.violaceum of 34% (trembl|Q7NQY6(SRS)). Pfam: FT Sporulation related repeat This 35 residue repeat is found FT in proteins involved in sporulation and cell division such FT as FtsN, DedD, and CwlM. This repeat might be involved in FT binding peptidoglycan (Bateman A pers obs). No TMHs. Signal FT peptide present" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007730" FT /db_xref="UniProtKB/TrEMBL:A1K2E3" FT /protein_id="CAL92998.1" FT /translation="MSRDRKPTRKPARSPARSGGGTLVGIFIGLVMGAVIAAGAAWYFT FT RANPFQAAAPAPARAPVAVDQPPAALPGKPGDRPVVKQDFEFYKILPQGDGATHAAVEP FT PKPVEKAPEKPAEKLWLQVGAFGAADEAENLKARLALSGIQASSQRAQLADGRVVQRVR FT IGPFDKPEDMNSIRARLASAGFEASVTKSAP" FT CDS 408982..409629 FT /transl_table=11 FT /gene="dsbA" FT /locus_tag="azo0382" FT /product="putative protein disulfide-isomerase" FT /function="Thiol-disulfide isomerase and thioredoxins" FT /EC_number="5.3.4.1" FT /note="Putative protein disulfide-isomerase. Homology to FT dsbA of P. flourescens of 34%. Involved in disulfide-bond FT formation. Acts by transferring its disulfide bond to other FT proteins. Tigrfam: redox_disulf_1: redox-active disulfid FT Pfam: DSBA Oxidoreductase signal peptide no TMHS" FT /note="Family membership" FT /db_xref="GOA:A1K2E4" FT /db_xref="InterPro:IPR001853" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR017937" FT /db_xref="InterPro:IPR023205" FT /db_xref="UniProtKB/TrEMBL:A1K2E4" FT /protein_id="CAL92999.1" FT /translation="MNRRIALKQLAGLAVLAGAAGPVVAQRAAAAPFVELDTVVATDSK FT GKVEVIEFFHYGCPHCRAFDPLLESWLKRLPTDVAFLRVPAIWGNAQLGKLAQLYYAIE FT LSGKVEPLHGKVFVAVQDDKVPLHTEEGVREWVAKQGVDTKAFMDAYKSFGMQALLKQA FT DQRARDYKIQGVPTMAVDGRFLTSASMTGSHEATLKVVDDLIARARSQPRRG" FT CDS 409658..410446 FT /transl_table=11 FT /locus_tag="azo0383" FT /product="short chain dehydrogenase family protein" FT /function="Dehydrogenases with different specificities FT (related to short-chain alcohol dehydrogenases)" FT /note="The short-chain dehydrogenases/reductases family FT (SDR) is a very large family of enzymes, most of which are FT known to be NAD- or NADP-dependent FT oxidoreductases,TREMBL:Q8Y2Q1 (42% identity); FT SWISSPROT:P25970 (34% identity). InterPro (IPR002198): FT Short-chain dehydrogenase/reductase (SDR). InterPro FT (IPR002347): Glucose/ribitol dehydrogenase. Pfam (PF00106): FT Short chain dehydrogenase." FT /note="Specificity unclear" FT /db_xref="GOA:A1K2E5" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K2E5" FT /protein_id="CAL93000.1" FT /translation="MLTAAAAGSPRVFLTGASSGLGAALARHYAARGASLGLVARRADA FT LHELVASLPGRHLALVADVADPAALRSAATRFEAAFGVPDIVIANAGVSVGTLTEYAED FT LDAFERVLRTNLLGMAATFQPFVEAMRARGRGRLAGIASVAGIRGLPGAGAYSASKAAA FT ITYLESLRVELHGSGVTVTTIAPGYVATPMTAVNPYPMPFMLPAAEAAARIARHIDTGR FT RYAVVPWQMALVAKLLRVLPDALFDRLFAHAGRKPRGLPL" FT CDS 410530..410949 FT /transl_table=11 FT /locus_tag="azo0384" FT /product="Hypothetical protein" FT /note="Hypothetical protein. No Good homologs in the DB FT matching the length of the protein. No Significant FT domains,features,motifs present." FT /db_xref="UniProtKB/TrEMBL:A1K2E6" FT /protein_id="CAL93001.1" FT /translation="MDMKSGLPPESPERRTRQRFLALRRGEPCFWASVAGRRVALVDLS FT IEGFAFVGPATTATEPFAVVLHRAGVPDEIHARASVVNVGGSGDDALLGCRFTSLGNAE FT AALLQDWLVAHVIMNATVRITEKDAIAIVRGGSLI" FT CDS 410991..412268 FT /transl_table=11 FT /locus_tag="azo0385" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. Homology to vng2292h FT of Halobacterium sp. of 25% (trembl|Q9HN16(SRS). no domains FT predicted .no signal peptide. 10 TMHs" FT /db_xref="GOA:A1K2E7" FT /db_xref="InterPro:IPR018584" FT /db_xref="UniProtKB/TrEMBL:A1K2E7" FT /protein_id="CAL93002.1" FT /translation="MTETEHGPVGPPGGRWVRVGAGGAILFALVVFGLQTLSLQGYVGS FT DYKIFHWAATRFLADPAALYDAGSAASLQGYLYPPPSIAFFLPLALGSVEAVFPVFSWL FT AFLAAGLALAVWMRYLQRAALAPASPLLRTALLTMMLVTAPVFHARGGQVDSFVLLLCV FT GAVVLLAAHPRLAGALAAVGAAVKIYPALLVVFAAARRDGRAAFLAGMVTMALVLGLAT FT LVWMPISVTQDYLALLPQLSARTIINIYNQSAQAIGMRLTVPLEEARTQFSAYPVPGWA FT RFATQFGLVAVIGFSIWLARRRADRAYLAGLVLATIPLAAPLGWGHAYVYVLPLFCLVL FT GVAIERRQPVALVALALAYVALLVPGYHRFPYLGGAPDALLHVLFARNALAAAAIIGVA FT WCQLARVPDARRAAVVPRTLAQEWAA" FT CDS 412265..413521 FT /transl_table=11 FT /locus_tag="azo0386" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No good homology to a FT protein of similar length in the data bank. no domains FT predicted no singal peptide 9 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K2E8" FT /protein_id="CAL93003.1" FT /translation="MNPLRAFSGADERLLLAVVVAIGLALRVAAMLFVGHTPESDELAY FT RAMAASLLAGEGIVDNMGNRAMYNVGYPLFVIAPVSWLFGDSVRAVQLANAVLGAVSVV FT LCYCVAAAAGAGRGGRLIAAAAWALYLPASVYGVYLLKENLMVPLMLGVVWCALRLVSR FT PALSTGVVCGVLFGALALSGNAALALALAVAYALMAAPVGWRRRLTVAAAIAALAIAVA FT TPWMVRNLVVLGAPVLNTNGGFNLYLGNNPAATGMFVSIGDTPHGEDWQSLRALGEVEA FT SAILRRDALAWIADHPGQFAALALKKALYFWTPPIHEGKGPPSRIESMVRAAWALQFFV FT LAGAALACLAVRRLWGPRLTVLMLAVAAYTAVHMLFYVIFRYREPIMPVVCVLAALALE FT ALVVRRVFPSEPVALASRG" FT CDS 413530..414396 FT /transl_table=11 FT /locus_tag="azo0387" FT /product="conserved hypothetical periplasmic binding FT protein" FT /note="Conserved hypothetical periplasmic binding proten. FT Homology to rs03250 of R. solanacearum of 53% FT (trembl|Q8Y2Q2). Interpro: Periplasmic binding protein FT (IPR002491). Pfam: Periplasmic binding protein (PF01497). FT This family includes bacterial periplasmic binding FT proteins. Several of which are involved in iron transport. FT no signal peptide. no TMHs." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2E9" FT /db_xref="InterPro:IPR002491" FT /db_xref="UniProtKB/TrEMBL:A1K2E9" FT /protein_id="CAL93004.1" FT /translation="MDVSRDVEEHMGGAGGGPPPDAAGWADAVGARHGRADAGARIVCL FT VPSITELLFDLGVGDRLVGRTGFCIHPRDRVRALPKLGGTKDVKLDALRGLAPTHVIVN FT IDENRRDTVEDISRFVPNVIVTHPCAPEDNLALYALLGGIFDCEAAATSLSVSLQTALA FT EAAELRAALVPERVLYLIWREPWMTVSSATYIAAMLAAVGWESMPRAPEPRYPVVDWED FT ASMADVARVFLSSEPYRFGPAHVGEVGALASRPAMLIDGEMCSWYGSRAIAGVRYLTAL FT RRRLAKG" FT CDS complement(414428..414877) FT /transl_table=11 FT /locus_tag="azo0388" FT /product="conserved hypothetical protein" FT /function="predicted nucleic acid-binding protein contains FT PIN domain" FT /note="Conserved hypothetical protein. Homology to ebA3626 FT of Azoarcus sp. EbN1 of 59% (gnl|keqq|eba:ebA3626(KEGG)). FT InterPro: Protein of unknown function DUF132 FT InterPro:IPR002850; DUF132. IPR002716; PIN. IPR006596; FT PINc. Pfam:PF01850; PIN; SMART:SM00670; PINc; FT TIGRFAMs:TIGR00305; DUF132 TIGR00305: conserved FT hypothetical protein T. Non-secretory protein with very low FT signalpeptide probability (0.003) (Signal P predicted). FT Absence of transmembrane helices" FT /db_xref="InterPro:IPR002850" FT /db_xref="UniProtKB/TrEMBL:A1K2F0" FT /protein_id="CAL93005.1" FT /translation="MSFPRRLVLDTNTVMALWLFRDPRLAALDAAIAAARFQPCCRPDA FT VEELRRVLAYTHFGIDADEQQRLIAGYSERVTLVDGLGDAADALPLPLCRDRDDQKFLE FT ISRAAQAEFLLTRDKALLRLARHRLVRERFSILTPERFVSDGWCQ" FT CDS complement(414946..416775) FT /transl_table=11 FT /gene="phbC1" FT /locus_tag="azo0389" FT /product="probable poly-beta-hydroxybutyrate synthase" FT /function="Poly(3-hydroxyalkanoate) synthetase" FT /EC_number="2.3.1.-" FT /note="Function:-Polymerizes d(-)-3-hydroxybutyryl-CoA to FT create PHB which consists of thousands of hydroxybutyrate FT molecules linked end to end. PHB serves as an intracellular FT energy reserve material when cells grow under conditions of FT nutrient limitation. Entry name TREMBL:Q8KXD5 Prim. FT accession # Q8KXD5 Identities = 354/607 (58%) InterPro FT IPR000073; A/b_hydrolase. IPR010941; PhaC_N. Pfam PF00561; FT Abhydrolase_1; 1. PF07167; PhaC_N; 1. Number of predicted FT TMHs: 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2F1" FT /db_xref="InterPro:IPR000073" FT /db_xref="InterPro:IPR010941" FT /db_xref="InterPro:IPR010963" FT /db_xref="UniProtKB/TrEMBL:A1K2F1" FT /protein_id="CAL93006.1" FT /translation="MAAPETQHMHPELPDPKEVARTYAEVAQRASHLISEHVQRQLKKG FT VSAPADELGIAQAFMDMMAKLLANPYKLAQAQMNLVWDYFSLWQHSMLRFMGVNAAPVA FT APEKSDKRFKDEEWQEHFMFDFIKQSYLIAARHIHDTVCCVEGLEEQTQKKVNFYTRQY FT IDALSPSNFAVTNPEVFRETVKSHGQNLLKGLNNLLRDVEEGGGNLRVKMTDTTAFELG FT KNVATTPGKVVFQTDMMQLIQYSPSTENVLKRPLLIIPPWINKFYILDLREKNSYIKWC FT VDQGHTVFVISWVNPDERQAEKTFESYVKEGVVAALDAIEKQTGEKEVNAAGYCLGGTL FT LSTTLAYLAAKKDKRIASATFFTTMTDFSEPGELGVFIDEGQVSSLEKKMFERGYLEGS FT EMAGTFNMMRANDLIWSFVVNNYLMGKDPFPFDLLYWNSDSTRMPAKMHSFYLRKMYME FT NRLVQPGGVEIDGVPIDLGKIKVPCYFISAIEDHIAPWKSTYMGARNFGGPVRFVLGGS FT GHIAGIVNPPAANKYGYWLNPVAKLPATADAWFEGAQQQPGSWWTDWQAWVSAHDTEQV FT APRDPAKGKLKALEDAPGSFVKIRLDAHKALAS" FT CDS complement(416816..417844) FT /transl_table=11 FT /locus_tag="azo0390" FT /product="conserved hypothetical protein" FT /function="Zn-dependent hydrolases including glyoxylases" FT /note="conserved hypothetical protein. TREMBL:Q8Y2Q4-47% FT identity, 61% similarity. Pfam: FT Lactamase_B,aminotransferase III, AP2 domain. TMHMM FT predicted transmembrane helices." FT /note="Specificity unclear" FT /db_xref="GOA:A1K2F2" FT /db_xref="InterPro:IPR001279" FT /db_xref="UniProtKB/TrEMBL:A1K2F2" FT /protein_id="CAL93007.1" FT /translation="MSTEQQIEYPVADLPAPGTAVEIAPGIRWIRMPLPFALDHINLWL FT LDDGDEVAVIDTGFGLEPIQANWEAVLAAEPRPLSRVFVTHHHPDHLGLASWLMQRNGA FT TLHMSLGEFLGGQAVWHQLPGYSVADMVAQFRIHGLDDARLSALAERGNAYRRGIPEIP FT QQYSRLFDGDQVEIGGQRWEVIVGYGHAPEHVSLYCERLGVLVSGDMLLPRISTNISVY FT AATPDDDPLGWFLDSLRRISHLPDNTLVLPSHGRPFKGIRARVAQLIAHHRERCDALVA FT ACTQPRSAADLLGTLFARALDTHQVMFAMGEAIAHLNYLVKRGELCRVGNPETGIRHTI FT TR" FT CDS 417987..418430 FT /transl_table=11 FT /locus_tag="azo0391" FT /product="putative MerR-family transcriptional regulator" FT /function="predicted transcriptional regulators" FT /note="Putative MerR-family transcriptional FT regulator,copper efflux regulator / copper export FT regulator) InterPro: IPR000551 HTH_MerR. HTH reporting FT nucleic acid binding motif." FT /note="Family membership" FT /db_xref="GOA:A1K2F3" FT /db_xref="InterPro:IPR000551" FT /db_xref="InterPro:IPR009061" FT /db_xref="InterPro:IPR015358" FT /db_xref="UniProtKB/TrEMBL:A1K2F3" FT /protein_id="CAL93008.1" FT /translation="MAREQTYTITELAREFDITPRAIRFYEDQGLLTPARAGRARVYTR FT SDRTRLKLTLRGKRLGFSLADIKELLDMYDGVRNSAPQLERFLTGLGARRAALEQQRLD FT IEAVLQEIDVLEDQCRALLGHNAEGAAAARAELVRRLDNAGTA" FT CDS 418560..419027 FT /transl_table=11 FT /locus_tag="azo0392" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein possibly involved in FT aromatic compounds catabolism" FT /note="Similar to TREMBL:Q8YBL0 (47% identity); FT TREMBL:Q987R7 (50% identity); TREMBL:Q7WA35 (55% identity). FT InterPro (IPR003736): Phenylacetic acid degradation-related FT protein. Pfam (DUF157): Uncharacterized protein PaaI, FT COG2050." FT /note="Function unclear" FT /db_xref="InterPro:IPR003736" FT /db_xref="InterPro:IPR006683" FT /db_xref="UniProtKB/TrEMBL:A1K2F4" FT /protein_id="CAL93009.1" FT /translation="MRHESPPFQPRDPDYAARVRASFAQQRAMALIGAELVAVEPGYTE FT IHLPHRAEVTQQHGYIHGGVVGMIADSAAGYAANTLTPAETSVLTVEYKLNLVAPADGQ FT RLVARGEVIKPGRTLLITRAEVFAVRDEKWTLCAVMQQTIMAMHGKKELAG" FT CDS 419104..420315 FT /transl_table=11 FT /gene="fadAx" FT /locus_tag="azo0393" FT /product="probable acyl-CoA thiolase" FT /function="Acetyl-CoA acetyltransferase" FT /EC_number="2.3.1.-" FT /note="Probable acyl-CoA thiolase. Homology to fadAx of P. FT putida of 67% (gnl|keqq|ppu:PP2215(KEGG)). IPR002155; FT Thiolase. Pfam PF02803; Thiolase_C; 1. PF00108; Thiolase_N; FT 1. Two different types of thiolase are found both in FT eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase FT (EC:2.3.1.9) and 3-ketoacyl-CoA thiolase (EC:2.3.1.16). FT 3-ketoacyl-CoA thiolase (also called thiolase I) has a FT broad chain-length specificity for its substrates and is FT involved in degradative pathways such as fatty acid FT -oxidation. Acetoacetyl-CoA thiolase (also called thiolase FT II) is specific for the thiolysis of acetoacetyl-CoA and FT involved in biosynthetic pathways such as poly FT -hydroxybutyrate synthesis or steroid FT biogenesis.Prediction: Non-secretory protein Signal peptide FT probability: 0.002 Number of predicted TMHs: 0" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2F5" FT /db_xref="InterPro:IPR002155" FT /db_xref="InterPro:IPR016038" FT /db_xref="InterPro:IPR016039" FT /db_xref="InterPro:IPR020610" FT /db_xref="InterPro:IPR020616" FT /db_xref="InterPro:IPR020617" FT /db_xref="UniProtKB/TrEMBL:A1K2F5" FT /protein_id="CAL93010.1" FT /translation="MSDPVVIVSVARTPMGGFQGDLSGLTGPQLGAIAIKSAVERARLA FT PEQVQEVIMGCVLPAGVGQAPARQAALGAGLPLAAGCTTINKVCGSGMKATMLAHDLLL FT AGTNEVMVAGGMESMSNAPYLLPKARGGYRLGHGQLLDHMFLDGLEDSYSKENKGRLMG FT TFAEDCAGHFDFSRSAQDAFAVASTERAQAAITEGAFSWEVVPVTVAGRKGDVVVDKDE FT QPLKAQLDKIGTLKPAFKKDGTVTAANSSSISDGAAALVLMRKSTADKLGLAPLATIVG FT HATHAQEPQWFTTAPVGAMQKVLAKAGWGVGDVDLWEINEAFAVVTMAAMKELNLPHDK FT VNVNGGACALGHPIGASGARILVTLIGALRRRGLKRGVASLCIGGGEATAMAIELNASV FT ACGG" FT CDS 420508..421641 FT /transl_table=11 FT /gene="fadfX" FT /locus_tag="azo0394" FT /product="probable acyl-CoA dehydrogenase" FT /function="Acyl-CoA dehydrogenases" FT /EC_number="1.3.99.-" FT /note="Activity:- Catalysis of the reaction: acyl-CoA + FT acceptor = 2,3-dehydroacyl-CoA + reduced acceptor. Entry FT name TREMBL:Q9AHX9 Prim. accession # Q9AHX9 InterPro FT IPR006089; Acyl-CoA_dh. IPR006090; Acyl-CoA_dh_C. FT IPR006091; Acyl-CoA_dh_M. IPR006092; Acyl-CoA_dh_N. FT IPR009075; AcylCoADH_C_like. IPR009100; AcylCoA_dehyd_NM. FT Pfam PF00441; Acyl-CoA_dh; 1. PF02770; Acyl-CoA_dh_M; 1. FT PF02771; Acyl-CoA_dh_N; 1. Identities = 244/375 (65%) FT Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K2F6" FT /db_xref="InterPro:IPR006089" FT /db_xref="InterPro:IPR006090" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR006092" FT /db_xref="InterPro:IPR009075" FT /db_xref="InterPro:IPR009100" FT /db_xref="InterPro:IPR013786" FT /db_xref="UniProtKB/TrEMBL:A1K2F6" FT /protein_id="CAL93011.1" FT /translation="MILTSEQELIRDSIRAFAQERLAPFAAEWDRNHTFPRQALKELAE FT LGALGMVVPEEWGGAGMDYMSLVLALEEIAAGDGATSTIVSVQNSLACGIPAKYGTDAQ FT KERWLKPLARGDMLGCFCLTEPHVGSDASALRTTAVRDGDDWVLNGVKQFITTGREADV FT AIVFAVTDKAAGKKGISCFIVPTATPGYIVARIEEKMGQKASDTAQILFENCRVPADAL FT LGAEGEGYKIALSNLEAGRIGIASQCLGMARAALEAAVKYAQERETFGKPIFEHQAVNF FT RLADMATQLEAARQLVWHAASLKDAGRPCLKEASMAKLFASEMAEKVCSDAIQIHGGYG FT YVSDFPVERIYRDVRVCQIYEGASDIQKLVIGRALAQ" FT CDS 421777..422394 FT /transl_table=11 FT /locus_tag="azo0395" FT /product="2-hydroxychromene-2-carboxylate isomerase family FT protein" FT /function="2-hydroxychromene-2-carboxylate isomerase" FT /note="Similar to TREMBL:Q8Y2R2 (42% identity); FT TREMBL:Q7WEK4 (30% identity); TREMBL:Q88IW7 (27% identity). FT Pfam (HCCA_isomerase): 2-hydroxychromene-2-carboxylate FT isomerase." FT /note="Family membership" FT /db_xref="GOA:A1K2F7" FT /db_xref="InterPro:IPR001853" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR014440" FT /db_xref="InterPro:IPR023169" FT /db_xref="UniProtKB/TrEMBL:A1K2F7" FT /protein_id="CAL93012.1" FT /translation="MTPPKTIDFWFDFSSPYGYFMSEKIDAVARRHGRDVRWRPFLLGV FT VYKEIGSRPLTEVPLKGEYTRRDLLRTARFLDLPFALPSPFPVATQHAARCFYWLQADD FT EALARRFAHAAYRAYFVEGRDISQQVEVVSIAAALEVDGAALSAALGDAPVKERLRAAS FT AEAIAAGVFGSPYVIIDGEPFWGVDRLPQIEAWLAERSAAGR" FT CDS 422445..422642 FT /transl_table=11 FT /locus_tag="azo0396" FT /product="conserved hypothetical protein" FT /function="predicted Fe-S protein" FT /note="Conserved hypothetical protein. Homology to cc1308 FT of C. crescentus of 35% (trembl|Q9A8P5). Pfam:DUF1289 This FT family consists of a number of hypothetical bacterial FT proteins. The aligned region spans around 56 residues and FT contains 4 highly conserved cysteine residues towards the FT N-terminus. The function of this family is unknown. no FT signal peptide no TMHs" FT /db_xref="InterPro:IPR010710" FT /db_xref="UniProtKB/TrEMBL:A1K2F8" FT /protein_id="CAL93013.1" FT /translation="MSPASPCINVCRMDAATGWCEGCLRTLDEIARWGRASDDDKRRIL FT AAVAERRATAAVPHPREAAA" FT CDS 422639..422824 FT /transl_table=11 FT /locus_tag="azo0397" FT /product="Hypothetical protein" FT /note="Hypothetical protein, 54% identity to TrEMBl;Q8YGQ7. FT Has PF06945, Protein of unknown function FT (DUF1289);IPR010710;This family consists of a number of FT hypothetical bacterial proteins. The aligned region spans FT around 56 residues and contains 4 highly conserved cysteine FT residues towards the N-terminus. The function of this FT family is unknown." FT /db_xref="InterPro:IPR010710" FT /db_xref="UniProtKB/TrEMBL:A1K2F9" FT /protein_id="CAL93014.1" FT /translation="MSSDALCVGVCMIDWDAGICLGCGRTPEEIEGVPVPSPAETMPEA FT VPLPPNVAAQVGEGSD" FT CDS 422821..423738 FT /transl_table=11 FT /locus_tag="azo0398" FT /product="putative beta lactamase" FT /function="Zn-dependent hydrolases including glyoxylases" FT /EC_number="3.5.2.6" FT /note="Probable Hypothetical protein ycbL. FT TREMBL:Q8Y2S7-43% identity,57% similarity. FT TIGRFAM:2A0115-Benzoate transport proteins belong to this FT group. Benzyl alcohol,benzaldehyde, benzoate, and FT anthranilate are metabolized via catechol, FT cis,cis-muconate, and the beta-ketoadipate pathway in some FT bacteria InterPro: Metallo-beta-lactamase superfamily FT Pfam:Metallo Beta lactamase superfamily, Phage lysozyme FT TMHMM predicted transmembrane heleces ftsZ: cell division FT protein FtsZ" FT /note="Function unclear" FT /db_xref="GOA:A1K2G0" FT /db_xref="InterPro:IPR001018" FT /db_xref="InterPro:IPR001279" FT /db_xref="UniProtKB/TrEMBL:A1K2G0" FT /protein_id="CAL93015.1" FT /translation="MSAPRLPASVQVFERGWLSANNVVLDDGGEVTLIDSGYVTHAAQT FT LALVAGALGGRRLAQLINTHSHSDHIGGNAAVQRAFGGRIVVPAGMADAVERWDEDALL FT LRTADQRGERFAHDAVLTAGDRFIAGGLEWQALPAAGHDMDALAFYNAERRILVSGDAL FT WRDGFGILFADVLGRGDALGAARETLEAFGRLAVDVVIPGHGAPFADVDGALERAFARL FT AAFEADGARMARNAIRACITFRLLEHRRLALDDLAAHLDATPLYRSANARFLGLEAQAL FT ADWLVAELLRAGVARREGETLVPA" FT CDS 423811..424689 FT /transl_table=11 FT /locus_tag="azo0399" FT /product="conserved hypothetical protein" FT /function="predicted P-loop-containing kinase" FT /note="Hypothetical UPF0042 protein YPO3586/Y0158. FT SWISPROT:Q82TN5: 6i% identity, 78% similarity This is a FT family of putative P-loop ATPases. Many of the proteins in FT this family are hypothetical and kinase activity has been FT proposed for some family members InterPro:IPR005337; FT UPF0042. Pfam: PF03668; ATP_bind_2 No Signal peptide FT (Signal P predicted) No transmembrane helices (TMHMM FT predicted) cmk: cytidylate kinase" FT /note="Function unclear" FT /db_xref="GOA:A1K2G1" FT /db_xref="InterPro:IPR005337" FT /db_xref="UniProtKB/Swiss-Prot:A1K2G1" FT /protein_id="CAL93016.1" FT /translation="MQIVLISGLSGSGKSIALHVLEDAGYYVVDNLPSALLLQLVLHLR FT GAGYQRVAVAVDMRSGSSIAALPEQVESLRGMVDDLRFIFLEARDDTLIARFSETRRRH FT PLADENVSLDEAIQRERDALASVAELGHRMDTSDIHANTLRAWIKDFIGAAASEGLTLM FT FQSFGFKYGIPLDADLVFDVRCLPNPYYDPLLRPLTGRDQGVIDYLEKVPEVGRMAEDI FT RRFVADWLPAYMRDNRSYLTVAIGCTGGQHRSVYMAEWLARRFADRVRVIVRHRSAARR FT VQDAPPAVSGK" FT CDS 424686..425081 FT /transl_table=11 FT /locus_tag="azo0400" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT TP1032 of Treponema pallidum of 32% FT (sprot|YA32_TREPA(SRS)). Has PF07009(IPR010739):Protein of FT unknown function (DUF1312);This family consists of several FT bacterial proteins of around 120 residues in length. The FT function of this family is unknown. No singal peptide. 1 FT TMH" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR010739" FT /db_xref="InterPro:IPR024045" FT /db_xref="UniProtKB/TrEMBL:A1K2G2" FT /protein_id="CAL93017.1" FT /translation="MRLAGDARAWLALLRPGDVLVAALGLLACAGSVVALWRGGAPDGA FT VIRAGGKVFAEVDLRQPRIIDVPGPIGTTRIEIAPGRARVAADPGPRQYCVRQGWLSRA FT GAVAICAPNEVSLALTGRGADYDSLNY" FT CDS 425062..425604 FT /transl_table=11 FT /locus_tag="azo0401" FT /product="heptaprenyl diphosphate synthase component I" FT /EC_number="2.5.1.30" FT /note="Heptaprenyl diphosphate synthase component I, 23% FT identity (45% similarity) to TrEMBL;Q896H9. Has FT PF07456,Heptaprenyl diphosphate synthase component FT I;IPR010898,Hpre_diP_synt_I: This family contains component FT I of bacterial heptaprenyl diphosphate synthase FT (approximately 170 residues long). This is one of the two FT dissociable subunits that form the enzyme, both of which FT are required for the catalysis of the biosynthesis of the FT side chain of menaquinone-7." FT /db_xref="GOA:A1K2G3" FT /db_xref="InterPro:IPR010898" FT /db_xref="InterPro:IPR014535" FT /db_xref="UniProtKB/TrEMBL:A1K2G3" FT /protein_id="CAL93018.1" FT /translation="MTPSTIELVPSAEDRRVARHAAAAIVLTVAEAAIPLPLPGVKPGL FT ANIVTLIVLARWGWREAVWVALLRVGAGSLLLGQFLAPGFFLSLSGALASLLTLGVAMH FT LPRRWFGPVSQSILAAFAHIGAQLVVARLWLVPHDGVFYLTPVFAAAAVVFGTINGLVA FT ARLLTELNAADSTRSAA" FT CDS complement(425612..426709) FT /transl_table=11 FT /gene="cheB1" FT /locus_tag="azo0402" FT /product="probable protein glutamate-methylesterase" FT /function="Chemotaxis response regulator containing a FT CheY-like receiver domain and a methylesterase domain" FT /EC_number="3.1.1.61" FT /note="Probable protein-glutamate FT methylesterase,CheB_methylest. IPR001789; Response_reg. FT IPR008248; RR_chemtxs_CheB. Pfam: PF01339; CheB_methylest. FT PF00072; response_reg. SMART: SM00448; REC. Chemotaxis FT response regulator protein-glutamate methylesterase (EC FT 3.1.1.61). Involved in the modulation of the chemotaxis FT system; catalyzes the demethylation of specific FT methylglutamate residues introduced into the chemoreceptors FT (methyl-accepting chemotaxis proteins) by cheR (By FT similarity)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2G4" FT /db_xref="InterPro:IPR000673" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR008248" FT /db_xref="InterPro:IPR011006" FT /db_xref="UniProtKB/TrEMBL:A1K2G4" FT /protein_id="CAL93019.1" FT /translation="MSNKIKVMIVDDSALVRQVVSQAISRDPGIEVIGTAQDPVFALAK FT LNSLAPDVLVVDIEMPRMDGLTFLKRIMAERPTPVIICSSLAEKGAQVTMEALSAGAVA FT IITKPKMGLKNFLEDASNDIVQAIKAAARANVRALGRAVSPAAVAADVRPKLSADAVIA FT PASAHQGAGMYGTTDRIVAIGTSTGGTQALEAVLTRLPAVSPGIVIVQHMPERFTAMFA FT ERLNGLCKIEVREARHGDRVIPGRALIAPGGKHMMLARSGAQYTVEVVDGPLVNRHRPS FT VDVLFRSCAKFAGRNALGVIMTGMGDDGARGLKEMREAGARTVAEDESTCVVFGMPKEA FT IRLGGVDEILPLDRIPAAILQSARG" FT CDS complement(426736..427560) FT /transl_table=11 FT /gene="cheR1" FT /locus_tag="azo0403" FT /product="probable chemotaxis protein methyltransferase" FT /function="Methylase of chemotaxis methyl-accepting FT proteins" FT /EC_number="2.1.1.80" FT /note="Probable chemotaxis protein FT methyltransferase,CheR_Metranf. IPR001601; Methyltransf. FT IPR000051; SAM_bind. Pfam: PF01739; CheR. PF03705; CheR_N. FT SMART: SM00138; MeTrc. Chemotaxis protein methyltransferase FT (EC 2.1.1.80). METHYLATION OF THE MEMBRANE-BOUND FT METHYL-ACCEPTING CHEMOTAXIS PROTEINS (MCP) TO FORM FT GAMMA-GLUTAMYL METHYL ESTER RESIDUES IN MCP.Annotation FT derived from meta auto annotator." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2G5" FT /db_xref="InterPro:IPR000780" FT /db_xref="InterPro:IPR022641" FT /db_xref="InterPro:IPR022642" FT /db_xref="UniProtKB/TrEMBL:A1K2G5" FT /protein_id="CAL93020.1" FT /translation="MDNPGITDREFALFQRLIYRLAGISMSDAKKVLMVGRLGKRLRHY FT DLASFGDYYRLLASGTHPDELQTMVDLLTTNETYFFREPAHFEFLREFAASRKGGAPFR FT IWSGACSSGEEPYTMALVLAETLGLSTSWEIVASDISMTVLERARAGLYPLERAEGIPQ FT PLLKKYCLKGVREQQGNFLICPELRERIDFRQLNLVALDAPNLGHFDVIFLRNVMIYFD FT TETKARVIANMLPHLKQDGRFIVGHSETLHGVTDELAALRPTLYKRASVQSS" FT CDS complement(427566..428156) FT /transl_table=11 FT /gene="cheD" FT /locus_tag="azo0404" FT /product="conserved hypothetical chemotaxis protein CheD" FT /note="Conserved hypothetical chemotaxis protein CheD. FT Homology to cheD of S. oneidensis of 41% (trembl|Q8EF62). FT Interpro: CheD (IPR005659). Pfam: CheD (PF03975). This FT chemotaxis protein stimulates methylation of MCP proteins. FT no signal peptide. no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2G6" FT /db_xref="InterPro:IPR005659" FT /db_xref="UniProtKB/TrEMBL:A1K2G6" FT /protein_id="CAL93021.1" FT /translation="MTDWDQLSPQEVERLARNIGPGEWAVDRQRPISTLLGSCVAVCMF FT DPVSRVGGMNHFMLPNIRRNDHHADDDMLLSGDYAMEALLNGLLNQGAVRHRVQAKAFG FT GGTIIHGMTSAGIGERNAAFAREWLTREGISLQAEDFLGPWSRKLLFIPATGTAWCKRM FT PTTMTTVEQIAREEADYAASLQRKPPKGNIELF" FT CDS complement(428223..428765) FT /transl_table=11 FT /gene="cheW1" FT /locus_tag="azo0405" FT /product="probable positive regulator of CheA protein FT activity" FT /function="Chemotaxis signal transduction protein" FT /note="Probable positive regulator of CheA protein FT activity, CheW. Pfam: PF01584; CheW. SMART: SM00260; CheW. FT Chemotaxis protein cheW.Involved in the transmission of FT sensory signals from the chemoreceptors to the flagellar FT motors. It physically bridges chea to the mcps FT (methyl-accepting chemotaxis proteins) to allow regulated FT phosphotransfer to cheY and cheB." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2G7" FT /db_xref="InterPro:IPR002545" FT /db_xref="UniProtKB/TrEMBL:A1K2G7" FT /protein_id="CAL93022.1" FT /translation="MNQIVASGQRKSGSPQDDGPQQYLTFSLGGEVFALGILNVKEIIE FT FGNVTEIPMMPSFIRGVINLRGAVVPVIDLSARFGGKNSTISRRTCIVIVEIDGEDGKQ FT DLGVIVDAVNEVLEIPRADIEPPPAFGAKIRADFIQGMGKVDGRFVIILNVERVLSTEE FT IAMLTRMGDEDGATSAA" FT CDS complement(428787..431225) FT /transl_table=11 FT /locus_tag="azo0406" FT /product="putative methyl-accepting chemotaxis protein" FT /function="Methyl-accepting chemotaxis protein" FT /note="Methyl-accepting chemotaxis protein, only very low FT similarity to SWISSPROT: sprot|Y4FA_RHISN (14% Rhizobium FT sp. (strain NGR234). InterPro: IPR004090; Me_chemotaxis. FT IPR004089; Chmtaxis_transd. IPR003660; HAMP. Pfam: PF00672; FT HAMP. PF00015; MCPsignal. SMART: SM00304; HAMP. SM00283; FT MA. Signal P reporting signal peptide. TMHMM reporting 2 FT transmembrane helices." FT /note="Family membership" FT /db_xref="GOA:A1K2G8" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004010" FT /db_xref="InterPro:IPR004089" FT /db_xref="UniProtKB/TrEMBL:A1K2G8" FT /protein_id="CAL93023.1" FT /translation="MKIATRTKLLVLVSVLGIAVSVIFALFSLRSSLLSDRQDKTKNLI FT EVAHSVLAHYHAREVAGQMTRDQAQTAAKDVIRGMRYDGEEYFWINDLEHRMLMHPIKP FT ELEGKDLSTLKDAAGKAFFVDMVAAVKQNDGGFVDYVWPRAGSDKPVPKLSYVKGFKPW FT GWMLASGIYIEDVDAALWREFSNQLIIGIVIVIALLVLAVATIRDVTRAIRGTVDSARH FT LADGDFDTVSDLQLKNELGAVLEANNAIRVSVQQMRAEAVSLSRAAVAGQLSSRADLSK FT YHGGYREVVEGVNATLDAVIGPLNVAADYVDRIAKGTIPPKITDSYNGDFNTIKNNLNT FT AIDAINALVADAAMLSRAAVEGKLATRADASRHQGDYQRIVQGVNDTLDAVIGPLNVAA FT DYVDRIAKGAIPPKITDSYNGDFNTIKNNLNTAIDAVGALVADAAMLAQAAVEGRLETR FT ADASRHQGDYRKIVEGVNHTLDAVIDPINEVKRVMIALSQGDLTQKIHAEYAGDFRVLQ FT DAVNGSLDKLGEIIEQVRGAADALSNAAAQVSATAQSLSQASSEQAASVEEVSSTIEEA FT AASINQNSENAKVTDGMATKSATEAAEGGEAVRNTVEAMKNIAGKIGIIDDIAYQTNLL FT ALNAAIEAARAGEHGKGFAVVAAEVRKLAERSQVAAQEIGQLAGNSVTLAERAGALLGE FT MVPSIRKTSDLVQEIASASQEQSAGVVQINHAMGQLNKATQQNASASEELAATAEELGG FT QAGQLQQLMGFFSVGDGAGAAAVIATASARKAPARAAATPAPRASRKPVSFSEADFERF FT " FT CDS complement(431253..433700) FT /transl_table=11 FT /locus_tag="azo0407" FT /product="putative methyl-accepting chemotaxis protein" FT /function="Methyl-accepting chemotaxis protein" FT /note="Methyl-accepting chemotaxis protein, only very low FT similarity to SWISSPROT: sprot|Y4FA_RHISN (14% Rhizobium FT sp. (strain NGR234). InterPro: IPR004090; Me_chemotaxis. FT IPR004089; Chmtaxis_transd. IPR003660; HAMP. Pfam: PF00672; FT HAMP. PF00015; MCPsignal. SMART: SM00304; HAMP. SM00283; FT MA. Signal P reporting signal peptide. TMHMM reporting 1 FT transmembrane helices." FT /note="Family membership" FT /db_xref="GOA:A1K2G9" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004089" FT /db_xref="InterPro:IPR024478" FT /db_xref="UniProtKB/TrEMBL:A1K2G9" FT /protein_id="CAL93024.1" FT /translation="MKNLKIGIRLGLGFGVTVLLLIVIAGIAMLRLGALDQAIRQVVDD FT AYPKTVIANRIIDNVNISAIALRNAALVKNPEAVNAEFERIAEARRNTAADFATLDRII FT VLPEGKRLLQKVLESRATTGAEQDKYMALLKAGQRDQAVDMLITSVRSTQAAYIANVNE FT MIDFQAKRMTDLGQDAGALANSTETLIGALAVAAVLLALGFAVFVTRSITRPIDEVLGA FT ARKMAAGDFKFVLESTARDEVGEVVRAVASVQASVRTMIDDAAVLATAAVEGRLATRAD FT AARHQGDFRRIVEGVNGTLDAVIGPLNVAADYVDRIAKGAIPPKIADSYNGDFNAIKNN FT LNTAIDAINALVADAAMLSRAAVEGKLATRADASRHQGDYQRIVQGVNDTLDAVIGPLN FT VAADYVDRIAKGAIPPRITDSYNGDFNTIKNNLNTAIDAVGALVADAAMLAQAAVEGRL FT ETRADASRHQGDYRKIVEGVNHTLDAVIDPINEVKRVMIALSQGDLTQKIHAEYAGDFR FT VLQDAVNGSLDKLGEIIEQVRGAADALSNAAAQVSATAQSLSQASSEQAASVEEVSSTI FT EEAAASINQNSENAKVTDGMATKSATEAAEGGEAVRNTVEAMKNIAGKIGIIDDIAYQT FT NLLALNAAIEAARAGEHGKGFAVVAAEVRKLAERSQVAAQEIGQLAGNSVTLAERAGAL FT LGEMVPSIRKTSDLVQEIASASQEQSAGVVQINHAMGQLNKATQQNASASEELAATAEE FT LGGQAGQLQQLMGFFSVGDGTGLKAGLPLPKKSASNRSAPAPAPARASRKPVSFSEADF FT ERF" FT CDS complement(433738..435933) FT /transl_table=11 FT /gene="cheA1" FT /locus_tag="azo0408" FT /product="putative chemotaxis protein histidine kinase" FT /function="Chemotaxis protein histidine kinase and related FT kinases" FT /EC_number="2.7.13.1" FT /note="Putative chemotaxis histidine kinase FT protein,ATPbind_ATPase. IPR004358; Bact_sens_pr_C. FT IPR002545; CheW. IPR004105; H-kinase_dim. IPR005467; FT His_kinase. IPR008207; Hpt. IPR008208; Hpt_N. Pfam: FT PF01584; CheW. PF02895; H-kinase_dim. PF02518; HATPase_c. FT PF01627; Hpt. SMART: SM00260; CheW. SM00387; HATPase_c. FT SM00073; HPT. Chemotaxis protein cheA (EC 2.7.3.-). FT INVOLVED IN THE TRANSMISSION OF SENSORY SIGNALS FROM THE FT CHEMORECEPTORS TO THE FLAGELLAR MOTORS. CHEA IS FT AUTOPHOSPHORYLATED; IT CAN TRANSFER ITS PHOSPHATE GROUP TO FT EITHER CHEB OR CHEY." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2H0" FT /db_xref="InterPro:IPR002545" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR004105" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR008207" FT /db_xref="InterPro:IPR009082" FT /db_xref="UniProtKB/TrEMBL:A1K2H0" FT /protein_id="CAL93025.1" FT /translation="MDEIISVFVTESREQLAALEAALLQLEDAPDDSDTLNAVFRSAHT FT IKGGAGVVECDFIVAFTHVVENVLDKLRNGEIKLNGDLAALLLACGDHIGNLLGVLEAG FT ASAPDADLAAEGDALLARLQRDWLDGGAHGASPHPAPAPAAAVEVSGGGVVDTDCWHIS FT LRFGPDVLKNGMDPLSFLRYLATLGTIVRIETLADAMPPADEMDAENCYLGFEISFASS FT ADKAAIERVFDFVRDDCTLHILPPHSRLHDYLEMIKALPEDNMRLGEILVRVGALTQAE FT LDDGLRTQHPPHEDGAAEEITAPIGEILVEQHVVQPELVEAAVVKQKQVSDKKAAEARL FT IRIQADKLDKLIDLVGELVIAGASVNLLAGKSGLSELVEATSLTGRLVESIRDAALQLR FT MVQIGETFNRFNRVVRDVSKELGKDIELAISGGETELDKSMVEKIGDPLMHLVRNAMDH FT GIEAPEVRVANGKPARGRLELNAYHDSGSIIIEVADDGGGLKRERIVAKAVERGLVQAG FT QQLSDAEIYNLIFEAGFSTAAQVSNLSGRGVGMDVVRRNIQSLRGTVEVSSVEGQGSRF FT AIRLPLTLAIIDGFLVGVGRAAYVIPLDTVVECIELNQDAGERDYINLRGEVLPFVRLR FT EMFEVAGEAPPRQNVVVVQYAGVKAGIVVDQLMGEFQTVIKPLGAIFRHIKGIGGSTIL FT GSGEVALILDVQALVQRCANREAHGMQPPRALAASLD" FT CDS complement(435947..436255) FT /transl_table=11 FT /locus_tag="azo0409" FT /product="putative STAS domain protein" FT /function="Anti-anti-sigma regulatory factor (antagonist of FT anti-sigma factor)" FT /note="Putative anti-sigma factor antagonists (STAS domain FT protein), STAS. Pfam: PF01740; STAS. The STAS (Sulphate FT Transporter and AntiSigma factor antagonist) domain is FT found in the C-terminal region of sulphate transporters and FT bacterial anti-sigma factor antagonists. It has been FT suggested that this domain may have a general NTP binding FT function." FT /note="Function unclear" FT /db_xref="InterPro:IPR002645" FT /db_xref="UniProtKB/TrEMBL:A1K2H1" FT /protein_id="CAL93026.1" FT /translation="MSTPATAPLAIVEDMTIYHAAEQKQQLVAALAQADELQIDLSAVA FT EIDTAGFQLLILVKREAQRLGKRARIVAHSAAVREVVDFFNMAAEFGDPMLMPAPEA" FT CDS complement(436258..437526) FT /transl_table=11 FT /locus_tag="azo0410" FT /product="putative methyl-accepting chemotaxis protein" FT /function="Methyl-accepting chemotaxis protein" FT /note="Putative methyl-accepting chemotaxis FT protein,Chmtaxis_transd. Pfam: PF00015; MCPsignal. SMART: FT SM00283; MA. Signal P reporting signal peptide. TMHMM FT reporting 2 transmembrane helices." FT /note="Function unclear" FT /db_xref="GOA:A1K2H2" FT /db_xref="InterPro:IPR004089" FT /db_xref="UniProtKB/TrEMBL:A1K2H2" FT /protein_id="CAL93027.1" FT /translation="MPFNTLLQRSLVVFATVAVLAGIAVFFLNDWFHGSFLPALGLAQP FT VGDAVGSMLIVTVAYFGQRVVSLAFFRDHMYGLTSSQEQMRDASHNVAAVGDEVAHELR FT AVPTYNDVLRRQLDSVVQQTEKAAYDITERLQSIDGVVSHLNTFVVESSSESDQMAHDS FT EERIAGNQKLIAEMRQYIDYRIQEARQDQERVAQVVHEARSLESLTRLIKDIAAQTNLL FT ALNAAIEAARAGEAGRGFAVVADEVRKLSAETEKAVLAINQGILGVANTIETQLQEKLS FT SINLDREQAALGQFADQLGALGHSYESILDHQGKVMSTVRDSSQQLAEMFMAALASVQF FT QDVTRQQLEHTADSLRRLDGHLGVLADRLEQSENADFRYTPLSEHLEEIYSRYVMDQQR FT HTHHNALQQADDVGGGGPKIELF" FT CDS complement(437534..437899) FT /transl_table=11 FT /gene="cheY1" FT /locus_tag="azo0411" FT /product="probable chemotaxis response regulator" FT /function="FOG: CheY-like receiver" FT /note="Probable chemotaxis response regulator," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2H3" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="UniProtKB/TrEMBL:A1K2H3" FT /protein_id="CAL93028.1" FT /translation="MKTIFLVDDSATILLSISNILSKAGYGVEKAGNAAEALSKFQSGV FT KVDLLITDLNMPGMNGIDFIKEVRKLPNYRFMPILFLTTESQQSKKAEAKAAGASGWIV FT KPASADELLNTIKLVIR" FT tRNA complement(438216..438288) FT /gene="tRNA-Lys" FT /locus_tag="azo_tRNA_0004" FT /product="transfer RNA-Lys" FT /anticodon=(pos:438253..438255,aa:Lys) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS complement(438349..439440) FT /transl_table=11 FT /locus_tag="azo0412" FT /product="conserved hypothetical membrane protein" FT /function="predicted transporter component" FT /note="Conserved hypothetical membrane protein. Homology to FT rsc0739 of R. solanacearum of 52% (trembl|Q8Y1F1). Pfam: FT DUF395 This family includes YeeE and YedE from E. coli. FT These proteins are integral membrane proteins of unknown FT function. Many of these proteins contain two homologous FT regions that are represented by this family. This region FT contains several conserved glycines and an invariant FT cysteine that is probably an important functional residue. FT signal peptide 8 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007272" FT /db_xref="UniProtKB/TrEMBL:A1K2H4" FT /protein_id="CAL93029.1" FT /translation="MEAALPAPAILALGFMLGGGFGALSSRTHFCTMGAVADIVAFGDW FT SRMRMWLAAIATAMLGTALLQAAGLFDPAHSLYAGARVPWLSHAVGGLCFGAGMTLASG FT CAGKTLVRLGGGSLKALVVATFLAIGASMTLRGLFAAWRSSWLDPHVLVLDHAQTLPAF FT LAAADLPSGALVGLVAGLALLIASLAPAGARRADILWSGAGVGLLCVAAWYVTGHLGYV FT AEDPQTLEEAFIATSSGRAESLSFVAPHAYTLDLLLLWTDRSRVLSFGVATLGGVIAGA FT LLYRLATRSLRLESFADPADLLRHVAGGLLMGFGGVTALGCSIGQGVGGLSTLSLGALI FT TTAAIIAGATATLRLQLWHLQRS" FT CDS complement(439455..440141) FT /transl_table=11 FT /gene="exsB" FT /locus_tag="azo0413" FT /product="conserved hypothetical ExsB protein" FT /note="Conserved hypothetical ExsB protein. Homology to FT exsB of P. syringae of 70% (trembl|Q87Y44). This protein FT family is represented by a single member in nearly every FT completed large (> 1000 genes) prokaryotic genome. In FT Rhizobium meliloti, a species in which the exo genes make FT succinoglycan, a symbiotically important exopolysaccharide, FT exsB is located nearby and affects succinoglycan levels, FT probably through polar effects on exsA expression or the FT same polycistronic mRNA. Interpro: ExsB (IPR004479). Pfam: FT ExsB (PF06508). Tigrfam: TIGR00364: exsB protein. Has FT signal peptide present. No TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2H5" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR018317" FT /db_xref="UniProtKB/Swiss-Prot:A1K2H5" FT /protein_id="CAL93030.1" FT /translation="MTDLPRAVVLLSGGLDSATCLAIARDMGLETYALSVAYGQRHAAE FT LTASRRVAHALGAREHRVASVSLGEFGGSALTDPAIAVPEDAAPGGIPVTYVPARNTVM FT LSMALAWAEVLGARHIFVGVNAVDYSGYPDCRPAFIQAFETMANLATKAGVEGHPTTIH FT APLIDLSKADIIRRGVALGVDYGLTVSCYQADDDGRACGRCDACRLRREGFAAAGIADP FT TRYQAR" FT CDS complement(440170..440832) FT /transl_table=11 FT /locus_tag="azo0414" FT /product="conserved hypothetical radical activating enzyme" FT /function="Organic radical activating enzymes" FT /note="Conserved hypothetical radical activating enzyme. FT Homology to xac3139 of X. axonopodis of 60% FT (trembl|Q8PHW0). InterPro: Radical activating enzymes FT (IPR001989) Pfam: Radical activating enzyme no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2H6" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR024924" FT /db_xref="UniProtKB/TrEMBL:A1K2H6" FT /protein_id="CAL93031.1" FT /translation="MTEVVRQPVKLRLTEIFASIQGESTRVGLPTTFVRLTGCPLRCSW FT CDTAYAFTGGEARALSDVLDDVAALGLRHVCVTGGEPLAQKYCLALLTALCDAGYSVSL FT ETSGALDIGGVDPRVSRVMDLKAPGSAEVTRNRLENIPLLRARDELKIVLADQADYDWA FT RAMIADHDLAARCPVLLSPVAGTLDPAQLAEWIVRDRLPVRFQLQLHKILWNDARGR" FT CDS complement(440843..441562) FT /transl_table=11 FT /locus_tag="azo0415" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein. Homology to FT RS05116 of R.solanacearum of 38% (trembl|Q8Y1F3(SRS)) No FT domains predicted. No TMHs Has signal peptide." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2H7" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="InterPro:IPR014162" FT /db_xref="UniProtKB/TrEMBL:A1K2H7" FT /protein_id="CAL93032.1" FT /translation="MKRLLPLAALLALSSAGPAHAGLFDDNEARRQIYEMRQDLENRIN FT ASQGSQLDLANQNEQLRGEVARLRGQIEVLMNEVESLKQRQRDFYVDLDNRLRKLETAP FT VAAESAAPAADPVAESTEYEAALNLLKGGKHRDALTAFEAFLARHPAGSFAPSAHFWAG FT NAALQAKEVASATTHFNAVLGKWPNDSVAPDAMLGLANSQQAMGDAKTAQRTLQSLVER FT YPSSNAAQAAKQRLGKR" FT CDS complement(441562..442080) FT /transl_table=11 FT /gene="pal" FT /locus_tag="azo0416" FT /product="putative peptidoglycan-associated lipoprotein" FT /function="Outer membrane protein and related FT peptidoglycan-associated (lipo)proteins" FT /note="Putative peptidoglycan-associated lipoprotein. FT Homology to pal of E. coli of 36% (sprot|PAL_ECOLI). FT Thought to play a role in bacterial envelope integrity. FT Very strongly associated with the peptidoglycan. Pfam: ompA FT family signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2H8" FT /db_xref="InterPro:IPR006664" FT /db_xref="InterPro:IPR006665" FT /db_xref="InterPro:IPR014169" FT /db_xref="UniProtKB/TrEMBL:A1K2H8" FT /protein_id="CAL93033.1" FT /translation="MKKLVLPALLSAVLAACSSTGPEATSGAAVTDRSGAGVATVTANT FT PSGSGIAALTDPNNILSKRNVFFDFDSYVIKADAKPLVEAHGRFLAQNPQMKMLVQGNA FT DERGSREYNLALGQKRADAVKQALLLLGAKEAQIESVSLGEEKPRCTESSEACFAQNRR FT GDMLYSGEF" FT CDS complement(442120..443403) FT /transl_table=11 FT /gene="tolB" FT /locus_tag="azo0417" FT /product="putative translocation protein TolB" FT /function="Periplasmic component of the Tol biopolymer FT transport system" FT /note="Putativ translocation protein tolB. Homology to tolB FT of P. aeruginosa of 39% Involved in the tonB-independent FT uptake of proteins. signal peptide probable 1 TMH (unusual FT for TolB)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2H9" FT /db_xref="InterPro:IPR007195" FT /db_xref="InterPro:IPR011659" FT /db_xref="InterPro:IPR014167" FT /db_xref="InterPro:IPR015943" FT /db_xref="UniProtKB/Swiss-Prot:A1K2H9" FT /protein_id="CAL93034.1" FT /translation="MKTFAQLRLLLAAAALALLSFSAQAQLSIEITGAGASRFPVIIPV FT FENEASLPRSVSDIVRADLERSGLFSLVDIGPLPLPEGQIPDLGSLRSRGADAALAASV FT FPQGDGRYEIRFRLFDTQKQTELGALALRMTAAQNRITAHRIADFVYEKLTGLPGYFAT FT RIAYVVKTGPRYELQVADADGMNAQAALVSREPIISPAWSPDGGRLAYVSFEAKKPIIY FT VHTLATGQRQVVANFKGSNSAPAWSPDGQQLSVVLTKDGLSQLYVLNADGSGVRRLASS FT SGIDTEPAWSPDGQWIYFTSDRGGSPQIYRIPTAGGAAQRVTFDGTYNVTARPSADGRL FT LAFITRNNGRFQVAVQDLTTRQTTILTDSARDESPSFAPNGRMILYATDAGGRGVLAAV FT SSDGRVKQRLSVQAADVREPAWGPLQKQ" FT CDS complement(443450..444292) FT /transl_table=11 FT /gene="tolA" FT /locus_tag="azo0418" FT /product="conserved hypothetical membrane protein" FT /function="Function unkown" FT /note="Conserved hypothetical membrane protein. Homology to FT tolA of N. europaea of 39% (trembl|Q82XP0). no domains FT predicted InterPro: Proline-rich region (IPR000694) no FT signal peptide 1 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2I0" FT /db_xref="InterPro:IPR006260" FT /db_xref="UniProtKB/TrEMBL:A1K2I0" FT /protein_id="CAL93035.1" FT /translation="MNERALPHEHPGKWASLALTFAVHIGLALFLFFGIRWQSEPPASL FT EVELAAPPPSRAPEPVDVRPEPEPKPEPPKPTPPRPEPKPEPKPEPPKAAAKPEIATKA FT PEKKPEPPKPEPKKPEPPKPEPKKPEPPKPEPKKPEPPKPEPKKPVEPPKDNYMDKLLE FT RETERAELDKMMRADAARAASARNKAATEGYINAIRTKVRGNLLRPPGLSGNPEAVFEV FT DQLPSGEVLNVRLKRSSGIPALDEAIERAIRRSSPLPLPDKGELFERTLELKFRPLEE" FT CDS complement(444289..444702) FT /transl_table=11 FT /gene="tolR" FT /locus_tag="azo0419" FT /product="putative translocation protein TolR" FT /function="Biopolymer transport protein" FT /note="Putative translocation protein TolR. Holomology to FT tolR of P. aeruginosa of 30% (sprot|TOLR_PSEAE) Involved in FT eth TonB-independent uptake of proteins. no signal peptide FT probable 1 TMH" FT /note="Family membership" FT /db_xref="GOA:A1K2I1" FT /db_xref="InterPro:IPR003400" FT /db_xref="UniProtKB/TrEMBL:A1K2I1" FT /protein_id="CAL93036.1" FT /translation="MRQRRLMNQINVVPYIDVMLVLLVIFMVTAPMVQPGNIDVPSAGP FT ISAPPAEAIVIELEKRNAIAIRKTSNAASRPVSSIEFQRVVKEALAANPEQPFLVAANK FT SLPYQDVIDILEAARQLGVKKISLQTQSGAAGR" FT CDS complement(444721..445395) FT /transl_table=11 FT /gene="tolQ" FT /locus_tag="azo0420" FT /product="translocation protein TolQ" FT /function="Biopolymer transport proteins" FT /note="Translocation protein TolQ. Homology to tolQ of R. FT solanacearum of 52%. Involved in the tonB-independent FT uptake of proteins. InterPro: MotA/TolQ/ExbB proton channel FT family Pfam: MotA/TolQ/ExbB proton channel family no signal FT peptide probable 3 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2I2" FT /db_xref="InterPro:IPR002898" FT /db_xref="InterPro:IPR014163" FT /db_xref="UniProtKB/TrEMBL:A1K2I2" FT /protein_id="CAL93037.1" FT /translation="MTVSHDLSIISLITQASVLVQLVMAMLAGLSVMSWYWIFRKWFQI FT RAARSKTTEFERDFWSGGDLNALFQSASAARHHTGGMERIFESGYREYNKLRAKSHDHG FT ATIDGARRAMRATFQREVDDLEAHLAFLASVGSVSPYIGLFGTVWGIMNAFRGLSNVGT FT ATLTQVAPGIAEALVATAIGLFAAIPAVVAYNRFAHDIDRIGIRFESFMEEFSNILQRN FT LR" FT CDS complement(445392..445859) FT /transl_table=11 FT /locus_tag="azo0421" FT /product="conserved hypothetical thioesterase" FT /EC_number="3.1.2.-" FT /note="Conserved hypothetical thioesterase. Homology to FT bb4233 of B. bronchiseptica of 41% (trembl|Q7WFN8). FT Tigrfam: TIGR00051: conserved hypothetical protein .Pfam: FT 4-hydroxybenzol-CoA thioesterase (PF0361). Interpro: FT 4-hydroxybenzol-CoA thioesterase (IPR006684); thioesterase FT superfamily (IPR006683) This family contains a wide variety FT of enzymes, principally thioesterases. This family includes FT 4HBT which catalyses the final step in the biosynthesis of FT 4-hydroxybenzoate from 4-chlorobenzoate in the soil FT dwelling microbe Pseudomonas CBS-3. This family includes FT various cytosolic long-chain acyl-CoA thioester hydrolases. FT Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to FT CoA and palmitate, they also catalyse the hydrolysis of FT other long chain fatty acyl-CoA thioesters. no signal FT peptide. no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2I3" FT /db_xref="InterPro:IPR006683" FT /db_xref="InterPro:IPR006684" FT /db_xref="InterPro:IPR014166" FT /db_xref="UniProtKB/TrEMBL:A1K2I3" FT /protein_id="CAL93038.1" FT /translation="MQTRSRPEPAGDAFVLPLRVYYEDTDAAGIVYYANYLRYCERART FT EWLRALGFEQQRLRAERGLVFVVKSVHAEYMSPALLDDALELRSVIETLGRASLAFRQQ FT VLRNGVCLFDARVVIACVDLVRNRPVAMPAEIREQFEHVLPPPQPEPPQPA" FT CDS 445887..447230 FT /transl_table=11 FT /locus_tag="azo0422" FT /product="hypothetical protein" FT /function="predicted Zn-dependent hydrolases of the FT beta-lactamase fold" FT /note="SPROT:P37718: 26% identity, 43% similarity Cellulose FT synthase operon protein C precursor. Required for maximal FT bacterial cellulose synthesis. InterPro: STAS domain. The FT STAS (Sulphate Transporter and AntiSigma factor antagonist) FT domain is found in the C-terminal region of sulphate FT transporters and bacterial anti-sigma factor antagonists. FT It has been suggested that this domain may have a general FT NTP binding function. InterPro:IPR008410; BCSC_C. FT IPR003921; Cell_synth_C. Pfam:PF05420; BCSC_C; 1. FT ant_ant_sig: anti-anti-sigma factor No signal peptide FT present SignalP predicted). No transmembrane helices FT present (TMHMM predicted)" FT /note="Function unclear" FT /db_xref="InterPro:IPR002645" FT /db_xref="UniProtKB/TrEMBL:A1K2I4" FT /protein_id="CAL93039.1" FT /translation="MRQVGRSETRPKATIPYTPKWAQALCWRPLAHHRRAVEVLSLPIP FT LFSAPLFRGAKNSVALPFFGKKTPPATPDRAAPGGGDVPKAPQPAPTELSSLDFSRGDA FT NRALAQFAGMVEVQEVETGIGAVFEEAAVLYANGADAEAEKVLVAVLDEPGSVTGEGLW FT MMLLDLYRLTGQRQKFESRVLDYATRFERSPPPWYDLSAGERRRSDSVPLVTLSGALNA FT QSAAQFQQIGIIGRKSGAVRIDLARVRGADDAGCALLRQVFAQLAADRVKVSLLNGGGL FT ADTLSAQIEAGRAEQRDTWLLVLELLQYTADCERFEQLAIDYAVTFEESPPSWEKKASA FT AAAAPVAEPSAPLVGAKGEFVLDGELGGASNDILRKLAAHAAERKSVVVECSRLRRIDF FT VCAGTLFNIIATLQAQGRVVELRGVNAMVGALLRVMSVDQVAQVTLRA" FT CDS 447262..447798 FT /transl_table=11 FT /gene="hslV" FT /locus_tag="azo0423" FT /product="ATP-dependent protease HslV" FT /function="ATP-dependent protease HslVU (ClpYQ) peptidase FT subunit" FT /EC_number="3.4.25.-" FT /note="ATP-dependent protease HslV (EC 3.4.25.-) (Heat FT shock protein HslV). Homology to hslV of E. coli of 69%. FT Protease subunit of a proteasome-like degradation complex. FT InterPro: Multispecific proteasome proteases (IPR004491) no FT signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2I5" FT /db_xref="InterPro:IPR001353" FT /db_xref="InterPro:IPR022281" FT /db_xref="UniProtKB/Swiss-Prot:A1K2I5" FT /protein_id="CAL93040.1" FT /translation="MEQYHGTTILSVRRGNSVALGGDGQVTLGNIVVKASARKVRTLYQ FT GQILAGFAGGTADAFTLFERFEAKLDKHQGNLLRSAVELAKDWRTDRMLRRLEAMLAVA FT DREHSLIITGNGDVLEPEQGIVAIGSGGAYAQSAARALIENTELSPRDVIAKSLAIAGD FT LCIYTNQCHTIEVLD" FT CDS 447833..449164 FT /transl_table=11 FT /gene="hslU" FT /locus_tag="azo0424" FT /product="ATP-dependent Hsl protease ATP-binding subunit" FT /function="ATP-dependent protease HslVU (ClpYQ) ATPase FT subunit" FT /note="ATP-dependent hsl protease ATP-binding subunit hslU. FT Homology to hslU of E. coli of 65% (sprot|HSLU_ECOLI). FT Chaperone subunit of a proteasome-like degradation complex FT (By similarity). InterPro: Heat shock protein HslVU ATPase FT subunit HslU(IPR004491),AAA ATPase,central region FT (IPR003959), AAA ATPase (IPR003593) Tigrfam: hslU: heat FT shock protein HslVU ATPas Pfam: ATPase family associated FT with varius cellular no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2I6" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003959" FT /db_xref="InterPro:IPR004491" FT /db_xref="InterPro:IPR013093" FT /db_xref="InterPro:IPR019489" FT /db_xref="UniProtKB/Swiss-Prot:A1K2I6" FT /protein_id="CAL93041.1" FT /translation="MTQMTPPEIVSELDKHIVGQARAKKAVAIALRNRWRRARIDEPLR FT SEITPKNILMIGPTGVGKTEIARRLARLANAPFIKVEATKFTEVGYVGRDVDTIIRDLV FT EIAIKDGRERAMRVVRDRALDAAEDRVLDVLLPPARPVGFSEPAQPQDSATRQKFRKKL FT REGELDDKEVEIEVASAPMQAEIFAPPGMEELTQQIQGMFQNLGNSRKKLRKLPIREAL FT KLLADEEAARLINDEEVKTEALRAVEQNGIVFLDEVDKIAARADAHGADVSRQGVQRDL FT LPLVEGTTISTKYGMIKTDHILFIASGAFHLSKPSDLIPELQGRFPIRVELESLSVEDF FT ERILTSTDACLTRQYEALLATDGVTLSFTPEGIRRLAEIAYQVNEKTENIGARRLYTVM FT EKLLEEVSFEAGKVGVDKLTVDAAYVDARLEVLAQREDLARYVL" FT CDS 449266..450138 FT /transl_table=11 FT /gene="mdcF1" FT /locus_tag="azo0425" FT /product="putative malonate transporter" FT /function="predicted permeases" FT /EC_number="2.7.7.-" FT /note="Putative malonate transporter. subcellular FT location:integral membrane protein (potential). similarity: FT belongs to the auxin efflux carrier (tc 2.a.69) family. FT SPROT:P56948:24% identity, 41% similarity. InterPro: FT IPR004776; Auxin_eff. Pfam:PF03547; Auxin_eff 2a69: Auxin FT Efflux Carrier" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2I7" FT /db_xref="InterPro:IPR004776" FT /db_xref="UniProtKB/TrEMBL:A1K2I7" FT /protein_id="CAL93042.1" FT /translation="MLTRIVAILFPLFAITAAGFFIGRRLKPDLSHANRLNMDVFVPAL FT VFAALANREFRIGEYLPLLGLTLALVAGSGLVGWVAARALKVEPRTLVPPLMFNNCGNL FT GLPLAVLAFGDAALMPAVVMFMVSNLLHFSFGAWLLDHRARLVNLWRVPSVAATFAGLA FT VGIAGIEVWPPLMTAIKMVGDISIPLMLFALGVRLTDARLTSVGLGVFVALLRPLSGMA FT LVWVLLQLVPLPPREAALLLVFGALPPAVLNYIFAERYRQEPEKVASMVLIGNLAAVLF FT LPLALALAL" FT CDS complement(450142..452085) FT /transl_table=11 FT /locus_tag="azo0426" FT /product="GGDEF/PAS-domain containing protein" FT /function="FOG: GGDEF domain" FT /note="GGDEF/PAS-domain containing protein," FT /db_xref="GOA:A1K2I8" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR006189" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K2I8" FT /protein_id="CAL93043.1" FT /translation="MSFPPRQPLIGRDASPAARGFLVTIAVVVLVVSIEWAAWRQYRAF FT EQRQATAEFARIADQATLSLMQQTAHYRNALLALRATWLASERFDPDEFARYVRALSAP FT QSLPGLRAFAFNRAVEERDRAAYVQRIRREYSAHDPIYNRFDIYPDGIRERYHVVEMIQ FT PPSGNQRSLGYDLGTSDVRRVTVEHALQHGFAATPPIQLQQAPGVLAILILAPLRNVAD FT TTASAADTRDTVAASFLVNEMVNAAISPSLRKQFHLRITDLGATEAAIDTATPLYADNT FT PPGVDSDPRTVTREESFGGRRWQLRFQPTEPAARPLADTVLFGLLAAGALLAGLVSHLA FT MQHARRVVRHQALVRLGSDCILELDAGGRVREADNAAQRITGLPPREWEGEPLWRKVAE FT EDALDVERAVRQCIERREPVVIECRVPDDSGGPPRWISMRLGNHLDHPYLGCLFAQISN FT IDARKEVEAEVARLAFYDPLTGLPNRRLLEARAELTLAAARRHNGHAAVMVLDLDGFKE FT INDSAGHAVGDEVLAQLATRLRHVVRDSDTVARLGGDEFVILLGEPAGEAEVRTAAVRI FT SHALTVPLTAAGHNWLVTASVGIALHPDHGDNFADLLGAADTAMYRSKRTGRGLTTVAS FT GRSAGATPRSTY" FT CDS complement(452338..452742) FT /transl_table=11 FT /gene="hslR" FT /locus_tag="azo0427" FT /product="heat shock protein" FT /function="Ribosome-associated heat shock protein FT implicated in the recycling of the 50S subunit (S4 FT paralog)" FT /note="Heat shock protein 15 homolog (HSP15). INVOLVED IN FT THE RECYCLING OF FREE 50S RIBOSOMAL SUBUNITS THAT STILL FT CARRY A NASCENT CHAIN. BINDS RNA MORE SPECIFICALLY THAN FT DNA. BINDS WITH VERY HIGH AFFINITY TO THE FREE 50S FT RIBOSOMAL SUBUNIT. DOES NOT BIND IT WHEN IT IS PART OF THE FT 70S RIBOSOME" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2I9" FT /db_xref="InterPro:IPR002942" FT /db_xref="UniProtKB/TrEMBL:A1K2I9" FT /protein_id="CAL93044.1" FT /translation="MTTSPSGSDDARTRIDKWLWAARFFKHRTGATDAVDGGKVKLNGS FT AVKPARDVKVGDRLDITIGEEQFTVVVRAIADKRGPASVAQTLYEETPDSVERRQASRE FT QRKLAATPGADLHGRPTKRDRRQIRRFTDF" FT CDS complement(452792..454072) FT /transl_table=11 FT /gene="cysN/C" FT /locus_tag="azo0428" FT /product="putative sulfate adenylyltransferase subunit 1 / FT adenylylsulfate kinase" FT /function="GTPases - Sulfate adenylate transferase subunit FT 1" FT /note="55% Adenylylsulfate kinase (EC 2.7.1.25) (APS FT kinase) (ATP adenosine-5-phosphosulfate FT 3-phosphotransferase)], from Pseudomonas aeruginosa. FT FUNCTION:ATP sulfurylase may be the GTPase, regulating ATP FT sulfurylase activity (By similarity). FUNCTION:APS kinase FT catalyzes the synthesis of activated sulfate (By FT similarity). CATALYTIC ACTIVITY:ATP + sulfate = diphosphate FT + adenylylsulfate. CATALYTIC ACTIVITY:ATP + FT adenylylsulfate=ADP +3'-phosphoadenylylsulfate. PATHWAY: FT Sulfate activation; cysteine biosynthesis reductive branch; FT first step. PATHWAY:Sulfate activation; cysteine FT biosynthesis reductive branch; second step. FT SUBUNIT:Heterodimer composed of cysD, the smaller FT subunit,and cysN (By similarity). SIMILARITY:In the FT N-terminal section; belongs to the GTP-binding elongation FT factor family. CysN/nodQ subfamily. SIMILARITY:In the FT C-terminal section; Belongs to the APS kinase family. FT SWISSPROT:CYSN_PSEAE:O50274. FT InterPro:IPR002891;APS_kinase.IPR004161;EFTU_D2.IPR009001; FT Elong_init_C.IPR000795; ProtSyn_GTPbind.IPR005225; FT Small_GTP.IPR009000; Translat_factor. Pfam:PF01583; FT APS_kinase; 1.PF00009; GTP_EFTU; 1.PF03144; GTP_EFTU_D2;1. FT TIGRFAMs:TIGR00455; apsK; 1.TIGR00231; small_GTP; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2J0" FT /db_xref="InterPro:IPR000795" FT /db_xref="InterPro:IPR004161" FT /db_xref="InterPro:IPR009000" FT /db_xref="InterPro:IPR009001" FT /db_xref="InterPro:IPR011779" FT /db_xref="UniProtKB/TrEMBL:A1K2J0" FT /protein_id="CAL93045.1" FT /translation="MSAPEQLPEIDNGLLRFLTCGSVDDGKSTLIGRLLFDTKAILADT FT MNAIEKTSAKRGMSAVDLSLLTDGLQAEREQGITIDVAYRYFSTGTRKYIIADAPGHEQ FT YTRNMVTAASTANLAIILVDARRGVLTQTRRHSYLASLVGIPHLLVAVNKMDLVDYDQK FT VFEQIRADYLAFADKLGIKDVRFIPISALAGDMIVDRGDRLGWYDGPTLLEILEAAPAA FT HTETAENFRFPVQFVCRPQDSANPELHDYRGFMGRVESGEVAVGDAITVLPSGATSKVK FT AIELGGEKLQRAIHEQSVTLLLEDEIDISRGDMIVKSAEAPEAVKQIDATVCWLSETPM FT STARTYLVRHTTREAKAKVAKIDYRLDVNTLEQEPATSLAMNDIARLTLKLAQPIVADA FT YADNRATGAFIIIDESTNNTVGAGMIG" FT CDS complement(454492..455406) FT /transl_table=11 FT /gene="cysD" FT /locus_tag="azo0429" FT /product="putative sulfate adenylyltransferase subunit 2" FT /function="3-phosphoadenosine 5-phosphosulfate FT sulfotransferase (PAPS reductase)/FAD synthetase and FT related enzymes" FT /EC_number="2.7.7.4" FT /note="84% PAPS_reduct. Pfam:PF01507; PAPS_reduct; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2J1" FT /db_xref="InterPro:IPR002500" FT /db_xref="InterPro:IPR011784" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:A1K2J1" FT /protein_id="CAL93046.1" FT /translation="MSTLTKQTLSHLDWLEAEAIHILREVAGQCSNPALLFSGGKDSLC FT LLRLAEKAFRPGRFPFPLLHVDTGHNYPEVIEFRDRRAAELGERLIVRSVEDSMARGTV FT VLKSPDESRNKHQSVTLLEAIEEFGFDACIGGARRDEEKARAKERIMSFRDEFGQWDPK FT NQRPELWNLYNARSHKGENIRAFPISNWTELDVWQYIEREKLELPSIYFAHVRPVVRKN FT GLLQPVTALTPAKPGDVIEDVLVRFRTVGDITCTAPVESDADTVAKILAETATTTITER FT GATRMDDQTSEASMEQRKKEGYF" FT CDS complement(455534..456304) FT /transl_table=11 FT /gene="cysH" FT /locus_tag="azo0430" FT /product="probable phosphoadenylyl-sulfate reductase" FT /EC_number="1.8.4.8" FT /note="Probabel phosphoadenylyl-sulfate reductase. Homology FT to csyH of V. sinosum of 55% (trembl|Q9L9V0). FT Phosphoadenosine phosphosulphate reductase (EC: 1.8.4.8) is FT involved in the assimilation of inorganic sulphate. In a FT reaction requiring reduced thioredoxin and NADPH, it FT converts 3'-phosphoadenylylsulphate (PAPS) to sulphite and FT adenosine 3',5' diphosphate (PAP). Interpro: FT Phosphoadenosine phosphosulfate reductase cysH-type FT (IPR004511); Phosphoadenosine phophsulfate reductase FT (IPR002500) Tigrfam: cysH: phosophoadenylyl-sulfate FT reductase Pfam: Phsphadenosine phosphosulfate reductase no FT signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2J2" FT /db_xref="InterPro:IPR002500" FT /db_xref="InterPro:IPR004511" FT /db_xref="InterPro:IPR011798" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:A1K2J2" FT /protein_id="CAL93047.1" FT /translation="MSGAVSMLRPAATNPATRPELTEALRASVSAKAAAARELLAAAVA FT ELGANGEITFANSFGAEDMVLTDLILGGKLPIEIFSLDTGRLPAETYTLMGAVEQRYGT FT KLKVFFPDATAVEQFVRSEGINAFYDSVELRKACCGIRKMEPLRRALAGKKAWVTGLRA FT AQSVTRTGLALREFDTANGLEKFNPLSDWTEAEVWAYIRINEVPYNALHDQFYPSIGCA FT PCTRAIALGEDIRAGRWWWEDPASKECGLHVKKT" FT CDS complement(456301..456831) FT /transl_table=11 FT /locus_tag="azo0431" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to PA1837 FT of P.aeruginosa of 50% (tremble:Q9I2Q8). Has FT PF06073,Bacterial protein of unknown function FT (DUF934);IPR008318 UCP030820: This family consists of FT several bacterial proteins of unknown function. One of the FT members of this family Q8YEW3 is thought to be an FT oxidoreductase. No signal peptide. No TMHs" FT /db_xref="InterPro:IPR008318" FT /db_xref="UniProtKB/TrEMBL:A1K2J3" FT /protein_id="CAL93048.1" FT /translation="MPKVIRNRRVEDDARQIVRLAEGETAETVAIPAGPVLVPLAVWQA FT RAEELAARGDVGVWLEAAEGAELIAADLPKLAAVAVNFPAFTDGRGYSTAALLRTRYGY FT SGELRAIGDVLRDQFQAYVRCGFDTLQPNAGRYTDAQLEAALASLGDFSVPYQGAVDEP FT RPLWARAQRGVAA" FT CDS complement(456824..458506) FT /transl_table=11 FT /gene="cysI" FT /locus_tag="azo0432" FT /product="putative sulfite reductase" FT /function="Sulfite reductase beta subunit (hemoprotein)" FT /EC_number="1.8.1.2" FT /note="49% Fd-NiR.IPR011255; NiR_SiRalpha_1/3.IPR006067; FT Nir_Sir_4Fe4S.IPR005117; NiR_SiR_beta_fer. Pfam:PF01077; FT NIR_SIR; 2.PF03460; NIR_SIR_ferr; 2." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2J4" FT /db_xref="InterPro:IPR005117" FT /db_xref="InterPro:IPR006067" FT /db_xref="UniProtKB/TrEMBL:A1K2J4" FT /protein_id="CAL93049.1" FT /translation="MYRYDDYDQRLVDERVAQFRDQTRRYLAGELSEDEFRPLRLQNGL FT YVQRHAPMLRIAVPYGLFSSAQLRTLADIARRYDRGYGHFTTRQNIQFNWPELAKVPEI FT LAQLATVQMHAIQTSGNCIRNITSDAFAGVAADELIDPRPWCEILRQWSSFHPEFAHLP FT RKFKFAVNGAKEDRAVIQAHDIGLDVVKNDAGEIGFRVLVGGGLGRTPIIGEEIAAFVP FT WQHIVTYCESILRVYNLHGRRDNKYKARIKILVKALGIEEFRRQVEAEWAFHKNGPSTL FT TEAEVARVAAHFVDPAYESLPATDAGYASLLDENKPFAAWVKRNVRAHKVPGYASVTIS FT LKKTGVPPGDITESQMELVADLADAYSYGEVRATHQQNLVLADVRQSDLFKVWQSLRDA FT GLATPNIGLLTDIISCPGGDYCALANAKSIPIANAIQERFDNLDYLYDIGEIELNISGC FT MNACGHHHVGHIGVLGVDKNGEEWYQVTIGGDQGNKAAIGKVIGPSFAAAEMPDVVTHL FT IETYIANRHEDERFVDTVRRIGIEPFKAHVYGNRQTEKKVAHA" FT CDS complement(458559..459338) FT /transl_table=11 FT /locus_tag="azo0433" FT /product="conserved hypothetical membrane protein" FT /function="predicted permeases" FT /note="Conserved hypothetical membrane protein. Homology to FT bll1489 of B. japonicum of 58% (trembl|Q89UC8(SRS)) FT InterPro:IPR002781; DUF81. Pfam:PF01925; DUF81 Presence of FT 8 transmembrane helices (TMHMM predicted) probable FT transmembrane protein of unknown function) no signal FT peptide" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2J5" FT /db_xref="InterPro:IPR002781" FT /db_xref="UniProtKB/TrEMBL:A1K2J5" FT /protein_id="CAL93050.1" FT /translation="MDFAYTVAGFAVGAIVGLTGVGGGSLMTPLLVLLFGIHPSVAVGT FT DLLYAAITKAGGTVAHGLKGTVDWTVTRRLASGSIPAAALTLVLVGTFAPGGMAGATGL FT IKVALGVALLLTAVALIFRKQIQAYAASRFGDEPNPQRTAWLTVVVGAVLGVLVSISSV FT GAGALGVTALFFLYPKMPALRIVGSDIAHAVPLTLVAGIGHWILGSVDWFLLGSLIVGS FT LPGIWLGSHISTKVPDRVLRPILATMLVLVGAKLIGH" FT CDS 459444..460385 FT /transl_table=11 FT /gene="cysB" FT /locus_tag="azo0434" FT /product="transcriptional regulator CysB" FT /function="Transcriptional regulator" FT /note="HTH-type transcriptional regulator cysB (Cys regulon FT transcriptional activator). this protein is a positive FT regulator of gene expression for the cysteine regulon, a FT system of 10 or more loci involved in the biosynthesis of FT l-cysteine from inorganic sulfate. the inducer for cysb is FT n-acetylserine. cysb inhibits its own transcription." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2J6" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K2J6" FT /protein_id="CAL93051.1" FT /translation="MNLQQLRYIQEVARRGLNVSDAADALYTSQPGVSKQIRLLEAELG FT IEIFARHGKRLVAVTEPGRAVLAIAERMLRDMDNLLQVGDEFSNEAAGGLSIATTHTQA FT RYALPPVVREFMRRYPQVKLSLHQGSPHQVCEMVLDGSADIAIATEAIAEYDELVMLPC FT HQWNRCVVASPRHPILREQPLTLEAIARYPLITYDDAFTGRSQINKAFLGRGLKPNVVL FT TALDSDVIKTYVAMDLGIGILARMAYDPEEDRKLGMIDAAHLFESSTTRIGLRRRAWLR FT GYVYAFVELFAPHLTRRMVETALAGGGSDPGL" FT CDS 460530..461414 FT /transl_table=11 FT /locus_tag="azo0435" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. Signal peptide present. No FT TMHs" FT /db_xref="InterPro:IPR013424" FT /db_xref="UniProtKB/TrEMBL:A1K2J7" FT /protein_id="CAL93052.1" FT /translation="MEIRKVVLGCATACCAIASPSVSAALLPLPDTVIDGVVVSIQYGD FT FYSYSTRVLDYLQPDAGWDKSAGTGTLDVIITTRSAGQSNSNGGLAPYNIPDPITNVNE FT NPTSGSWGMGGTSATTMLVSDLYRYLQDTFDATIPVFTFDQNETGGNPSLFAMAKVEIF FT DKDGNLLEDWILGDGVNPVEAPGTVCVDPDSLPLKCFSNNVGSGAFDYILFAPTMDLTN FT YNAEGNIFKVSWTFSSVDDGGEEATLTGRFTGSICVENPSAPQCQVIPEPGALALIGGG FT LLALFALRRRWGA" FT CDS complement(461424..462398) FT /transl_table=11 FT /locus_tag="azo0436" FT /product="L-asparaginase II precursor" FT /function="L-asparaginase/archaeal Glu-tRNAGln FT amidotransferase subunit D" FT /EC_number="3.5.1.1" FT /note="L-asparaginase precursor (EC 3.5.1.1) (L-asparagine FT amidohydrolase) (L-ASNase)." FT /note="Family membership" FT /db_xref="GOA:A1K2J8" FT /db_xref="InterPro:IPR006034" FT /db_xref="InterPro:IPR020827" FT /db_xref="UniProtKB/TrEMBL:A1K2J8" FT /protein_id="CAL93053.1" FT /translation="MPRQPVIALVATGGTIAGTADTPGAVTGYTAGVLGAEALLAAFPG FT LGEIAALRAETLFSLDSKDMAPAHWLALAQRVQALADDPAVDGVVITHGTDTLEESAFF FT VHLTVATAKPVVFTAAMRPATALSADGPMNLLAAVRVAAAPAFHGLGTLVAINDRVYAA FT RDVQKQRTHGLDAFGAGEGAAVGRSDPARPGLLVNRDGGSCAAALASAALPAVEVLYVA FT AGASPALLDAVRGSGAAGAVLAFPGNGSVPEAWKPAIDAALHAGMVLVRASRVPAGPVG FT HDTRLPASLLSAGDLPPSKARVALMLALACDRPQRFCTLAAPH" FT CDS complement(462427..463827) FT /transl_table=11 FT /locus_tag="azo0437" FT /product="probable aspartate ammonia-lyase" FT /function="Fumarase" FT /EC_number="4.3.1.1" FT /note="Region start changed from 463959 to 463827 (-132 FT bases)" FT /db_xref="GOA:A1K2J9" FT /db_xref="InterPro:IPR000362" FT /db_xref="InterPro:IPR004708" FT /db_xref="InterPro:IPR008948" FT /db_xref="InterPro:IPR018951" FT /db_xref="InterPro:IPR020557" FT /db_xref="InterPro:IPR022761" FT /db_xref="InterPro:IPR024083" FT /db_xref="UniProtKB/TrEMBL:A1K2J9" FT /protein_id="CAL93054.1" FT /translation="MQTTRIEHDLLGEREIPADVYWGIHSLRALENYPITGKSIGAYPE FT LVKALALVKQAAARTNHQLGQLDEGRFHAIDEACREIAEGRLHNQFVVDVIQGGAGTST FT NMNANEVIANLALEKLGWPKGHYKELHPINHVNMSQSTNDVYPTALKLAVVFAIQGLLD FT AMETLRLAYLAKAEEFKDILKIGRTQLQDAVPMTLGQEFSTYAVMMKEDVARLREAICL FT IQEINLGATAIGTGINTDIRYAKMATEHLAELSGVKLVPAENLIEATQDTGAFVQLSGV FT LKRIACKLSKVCNDLRLLSSGPQAGFNEINLPERAAGSSIMPGKVNPIIPEVVNQIAFE FT VIGNDVTITLASEGGQLQLNAFEPIIGHSLFKSIEHLEAGCRTLTDNCVRGITANRELL FT AERVRTSAGLATALNPHIGYENATWAAREALKTGRSVAELVLERGLMDKESLERTLRPE FT VLTAPRAE" FT CDS complement(463964..465061) FT /transl_table=11 FT /gene="ansB2" FT /locus_tag="azo0438" FT /product="periplasmic L-asparaginase II" FT /function="L-asparaginase/archaeal Glu-tRNAGln FT amidotransferase subunit D" FT /EC_number="3.5.1.1" FT /note="L-asparaginase precursor (EC 3.5.1.1) (L-asparagine FT amidohydrolase) (L-ASNase)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2K0" FT /db_xref="InterPro:IPR004550" FT /db_xref="InterPro:IPR006034" FT /db_xref="InterPro:IPR020827" FT /db_xref="UniProtKB/TrEMBL:A1K2K0" FT /protein_id="CAL93055.1" FT /translation="MPLSSQLRHLLLPALAAAALLLPPAAHAREAAAPARLAKVVILAT FT GGTIAGAGADAASSATYQAAKVPVEKLVAGIPELKNLAEVRGEQVFQIASESFTNEHLL FT QLGRRVAELSASADVDGIVITHGTDTLEETAFFLNLVIRSDKPVVVVGSMRPGTALSAD FT GALNLYDAVAVAASSDARGKGVLVTMNDEIHSGRDVSKAVNIRPDAFRSPWGPLGMVVE FT GKPYWFRLPAKRHTLNSEFDIARIQSLAPVEIAYGYGNVSDTAYKAFAAAGAKAIIHAG FT TGNGSVSNRVVPGLQALRAQGVHIVRSSRVDGGGFVLRNAEQPDDKYDWVAAHDLNPQK FT ARILAAVALTTTSDSRELQRIFWEY" FT CDS complement(465187..465915) FT /transl_table=11 FT /gene="glnQ1" FT /locus_tag="azo0439" FT /product="probable glutamine transport ATP-binding protein" FT /function="ABC-type polar amino acid transport system FT ATPase component" FT /note="Glutamine transport ATP-binding protein glnQ. FT Homology with glnQ of B. stearothermophilus of 56% FT (sprot|GLNQ_BACST). PART OF THE BINDING-PROTEIN-DEPENDENT FT TRANSPORT SYSTEM FOR GLUTAMINE. PROBABLY RESPONSIBLE FOR FT ENERGY COUPLING TO THE TRANSPORT SYSTEM. InterPro: AAA FT ATPase superfamily (IPR003593), ABC_transporter FT (IPR003439), ATP/GTP_binding site motif A (P-loop) FT (IPR001687) Pfam: ABC transporter no signal peptide no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2K1" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K2K1" FT /protein_id="CAL93056.1" FT /translation="MIEINNVSKWYGDFQVLTDCTTGVKKGEVVVVCGPSGSGKSTLIK FT CVNALEPFQQGSIKVNGIAVEDPKTNLPKLRSHVGMVFQHFELFPHMTITDNLAIAQIK FT VLGRKRDEAVEKGLKLLDRVGLKAHAHKFPGQLSGGQQQRVAIARALAMDPICMLFDEP FT TSALDPEMINEVLDVMVELAREGMTMMCVTHEMGFARKVAHRVIFMDRGAIVEDAAKDE FT FFGQPRSERAQSFLAKILQH" FT CDS complement(465947..466627) FT /transl_table=11 FT /gene="glnM" FT /locus_tag="azo0440" FT /product="putative glutamine transport permease protein" FT /function="ABC-type amino acid transport system permease FT component" FT /note="Putative glutamine transport permease protein. FT Homology to glnM of B. subtilis of 30% (TREMBL:O34671) FT Probably part of the binding-protein-dependent transport FT system of amino acids. Probably responsible for the FT translocation of the substrate across the membrane FT InterPro: Binding-protein-dependent transport systems inner FT membrane component (IPR000515) Pfam: FT Binding-protein-dependent transport systems inner membrane FT component no signal peptide probable 5 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2K2" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR010065" FT /db_xref="UniProtKB/TrEMBL:A1K2K2" FT /protein_id="CAL93057.1" FT /translation="MGDFEFGVIADNWRFLAEGLRYTVQVTLVATIGGIFLGTLLALMR FT LSSVKPLQWFAVGYINFFRSVPLVQVILAFYLIIPMVLQMFTGKPMPIGAENSAYFTFT FT VFEAAYFAEIMRSGIQSIPRGQIGAGYALGFTYGQTMRLVVLPQAFRNMLPVLLTQTIV FT LFQDVSLVYAIGATDFFGAADKITQRDLRPVEMYTTVAAVYFVLCFSLSRLVKRLQTRI FT AIIR" FT CDS complement(466629..467366) FT /transl_table=11 FT /gene="glnP" FT /locus_tag="azo0441" FT /product="putative glutamine transport permease protein" FT /function="ABC-type amino acid transport system permease FT component" FT /note="Glutamate/aspartate transport system permease FT protein gltJ. Homology to glnP of B. subtilis of 23% FT (CAA93320). PART OF THE BINDING-PROTEIN-DEPENDENT TRANSPORT FT SYSTEM FOR AMINO ACID; PROBABLY RESPONSIBLE FOR THE FT TRANSLOCATION OF THE SUBSTRATE ACROSS THE MEMBRANE. FT InterPro: Binding-protein-dependent transport systems inner FT membrane component (IPR000515) Pfam: FT Binding-protein-dependent transport systems inner membrane FT component HTH-motif probable 4 TMHs no signal peptide" FT /note="Family membership" FT /db_xref="GOA:A1K2K3" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR010065" FT /db_xref="UniProtKB/TrEMBL:A1K2K3" FT /protein_id="CAL93058.1" FT /translation="MNYHWDWAFFFQETDDGLKYIDWVISGMGWTTAVSLSALAIALLV FT GSVLGVMRTTPSKLLVAIGDTYVDIFRNVPLIVQLFMWFFVVPELVPESIGLWMKQDLP FT YFVTAVIGLGLYTAARIAEQVKSGINALARGQRFAGLALGFTEWQTYRYVRLPMAYRIV FT LPALTSEAMNIFKNSAVTYAVGILELYFQYKQIIEKTSQVLEITIVVTLTYFVLAFAMN FT RLLGFIEKRTRVPGLITGGSGGH" FT CDS complement(467763..468662) FT /transl_table=11 FT /gene="glnH" FT /locus_tag="azo0442" FT /product="putative glutamine-binding protein" FT /function="ABC-type amino acid transport/signal FT transduction systems periplasmic component/domain" FT /note="Putative glutamine-binding protein. Homology to glnH FT of B. stearothermophilus of 28% (sprot|GLNH_BACST). FT Involved in glutamine-transport system. Interacts with the FT glutamine-transport system glnPQM. Pfam: Bacterial FT extracellular solute binding protein no TMHs signal FT peptide" FT /note="Family membership" FT /db_xref="GOA:A1K2K4" FT /db_xref="InterPro:IPR001638" FT /db_xref="UniProtKB/TrEMBL:A1K2K4" FT /protein_id="CAL93059.1" FT /translation="MRTSLSVLALCFAAAGLAAPAHAAEPTGTLKKIKDSGTITVGHRE FT SSVPFSYLDADQKPVGYAMDLCAKVVDAVKDELKLPKLEVKYQAVTSQNRIPLMQNGTI FT DIECGSTTNSVQRQQQVGFSVNYFVTSVRMAVRKDSGIKDIGDLNGKPVATTTGTTSDA FT LIKQNEKGKSIDVRNIYGKDHADSFLMVESGRAAAFVMDDILLAGLIASSKNPAAYEIV FT GPSLRDEPYGVMLRKDDTEFKAVVDKALTGLMKSGEAEKMYTKWFTQPIPPRNVNLNFP FT MSAATKAALTNPTDKGVE" FT CDS 468959..470002 FT /transl_table=11 FT /locus_tag="azo0443" FT /product="beta-lactamase" FT /function="predicted exonuclease of the beta-lactamase fold FT involved in RNA processing" FT /EC_number="3.5.2.6" FT /note="Conserved Hypothetical FT protein(Metallo-beta-lactamase superfamily). Has PF00753, FT Metallo-beta-lactamase superfamily; IPR001279, FT Blactmase-like;These proteins include thiolesterases, FT members of the glyoxalase II family, that catalyse the FT hydrolysis of S-D-lactoyl-glutathione to form glutathione FT and D-lactic acid and a competence protein that is FT essential for natural transformation in Neisseria FT gonorrhoeae and could be a transporter involved in DNA FT uptake. Except for the competence protein these proteins FT bind two zinc ions per molecule as cofactor." FT /note="Family membership" FT /db_xref="GOA:A1K2K5" FT /db_xref="InterPro:IPR001279" FT /db_xref="UniProtKB/TrEMBL:A1K2K5" FT /protein_id="CAL93060.1" FT /translation="MDLIVARPEGLYCPPGDFYIDPWRPVDRAVITHGHGDHARPGHRH FT YLAAAPGEGVLRARLGEIPLQTLGYGEEVRHHGVGIRFHPAGHVLGSAQVRIEYRGEVW FT VASGDYKLEADGTCDAFEPVRCDTFITESTFGLPIYRWPPQAELGAAINAWWQANAAAG FT RASVLFCYAFGKAQRILHLLDPAIGPIVVHGAVEPLNAVYRAAGVALPATRKVGEVAAE FT ELRRALVLAPPSAQGSPWLRRFGDYADAFASGWMRIRGTRRRRGVDRGFVLSDHADWPG FT LLRAIEATGAQRVFVTHGSVAVLVRWLGEQGLAAQAFATEYGEEDDAGQGGAGDSARPD FT DAAEPPQ" FT CDS 469999..471642 FT /transl_table=11 FT /gene="lig2" FT /locus_tag="azo0444" FT /product="DNA ligase" FT /function="ATP-dependent DNA ligase" FT /EC_number="6.5.1.1" FT /note="DNA ligase (EC 6.5.1.1) (Polydeoxyribonucleotide FT synthase [ATP]). This protein seals during DNA replication FT DNA recombination and DNA repair nicks in double-stranded FT DNA (By similarity)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2K6" FT /db_xref="InterPro:IPR012308" FT /db_xref="InterPro:IPR012309" FT /db_xref="InterPro:IPR012310" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR016059" FT /db_xref="UniProtKB/TrEMBL:A1K2K6" FT /protein_id="CAL93061.1" FT /translation="MKAFAALYAELDATTSSNAKLAAMVAYFRAAPAADAAWAAYFLAG FT GKPRQLVPVRQLREFAMRIAGVPEWLFEESYQAVGDLAETLALLLPEGVAGDDAPLAEW FT VEARLLPLRGLPPDVLQPRLEMLFGALSTLQRFVCAKLITGSFRVGVSRLLVTRALGEA FT GGVDTRRVAERLIGYTDIGARPDAASYRALLAPPAPAEGAREDGLPYPFFLAHPLQAPV FT EALEDRLGPPENWLIEWKWDGIRAQLVRRGGRSWLWSRGEDLVTERFPELAALGAELPE FT GTVIDGEILVWKAGRVQPFAALQKRLGRKTVGTRLLAEAPVVLCAYDLLEWQGEDLRAQ FT PQHARRAALERLAQHHPQRALQLSPLLHGEDWAALARLREEARERGVEGMMLKGRDAPY FT GVGRSKEGGVWWKWKIDPYSIDAVLIYAQRGHGRRASLYTDYTFAVWDAPPDAPQRRLV FT PFAKAYSGLTDAEIRQVDAIVRKTTQEKFGPVRSVTPEQVFELGFEGIARSARHKSGIA FT VRFPRILRWRHDKPAAEADTLQTLAELLPP" FT CDS 471695..474442 FT /transl_table=11 FT /locus_tag="azo0445" FT /product="probable ATP-dependent helicase" FT /function="Lhr-like helicases" FT /EC_number="3.6.1.-" FT /note="Putative ATP-dependent helicase MTH1802. FT TREMBL:Q88NV1: 57% identity, 66% similarity FT InterPro:IPR001410; DEAD/DEAH box helicase IPR001650; FT Helicase_C. Pfam: PF00270; DEAD; 1. PF00271; Helicase_C; 1. FT SMART: SM00487; DEXDc; 1. SM00490: HELICc livcs: FT branched-chain amino acid trans Non secretory protein with FT low probablity of cleavage site (0.167): Signal P FT predicted. No transmembrane helices (TMHMM predicted)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2K7" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR013701" FT /db_xref="InterPro:IPR014001" FT /db_xref="InterPro:IPR017170" FT /db_xref="UniProtKB/TrEMBL:A1K2K7" FT /protein_id="CAL93062.1" FT /translation="MSPPRKPPSRRATPRPPGSLPRLAPRRGAAAAARARAAAIEAVDA FT ARAAAAGAGVAEPTVECAPLPGCEPGSSLPMAARIERWYAARGWAPFDFQRALATAVAA FT GESGLLHATTGAGKTYAAWFAALARWAAAGAPSPSGTRRGPPAPPLTLLWLTPMRALAA FT DTGRALQAPLAELGCDWRVGVRSGDTAASERAAQDRRLPTALVTTPESLSLLLSRAEAA FT QTLGAVAIVVVDEWHELLGNKRGVQVQLALARLRRWNPALVVWGLSATLGNLDHARAAL FT LGPAHAAQGRLLRGEVPKQLQIDTLLPSAPARFPWAGHLGMQMLPQVVAEIDASATALV FT FVNTRSQAELWYQALLDARPDWAGLLALHHGSLDADSRAWVEAGLKAGTLKAVVCTSSL FT DLGVDFLPVERVLQIGSPKGVARLLQRAGRSGHAPGRPSRVTLVPTQSLELVEAAAARA FT AAEAGHVEARRSPEQPMDVLVQHLVTVALGGGFRPDALLAEVRGCHAYRALDEAAWQWA FT LDFVGRGGAALVAYPDYRRVAPDEGGVWRVPDARLARRHRMGIGTIVSDAGISVRYWGG FT RGAAGGRLGTVEESFVARLRPGDCFLFAGRLLELVRVHEMTAWVRRASGARPAVPRWNG FT GRMPLSSELAAAVVAALDDAADGRFDAPELERARPLLELQARWSALPRRGALLAETLKT FT REGHHLFLYPFAGRAVHLGLASLFAWRLARTRPLSFSIAVNDYGLTLLCAEDPDWDAAL FT GAGLFEAGDLLGDVLASLNAGELARRRFREIARVSGLVFTGYPGEARSTRQLQASAGLF FT YEVFRNHDPANLLLDQAEQEVLRQELELGRLEAALAAMRAARLLRAPLRRPSPFAFPLL FT VERMREKLSTEKLADRIRRMLDELERAADAPAVSRAAPSAAREG" FT CDS 474445..475113 FT /transl_table=11 FT /locus_tag="azo0446" FT /product="conserved hypothetical protein" FT /function="predicted ICC-like phosphoesterases" FT /note="Probable Hypothetical protein MJ0037. Members of FT this uncharacterized family share a motif approximating FT DXH(X25)GDXXD(X25)GNHD as found in several FT phosphoesterases, including the nucleases SbcD and Mre11. FT SbcD is a subunit of the SbcCD nuclease of Escherichia coli FT that can cleave DNA hairpins to unblock stalled DNA FT replication. All members of this family are archaeal FT TREMBL:Q88NV2: 46% identity, 59% similarity FT InterPro:IPR004843; M-ppestrase. Pfam: PF00149; FT Metallophos; No transmembrane helices TIGR00024: conserved FT hypothetical prot" FT /note="Function unclear" FT /db_xref="GOA:A1K2K8" FT /db_xref="InterPro:IPR004843" FT /db_xref="InterPro:IPR024173" FT /db_xref="UniProtKB/TrEMBL:A1K2K8" FT /protein_id="CAL93063.1" FT /translation="MPAHVDLERAGLRLRLLPERAVWWADEATLFIADPHFGKAAAYRA FT LGQPVPRGTTGETLARLDRLLAQWPARRLVVLGDFLHAPEAHAPATLAAMQRWRERHPR FT LDCVLVRGNHDDRAGDPPPALGIAVVDEPLALGPLRLWHAPPPPERVPPGCFALGGHLH FT PAYVLRTRHERLRLPCYLFGPAVGVLPAFGAFTGSAEVWPGPLDTVCVVGDGEVFRVAG FT " FT CDS complement(475122..476456) FT /transl_table=11 FT /gene="dctD1" FT /locus_tag="azo0447" FT /product="transcriptional regulatory protein" FT /function="Response regulator containing CheY-like receiver FT AAA-type ATPase and DNA-binding domains" FT /note="C4-dicarboxylate transport transcriptional FT regulatory protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2K9" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR002078" FT /db_xref="InterPro:IPR002197" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR020441" FT /db_xref="UniProtKB/TrEMBL:A1K2K9" FT /protein_id="CAL93064.1" FT /translation="MTAPLHVLVIEDDPNVRLGCEQALQLAGIAVDAVGSAEAGLAKLG FT AGFPGIVVTDMRLPGADGLAVVRRARELDPDLPVIMITGHGDVTLAVEAMRSGAYDFIQ FT KPFAPDLLVEVVRRALDKRALALEVVELRRRLEQRDGLDAALIGRSPQMERLRRLILDV FT AGQTVDVLIHGETGTGKELVARCLHDRGPRRKANFVALNCGGLPDNLLDSELFGHEAGA FT FTGAQKRRVGKIEHASGGTLFLDELESMPMAVQIKLLRVLQERVIERLGSNQLLPVDTR FT VVAATKDDLLELANQGKFRADLYYRLNVVTIELPPLRERREDIPLLLEHFLLQAAQRFE FT RPLPAVSPEHMSRLMAHGWPGNVRELRNVADCLVLGVANAVLGTAGSVATLSLAEQVEH FT FERSLIDAELRRQAGNLSRAAEALHVAKTTLHDKIRKYGLGARDA" FT CDS complement(476453..478414) FT /transl_table=11 FT /gene="dctB1" FT /locus_tag="azo0448" FT /product="sensor histidine kinase" FT /function="Signal transduction histidine kinase regulating FT C4-dicarboxylate transport system" FT /EC_number="2.7.13.1" FT /note="C4-dicarboxylate transport sensor protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2L0" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="InterPro:IPR017055" FT /db_xref="UniProtKB/TrEMBL:A1K2L0" FT /protein_id="CAL93065.1" FT /translation="MTAASSPSAKADSAAEAVPRPAPERPRPGHGPLLAALAVLLVSLA FT GFGGYRLGEGLGMRALQVEASHRLDLGAAAIDGVVNRYAHIPATIELSPEVLALLRAPD FT SEARAAAANRYLERLNGHIGSIALFVLDRRGEVRAASNWAHGDSFIGEDLSFRPYFQRA FT IAGQAGRHFAIGTTRGDPGYFVSHPIRDGSEIIGVAVIKIPLGGLEETWLSLGTPALIS FT DENGVVILTAVPGWLYRSLAPLSAATVAEIEANRLYNGRPIQPLTIGPEPVAAQLPMAD FT EDGVELRLDRRIALPPELPRNSGYYLAQGRTLPDTGWRLLVFSDLTPVRHQAASQAALA FT LVAAAFVVLLAIFIAQRRRILRQRLEAQRLLERSNAELENKVARRTRALTESIARLRKE FT IAERQHAEQTLHAAQDELVQAGKLAVLGQLATSVTHELTQPLGAMRTLAGNAVEFMRRG FT DQDTAAKNLDIVGRLADQMASIITPLKTFARKSPAVPAAVDVTHAVGNALFLLEQRLKS FT ADITVDNACVAGEAIAWCDQNRLEQVLINLIGNAIDAMRGQPRRELSIHAVRHADGRIL FT LRIGDTGCGVPEALRGRLFEPFFTTKPAGEGLGLGLAISRDIVREFGGDLDADNRASGG FT TYFTVFLNPAPATESAAP" FT CDS complement(478380..480146) FT /transl_table=11 FT /gene="kefB" FT /locus_tag="azo0449" FT /product="putative glutathione-regulated potassium-efflux FT system protein" FT /function="Kef-type K+ transport systems membrane FT components" FT /note="Glutathione-regulated potassium-efflux system FT protein kefB,(K+/H+ antiporter).Transport system that FT facilitates potassium-efflux possibly by potassium-proton FT antiport. 32% K_eff.IPR006153; FT Na_H_porter.IPR006036;TrkA_Kuptake. IPR003148; TrkA_N. FT Pfam:PF00999; Na_H_Exchanger; 1.PF02254; TrkA-N; 1. FT TIGRFAMs:TIGR00932; 2a37; 1. TMHelix:12. Belongs to the FT monovalent cation:proton antiporter 2 (cpa2) transporter FT (TC 2.A.37) family. KefB subfamily." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2L1" FT /db_xref="InterPro:IPR003148" FT /db_xref="InterPro:IPR006153" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K2L1" FT /protein_id="CAL93066.1" FT /translation="MHHFSASRYRMDHEAFPFLKETILFLALSGVLIPLLARLRINPVL FT GFLAVGTALGPYGLASFVPAHPWLAYVTFPRQEEVETLAELGVIFLMFMIGLELSVDRL FT WSLRRQVFGLGTLQVALTAALIGGIAHLFGNTTEASVILGLVLSFSSTAIVMQLLIQRG FT ELGGPLGQAAFAILLLQDLAVVPLLVLLSILGAGNSEGSFALLLGTAAAKGLVTVGLIY FT LIGRRLVRPVFHQITVSRQPDTFMALTLLTTLGVAAMTWAAGLSMALGALLAGLIIAET FT EFRHEVEVTIEPFKGLLMGLFFLSVGMGIDLRALLAEPLWIPLAVAGLMIIKGAVVFAL FT LRLFGLSWGRAVEGGFLLGQGGEFAFIVIGLALSFKLLPRDVGQFMLLAVGLSMLATPV FT VARLGRELGAAMDRRQPPAAQEDAEFGTLRGHVLIAGYGRVGQMVGQMLAEQGVPHVAV FT ETDAKLVAGQRKTGAAVIYGDASRPELLRKLHLDRALAVVLTMDHTAAAVHAVKGIRQS FT NPHVRIIARARDEKHALTLREAGASVVVPETLESGLKLTGSVLETLGVPADAASRLLEQ FT ERDRRIVAFRES" FT CDS 480291..482036 FT /transl_table=11 FT /locus_tag="azo0450" FT /product="PAS/PAC/GGDEF-domain containing protein" FT /function="predicted periplasmic ligand-binding sensor FT domain" FT /note="PAS/PAC/GGDEF-domain containing protein,implicating FT involvement into signalling processes. Similarity to FT TREMBL: trembl|Q98JA6 (30% Rhizobium loti,hypothetical FT protein mlr2027) InterPro: IPR000160 GGDEF. IPR001610 PAC. FT IPR000700 PAS-assoc_C. IPR000014 PAS_domain. Pfam: PF00990 FT GGDEF. SMART: SM00086 PAC. SM00091 PAS. TIGRFAM: TIGR00254 FT GGDEF. TIGR00229 sensory_box." FT /db_xref="GOA:A1K2L2" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR006189" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K2L2" FT /protein_id="CAL93067.1" FT /translation="MLATLGVAAAGLVLFTGDLLEGRLHERWRAERLSELSGLRAQLEG FT RLNGAINLTAGLVAHVAVHGGIGEEEFERLAAELMVERSLLRNITLAPGNVIGMVYPLR FT GNERAIGLDLLNHPVQGAATRRMLALNRPVLAGPVDLVQGGRALIHRVPIFLSPPDGPP FT RSGSYWGLMSTPIDFDGLLAQAGLTDPRLRFRIALRGVDGMGADGAVFWGDAALFDDRD FT AIALDIQVLNGSWRMAALPLDEPAVGNTVWAARAAAVLLVLVTLAMVLRLRSMDLRLTE FT SEALHRELAEQIRDVLFRTDAAGRVIYLNPAWTQITGREVSTCLGYHWTELVEVEPGDG FT VRLRTAKLLSDARHDGGNTPALQNERVHLTDCDGTRRTLVVRAGVHRNPAGAVEGVVGI FT MVDISEQERLEARVRHLALHDSLTGLANRVLLASRFQQAAEFARRMGHRMAVLYLDLDG FT FKPINDGYGHETGDRVLCGIGERLQLSVRESDTVARVGGDEFVILLGQVLSVDDARAVA FT LKVQDVLAPALVVGEQRFSVRASIGISVFPDHGGSLDELLRAADRAMYRVKSAAAGGHI FT GVIDA" FT CDS complement(482053..482613) FT /transl_table=11 FT /locus_tag="azo0451" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology with hits FT in the Database. No domains predicted. Signal peptide FT present. No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K2L3" FT /protein_id="CAL93068.1" FT /translation="MKPLAALFAAVLCAAAPAVHAQSGAGYEAAVAGWSRYQDVAGWLE FT GNFSFDRGRLDTILQRTRQNGPAGLLARAADGTFALRSGYCTDAAAFAIQSLNRINPGY FT RARYVFIKNRYGQPHHWVAGFMDGDKLMVMDYGAGPEWSAMRGVHGPYASLDDYAAFLG FT SLRIARFAPESVEWRDTFPGQQD" FT CDS complement(482675..483571) FT /transl_table=11 FT /gene="trxB1" FT /locus_tag="azo0452" FT /product="putative thioredoxin-disulfide reductase" FT /function="Thioredoxin reductase" FT /EC_number="1.8.1.9" FT /note="Putative thioredoxin reductase. Homology to trxB of FT S. coelicolor of 25% (sprot|TRXB_STRCO). Catalyse the FT reaction: thioredoxin + nadp(+) = thioredoxin disulfide + FT nadph. InterPro: FAD-dependent pyridine FT nucleotide-disulphide oxidoreductase (IPR001327) Pfam: FT Pyridine nucleotide-disulphide oxidoreductase no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2L4" FT /db_xref="InterPro:IPR000103" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K2L4" FT /protein_id="CAL93069.1" FT /translation="MSQDFDALVIGGGPAGLTGALYLARFRRRVRLVDDGCSRATRIPR FT SHNMPGYPDGVRGGELVAAIRLQATRYGVDFASGRVTALEREGTRFSARLADGSTTHAR FT AVLLATGVTDVEPPMPYLAEAVRSGALRYCPVCDGYEVSGQTVGVLADGDAGAREALYL FT RGFTARLHVFPLSDTVEISARERQRLRDADIMLAEHAVASLRLADGGVVVRHGDYETRC FT DSVYSALGTRIQADLAPDAERDEQGYLLTDRHHMTSIGGLYAAGDVVQGLNQISVATGG FT AAIAAAAIHRALGPAWA" FT CDS complement(483653..485464) FT /transl_table=11 FT /gene="atm1" FT /locus_tag="azo0453" FT /product="probable composite transport ATP-binding permase FT protein" FT /function="ABC-type transport system involved in Fe-S FT cluster assembly permease and ATPase components" FT /note="Probable composite transport ATP-binding permease FT protein. Homology to amt1 of S. cereviciae of 48% FT (sprot|ATM1_YEAST). COULD BE INVOLVED IN THE TRANSPORT OF FT yet unknow substrates (probable HEME) FROM THE MITOCHONDRIA FT TO THE CYTOSOL. InterPro: ABC transporter transmembrane FT region (IPR001140), ATP/GTP-binding site motif A (P loop) FT (IPR001687), ABC transporter (IPR003439),AAA_ATPase FT sperfamily (IPR003593) Pfam: ATP transporter,ABC FT transporter transmembrane region no signal peptide probable FT 6 TMHs" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2L5" FT /db_xref="InterPro:IPR001140" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR011527" FT /db_xref="InterPro:IPR017871" FT /db_xref="InterPro:IPR017940" FT /db_xref="UniProtKB/TrEMBL:A1K2L5" FT /protein_id="CAL93070.1" FT /translation="MRRAPAPLPAPASGERHDWQTLKSLVPFIWAYKGRVIFALGCLLA FT AKGANVTVPIIFKHLVDALTITPQQALIVVPAALLLAYGVLRFSTSLFTELREIVFARV FT TQQAVREISLRVFRHLHALSLRFHLERQTGGLTRDIERGTRSIGSLISYTLYSILPTLV FT EIGLVVGILLVQYDAVFALITLGTLAFYIVFTVKVTNWRTALRRQANELDSAANARAID FT SLLNFETVKYFNNEAFEARRYDEQLKQWTRAQVRNQYSLSALNIGQAAIIAVGVTAMMW FT AAASRVAAGSMTLGDIVLVNAFLIQLYIPLNFLGVIYRELRQALTDIERMFGLMHEHRE FT IADRPDARVLPPGPASVRFERVGFAYDAKRPILFEVDFEIPAGRTVAVVGHSGSGKSTL FT ARLLYRFYDVQSGAIRVNGHDVRDLTQDSLRAAIGIVPQDTVLFNDTLFYNIQYGRPDA FT SRDEVEAAARAAQLEDFIRRLPDGYETRVGERGLKLSGGEKQRVAIARALLKNPAILIF FT DEATSALDSRTEKAIQAQIERAASGRTALVIAHRLSTVMDADEIIVLDQGRIAERGHHL FT DLLAQEGLYTQMWLLQQQEAERAEAAT" FT CDS complement(485487..486122) FT /transl_table=11 FT /locus_tag="azo0454" FT /product="conserved hypothetical threonine efflux protein" FT /function="Putative threonine efflux protein" FT /note="Conserved hypothetical threonine efflux protein. FT Homology to rsc0148 of R. solanaxearum of 52% FT (trembl|Q8Y2B8). InterPro: Lysine exporter protein FT (LYSE/YGGA) (IPR001123) Pfam: LysE type translocator FT Tigrfam: 2A76: Homoserine/Threonine efflux protein signal FT peptide Probable 6 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2L6" FT /db_xref="InterPro:IPR001123" FT /db_xref="UniProtKB/TrEMBL:A1K2L6" FT /protein_id="CAL93071.1" FT /translation="MPSFDTLAAFLAISVAITFAPGPDNLMVLGHSLARGRLAGFGIAL FT GCALGCFTHTLWAALGVSAALASSPQVFLALKLAGAAYLAWLGVQALRFAAAPRLDGVA FT ATRAPWLRDVRRGFVANAINPKVALFFLAFLPQFVSADGGHATLQMVALGSLFAVQTVL FT VFGGFALAAGTLGRAIARRPAAGAWLDRIAGLIFIGLALRLATDDHTL" FT CDS 486445..487725 FT /transl_table=11 FT /locus_tag="azo0455" FT /product="putative cobalmin snthesis protein" FT /function="Putative GTPases (G3E family)" FT /note="This family of proteins contains P47K, a Pseudomonas FT chlororaphis protein needed for nitrile hydratase FT expression, and the cobW gene product, which may be FT involved in cobalamin biosynthesis in Pseudomonas FT denitrificans [1]. TREMBL:Q8YJP6: 40% identity, 54% FT similarity. Pfam:PF02492; Cobalmine synthesis protein; pfkB FT family carbohydrate kinase; FAD binding domain. FT TIGRFAM:proC: pyrroline 5 carboxylate reductase. mobB: FT molybdopterin-guanine dinucleotide" FT /note="Family membership" FT /db_xref="InterPro:IPR003495" FT /db_xref="InterPro:IPR011629" FT /db_xref="UniProtKB/TrEMBL:A1K2L7" FT /protein_id="CAL93072.1" FT /translation="MKGRGQSVGPGSFRVYWQAASRAGLPPSSRPVRTEGKGRYRSWTA FT RPYHSLLTSPHHAVPMTPDTPDRRIPVTVLTGFLGAGKTTLLNHLLRQPGMEGCAVLIN FT EFGEVGVDHHLVEKVDETLIVLDSGCICCSVQGDLVKALKGLFMRALRREIPALRRVLI FT ETTGLADPAPVIFTLMEEPFIAERYRCDGVVTAVDATHADGQLDRQREAVRQVAMADRL FT LITKCDLADAAVRAGLSVRLAQLNPAAQQIEVVRGEVAPDALFGCGLYDAAGKIPDVAA FT WLGEERARAAAARAAAAAPAWRKPGAAPRHGAAARHDEGIASHVLVFDAPLTWYGFSDA FT LGVILQAYGDRILRVKGLMNIAGDPLPRVVQCVQHVAYPPASLPAWPTRPPYDDRRSRL FT VFIVRDLPRSELEQIFFGVAGVPVMPQ" FT CDS 487845..488045 FT /transl_table=11 FT /locus_tag="azo0456" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. signal peptide. no TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K2L8" FT /protein_id="CAL93073.1" FT /translation="MNATQIKALVAGAAAALALTATAVQAADAPAGDATAPAVTKKHTA FT KKTTHKKTSHKKAAAKPADAQ" FT CDS 488198..488884 FT /transl_table=11 FT /gene="ragA" FT /locus_tag="azo0457" FT /product="two-component response regulator" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="Response regulator," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2L9" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K2L9" FT /protein_id="CAL93074.1" FT /translation="MKILLVEDDAQQAGYIRKGLQEAGHTVDVAADGRDGLFLATTASF FT DAIVLDRMLPRVDGLTVLRTLRASRIATPVVVLSALGEVDDRVAGLRAGSDDYLVKPFA FT LSELLARLDALQRRGNGRAEAEQTRLQTADLEMDLLRRSVSRGATRIELKPKEFRLLEF FT LLRHSGQVVTRSMLLEAVWDYHFDPQTNVIDVHISNLRAKIDLPGLPPLIHTVRGAGYR FT LGGDAA" FT CDS 488874..490262 FT /transl_table=11 FT /gene="ragB" FT /locus_tag="azo0458" FT /product="putative two component sensor kinase" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.13.1" FT /note="Putative sensor kinase," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2M0" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="UniProtKB/TrEMBL:A1K2M0" FT /protein_id="CAL93075.1" FT /translation="MPRERAGGLRAWFASPFHRFAVALPAAIALIVGALFYPLFIEAEA FT HIREEVQAAIEFEIAGLEAHFHERGLAGLRDALQRRIEISPDRAAVYLLADRDGRPLAG FT NLAQWPAGVSANDEAWFHVAEADGETLEGRVFILFGGERLLVGRRSPLEAFQRNMTVRL FT WWSAALIILVAGVIGGRFMQHLHRRLARLAAEAGRIQEGHLAQRLSLSARGDELDALAE FT RFNSAFDEIERLVDAAKHVSSAIAHDMRRPLIALRNAIDEARRSPGADPALRTQLEGLR FT DQTEELLRTFSALLSLARIEAGALGPLLQAVNLTEIARDAIDLYEPLAASQGRALNPRL FT APACVRGDRDLLFQVLQNLIENALKHGAGDIDIGIDTLPDGGARLTVRDHGEAVAAADL FT PHLFERFFRADSSRSAAEGAGIGLALVRGIAEAHGGSIRATDARPGLCVEILLAPGRRG FT VEKS" FT CDS 490448..491650 FT /transl_table=11 FT /gene="amtD" FT /locus_tag="azo0459" FT /product="probable ammonia permease" FT /function="Ammonia permease" FT /note="Putative ammonium transporter MJ1343. A number of FT evolutionarily-related proteins have been found to be FT involved in the transport of ammonium ions across FT membranes.Represent a family of high affinity ammonium FT transporters. These proteins are highly hydrophobic and FT seem to contain from 10 to 12 transmembrane domain. FT TREMBL:Q88L29: 73% identity, 84% similarity InterPro: FT Ammonium transporter family InterPro: IPR001905; FT Ammonium_transpt. IPR010256; RH_like_transpt. Pfam: FT PF00909; Ammonium_transp; 1. PROSITE: PS01219; FT AMMONIUM_TRANSP amt: ammonium transporter Non secretory FT protein with signal peptide probability of 0.174 (SignalP FT predicted) TMHMM predicted 11 TMH's" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2M1" FT /db_xref="InterPro:IPR001905" FT /db_xref="InterPro:IPR018047" FT /db_xref="InterPro:IPR024041" FT /db_xref="UniProtKB/TrEMBL:A1K2M1" FT /protein_id="CAL93076.1" FT /translation="MELHHPDNDVLFILLGAIMVLAMHAGFAFLELGTVRKKNQVNALV FT KILSDFSVSALAYFFIGYGVAYGIHFFSGAEVLLERSGFELTRFFFLLTFAAAIPAIIS FT GGIAERARFGPQLIATFVLVGLVYPFFEGIAWNQHFGFQAWLKDSFGAEFHDFAGSVVV FT HAVGGWIALPAVLLLGARRGRYHSNGAIAAHPPSSIPFLALGAWILIIGWFGFNVMSAQ FT TLEKISGLVAINSLMAMVGGTLAALALGRNDPGFAHNGPLAGLVAVCAGSDVMHPLGAL FT AVGAVAGALFVQMFTLTQNRWKIDDVLGVWPLHGLCGAWGGIAAGIFGSTALGGAGGVA FT FLPQLAGTVLGVAIAAGGGFAVYGALKLLVGLRLDPEAEFEGADLSIHKISATAERETA FT W" FT CDS complement(491666..492280) FT /transl_table=11 FT /gene="dnr" FT /locus_tag="azo0460" FT /product="putative Dnr-like transcriptional activator" FT /function="cAMP-binding proteins - catabolite gene FT activator and regulatory subunit of cAMP-dependent protein FT kinases" FT /note="Putative Dnr-like transcriptional activator. Similar FT to SWISSPROT: sprot|FIXK_RHIME (28% Rhizobium meliloti, FT FixK) InterPro: IPR000595 cNMP_binding. IPR001808 HTH_Crp. FT Pfam: PF00027 cNMP_binding. HTH reporting nucleic acid FT binding motif." FT /note="Family membership" FT /db_xref="GOA:A1K2M2" FT /db_xref="InterPro:IPR000595" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014710" FT /db_xref="InterPro:IPR018490" FT /db_xref="UniProtKB/TrEMBL:A1K2M2" FT /protein_id="CAL93077.1" FT /translation="MDIPTAPDWPQRPAFEAMPPALRAAARRRAFRRGETLFATGAAPR FT EMFFILRGEVRLSRLSPDGTETVMQRARDAFLAEASLESHTYHCSAIAGEDGLALVFPL FT AEFRRSLADSAAFRAQWMSHLLQEVRKRRAQCERLALRSARARILHYIEAEGADGELHL FT PGSRKALAAELGLTHEALYRALARLTRDGTLEVGADFIRRR" FT CDS 492369..492854 FT /transl_table=11 FT /locus_tag="azo0461" FT /product="hypothetical secreted protein" FT /note="Hypthetical secreted protein. No homology to the FT data bank. No domains predicted. No TMHs. Has signal FT peptide." FT /db_xref="GOA:A1K2M3" FT /db_xref="InterPro:IPR010980" FT /db_xref="UniProtKB/TrEMBL:A1K2M3" FT /protein_id="CAL93078.1" FT /translation="MRRHLPLLLLLVLPLAAPAQHDPAMHGGHHHAAGAAEVPDTREWV FT RFPPAMTAHTLANMRDHLLALQQIQSALGEARYDDAAEIAEQRLGLSALRSHGAAESSR FT FMPAGMQEAGTAMHRSASRFGLAARDAAATGDLAPALKSLAQVTAACVSCHAAYRLQ" FT CDS complement(492897..495704) FT /transl_table=11 FT /locus_tag="azo0462" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT an orf of Trichodesmium erythraeum of 45% FT (gi|48892210|ref|ZP_00325608.1|(NBCI ENTREZ)). No domains FT predicted. Signal peptide present. No TMH present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR011042" FT /db_xref="InterPro:IPR015943" FT /db_xref="UniProtKB/TrEMBL:A1K2M4" FT /protein_id="CAL93079.1" FT /translation="MLPTRRLSCRVARRASAVAVSLALAALAGGAGAAPQFEPLGAYAT FT GLAHLESSGETAALRGDRLYVTNAKDVSLDIVDVADPTAPRLLKRVDLRAWGAGVNSVA FT VSSKNLIAVALQAQKKTDPGTIVFLTPDGTVKRSATVGALPDMVTFTHDGRRLLVANEG FT EPDCYGAGCTDPEGTVSIIDVVPMKPELEVRTVSFAGVPLPAGVRIFGPGASAAQDLEP FT EYITVGEDDRTAYVTLQENNAIAVIDIDKARVTEVRALGYKDFNAAPQLSIHELKDLPL FT VGTTAAGQSIALGGFSGLHFEGRGADGKLHFITHTDRGPNGEPTGINRPFLLPDFTPRL FT VRLTLDPATGAVELGEQILLRRGDGTPLTGLPNTALSGDTNAAYNDEVPVDLRGKVLPL FT DPLGGDFEGIAVDTDGSFWLADEYRPAIYHFDPSGRLLDRFVPVGTAAAAGKAAGTFGT FT EALPAVLAQRRQNRGFEAIVLQGGKLYAFVQSPLRNPAGLANSALNAMKNVRVVEFDPV FT TRATRQFIYIMDNPAATGADDTRADKIGDAAALPGGGFLVVERDDDARPDDALATITKK FT VYAFSLTGATDISTKDTLYTVGGVSKSLDQMTANELSSVGVKPVAKVLHVDLASAGYNA FT VQKVEGLAVIDADTIALINDNDFGVAQINIDAAAGSYTLAPGYTPEPVQLGILRTGGLD FT ASDKDNVVNIRNWPLRGMYQPDAIASYTVGGQRYLVTANEGDARDYPGFAEEARAKSLK FT ASYPNLPEVADDLQLGRLTVTSVPPAGGVPYVFGTRSFSIWNATTGAQVWDSGSELEVR FT TAAAFPKHFNSNNDENNFDNRSDNKGPEPEGVAVGTIGNNTYAFVGLERIGGVMVYDVT FT RPAAPAFVQYLHSRNFAGSAVGPDSGPEIVRFIAAKDSPTGKPMVVVANEISGTVNLWG FT LGAED" FT CDS 495962..498433 FT /transl_table=11 FT /gene="fadE" FT /locus_tag="azo0463" FT /product="probable acyl-CoA dehydrogenase" FT /function="Acyl-CoA dehydrogenases" FT /EC_number="1.3.99.3" FT /note="Probable acyl-CoA dehydrogenase. Homology to fadE of FT E. coli of 55% (trembl|Q8KTJ8(SRS)) Catalyzes the FT dehydrogenation of acyl-CoA (By similarity). Reaction: FT acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced FT acceptor. InterPro: Acyl-CoA dehydrogenase (IPR006089) FT Pfam: Acyl-CoA dehydrogenase, N-terminal domain; Acyl-CoA FT dehydrogenase, C-terminal domain signal peptide 2 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2M5" FT /db_xref="InterPro:IPR006090" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR006092" FT /db_xref="InterPro:IPR009075" FT /db_xref="InterPro:IPR009100" FT /db_xref="InterPro:IPR013786" FT /db_xref="InterPro:IPR015396" FT /db_xref="UniProtKB/TrEMBL:A1K2M5" FT /protein_id="CAL93080.1" FT /translation="MVWWILLGLPPLLVALAYRRVPPVASALAVLAWLAALAWAGGWPP FT MLAVGALLALGVALALLLVAPLRRRVVTAPVFAAFRRALPAMSQTERDALEAGTVWWEG FT ELFRGDPDWRRFAGFPWPRLSAAEQAFLDDDTEALCRLVKDWDTTRLQDMPAPVWQFIK FT ERGFLGLIIPAEYGGKGFSAYAHSQVITKLSTRSSAPAVTVMVPNSLGPAELLLHYGTP FT AQKQHYLPRLAQGLEIPAFALTSPWAGSDAASIPDAGVVCTGQWQGREVLGMRVSFDKR FT YITLAPVCTVFGLAFRLYDPDHLLGDTVDLGITCALVPREHPGVEIGRRHVPLNAVWMN FT GPIRGKDVFMPLDFIIGGPQMAGQGWRMLMECLAAGRSISLPGSNAGMQQLTARAVGAY FT ARVRHQFKTAIGRFEGVEEALTRIGANTYLSDAARVMTAGAIDLGEKPAVVSAIVKYHV FT TERARQTVNDGMDVIGGKGICLGPQNFLGRAYQQVPVGITVEGANILTRSLILFGQGAI FT RCHPHVLDEMHAAGRGDLTAFDRAFWGHIGYTLGNAARALVTGLTGSHVVAVPIDVAPE FT TRRYYQQLTRFSAAFAFIADISMGTMGGALKRKEKLSARLGDILSLLYLATAVLKRYEA FT EGRQAEDAPLMHWAIWDCMFRAQNAFEGVIANFPNPVLATLLRRLVFPLGRPYVVPSDA FT LGHAVADRLIAPSATRDRLTAAVHLPADLDEPLGALEAALAATIAAEPVEAKVKAAQRE FT GRFAPGALVAGGVDALWARAHADGIIDNAEFALLQRRAELRDKVIRVDDFPFDLAAETG FT SEAAPKMRVVA" FT CDS 498430..499902 FT /transl_table=11 FT /gene="fadA1" FT /locus_tag="azo0464" FT /product="probable 3-ketoacyl-CoA thiolase" FT /function="Acetyl-CoA acetyltransferase" FT /EC_number="2.3.1.16" FT /note="subunit of fatty acid oxidation complex, FT 3-keto-acyl-coa-thiolase. Activity:-acyl-CoA + acetyl-CoA = FT CoA + 3-oxoacyl-CoA Entry name TREMBL:Q8G967 Prim. FT accession # Q8G967 Identities = 284/425 (66%) InterPro FT IPR002155; Thiolase. Pfam PF02803; Thiolase_C; 1. PF00108; FT Thiolase_N; 1. Number of predicted TMHs: 0 Prediction: FT Non-secretory protein Signal peptide probability: 0.000" FT /note="Family membership" FT /db_xref="GOA:A1K2M6" FT /db_xref="InterPro:IPR002155" FT /db_xref="InterPro:IPR016038" FT /db_xref="InterPro:IPR016039" FT /db_xref="InterPro:IPR020610" FT /db_xref="InterPro:IPR020613" FT /db_xref="InterPro:IPR020616" FT /db_xref="InterPro:IPR020617" FT /db_xref="UniProtKB/TrEMBL:A1K2M6" FT /protein_id="CAL93081.1" FT /translation="MSTRARPPEAGASSLGEDVAQRQEGGGMSTRARPPEAGAPSLGED FT VAQRQEDGGVSMNAMPEARDVYIIDGARTPFLKARNAPGPFAAADLATAAGSALLLRQS FT FAPDALDEVILGCASPSPDEVNIGRVVALRMGCGPRVPGWTVMRNCASGMQALDSACAN FT IRGGRADLVLAGGVDALSRAPLLFSDAMVRWLAGWYAAKGAGQKLAALRHFRPAYLAPV FT IGIVRGLTDPYVGQMMGQTAENLAWQFRISREEMDVYAAESHRRAIAAHDGGRFADELA FT PLVGRDGTVYAADDGVRRDSTPAALARLKPFFDKRYGRVTAGNSSQVSDGAAWLLLASA FT AAVERHGLQPLGRIVDSAWAALPPEHMGLGPVHAAMPLLARHQLATRDLAAWEINEAFA FT AQLIACLRALDDDGYCQDHFGLPAPGAPDPARLNVDGGAVALGHPVGASGARIVLHLLH FT VLRREGVAGARGIASLCVGGGQGGAMLVEAMA" FT CDS 499899..501935 FT /transl_table=11 FT /gene="fadB1" FT /locus_tag="azo0465" FT /product="probable enoyl-CoA hydratase / 3-hydroxyacyl-CoA FT dehydrogenase" FT /function="3-hydroxyacyl-CoA dehydrogenase" FT /EC_number="5.1.2.3" FT /note="alpha-subunit of fatty acid oxidation complex. Entry FT name TREMBL:Q8G968 Prim. accession # Q8G968 Identities = FT 373/642 (58%) InterPro IPR006108; 3HCDH_C. IPR006176; FT 3HCDH_N. Prediction: Non-secretory protein Signal peptide FT probability: 0.000 Number of predicted TMHs: 0 IPR008927; FT 6DGDH_C_like. IPR001753; EnCoA_hydrtse. Pfam PF00725; FT 3HCDH; 1. PF02737; 3HCDH_N; 1. PF00378; ECH; 1." FT /note="Family membership" FT /db_xref="GOA:A1K2M7" FT /db_xref="InterPro:IPR001753" FT /db_xref="InterPro:IPR006108" FT /db_xref="InterPro:IPR006176" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K2M7" FT /protein_id="CAL93082.1" FT /translation="MNAVADLARSDWHHWRIERSPDAILWLWLDRAGASANTLSAAVLD FT EFEVVLAALEANLPAALVIASAKPAGFVAGADIEEFSALPDPHAARALVERGWRLFDRL FT AALRCPTLALIRGHCMGGGLELALACRYRLVVDEPATRLALPEVMLGIVPAWGGMRRLP FT ALIGPVAALDMMLTGRSLDARRARRIGLADDCVPPRVMENAARVLVSSGQRPALPGLLA FT RLLNGPLKPLVAARAQRQTAARVSRAHYPAPFAIIDIWARHGGNALAVPAGDPASLETI FT FASPTAHNLARVFFLRERLKGFGKQAAFAPRQVHVVGAGIMGGDIAAVCALAGLRVTLQ FT DQGVDRIAPAIARAARLFERRLRGDARAQRLALDRLIPDPQGRGVAAADLVIEAISENL FT DAKRALFADLEARARPDALLATNTSSLRLADIAAGMRTPARLVGIHFFNPVAKMPLVEV FT VSAAATAAEDAARAAAFVRLLDKLALPVRDVPGFLVNAALAPYMLEALRCVEEGVAPAV FT VDAALTRFGMAMGPVELVDTVGLDVALAAGKALAAGAEVPPQLAARVAEGKLGRKTGEG FT YYRWAPQPGGEARIVGRAPVEAVPEGLAERVLAPLLAAVRHSVAEGVVADADLADAGLI FT FGAGFAPWTGGPLHHAQGRDFRIGASAAKQQTGPAPTTQQVSR" FT CDS 501932..502336 FT /transl_table=11 FT /locus_tag="azo0466" FT /product="conserved hypothetical acyl-CoA thioesterase" FT /EC_number="3.1.2.-" FT /note="Conserved hypothetical acyl-CoA thioesterase. FT Homology to an orf of Azoarcus sp. EbN1 (trembl|Q8G9D6). FT Pfam: cytosolic long-chain acyl-CoA thioesterase Long-chain FT acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and FT palmitate, they also catalyse the hydrolysis of other long FT chain fatty acyl-CoA thioesters. Interpro: Thioesterase FT superfamily (IPR006683) no signal peptide no. TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2M8" FT /db_xref="InterPro:IPR006683" FT /db_xref="UniProtKB/TrEMBL:A1K2M8" FT /protein_id="CAL93083.1" FT /translation="MTPPVENISLPDDKFLTLRVVPMPGDLNPSGDVFGGWIMSMVDIA FT GAIPANRRAKSRVATVAVNSFVFKQPVSVGDLVSFYARVVATGRTSVTVDVEVYAERGH FT ANPFVVKVTEAKLTYVAMDEKGGKRPIPAE" FT CDS 502438..503721 FT /transl_table=11 FT /gene="fadL" FT /locus_tag="azo0467" FT /product="probable long-chain fatty acid transport protein" FT /function="Long-chain fatty acid transport protein" FT /note="Long-chain fatty acid transport protein precursor FT (Outer membrane fadL protein) (Outer membrane flp protein). FT Involved in translocation of long-chain fatty acids across FT the outer membrane. FadL may form a specific channel (By FT similarity). Entry name:- Q8G9D7 Primary accession number:- FT Q8G9D7 InterPro:- IPR005017; Toluene_X. Pfam:- PF03349; FT Toluene_X; 1. identity:- 66% Prediction: Signal peptide FT Signal peptide probability: 1.0 Number of predicted TMHs: FT 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2M9" FT /db_xref="InterPro:IPR005017" FT /db_xref="InterPro:IPR011250" FT /db_xref="UniProtKB/TrEMBL:A1K2M9" FT /protein_id="CAL93084.1" FT /translation="MQTTTLTRVAAALALAAGPAPAFAAGFQLLEQNASGIANAYAGSA FT AVAEDASTIFFNPAGMTALRERELSVGLAAVRPRFEFSDRGSTATGALGGDGGDAGSWA FT YLPNAYVSWALRPDLYVGVGLGAPFGLITEYDDNWVGAAHSVSFDIKTYNINPSIAWRI FT NERVSVGGGLSWQRMEVEYERVAAVLPAPLPLSSTRAILDADSDAWGWNVGALITLSPA FT TRLGLSYRSAIKHTLEGDLKVKGAAAGLSPALSSGKAKADVELPDTFILSAVHRLDERW FT ELLGDISWTGWSKIDKVDIVRDSGPLSGVTVQTLDTDFRDTWRVALGAGYRLNAAWKLK FT AGLAWDQSPVKDRAHRLVSLPDNDRTWFAAGAQWMPGGGARVDLGLAYLYVPKTKIDND FT QAALGRGRVTGEYDSSVWILGAQYSVAF" FT CDS 503770..506154 FT /transl_table=11 FT /gene="fadB2" FT /locus_tag="azo0468" FT /product="probable 3-hydroxyacyl-CoA dehydrogenase / FT enoyl-CoA hydratase" FT /function="3-hydroxyacyl-CoA dehydrogenase" FT /EC_number="4.2.1.17" FT /note="Short-chain enoyl-CoA hydratase activity . FT Activity:- 3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA FT + H2O Entry name TREMBL:Q8P986 Prim. accession # Q8P986 FT InterPro IPR006108; 3HCDH_C. IPR006176; 3HCDH_N. IPR008927; FT 6DGDH_C_like. IPR001753; EnCoA_hydrtse. IPR000205; NAD_BS. FT Pfam PF00725; 3HCDH; 1. PF02737; 3HCDH_N; 1. PF00378; ECH; FT 1. Identities = 468/796 (58%) Prediction: Signal peptide FT Signal peptide probability: 0.980 Number of predicted TMHs: FT 0" FT /note="Family membership" FT /db_xref="GOA:A1K2N0" FT /db_xref="InterPro:IPR001753" FT /db_xref="InterPro:IPR006108" FT /db_xref="InterPro:IPR006176" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K2N0" FT /protein_id="CAL93085.1" FT /translation="MLIRKVAVLGAGVMGAQIAAHCANAGLQVILFDLPAPAGPPDTVV FT EKAIAGLAKLDPAPLASRALAAAITPANYASDLARLGECELVIEAIAEKMAWKLDLYAK FT VAPHLAPGAVFASNTSGLSIARLAEGLPAALRPRFCGVHFFNPPRYMALVELIPAPDTD FT PALLDALEGWLTTRLGKRIVRARDTPNFIANRIGVFSVLAVMHHTTRLGLAFDEVDAIT FT GPRIGRPKSATYRTADLVGLDTLAHVVGTMQDGLPDDPWHGHFALPGWLDTLIANGALG FT QKTQAGIYRKEGRQILVFEPAQLDYRAAAGEVAVEVAEILALRDPAEKLAGLAACAHPQ FT AQLLWSSFRDVFHYCAYHLEHIADNARDVDSAMRWGFGWAQGPFETWQAAGWAEVAAAI FT REDIAAGRAMSDAPLPDWVFERDGVHAAGGSWSPAAAALQPRPALPVYGRQLQAERLVG FT EAPPERGETLWECGERGDGVRLWRLPALDAGIGVLSFKSKMHTVGGAVLEGVLEAVARA FT QRDLDGLVLWQPAPFSVGANLQQVGEACSAGEFARLEQTVARFQQAALALRHAQVPVVA FT AVEGMALAGGCEFLMHCAHRVLALESYVGLVEAGVGLIPAGGGSKQFALQAHRLAQRAA FT GGDVFPFIQRSFETIAKATVAKSAHEAVQLGFAAPGDDIVLHAQEVLYVALRRARALAE FT AGWHPPLPERAVVVAGRNGIATCELMLVNMAEGGFISAHDYKVAKAAATALCGGEVDTN FT ARVSEQWILDVERALFVELLQTEATQQRIAHMLRTGKPLRN" FT CDS 506636..507868 FT /transl_table=11 FT /gene="fadA2" FT /locus_tag="azo0469" FT /product="probable 3-ketoacyl-CoA thiolase" FT /function="Acetyl-CoA acetyltransferase" FT /EC_number="2.3.1.16" FT /note="Activity:- acyl-CoA + acetyl-CoA = CoA + FT 3-oxoacyl-CoA Entry name:- SWISSPROT:THIK_ECOLI Prim. FT accession # P21151 InterPro:- IPR002155; Thiolase. Pfam:- FT PF02803; Thiolase_C; 1. PF00108; Thiolase_N; 1. Identities FT = 177/400 (44%) Number of predicted TMHs: 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2N1" FT /db_xref="InterPro:IPR002155" FT /db_xref="InterPro:IPR016038" FT /db_xref="InterPro:IPR016039" FT /db_xref="InterPro:IPR020610" FT /db_xref="InterPro:IPR020613" FT /db_xref="InterPro:IPR020615" FT /db_xref="InterPro:IPR020616" FT /db_xref="InterPro:IPR020617" FT /db_xref="UniProtKB/TrEMBL:A1K2N1" FT /protein_id="CAL93086.1" FT /translation="MRGTERHEENRHMSTQIQDAYIVAAVRTPVAKRNGAFRHVRPDDM FT LAHVLRAVVAQVPALDAGEIGDVITGCAMPEAEQGMNVARIGLLLAGLPERVPGVTLNR FT FCASSLQAVADAANRIRLGEADVMIAAGTESMSAMPQIMGNKVSLNPEIFARQENIDIA FT YGMGLTAEKVAEEWKVSRADQDAFALQSHQRASAAIADGSFGDEIAPYTVRSHLPGEGG FT TVRIAERIVDTDEGPRADATLEALARLKPVFAARGSVTAGNSSQMSDGAGAVLLMSETA FT LQRYGVTPLARFRSYAVAGVPPRVMGIGPVEAIPRALRLAGLGLDALDRIELNEAFAAQ FT ALAVIRTLGLDPARVNPQGGAIALGHPLGATGAIRTATLMRAMRQGGVRHGMITMCVGT FT GMGAAAIFERV" FT CDS 507945..508745 FT /transl_table=11 FT /gene="paaG2" FT /locus_tag="azo0470" FT /product="putative enoyl-CoA hydratase" FT /function="Enoyl-CoA hydratase/carnithine racemase" FT /EC_number="4.2.1.17" FT /note="Function:- COULD POSSIBLY OXIDIZES FATTY ACIDS USING FT SPECIFIC COMPONENTS (BY SIMILARITY). CATALYTIC FT ACTIVITY:-(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA FT + H(2)O. Entry name SWISSPROT:PAAG_ECOLI Prim. accession # FT P77467 InterPro:- IPR001753; EnCoA_hydrtse. Pfam:-PF00378; FT ECH; 1. Identities = 92/265 (34%) Prediction: Non-secretory FT protein Signal peptide probability: 0.000 Number of FT predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K2N2" FT /db_xref="InterPro:IPR001753" FT /db_xref="UniProtKB/TrEMBL:A1K2N2" FT /protein_id="CAL93087.1" FT /translation="MADTVLLDVADGVATLTLNRPDVLNVLSVAMMQDLAEAVRALAAR FT KDVAVVVITGAGAHFMAGGDLKDFSEHLHLSSEARLATFRAMIAQHINPTVETLQGLPQ FT PVIAKVRGACAGFGLSLMLGCDFALCADNSVFTTAYSAIGLPGDGGASYFLPRLVGRRK FT AAELLLLAERFDTAEALRLGLINRAVPEAELDAVTDQFVARLKAGPRHAYAEIKRLLAG FT SHDNQLESQLQNEAEAFGRCGATADFAEGVTAFLGKRKPGFKGV" FT CDS complement(508774..509625) FT /transl_table=11 FT /locus_tag="azo0471" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT cv1508 of C. violaceum of 37% (trembl|Q7NXW8). Pfam: FT uncharacterized ACR, COG1434. no signal peptide. 2 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR003848" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:A1K2N3" FT /protein_id="CAL93088.1" FT /translation="MGAGTLRNCADNTGPTLARQIPMTFDFALLLFWLKKLVAAFVLPP FT LLPLVLGAAGLLLLRRRRRLGLALAWSGIAAGLLLSTPASVSRMLVPLEPTAVVDMEAA FT RGAQAIVILGGGRRSHAAEYGGDTVNRLTLERLRYGARLARATGLPLLVSGGAPSGDVP FT EATLMAAALREDFGIAPRWEEGGSFDTRDNARLSAAMLRADGVTRVVLVTHAAHMRRAE FT AEFALHGLAVVPAPTAWLGPGPERADDDDEVWPSLPSQGTAYAGWYALHEWMGLLAYRL FT SR" FT CDS 509624..510913 FT /transl_table=11 FT /locus_tag="azo0472" FT /product="probable O-acetylhomoserine FT aminocarboxypropyltransferase" FT /function="O-acetylhomoserine sulfhydrylase" FT /EC_number="2.5.1.49" FT /note="Probable O-acetylhomoserine FT aminocarboxypropyltransferase. Homology to cysD of A. FT nidulans of 54% (sprot|CYSD_EMENI). Transforms FT O-acetylhomoserine into homocysteine. InterPro: Cys/Met FT metabolism pyridoxal-phosphate-dependent enzymes FT (IPR000277) Pfam: Cys/Met metabolism PLP-dependent enzymes FT no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2N4" FT /db_xref="InterPro:IPR000277" FT /db_xref="InterPro:IPR006235" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:A1K2N4" FT /protein_id="CAL93089.1" FT /translation="MPDHRFGIESLCLHAGQQPDAETGARAVPIYQTTSFVFDSPEHAA FT ELFNLQTFGNVYSRISNPTVAVFEERMAALEGGRAALATSSGLAAQMTALLTLAQAGDE FT IVAARTLYGGSYSQLDVSLRRLGISTVFVDPSDPENFRAAITDRTKAVYGEIIGNPSLN FT VFDVAAVAAITRAAGVPLVIDSTLASPYLCRPLEHGADIVIHSATKYIGGHGTTMGGVL FT VESGTFPWDNGRFPQMVEPSPGYHGVRFYETFGNFGFTMKARMETLRTFGQALSPFNAF FT MLLQGLETLHVRMDRHVANARAVADFLAAHPAVAWVNYPGLAASPEHALAQRYFPKGPG FT AILSFGIRGGQPAGERFIEALQMISHLANVGDAKTLVIHPASTTHRQLSEEEQRAAGVP FT PDMVRLSVGIETLDDILWDLDQALARGAAA" FT CDS 510910..511497 FT /transl_table=11 FT /locus_tag="azo0473" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No good homology to FT the data bank. No domains predicted. 1 TMHs No signal FT peptide present." FT /db_xref="InterPro:IPR021244" FT /db_xref="UniProtKB/TrEMBL:A1K2N5" FT /protein_id="CAL93090.1" FT /translation="MSLRLLLGIAIALLLVYGGWQLLRAVRGGWRAGRADRPAPQRLAP FT VTDDDAPDDDEDDGGFDYAPLPAAAERTPAPVATPAAGPAPVRSPPPAGPDAFQLELEL FT QRLRREVADLRAALDVQQQEIGGLHDSLRTLREQLESGLAGQNASPEYSEALVFARRGL FT PVEAIAERCGITVAEAELVRALAARSDDGAAR" FT CDS 511494..512357 FT /transl_table=11 FT /locus_tag="azo0474" FT /product="peptidoglycan-binding protein" FT /function="Might bind murein" FT /note="Exported protein with sporulation related repeat. FT Pfam: Sporulation related repeat. InterPro: Proline-rich FT region" FT /note="Function unclear" FT /db_xref="InterPro:IPR007730" FT /db_xref="UniProtKB/TrEMBL:A1K2N6" FT /protein_id="CAL93091.1" FT /translation="MSEDTRAGRNAALLRAGIAVAAALALLVGLLVVEDGRDPAADLTA FT AAVQPAAVPGAAAQPAPPAQADTDKAAAAVALPPISAPAATVPAPAATAPGATAPGATA FT PGATAPGATAPAATAPAATAPAATAPAAAAEAAATPAPPTAAAPTSASLPSPAEPAGAA FT VSPQPAAAAIAGVAARTLPEAPASAPVTPPGAPRPPAVPAVPPVPAVVAAPVKDGYLLQ FT LGVFGNPVNASALQAELAAKGLPARVESRVVLGPFPDRKSMEAAQRQLQRAHRQEGIVV FT PPRGGR" FT CDS 512441..512881 FT /transl_table=11 FT /locus_tag="azo0475" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein, 35% identity to FT TrEMBL;Q8ENH9 Has PF02623, Uncharacterized BCR, COG1699; FT IPR003775, DUF180 :This entry describes proteins of unknown FT function." FT /note="Function unclear" FT /db_xref="GOA:A1K2N7" FT /db_xref="InterPro:IPR003775" FT /db_xref="InterPro:IPR024046" FT /db_xref="UniProtKB/Swiss-Prot:A1K2N7" FT /protein_id="CAL93092.1" FT /translation="MKIESPVFGSAEVSDDKVIEFPAGLPGFEHCKRFVLVHEEGSDTA FT VFLLQSVDDADVAFSITGPEQLGINYEFALSDEEVATLGLASPAEALVAVIVRKDGEAG FT SPASTGLRANFMAPLVINVEGRRGLQKVINRLGCDIVLRERA" FT CDS 512981..513361 FT /transl_table=11 FT /locus_tag="azo0476" FT /product="conserved hypothetical endoribonuclease L-PSP" FT /function="Putative translation initiation inhibitor yjgF FT family" FT /note="Conserved hypothetical endoribonuclase L-PSP. FT Homology to orf1 of A. vineladii of 74% FT (sprot|YVN1_AZOVI(SRS)) This protein was described FT initially as an inhibitor of protein synthesis intiation FT but is now viewed as an endoribonuclease active on FT single-stranded mRNA. The cleavage of mRNA is responsible FT for the inhibition of protein synthesis. A role in purine FT regulation has also been suggested. Tigrfam: FT Endoribonuclease L-PSP, putative Pfam: Endoribonuclease FT L-PSP (=YipgF family) no TMHs weak indication for signal FT peptide" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR006056" FT /db_xref="InterPro:IPR006175" FT /db_xref="InterPro:IPR013813" FT /db_xref="UniProtKB/TrEMBL:A1K2N8" FT /protein_id="CAL93093.1" FT /translation="MSRSIVSTPNAPAAIGTYSQAVKAGGTVYLSGQIGLDPATMQLVD FT GFEAQTVRVFENLKAVAEAAGGSLADVVKLTIYLTDLANFAKVNEIMARYFAEPYPARA FT AVGVKELPKGAVVEADAILVLG" FT CDS 513369..515408 FT /transl_table=11 FT /gene="recG" FT /locus_tag="azo0477" FT /product="ATP-dependent DNA helicase" FT /function="RecG-like helicase" FT /EC_number="3.6.1.-" FT /note="ATP-dependent DNA helicase recG (EC 3.6.1.-). FT Critical role in recombination and DNA repair. Help process FT Holliday junction intermediates to mature products by FT catalyzing branch migration. Has a DNA unwinding activity FT characteristic of a DNA helicase with a 3 to 5 polarity. FT recG unwind branched duplex DNA (Y-DNA). Has a role in FT constitutive stable DNA replication (csdR) and R-loop FT formation (By similarity). InterPro: ATP-dependent DNA FT helicase RecG recG: ATP-dependent DNA helicase RecG" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2N9" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR004609" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR014001" FT /db_xref="InterPro:IPR016027" FT /db_xref="UniProtKB/TrEMBL:A1K2N9" FT /protein_id="CAL93094.1" FT /translation="MQSGWAGLGEQLASRLRKLDLHRQEDLVVHLPLRYEDETRLTPIG FT VARAGFPAQIEGEVTSCEVVLRPRRQLVARVRDDSGTLVARWINFYPSQQKQLAVGRRV FT RLFGEVRGGFFGDEMVHPRVRNIDPGEGLPEALTPVYPTTAGLGQTTLRKLIDRALKTV FT PLQDLLPEDARRALDLPGFAEALTALHHPAPDADPIALENREHPAWRRIKFEELLVQQL FT SLRRAYNARRAREAVVLPARQQLTAGLVRGLPFALTSAQQRAVGEIAADLGAAHPMQRL FT LQGDVGSGKTIVAALAMLQAAENGWQAALMAPTEILAEQHYKKLAAWLEPLGVGIAWLS FT GSRRKREREAELARLQSGEVLLAVGTHALIEDEVALPRLALAIIDEQHRFGVRQRLALR FT EKGAHGLRPHMLMMSATPIPRTLAMTHYADLDVSVLDELPPGRTPIRTKLVSDARREEV FT VGRVRDACLQGRQAYWVCPLIEESEALQLQTALDTYAALSEALPELRVGLVHGRLKADE FT KSATMAAFSAGELQVLVATTVIEVGVDVPNASLMVIEHAERFGLAQLHQLRGRVGRGTA FT ESVCILLFAQPLSENGRARLKVIYEHTDGFAIAREDLQLRGPGEFVGARQSGVPLLRYA FT DLELDAGLIEPARALAERMLRDAPAQADALMQRWLGGRESLLRA" FT CDS 515463..516032 FT /transl_table=11 FT /gene="ubiC" FT /locus_tag="azo0478" FT /product="putative chorismate:pyruvate lyase" FT /function="4-hydroxybenzoate synthetase (chorismate lyase)" FT /EC_number="4.1.3.-" FT /note="Chorismate:pyruvate lyase (EC 4.-.-.-). catalytic FT activity: chorismate = 4-hydroxybenzoate + pyruvate. FT pathway: ubiquinone biosynthesis; first step." FT /note="Specificity unclear" FT /db_xref="GOA:A1K2P0" FT /db_xref="InterPro:IPR007440" FT /db_xref="UniProtKB/Swiss-Prot:A1K2P0" FT /protein_id="CAL93095.1" FT /translation="MQHPASGESWLARPPRTAERRLRPWLTDPASLTARIRMRCGMFGV FT RVLRQSAGALTPDERRLLGLRAGERALLREVLLIADGRPVVFARSVLAQREQRGGWLRL FT WRGIGSRPLGAALFSDPRIRRQPLACARIGAADARYHLARRALAGAATLPPALWARRSV FT FRLHGRSLLVSEFFLPAILGLPDDPL" FT CDS 516019..516882 FT /transl_table=11 FT /gene="ubiA" FT /locus_tag="azo0479" FT /product="4-hydroxybenzoate octaprenyltransferase" FT /function="4-hydroxybenzoate polyprenyltransferase and FT related prenyltransferases" FT /EC_number="2.5.1.-" FT /note="4-hydroxybenzoate octaprenyltransferase (EC 2.5.1.-) FT (4-HB polyprenyltransferase). Synthesis of FT 3-octaprenyl-4-hydroxybenzoate. InterPro: UbiA FT prenyltransferase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2P1" FT /db_xref="InterPro:IPR000537" FT /db_xref="InterPro:IPR006370" FT /db_xref="UniProtKB/Swiss-Prot:A1K2P1" FT /protein_id="CAL93096.1" FT /translation="MTLSDRLPLYGRLMRLDKPIGSLLLLWPTLWALWLAADGKPPLHV FT LVIFTIGTVLMRSAGCVINDYADRDFDGHVERTRNRPLATRAVSTREALALAAGLSALS FT FVLILPLDPLVIWLSFPALFLAASYPFTKRFFAIPQAYLGIAFGFGIPMGFAAVQGEVP FT PIAWVMLLANIFWAVAYDTEYAMVDRPDDLKIGIKTSAITFGRFDVAAVMLCYAVALGL FT LGWVGAQAGRGALYFAGLAVAAGMALYHYTLIRHRERAPCFKAFRHNNWLGAAVFAGLA FT LDYLIG" FT CDS complement(516980..520849) FT /transl_table=11 FT /locus_tag="azo0480" FT /product="conserved hypothetical iron-sulfur binding FT oxidase" FT /function="FAD/FMN-containing dehydrogenases" FT /note="Conserved hypothetical irons-sulfur binding oxidase. FT Homology to cv4235 of C. violaceum of 70% (trembl|Q7NQA5) FT Pfam: FAD binding domain; FAD linked oxidase, Cterminal FT domain Tigrfam: glcD: glycolate oxidase subunit GlcD no FT signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2P2" FT /db_xref="InterPro:IPR004017" FT /db_xref="InterPro:IPR004113" FT /db_xref="InterPro:IPR006094" FT /db_xref="InterPro:IPR009051" FT /db_xref="InterPro:IPR012285" FT /db_xref="InterPro:IPR016164" FT /db_xref="InterPro:IPR016166" FT /db_xref="InterPro:IPR016167" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="InterPro:IPR021817" FT /db_xref="InterPro:IPR022153" FT /db_xref="UniProtKB/TrEMBL:A1K2P2" FT /protein_id="CAL93097.1" FT /translation="MTQRLREIPYNYTSFSDREIVIRLLGAEAWSVLDELRSERITGRS FT ARMLYEVLGDIWVVRRNPYLEDDLLASRERREALVGALNHRVSEVEKRRQGNDRVALLI FT GRAREAVADFERWFDDSARKRKAVLKSLGRLTRRDNICFDGHARVSHVTDATDWRVEYP FT FVVLYPDTEEEMAPLVRACIELGMTIIPRGGGTGYTGGAVPLDANSVVINTEKLLAMSA FT VEDIPLPDADGKPMAAPYATIRTGAGVVTDRVSEAASAAGRVFAVDPTSASASCIGGNI FT AMNAGGKKAVLWGTALDNLAWWKMVTPDGNWLEVERLDHNFGKIHEQETVRFRLRRFDG FT ISYKPLGEEILAMPGAACRKDGLGKDVTDKFLGGVPGVQKEGTDGLIVAARWVLHKMPP FT VTRTVCLEFFGQVREAVPAIVEITDYFKPGGAGNAAGVLLAGLEHLDERYVKAVGYTTK FT AKRHGRPKMVLIGDIVGHDENAVMAAASEVVRMTNVRGAEGFIAVSPEQRKRFWLERSR FT TAAISRHTNAFKVNEDVVIPLPRMGDYCDGIERINIELSIQNKLELCDTLAGFLRGELP FT LDQGDANLASEELIGDRREAALNYVEAVRLRWEWLLENLDLPLAEAESRFAAYGIVAGE FT LSNRAANPRLFHRLQDYSIRVSWKTELKPRLDKIFDGVVFRPVLARIAELHKQVLRGRV FT FVALHMHAGDGNVHTNIPVNSDHYEMLQTANRAVDRIMALARSLDGVISGEHGIGITKL FT DYLTDAEMANFWAYKQKVDPEGRFNRGKLMKGGNLDNAYTPSFNLMGHESLIMEQTEIG FT EIAHDIKDCLRCGKCKPVCSTHVPRANLLYSPRNKILSTSLLVEAMLYEEQTRRGVSLA FT HWAEFEDVADHCTVCHKCEKPCPVDIDFGDVSIKMRNLLRKQGKKSFNPGKAAAMAFLT FT VKDPATIKLIRTGMLEWGFKAQRFAHKVGKSLGLVQPQVKAPPATLGKAPIKAQVIHLI FT NKPMPGKLPKRTSRALLDIEDDKVIPVIRDPQKVNGDSEAVFYFPGCGSERLFSQVGLA FT TQAMLYHVGAQTVLPPGYLCCGYPQTSAGEDDKGQKITTDNRVLFHRVANTLNYLDIKT FT VIVSCGTCMDQLQKYEFEKIFPGCRLLDIHEYLMEKGVKLEGIQGVNYMYHEPCHTPMK FT VHSGIKVANALMGTRVDLNDRCCGESGTLAVARPDISTQVRFRKQEEIEKGVAKLRESQ FT PTAPTKILTSCPACLQGLHRYADDAGGVEPDYIVVEIAKHLLGDNWMPDYVAKANSGGI FT ERVLL" FT CDS complement(520972..521325) FT /transl_table=11 FT /locus_tag="azo0481" FT /product="conserved hypothetical protein" FT /function="Putative translation initiation inhibitor yjgF FT family" FT /db_xref="InterPro:IPR006175" FT /db_xref="InterPro:IPR013813" FT /db_xref="InterPro:IPR019897" FT /db_xref="UniProtKB/TrEMBL:A1K2P3" FT /protein_id="CAL93098.1" FT /translation="MQPIVRKGVTARYADAVIHNQTVYLVEVPSSTGGDVTTQAGEIFA FT SLERQLMDAGSSKARILMATVYLTDMADYDAMNAAWEAWLPPGEAPSRACVRVAGLAQA FT GWRIEIALTAAVA" FT CDS complement(521370..521783) FT /transl_table=11 FT /locus_tag="azo0482" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT yqaA of Nitrosomonas europaea of 50% (trembl|Q82TH7(SRS)) FT No domains predicted. Signal peptide present. TMHMM2 FT reporting presence of 2 TMH's." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K2P4" FT /protein_id="CAL93099.1" FT /translation="MELIAAAEPATTLGALFISALLAATVLPGGSEAAFAALLLASPQL FT LWPALAAATLGNTLGGTSTYLLGRLLPRKEVPPRLALVRRYGSLSLLLSWVPLIGDALC FT AGAGLLRLPWLPCLLWMAIGKGARYAAIAWLLG" FT CDS 521919..522353 FT /transl_table=11 FT /locus_tag="azo0483" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT PA4874 of P.aeruginosa of 36% (trembl|Q9HUT9(SRS)) No FT domains predicted. Signal petide present. No TMH present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR011690" FT /db_xref="UniProtKB/TrEMBL:A1K2P5" FT /protein_id="CAL93100.1" FT /translation="MKKLLSAFALAVSCTAMLPAEAQANPQHERMRRCSQEAKEQTLKG FT DERKAFMSTCLKGKHDTGAETATAPAKPAAKAAAAKPAAEKSAADKTSTAKPAAADKVA FT EADAAPVAQRSKMKTCNQSATEQSLKGDARKAFMSECLKG" FT CDS complement(522433..523299) FT /transl_table=11 FT /locus_tag="azo0484" FT /product="FHA domain containing protein" FT /function="Adenylate cyclase family 3 (some proteins FT contain HAMP domain)" FT /note="FHA domain containing protein. Best similarity to FT SWISSPROT: sprot|REPB_AGRRH (9% Agrobacterium FT rhizogenes,possible replication protein b) Pfam: PF00211 FT Adenylate and Guanylate cyclase catalytic domain. SMART: FT SM00240 FHA Forkhead associated domain." FT /db_xref="GOA:A1K2P6" FT /db_xref="InterPro:IPR000253" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR008984" FT /db_xref="UniProtKB/TrEMBL:A1K2P6" FT /protein_id="CAL93101.1" FT /translation="MSDRRNLCLLVAEVLGHDRLVGRLGATEAGHAVERCLNRIDRAIE FT GNGGTIVARADGHVDVVFERCDAAVLASCEMLERVLSLPPVSGTRLTMRIGLHYGAAEG FT DSASGEGFDVARRLASLSRPGQALASGAAVMLLSASTRHFAGTEAIHDADLDKLEWPVY FT AIGQRVGLVTSVPPSARVSQRLRLRHQQEILFVEEQRPVLLLGRELGNDVVIIDARASR FT QHARIERRREGFILIDQSTNGSFVSIDGVGERCVKDDEIVLSGPGRIGCGFSANEIERD FT LVFFDIV" FT CDS complement(523396..524316) FT /transl_table=11 FT /locus_tag="azo0485" FT /product="conserved hypothetical protein" FT /note="Homology to hypothetical protein ydaO. InterPro: FT Uncharacterized protein family UPF0021" FT /db_xref="GOA:A1K2P7" FT /db_xref="InterPro:IPR011063" FT /db_xref="InterPro:IPR012089" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/Swiss-Prot:A1K2P7" FT /protein_id="CAL93102.1" FT /translation="MPAVAPSAAESRHSNTFLRLKKKLERGVGEAIADYNMIGDGDTVM FT VCVSGGKDSYTLLSCLLALRERAPVDFRIVAMNLDQKQPGFPDDVLPAYFESIGVEYRI FT VTEDTYSIVKDKIPEGKTTCSLCSRLRRGIIYRTAKEIGATRIALGHHRDDMLETLFLN FT MFFGGKIKAMPPKLVSDDGQHVVIRPLAYCTENDIERFARGMDFPIIPCNLCGSQENAQ FT RKQIKTMLQGWARDYPGRIESLATSLRNVVPSHLSDSALFDFVGLTRDTRVGEGDTVFD FT PPELPAAAAPITLRRADDDGDRSAT" FT CDS complement(524389..525135) FT /transl_table=11 FT /locus_tag="azo0486" FT /product="conserved hypothetical short-chain dehydrogenase" FT /note="Conserved hypothetical short-chain dehydrogenase. FT Homology to cv4132 of C. violaceum of 60% (trembl:Q7NQK5). FT Pfam: short-chain dehydorgenase (PF00106). no signal FT peptide. no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2P8" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K2P8" FT /protein_id="CAL93103.1" FT /translation="MDTAEAPVILVTGAARRVGAEIARLVHASGARVIVHHRRSAAEAE FT TLAAGLNALRPGSAAVVAGDLAADGEPARVAAAALDCFGRIDGLVNNASSFFPTALGTI FT DETAWSDLVGSNLKGPLFLSQALAAELTRRAGSIVNIVDIHAERPLKGYLLYCTAKAGL FT VGLTRALAVELAPAVRVNGVAPGPIVWPEDTQFDAEARAQIVRHTLLQREGAPADIARA FT VRFLLVDAPYVTGQILAVDGGRSAHL" FT CDS 525247..526419 FT /transl_table=11 FT /locus_tag="azo0487" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical protein. Homology to NE1166 FT of N.europaea of 49% (tremble:Q82VC8) Has FT PF02636,Uncharacterized ACR, COG1565;IPR003788 ,DUF185; FT This family contains several uncharacterised proteins. FT Q8YI87 has been described as an ATP synthase beta subunit FT transcription termination factor rho protein. No signal FT peptide. No TMHs." FT /db_xref="InterPro:IPR003788" FT /db_xref="UniProtKB/TrEMBL:A1K2P9" FT /protein_id="CAL93104.1" FT /translation="MSSLPEPSADALDQSARLVALLHAEIAAAGGWLSFARYMEITLYA FT PGLGYYSGGARKFGPGGDFITAPELTPLFGQALASQVEQVMRASAPAVIEVGAGTGLLA FT TDLLLELERRGCLPDSYGILELSGELRERQFDTLASQAPHLAGRVRWLESLPESFSGAV FT VANEVLDVMPVHLVVARAEGLFERGVAVVQREDGPALQWADVPAAGAVREAALALQLPT FT PSSGEYVTEINLAGGAWVAAWAERLRQGAMLLIDYGYPRAEYYLPSRSGGTLLCYYRHH FT AHGDPFLWPGLNDITAFVDFTAVAEAAFGAGLDVTGYTTQAQFLFNCGVLECLARRGPE FT ERPEYIRAARAVQRLTAPQEMGELFKVLAVSRGLSEPLLGFARGDRLHAL" FT CDS complement(526459..526677) FT /transl_table=11 FT /locus_tag="azo0488" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ebA3372 FT of Azoarcus sp. EbN1 of 47% (gnl|keqq|eba:ebA3372(KEGG)). FT No domains predicted. No signal peptide. No TMHs." FT /db_xref="UniProtKB/TrEMBL:A1K2Q0" FT /protein_id="CAL93105.1" FT /translation="MVIVMEMNSGKALTEPPAYGEEILNASWLPQPTPEVAVQLQEIEL FT APRRRHDSMPPPADIEAFLAAIYRNQE" FT CDS 526664..526792 FT /transl_table=11 FT /locus_tag="azo0489" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. No TMHs. Signal peptide FT present." FT /db_xref="UniProtKB/TrEMBL:A1K2Q1" FT /protein_id="CAL93106.1" FT /translation="MTITMMASAVLVDVLSPCLLNGRAAADLSGRRIQGKSRVALR" FT CDS complement(526887..527693) FT /transl_table=11 FT /locus_tag="azo0490" FT /product="putative acetone-cyanohydrin lyase" FT /function="predicted hydrolases or acyltransferases FT (alpha/beta hydrolase superfamily)" FT /EC_number="1.11.1.10" FT /note="TREMBL:Q8F3A6: 43% identity, 60% similarity Non-heme FT chloroperoxidase (EC 1.11.1.10) (Chloride peroxidase) FT (CPO-P) (Chloroperoxidase P). CHLORINATES AND BROMINATES FT SUITABLE ORGANIC COMPOUNDS. INVOLVED IN THE BIOSYNTHESIS OF FT THE ANTIBIOTIC PYRROLNITRIN. InterPro: Alpha/beta hydrolase FT fold InterPro:IPR000073; A/b_hydrolase. IPR003089: FT AB_hydrolase. IPR000379: Ser_estrs. Pfam:PF00561; FT Abhydrolase_1; 1 TIGRFAM:dsbE: periplasmic protein FT thiol:disulf" FT /note="Family membership" FT /db_xref="GOA:A1K2Q2" FT /db_xref="UniProtKB/TrEMBL:A1K2Q2" FT /protein_id="CAL93107.1" FT /translation="MNSTRFGELEVICHAPAGTPAFETPLLFIHGAYVGAWCWEEYFLP FT WFARHGWAAYALSLSGHGGSRRRDRLDAYSIADYVADVVEVAGKLPAPPILIGHSMGGM FT VVQKYLERHRVPAAVLMSSVPPQGLMGSALGLMMSHPHLLNDLNRILGGSEVDIASLRE FT ALFHQPVDEATLERYYRLSQPESHRAIWDMTLFNLPTPLLMHRPPLQVLGAQHDVLIPP FT DQVHMTAATYGTTATIFGGMGHGLMLEQDWEQVARHMHAWLEPFGG" FT CDS complement(527690..528310) FT /transl_table=11 FT /gene="isoJ" FT /locus_tag="azo0491" FT /product="probable glutathione S-transferase" FT /function="Glutathione S-transferase" FT /EC_number="2.5.1.18" FT /note="Probable glutathione S-transferase. Homology to isoJ FT of Rhodococcus sp AD45 of 48% (trembl|Q9RBP3). Catalysis of FT the reaction: R-X + glutathione = H-X + R-S-glutathione. R FT may be an aliphatic, aromatic or heterocyclic group; X may FT be a sulfate, nitrile or halide group. Pfam: Glutathione FT S-transferase, N-terminal domain; Glutathione FT S-transferase, C-terminal domain no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Q3" FT /db_xref="InterPro:IPR004045" FT /db_xref="InterPro:IPR004046" FT /db_xref="InterPro:IPR010987" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR017933" FT /db_xref="UniProtKB/TrEMBL:A1K2Q3" FT /protein_id="CAL93108.1" FT /translation="MITLYTWGTPNGRKISIALEELGLDYTVRPIDITRGEQHEAGFVA FT LSPNNKIPVLVDDEGPGGAPITLIESGAILIYLAEKHGQLLSAEPRERLETLQWLMLQM FT GSIGPMLGQAHHFLRFAPDVIPYAIDRYSKEAVRLYGVLNTRLAGRDWLAGAAYSIADI FT ATWPWIDRHKWQGIDLARYPEVKRWYETIAARPAVQRGMEVPR" FT CDS 528392..528589 FT /transl_table=11 FT /locus_tag="azo0492" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT BH1226 of Bacillus halodurans of 40% (pir|B83803) no FT domains predicted. signal peptide. 1 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR021320" FT /db_xref="UniProtKB/TrEMBL:A1K2Q4" FT /protein_id="CAL93109.1" FT /translation="MLKWFVVVVIVVLVSGLIQPGLARRLRLGYLPGDVAIRVRGRSYR FT FPFATTLLLSLLAWLLLRAL" FT CDS complement(528605..529843) FT /transl_table=11 FT /gene="cca1" FT /locus_tag="azo0493" FT /product="tRNA-nucleotidyltransferase" FT /function="tRNA nucleotidyltransferase/poly(A) polymerase" FT /EC_number="2.7.7.25" FT /note="tRNA nucleotidyltransferase (EC 2.7.7.25) (tRNA FT adenylyltransferase) (tRNA CCA-pyrophosphorylase) FT (CCA-adding enzyme). This enzyme carries out synthesis of FT the tRNA CCA terminus without the direction of a template FT using the multiple accepting and donating subsites within FT its active site. HDIG: uncharacterized domain HDIG" FT /note="Family membership" FT /db_xref="GOA:A1K2Q5" FT /db_xref="InterPro:IPR002646" FT /db_xref="InterPro:IPR003607" FT /db_xref="InterPro:IPR006674" FT /db_xref="InterPro:IPR012006" FT /db_xref="UniProtKB/Swiss-Prot:A1K2Q5" FT /protein_id="CAL93110.1" FT /translation="MRTYVVGGAVRDALLGLPVKDRDWVVVGATPDEMLARGFRPVGKD FT FPVFLHPQTQEEHALARTERKTGRGYAGFAFHTAPDVTLEEDLARRDLTINAIARDADG FT TLIDPYGGVADLHGRVFRHVSPAFAEDPVRILRVARFAARFADFSVAPETLALMRAMVD FT NGEVDHLVAERVWQEFARGLMEAHPARMIRVLRDCGALARLLPELDRLFGVPQPAQHHP FT EIDTGEHVLMVVEQAAARAHSLPVRWATLLHDLGKGETPAAILPHHYGHEARSADLARQ FT VSERLKAPVDCRDLAVMVAREHGILAQAAVLRAETMVKVLERCDALRRPERFALMLEAA FT ACDHLGRGGERPENWAPAAQWQAALAAVRSVEAGAIARACADKAQVPQRIHAARVAAVK FT ALRAHPPPAEGIS" FT CDS complement(529843..530487) FT /transl_table=11 FT /gene="sspA1" FT /locus_tag="azo0494" FT /product="putative stringent starvation protein A" FT /function="Glutathione S-transferase" FT /note="Putative stringent starvation protein A. Homology to FT sspA of E. coli of 26% (sprot|SSPA_ECOLI). FORMS AN FT EQUIMOLAR COMPLEX WITH THE RNA POLYMERASE HOLOENZYME (RNAP) FT BUT NOT WITH THE CORE ENZYME. IT IS SYNTHESIZED FT PREDOMINANTLY WHEN CELLS ARE EXPOSED TO AMINO ACID FT STARVATION AT WHICH TIME IT ACCOUNTS FOR OVER 50% OF THE FT TOTAL PROTEIN SYNTHESIZED. InterPro: Glutathione FT S-transferase N terminus (IPR001045) Pfam: Glutathione FT S-transferase, N-terminal domaine no signal peptide no FT TMHs" FT /note="Family membership" FT /db_xref="InterPro:IPR004045" FT /db_xref="InterPro:IPR010987" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:A1K2Q6" FT /protein_id="CAL93111.1" FT /translation="MKLIIGNKNYSSWSLRAWLAARAGGFAFEEIRIPLFLPGSREHIL FT SHSPSGKVPCLIDRGLAVWDSLAICEYLAEQAPQLWPADPAARAVARAVSAEMHSGFQN FT LRQRMGMNIRKDYAGHGRSAEVDADIARITAIWNDCRARFGADGPYLFGRFSVADAMYA FT PVCFRFKTYGIAPEGAAGAYLATMLAHPDMRAWQAGALAETEAIPGEDLYG" FT CDS complement(530568..531536) FT /transl_table=11 FT /locus_tag="azo0495" FT /product="putative NADH dehydrogenase" FT /function="NADH dehydrogenase" FT /EC_number="1.6.5.3" FT /note="33%" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2Q7" FT /db_xref="InterPro:IPR001509" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K2Q7" FT /protein_id="CAL93112.1" FT /translation="MKSTRVVLIGGSGFVGSVIANRLSAAAIDLCIPTRRPARAAHLLP FT LPTAQILEADVHDPVTLARLLEGADAVVNLVGILHSRPGSPYGRDFARAHVELPRKLVS FT ACRSAGVRQLIHISALGANPDGPSEYQRSKAAGEAEIHAAGDDVMWTVLRPSVIFGRAD FT RFLNLFADLARTLPVLPLAGARTRFQPVYVEDVAEVVWRCLGDPACARETFEVAGPTVY FT TLRELVEYVSALAGHPRPVIALPEGVAMLQARLMSLLPQPLISPDNIRSMRVDNVASGA FT PLPFGLRPTAVEEAAPEWIAPRVSPRAHFDEFRRRASRPRG" FT CDS complement(531552..533480) FT /transl_table=11 FT /gene="sltY" FT /locus_tag="azo0496" FT /product="putative soulbe lytic murein transglycosylase" FT /function="Soluble lytic murein transglycosylase and FT related regulatory proteins (some contain LysM/invasin FT domains)" FT /EC_number="3.2.1.-" FT /note="Putative soluble lytic murein transglycosylase. FT Homology to slt of E. coli of 24% (sprot|SLT_ECOLI). FT Murein-degrading enzyme. Catalyzes the cleavage of the FT glycosidic bonds between N-acetylmuramic acid and FT N-acetylglucosamine residues in peptidoglycan. May play a FT role in recycling of muropeptides during cell elongation FT and/or cell division. InterPro: SLT domain (IPR000189) FT Pfam: Transglycosylase SLT domain singal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Q8" FT /db_xref="InterPro:IPR008258" FT /db_xref="InterPro:IPR008939" FT /db_xref="InterPro:IPR012289" FT /db_xref="InterPro:IPR016026" FT /db_xref="InterPro:IPR023346" FT /db_xref="UniProtKB/TrEMBL:A1K2Q8" FT /protein_id="CAL93113.1" FT /translation="MKQFLWGALAAALMWFSGAAGAQTAKSGDERILAARDAIRNGDRA FT ALEWLAASTENHVLNPYVRYWLLFNKLARPEPPPAAELSDFLLREAGSMLADRLRGDWL FT RRMAKDGDWAGFVALYPDLVAPDAELRCLGWTARLMTGDRAVLDEVARQWMDLVDSHAA FT CETSLRATLSAGLVGEDEVWWRIRRQVEGKNPAQARTTLTWLPATSAPLPGALEQALNA FT PAPYLDRLPPNFAITRAGRELALAALVRLARDDLSGAYSRLIRLQDRLETGERAYAYAA FT LALRAAFAQQPDAVAWFQAAGNVLLTAEQRAWRVRVALRASDWSAVRHAIAALPPAEQN FT EPEWIYWLGRAHAAAGQRAEAEALYARIADQSGFYGLLAAEELGRPFAPPLKGGAITAA FT DLRQAESDLGLQRALALFRLDMRTEGVREWNWSLRNQTEAFTLAAARIALDAGIYDRAI FT NTAERGNPNGNFEMRFLTPYRQLIEPQVRGQGLDLSWVYGLMRQESRFVVPARSSSGAQ FT GLMQVMPATGKWVAAKIGMRGYHPGLLSDPDTNVQLGTSYMRMILEDLDNHPVLASAGY FT NAGPSRAKRWRDAKPLEGAIYAETIPFDETRDYVKKVMTNTVIYAAMLEGRPQSLKTRL FT GTIAARN" FT CDS 533521..534114 FT /transl_table=11 FT /locus_tag="azo0497" FT /function="5-formyltetrahydrofolate cyclo-ligase" FT /EC_number="6.3.3.2" FT /note="5-formyltetrahydrofolate cyclo-ligase InterPro: FT 5-formyltetrahydrofolate cyclo-ligase" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2Q9" FT /db_xref="InterPro:IPR002698" FT /db_xref="InterPro:IPR024185" FT /db_xref="UniProtKB/TrEMBL:A1K2Q9" FT /protein_id="CAL93114.1" FT /translation="MTGSDSPQPDAVAALRRAAREGAIAAREALPPARRAALTLHIERH FT LDALLAQLAPRVLAFCWPYRAEPDLRAWVGRWLAADPRRVAALPVVLDKGAPLAFRRWT FT ADVAMALDRHGIPYPAVDDPVRPELALVPLNAFDAAGFRLGYGGGYFDRTLAQLDLVAV FT GVGFECGRVATVHPQPHDLPMRWIVTEGGIHAAA" FT CDS complement(534121..536826) FT /transl_table=11 FT /locus_tag="azo0498" FT /product="GGDEF/PAS/PAC-domain containing protein" FT /function="FOG: PAS/PAC domain" FT /note="GGDEF/PAS/PAC-domain containing protein. Similarity FT to SWISSPROT: sprot|Y4LL_RHISN (13% Rhizobium sp. (strain FT NGR234), hypothetical 91.8 kda protein y4ll) / TREMBL: FT trembl|Q55955 (14% Synechocystis sp. (strain PCC FT 6803),sll0779) Pfam: PF00990 GGDEF domain. PF00989 PAS. FT PF00785 PAC. TIGRFAM: TIGR00254 putative diguanylate FT cyclase (GGDEF) domain. TIGR00229 PAS domain S-box. TMHMM FT reporting 2 transmembrane helices." FT /db_xref="GOA:A1K2R0" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR013655" FT /db_xref="InterPro:IPR013656" FT /db_xref="InterPro:IPR013767" FT /db_xref="UniProtKB/TrEMBL:A1K2R0" FT /protein_id="CAL93115.1" FT /translation="MDRSSVTAAPAVGAAGRRRQHLADAGFVGFIALCIVVAWYSLHYH FT GQRLEQETLAARAQVADLDTQHLASHLSLTLRGVDLTLQTLLETGPPVDAVYTWNGLLR FT EALRNSPQLRSLSLLDGTGTVIASSNPANLGQHPSLARFLPQAAPFAPTLRLGPPQGGR FT DLADAAPISAEEAPPPLYFVPLLRGLHTPDGDGVYLLAALNMDFFTNGGALPVRGATDH FT LEVINFEGQRVLDDDAPRTPEMRAADLALVERWKAGDEHGVVHLDTADGATYSVAYRLP FT RNLPLGVVARFNHAEALSGARAERARQERYLLPAVGLSLGGTLFGYFLFRRAGRRERLA FT REAAESALRASEERYRLTMGAVRDGMWEWHVDTGALCWDARCFEQLGFPPDGFELDIER FT WKARIHPEDHARLSPMMDEMATSPEGFRIEFRMPDIQGEWHWLEARGKVVEWRGDAPLR FT VVGTQTDIHVRKTGEIRLRLLEAALNAAANAVVITNANAVIEWVNPAFAALSGYNQDDA FT IGRTPRELINSGAQSGEYYAALWNTILAGDVWRGELINRRRDGQLYHEALTITPMRDEN FT GTLDHFIAVKEDISARKAAEAELEATHARLQAVVDNFPGAVLFEDADGTITLANQMLCS FT LLGIDERASALVGRPSVELVADAAPNFTDAAAFVARIRDLRAAARPVHGEELETLGGRW FT LERDFLPVRSGDTLLGFLRLYRDVTERKHHEQALQRLATLDPLTGTWNRRAFLERAEHE FT RLRYLRSEHPASLVMLDLDHFKRVNDTWGHAAGDAVLCHFVRVLQQRLRATDLLGRLGG FT EEFALLLVDTTPEGAAELTERLRAAIAEHPLPLGDRTISITVSAGIAPFVQDDQNVEAA FT LARADAALYRAKARGRNQVVLADDECGTAR" FT CDS complement(536846..537652) FT /transl_table=11 FT /gene="pheC" FT /locus_tag="azo0499" FT /product="putative cyclohexadienyl dehydratase" FT /function="ABC-type amino acid transport/signal FT transduction systems periplasmic component/domain" FT /EC_number="4.2.1.91" FT /note="Putative cyclohexadienyl dehydratase precursor. FT Homology to pheC of P. aeruginosa of 36% (sprot|PHEC_PSEAE) FT FORMS ALTERNATIVE PATHWAY FOR PHENYLALANINE BIOSYNTHESIS. FT CAN CATALYZE TWO REACTIONS: PREPHENATE DEHYDRATASE AND FT AROGENATE DEHYDRATASE. MAY HAVE A ROLE IN CHEMOTAXIS OR FT TRANSPORT. InterPro: Bacterial extracellular solute-binding FT proteins family 3 (IPR001638), solute-binding FT protein/glutamate receptor (IPR001311) Pfam: Bacterial FT extracellular solute-binding proteins signal peptide no FT TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K2R1" FT /db_xref="InterPro:IPR001638" FT /db_xref="UniProtKB/TrEMBL:A1K2R1" FT /protein_id="CAL93116.1" FT /translation="MASLARLALGLLVSLTLLYTTLYAQPAQSHLDRILAERVLKVCVW FT PDYYGISFRNPRTQELAGIDVDLARELARDLDVRLEFVDSSFANLIGDVLGDRCDVAMF FT AIGITAQRAEKLRFTSPHLASDIYAITTRTNRRIRSWDDIDQPGVIVAVAKGTLHEPVM FT RDKLRHAQLQVLASPHAREQEVESGRADVFMTDFPYSRRMLDNADWARLVAPSTRYHVT FT PYAWAIAPGDDRWHQRLEAFLATIRDDGRLMAAARRHGLDPIIVNR" FT CDS complement(537808..539328) FT /transl_table=11 FT /gene="ilvA" FT /locus_tag="azo0500" FT /product="probable threonine dehydratase" FT /function="Threonine dehydratase" FT /EC_number="4.3.1.19" FT /note="Probable Threonine dehydratase(EC 4.3.1.19) FT (Threonine deaminase, Threonine ammonia-lyase). Homology to FT ilv1 of A. adeninovorans of 52% (sprot|THDH_ARXAD). FT Catalyzes the formation of alpha-ketobutyrate from FT threonine in a two-step reaction. The first step is a FT dehydration of threonine followed by rehydration and FT liberation of ammonia. InterPro: FT Pyridoxal-5-phosphate-dependent enzymes beta family FT (IPR001926),Serine/Threonine dehydratase FT pyridoxal-hposphate attachment site (IPR000634), C-terminal FT domain of threonine dehydratase (IPR001721) Pfam: FT Pyridoxal-phosphate dependent enzyme, C-terminal doman of FT threonin dehydratase no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2R2" FT /db_xref="InterPro:IPR000634" FT /db_xref="InterPro:IPR001721" FT /db_xref="InterPro:IPR001926" FT /db_xref="InterPro:IPR005787" FT /db_xref="UniProtKB/TrEMBL:A1K2R2" FT /protein_id="CAL93117.1" FT /translation="MTSASPDYLERILNAQVYDLAVETPLDLATNLSARSGNRIYLKRE FT DMQPVFSFKLRGAYNKMANLSPQALQRGVICASAGNHAQGVALSAQKLGVRAVIVMPTT FT TPQIKIDAVRSRGGEVVLAGESYSDAYAHALELEKAEKLTFVHPYDDPDVIAGQGTIGM FT EILRAHAKPIHAIFCAVGGGGLIAGVAAYVKRLRPETRIIGVESEGAAAMTESLARGER FT VSLEQVALFADGTAVKQVGGETFRLCQQYVDEMIVVDNDAICAAIKDVFEDTRSILEPS FT GALAVAGAKEYARRHQLSDRSLVAVASGANMNFDRLRFVAERAELGEQREAVLAVTIPE FT QPGSFRKFINILGNRDITEFNYRYADSERAHIFVGVTVRSRDEATRLVEMLGQHDLPAL FT DLTDDELAKSHVRYMVGGRAPQVANELVYRFVFPERPGALLNFLSNLRSDWNISLFHYR FT NHGADFGRVLVGMQVPPQDIDAFEAFLQRLGYEYAAETENPAYRLFLA" FT CDS complement(539453..540394) FT /transl_table=11 FT /gene="hprK" FT /locus_tag="azo0501" FT /product="probable Hpr serine kinase/phosphatase" FT /function="Serine kinase of the HPr protein regulates FT carbohydrate metabolism" FT /EC_number="3.1.3.3" FT /note="Probable Hpr kinase/phosphorylase, Hpr_kinase. Pfam: FT PF02603; Hpr_kinase. TIGRFAM:TIGR00679; hpr-ser." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2R3" FT /db_xref="InterPro:IPR003755" FT /db_xref="InterPro:IPR011104" FT /db_xref="InterPro:IPR011126" FT /db_xref="UniProtKB/Swiss-Prot:A1K2R3" FT /protein_id="CAL93118.1" FT /translation="MRQTSVARLYEDQGPRLQLTHVSGPLDAVLSVAEERMWPADLVGH FT LNLIHPTRLQVLGAAELEWARRQSREKVAHHLNGILSARPPAIIVADGCETPNIVHGVC FT TAHNVALFSTPHPSASVIDQLRLYLSRQLAEKISLHGVFMDVLGIGVFITGNSGAGKSE FT LALELISRGHGLVADDIVEFSRTAPTVLEGRCPELLKDFIEVRGLGILNIRTIFGETAC FT RRKMRLRLVCHLERRQPGQDDPNRLPVQQEQQVILGVSTPRVTLPVAAGRNLAVLLEAA FT VRSTILQLRGVDSTQEFIDRQSRMLMGDGDGL" FT CDS complement(540363..540848) FT /transl_table=11 FT /gene="ptsN" FT /locus_tag="azo0502" FT /product="protein-Npi-phosphohistidine-sugar FT phosphotransferase" FT /function="Phosphotransferase system FT mannitol/fructose-specific IIA domain (Ntr-type)" FT /EC_number="2.7.1.69" FT /note="Probable nitrogen regulatory IIA protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2R4" FT /db_xref="InterPro:IPR002178" FT /db_xref="InterPro:IPR006320" FT /db_xref="InterPro:IPR016152" FT /db_xref="UniProtKB/TrEMBL:A1K2R4" FT /protein_id="CAL93119.1" FT /translation="MSLIAQLLPLSNVVVDLDASSKKRVFEHAGLLFENNQGIARSTVF FT DSLFSRERLGSTGLGQGIAIPHGRIKGLKEAAGAFLRLSAPVQFDAPDGRPVNLLFVLL FT VPEQANETHLQLLSELAQMFSERAFREQLLVAPDAATIHALFANWGPDAADQRRAAV" FT CDS complement(540982..541305) FT /transl_table=11 FT /gene="rpoX" FT /locus_tag="azo0503" FT /product="probable sigma-54 modulation protein" FT /function="Ribosome-associated protein Y (PSrp-1)" FT /note="Probable sigma 54 modulation protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2R5" FT /db_xref="InterPro:IPR003489" FT /db_xref="UniProtKB/TrEMBL:A1K2R5" FT /protein_id="CAL93120.1" FT /translation="MNLNITGHHVEVTPAIREYVVTKLDRVIAHFDNVTSVNVILSVEK FT LKQKAEVTVHVRGKDIYVESDDANLYAAIDSMADKLDRQVQKYKQKVSDHNHDALKHQS FT PEA" FT CDS complement(541320..542780) FT /transl_table=11 FT /gene="rpoN1" FT /locus_tag="azo0504" FT /product="RNA polymerase sigma-54 factor" FT /function="DNA-directed RNA polymerase specialized sigma FT subunit sigma54 homolog" FT /note="RNA polymerase sigma-54 factor. The sigma factor is FT an initiation factor that promotes attachment of the RNA FT polymerase to specific initiation sites and then is FT released. Similar to SWISSPROT: sprot|RP54_PSEAE (51% FT Pseudomonas aeruginosa, RNA polymerase sigma-54 factor FT RpoN) / sprot|RP54_ECOLI (46% Escherichia coli, RpoN or FT NtrA) InterPro: IPR000394 Sigma54_factor. Pfam: PF00309 FT Sigma54_AID. PF04963 Sigma54_CBD. HTH reporting nucleic FT acid binding motif." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2R6" FT /db_xref="InterPro:IPR000394" FT /db_xref="InterPro:IPR007046" FT /db_xref="InterPro:IPR007634" FT /db_xref="UniProtKB/TrEMBL:A1K2R6" FT /protein_id="CAL93121.1" FT /translation="MKPTLQLKLSQHLTLTPQLQQSIKLLQLSTLELNTEIERFLLENP FT MLEREEMDGGGHDFQAQLSSGTTTASTTTESSGESGGEAESRADSAESGSFDEGMDWSS FT GSGSGSSSNRDDDDDVDFQEFQAAGISLRDHLDQQVALSPLSDRDRALVRFLIEALDDD FT GYLHQELEELLELLPPELDVELDDLCIALKHVQSLEPAGIGARTPQECLALQLRAMPAE FT PVRDLALQIVSQHLELLAERNFAKLKKLTGCDDDALRAAHALICRLDPHPGAQHSVEET FT RYVLPDVVVRKLRGRWTVQLNPEAMPRLRINQLYASILQQNRGQGGGLTSQLQEARWLI FT KNVQQRFDTILRVSQAIVDQQRQFFDHGEVAMRPLTLREIADQLELHESTVSRVTTQKF FT MATPRGVFELKYFFGSHVATDTGGAASSTAIRALIRQLVDAEDRKKPLSDARIAELLGQ FT QGIVVARRTIAKYRESLNIPPVSLRKTI" FT CDS complement(542790..543512) FT /transl_table=11 FT /gene="yhbG" FT /locus_tag="azo0505" FT /product="probable ATPase component of ABC transporter" FT /function="ABC-type (unclassified) transport system ATPase FT component" FT /note="Probable ABC transporter ATP-binding protein HI1148. FT ATP-binding cassette (ABC) transporters are multidomain FT membrane proteins, responsible for the controlled efflux FT and influx of substances (allocrites) across cellular FT membranes. TREMBL:Q7NST9: 64% identity,75% similarity FT InterPro: IPR003593; AAA_ATPase. IPR003439; FT ABC_transporter. IPR000767; Disease_resist. IPR003016; FT Lipoyl_BS. Pfam PF00005; ABC_tran; 1 mobB: FT molybdopterin-guanine dinucleoti TMH's present 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2R7" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A1K2R7" FT /protein_id="CAL93122.1" FT /translation="MSLLKVTGLQKRYKARTVVHDVGFEVGSGEVVGLLGPNGAGKTTC FT FYMIVGLVRADGGEITLDDARLTHLPIHERARLGLSYLPQEMSVFRKLTVAENIQSVLE FT LRGLNATRIAERLEELLEELGIAHLRNNTAVSLSGGERRRCEIARALATDPRLILLDEP FT FAGVDPIAVLDIQKIIRFLKERGIGVLITDHNVRETLGICDRAAIISEGRVLASGQPRE FT IIDNEKVRQVYLGEHFRL" FT CDS complement(543499..543948) FT /transl_table=11 FT /gene="recX" FT /locus_tag="azo0506" FT /product="probable RecX-family regulatory protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Regulatory protein recX. Modulates recA activity (By FT similarity). TREMBL: Q7WKM9: 45% identity, 63% similarity FT InterPro: RecX regulatory protein InterPro; IPR003783; FT RecX. Pfam: PF02631; RecX PPR: pentatricopeptide repeat FT domain No transmembrane helices present" FT /note="Family membership" FT /db_xref="GOA:A1K2R8" FT /db_xref="InterPro:IPR003783" FT /db_xref="UniProtKB/TrEMBL:A1K2R8" FT /protein_id="CAL93123.1" FT /translation="MGEPSLRERAIRHLARREHSRSELARKLAAHGDADAVAEVLARMD FT ELGLQSDTRFAEAWVRGKAGRFGAARLRNELARRGVAAETIAEALASGCADGDFERARA FT VWQSRFGAAPADAREWARQARFLQNRGFATDVIRKLLKESPDESA" FT CDS complement(543971..545005) FT /transl_table=11 FT /gene="recA" FT /locus_tag="azo0507" FT /product="recombinase A" FT /function="RecA/RadA recombinase" FT /note="Recombinase A. Homology to recA of H. seropedicae of FT 80% (sprot|RECA_HERSE) Can catalyze the hydrolysis of ATP FT in the presence of single-stranded DNA the ATP-dependent FT uptake of single-stranded DNA by duplex DNA and the FT ATP-dependent hybridization of homologous single-stranded FT DNAs. It interacts with lexA causing its activation and FT leading to its autocatalytic cleavage (By similarity). FT InterPro: RecA bacterial DNA recombination protein mobB: FT molybdopterin-guanine dinucleotid" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2R9" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR013765" FT /db_xref="InterPro:IPR020584" FT /db_xref="InterPro:IPR020587" FT /db_xref="InterPro:IPR020588" FT /db_xref="InterPro:IPR023400" FT /db_xref="UniProtKB/Swiss-Prot:A1K2R9" FT /protein_id="CAL93124.1" FT /translation="MDDNKAKALAAALSQIEKQFGKGSIMRMGDGNVEKDIQTVSTGSL FT GLDIALGLGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDVGYA FT EKLGVNITDLLISQPDTGEQALEIADMLVRSGGVDVVVIDSVAALTPKAEIEGEMGDQL FT PGLQARLMSQALRKLTANIKRTNTLVIFINQIRMKIGVMFGNPETTTGGNALKFYASVR FT MDIRRTGTIKRGDEVVGSETKVKVVKNKVSPPFKEAHFDILYGEGVSREGEIIDLGVDH FT KIVDKSGAWYAYNGDKIGQGKDNAREFLRANPALAREIENKVRVVLGLKELPVDGAQPA FT AAEA" FT CDS complement(545130..545615) FT /transl_table=11 FT /gene="ygaD1" FT /locus_tag="azo0508" FT /product="probable CinA-related protein" FT /function="uncharacterized protein (competence- and FT mitomycin-induced)" FT /note="Hypothetical 17.2 kDa protein 1 in recA 5region. FT TREMBL:Q9KUH9: 54% identity, 64% similarity CinA is the FT first gene in the competence-inducible (cin) operon, and is FT thought to be specifically required at some stage in the FT process of transformation [1]. This is a C-terminal region FT of putative competence-damaged proteins from the cin operon FT InterPro:IPR008136; CinA_C. Pfam: PF02464; CinA cinA_cterm: FT competence/damage-inducible p No signal peptide. No FT transmembrane helices" FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR008136" FT /db_xref="UniProtKB/TrEMBL:A1K2S0" FT /protein_id="CAL93125.1" FT /translation="MDTELATLSRQVGDALARRGWLLATAESCTGGWIAEVVTATAGSS FT AWFDRGFVTYSNVAKTEMLGVSAATLGSAGAVSIATVGEMAQGAQARSAAQIAVAVSGV FT AGPTGGSAEKPVGMVCLAWAWGDGQLDAETCHFAGDREAVRRQTVIRALEGVLVRCG" FT CDS complement(545618..546100) FT /transl_table=11 FT /locus_tag="azo0509" FT /product="putative phosphatidylglycerophosphatase A" FT /function="Phosphatidylglycerophosphatase A and related FT proteins" FT /EC_number="3.1.3.27" FT /note="Region start changed from 546007 to 546100 (93 FT bases)" FT /db_xref="GOA:A1K2S1" FT /db_xref="InterPro:IPR007686" FT /db_xref="UniProtKB/TrEMBL:A1K2S1" FT /protein_id="CAL93126.1" FT /translation="MRPTLRLLLSHPAHFISLGFGAGLSPRAPGTVGTLLGWALFPLLH FT APLADGVFLALLVALFVAGILATERTGRALGVSDHGGIVWDEIVAIWLVLLLTPATLAW FT QAAAVALFRFFDIVKPPPVSWADRRFKGGFGVMLDDLIAAGYTLLVLAALVRLLGA" FT CDS complement(546104..547114) FT /transl_table=11 FT /gene="thiL" FT /locus_tag="azo0510" FT /product="thiamine-phosphate kinase" FT /function="Thiamine monophosphate kinase" FT /EC_number="2.7.4.16" FT /note="Thiamine-phosphate kinase. catalytic activity: atp + FT thiamine phosphate = adp + thiamine diphosphate. pathway: FT thiamine biosynthesis." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2S2" FT /db_xref="InterPro:IPR000728" FT /db_xref="InterPro:IPR006283" FT /db_xref="InterPro:IPR010918" FT /db_xref="InterPro:IPR016188" FT /db_xref="UniProtKB/TrEMBL:A1K2S2" FT /protein_id="CAL93127.1" FT /translation="MPSSAPASRQNAPDAAATTAGEFALIQRHFSRPCGHTALAGGDDA FT ALLHPRPGMELAVSADMLVAGTHFFPDADPHDLGWKTLAVNVSDLAAMGADPRWALLSL FT ALPAADDAWIAAFADGFYACAERFGVDLAGGDTTRGPLTLSVTILGEVPRGQALTRAGA FT NAGDDIWVSGQPGLAALGLEMLRGTFAPTADGERCLAALHRPQPRVALGQALRGLASAA FT LDISDGLLGDLGHILVQSRCGATLHEDALPLAALYATGASPALARRCLLAGGDDYELLF FT CAPPAARAAITALGPALALPLTRIGTLSDAPGTVALRSADGTLTALAARGYDHFG" FT CDS complement(547249..547530) FT /transl_table=11 FT /locus_tag="azo0511" FT /product="UPF0125 family protein" FT /db_xref="InterPro:IPR005346" FT /db_xref="UniProtKB/TrEMBL:A1K2S3" FT /protein_id="CAL93128.1" FT /translation="MRIGVAYADVAQPVWLKIDVPDTATVQEAIEISGILKAFPQIDLG FT TQKVGIFGKLAKLDAPLKPGDRVEIYRPIICDPSQVPRKNGSDDDEDE" FT CDS complement(547551..548285) FT /transl_table=11 FT /gene="rnfE1" FT /locus_tag="azo0512" FT /product="probable electron transport complex protein RnfE" FT /function="predicted NADH:ubiquinone oxidoreductase subunit FT RnfE" FT /note="Probable electron transport complex protein rnfE. FT Homology to rnfE of r. capsulata of 62% (sprot|RNFE_RHOCA). FT Required for nitrogen fixation. May be part of a membrane FT complex functioning as an intermediate in the electron FT transport to nitrogenase. InterPro: RnfA-Nqr electron FT transport subunit ((IPR003667) Pfam: Rnf-Nqr-subunit, FT membran protein no signal peptide 5 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2S4" FT /db_xref="InterPro:IPR003667" FT /db_xref="InterPro:IPR010968" FT /db_xref="UniProtKB/TrEMBL:A1K2S4" FT /protein_id="CAL93129.1" FT /translation="MSEACASAAADGAAKPAPSGPSYASLIKDGLWSNNPVLAQMVALC FT PTLAVTSSATNGLGMGLATTAVLILSNMLISSIRNLVSPNVRIPVFVVVIATLVSLIDM FT SMNAWMYELYQVLGLFIALIVVNCAILGRAEAFASKNTVLSSAVDGLGMGLGFTATLVV FT LGGVREILGSGTLFAGASNMLGSQFAFLELTLIPGYKGFLMMILPPGAFFVIGCLIAAH FT RVLSQRAERRAAAAPGADTAPA" FT CDS complement(548296..548922) FT /transl_table=11 FT /gene="rnfG1" FT /locus_tag="azo0513" FT /product="probable electron transport complex protein RnfG" FT /function="predicted NADH:ubiquinone oxidoreductase subunit FT RnfG" FT /note="Probable electron transport complex protein rnfG. FT Homolog to rnfG of R. capsulata of 51% (sprot|RNFG_RHOCA). FT Required for nitrogen fixation. May be part of a membrane FT complex functioning as an intermediate in the electron FT transport to nitrogenase. signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2S5" FT /db_xref="InterPro:IPR007329" FT /db_xref="InterPro:IPR010209" FT /db_xref="UniProtKB/TrEMBL:A1K2S5" FT /protein_id="CAL93130.1" FT /translation="MDIAKQFDTLWYQGASLAAVALITGAALAVAYQSAAPRIAEAQMR FT KTQAALAEVLPQGSFDNDLMADTVTIKDAAGREVTVYRARKAGAVTGVVFGMENKGYSG FT TIKLVMGVDLDGRLTGVRVTGHTETPGLGDKIELAKTPWVLGFNGKSLDDPAPALWAVK FT KDGGVFDQFAGATITPRAVVGAVKRGLELYTGNREAMIAAGAPRS" FT CDS complement(548939..549994) FT /transl_table=11 FT /gene="rnfD1" FT /locus_tag="azo0514" FT /product="probable electron transport complex protein RnfD" FT /function="predicted NADH:ubiquinone oxidoreductase subunit FT RnfD" FT /note="Probable electron transport complex protein rnfD. FT Homology to rnfD of R. capsulatus of 42% FT (sprot|RNFD_RHOCA). Required for nitrogen fixation. May be FT part of a membrane complex functioning as an intermediate FT in the electron transport to nitrogenase (By similarity). FT InterPro: NQR2 and RnfD/E related proteins (IPR004338) FT Pfam: NQR2, RnfD, RnfE family no signal peptide probable 7 FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2S6" FT /db_xref="InterPro:IPR004338" FT /db_xref="InterPro:IPR011303" FT /db_xref="UniProtKB/TrEMBL:A1K2S6" FT /protein_id="CAL93131.1" FT /translation="MNAISSPHAHGARKVGRVMTLVMLALVPATLAGFWRFGWPAVYLW FT LVTLLSCLLAEAFSTRIRGIDTRRALFDGSAVLTGWLLALSLPPWAPWWIGALGGAFAI FT IVTKHLFGGLGQNLFNPAMAARVMLLISFPVEMTQWLLPTPETLPGAIEALSITFGAGV FT PDAMSSASLLGHVKSEATKGILLGQSLTGHYSAAAFGLGDRQGSLGETSALLLLAGGVF FT LIFQRIITARIPLAFLAGVAAPAALASAIAPDLYLGPLTHLLSGGVMLAAFFIATDYVT FT SPSTPLGQWIFGIGCGLLTWIIRTWGAYPEGIAFAVMLMNATAPLIDQYTRPRIFGRSR FT DGRALNPAESR" FT CDS complement(549991..551550) FT /transl_table=11 FT /gene="rnfC1" FT /locus_tag="azo0515" FT /product="probable electronen transport complex protein FT RnfC" FT /function="predicted NADH:ubiquinone oxidoreductase subunit FT RnfC" FT /note="Probable electron transport complex protein RnfC. FT Homology to rnfC of R. capsulatus of 48% (sprot|RNFC_RHOCA) FT Required for nitrogen fixation. May be part of a membrane FT complex functioning as an intermediate in the electron FT transport to nitrogenase. Stabilizes rnfB. InterPro: FT Respiratory-chain NADH dehydrogenase 51 Kd subunit FT (IPR001949); 4Fe-4S ferredoxin, iron-sulfur bidning domain FT (IPR001450) Pfam: Respiratory-chain NADH dehydrogenase; FT 4Fe-4S binding domain no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2S7" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR009051" FT /db_xref="InterPro:IPR010208" FT /db_xref="InterPro:IPR011538" FT /db_xref="InterPro:IPR012285" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="InterPro:IPR019554" FT /db_xref="UniProtKB/TrEMBL:A1K2S7" FT /protein_id="CAL93132.1" FT /translation="MGSPSIPPLARLARLLNPWGVHPEGRKQLTADTEIALVPLPDRLV FT LPLSQHIGAPARPIVEVGTRVLRNQLLAEAQGAISAPIHAPTSGIVVGIAEVPVPHPSG FT LPGPAILLEPDGADEALPAEHNDPFALSAAEISRRVAEAGIVGMGGATFPAAVKLSLGQ FT KTAIPTLILNGGECEPYLTCDDRLMRDRADQVIDGARIILHAMGGREVLIGVENNKPVA FT IAALEAAAGAFPEVKVVAVPSRYPMGSEKQLIEWLTGREIPAGGRPADIGVMVQNVGTA FT AAIHRAIRFGEPLTRRIVTVSGGGVRTPRNVEVRIGTPLSALLAFCGGLKAEAVRYVMG FT GPMMGLAVQSLEIPVIKGSGGLLALVAGEVGSYGTEDTSAGPCIRCASCVGACPIGLMP FT LDMAALIKHGDLAASVDIGLKDCIGCGTCSYVCPSKIPLVHYFNHAKGELAAQDRNKMK FT QDAIKQLADARTARMEQEAREKAEAAARRKAEREKAKAEAAAKAAAKKAAAPAPASEES FT PA" FT CDS complement(551561..552088) FT /transl_table=11 FT /gene="rnfB1" FT /locus_tag="azo0516" FT /product="probable electron transport complex protein RnfB" FT /function="predicted NADH:ubiquinone oxidoreductase subunit FT RnfB" FT /note="Probable electron transport complex protein rnfB. FT Homology to rnfB of R. capsulatus of 48% FT (sprot|RNFB_RHOCA). Required for nitrogen fixation. May be FT part of a membrane complex functioning as an intermediate FT in the electron transport to nitrogenase. Stabilizes rnfC. FT Pfam: 4Fe-4S binding domain signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2S8" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR007202" FT /db_xref="InterPro:IPR010207" FT /db_xref="InterPro:IPR016463" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K2S8" FT /protein_id="CAL93133.1" FT /translation="MLIAVTSVALIGAFCGVALGVAARRFYVEPDSAVAEIEAMMPGSQ FT CGQCGFPGCAGAAAAIVAGEAPVTCCPPGGKALAVALAEKLGITVDTSGMSDDGPRIAG FT VTEEICIGCTKCYKSCPTDAILGAVKQVHTVIRDACTGCAKCEDVCPTGAITLSPIPVT FT QQSWVWPKPVAA" FT CDS complement(552106..552687) FT /transl_table=11 FT /gene="rnfA1" FT /locus_tag="azo0517" FT /product="probable electron transport complex protein RnfA" FT /function="predicted NADH:ubiquinone oxidoreductase subunit FT RnfA" FT /note="Probable electron transport complex protein RnfA. FT Homology to rnfA of R. capsultatus of 66% (RNFA_RHOCA). FT Required for nitrogen fixation. May be part of a membrane FT complex functioning as an intermediate in the electron FT transport to nitrogenase. Required for stable existence of FT rnfB and rnfC. InterPro: RnfA-Nqr electron transport FT subunit (IPR003667) Pfam: Rnf-Nqr subunit, membrane protein FT no signal peptide 6 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2S9" FT /db_xref="InterPro:IPR003667" FT /db_xref="InterPro:IPR011293" FT /db_xref="UniProtKB/Swiss-Prot:A1K2S9" FT /protein_id="CAL93134.1" FT /translation="MSEWLMLLLGTALVNNVVLVKFLGLCPFMGVSKKVDSAIGMGMAT FT TFVLTLASALTWLIEHFLLVPFDFGYLRILSFILVIAATVQFVEMVIKKTAPDLYKVLG FT IYLPLITTNCAVLGVALLNAGEGAGFVRSVLYGFGSALGFTMVMVLFAGLRERLALTSV FT PAAFSGAPISFITAGLLSLAFMGFAGLTNH" FT CDS 553036..554607 FT /transl_table=11 FT /gene="nifL" FT /locus_tag="azo0518" FT /product="nitrogen fixation regulatory protein" FT /function="FOG: PAS/PAC domain" FT /EC_number="2.7.13.1" FT /note="Nitrogen fixation regulatory protein (EC 2.7.3.-). FT Required for the inhibition of nifA activity in response to FT oxygen and low level of fixed nitrogen. Similar to FT SWISSPROT: sprot|NIFL_AZOVI (41% Azotobacter FT vinelandii,nitrogen fixation regulatory protein (EC FT 2.7.3.-), NifL) InterPro: IPR003661 His_kinA_N. The FT histidine kinase A (phosphoacceptor) N-terminal domain is a FT dimerisation and phosphoacceptor domain of histidine FT kinases. It has been found in bacterial sensor FT protein/histidine kinases. IPR000014 PAS. PAS domains are FT involved in many signalling proteins where they are used as FT a signal sensor domain. IPR000700 PAS-assoc_C. IPR004358 FT Bact_sens_pr_C. IPR003594 ATPbind_ATPase. Pfam: PF00512 FT HisKA. PF00989 PAS. PF00785 PAC. TIGRFAM: TIGR00229 PAS FT domain S-box." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2T0" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR013767" FT /db_xref="InterPro:IPR014285" FT /db_xref="UniProtKB/TrEMBL:A1K2T0" FT /protein_id="CAL93135.1" FT /translation="MHEIIMPAPVPTPTIFADAIFHYAVEQSAIAISITDQHANILYVN FT PAFCAITGYAAHEVVGHKQSLLSYKSTPKVVYQELWGALKKGRSWTGRLLNRRRDGSPY FT VAELTVTPLKTPEHEDEDINYLGMHWDATEEHRLSRQLANHKQLIESVISVAPVAVALL FT DVDGRVVLDNPAYKRIVAEMKVDEPAHAVIESLRHNLGDSFEKAFASRRALLNQEVRFD FT RAGGEPRWYACSLSWFEEHHTSPDAFYGDGCSDYMLLVMHDISASKRQQEALRLAAMRA FT MLSEGELNQSLREALAGAVFQLQGPVNLISAAAGLQRRRAGPGAGSDPLARALSEAQRA FT GEEAIATLQAAMPPEPEEPSGPVNLNEVLRDVLMLETDALLSAGITVDWHPAHVLPTVQ FT GDPTALRTLFRQLVSNAIEAMNVRGWKERALVLRTSTQNGQVDVEVTDTGPGIPEALRL FT KVFEPFFSTKKARAAGRGVGLSLAQEIVTRHRGMLEIDPEYSGGCRLRISFPALRSAPL FT DLEGGR" FT CDS 554604..556157 FT /transl_table=11 FT /gene="nifA" FT /locus_tag="azo0519" FT /product="nif-specific regulatory protein" FT /function="Transcriptional regulator containing GAF FT AAA-type ATPase and DNA binding domains" FT /note="Nif-specific regulatory protein. NIFA A FT TRANSCRIPTIONAL ACTIVATOR IS REQUIRED FOR ACTIVATION OF FT MOST NIF OPERONS WHICH ARE DIRECTLY INVOLVED IN NITROGEN FT FIXATION. NIFA INTERACTS WITH SIGMA-54. InterPro: Sigma-54 FT factor interaction domain" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2T1" FT /db_xref="InterPro:IPR002078" FT /db_xref="InterPro:IPR002197" FT /db_xref="InterPro:IPR003018" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR010113" FT /db_xref="InterPro:IPR020441" FT /db_xref="UniProtKB/TrEMBL:A1K2T1" FT /protein_id="CAL93136.1" FT /translation="MSAAGPMPAAEERVAWLEATLEALYRVSRVLSRSLELRETLSEVL FT RVLDEECGFNRALVTLNEPDGESMAISALHGVDAPIDPDIRWRSGEGVIGSTQQRSRPL FT VVARLADDPNFLSRRGLFDGEAPFIGAPIRAGHETVGVLALQPSPTSREHLDDYAHFAE FT MVANLVGQTVRLSCQVRQERRDIAEERDNLRRTVRNRFGFDNIVGHTQRMRQVFEQIRQ FT VAKWNTTVLVRGETGTGKELIAQAIHYNSPRAAGPFVKLNCAALPENLLESELFGHEKG FT AFTGALTQRKGRFEMADGGTLFLDEIGEISASFQAKLLRVLQEGELERVGGARTLRVDV FT RVIAATNRDLELEVEAGKFREDLYYRLNVMPIMLPPLRERVEDIPEIARFLVEKVSGQQ FT GRPLSITDSALRILLHHAWPGNVRELENCIERAAVMSEDGTIDRDLILISGIEERVTPL FT RGGGGTVDLDDPGLDERERVIAALEQAGWVQAKAARLLGMTPRQIAYRIQTLNIKVRQI FT " FT CDS complement(556202..557770) FT /transl_table=11 FT /locus_tag="azo0520" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT Gmet02000900 of Geobacter metallireducens of 45% FT (gi|48846570|ref|ZP_00300831.1|(NBCI ENTREZ)). No domains FT predicted. Signal peptide present. No TMH reported FT present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K2T2" FT /protein_id="CAL93137.1" FT /translation="MRPNAPRLSTPLRRAAAILCLAACGSAGAVADLGAIAAAADIDDI FT SAPCRALPAALEPALARAEMTQQLAAYQQLSEEALAMRAEAIRLFHALKARSARGEALS FT GADLQRLHAGAAALLAQRRSLLQTAFAHECWLDAPAATDPALAAVQHAGILMSLAAALT FT LYDNYLLAISLYQDDSVLRLKLNRGDRGFALDRGELDRITRAFASPENRRRVRRGIDWF FT ERNRSTASAEAIDGSAYLGALIAQSPSYQMVREASPLAELGAHFGIFRVATADTLATLR FT DESLNLYSLLFGNTVGLVETRRGKLDRRADVEARVAGTLRAGDILLEKTPFRLTDTFIP FT GHWGHAAIWVGDEAELRALGIWEHPLVQAHAAQIRAGRGVVEALRSGVEMNPLAHFLNI FT DDLAVLRADTMTPEGRVAVVLQALRQVGKAYDFNFDAESTQRVFCSKLVYLAYGDMQWP FT TARIFGRVTVSPDNIAARATGDGPLSVALLYHDGEEVSRAPRALMEKLVPTAAPSLARS FT EATLR" FT CDS complement(557796..558329) FT /transl_table=11 FT /locus_tag="azo0521" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No Hits in the PDB. FT No domains predicted. No TMHs. Signal peptide present." FT /db_xref="UniProtKB/TrEMBL:A1K2T3" FT /protein_id="CAL93138.1" FT /translation="MSPRRRPCRAAAVLLAALLTGPATAAPGAALGARGIGPLQLGAPL FT QAAAAQALPLDPAAALVGPGCDSRDQVTIRVRSAGLDFEVMAMARADGRIEEVIALPQP FT ASAQAADAPACRARVADLAARLAPALGQSRRESHERKPVSEEFQFHFPGAARAVARWFP FT GGRSCDLALVFNLP" FT CDS complement(558326..558853) FT /transl_table=11 FT /gene="sodC" FT /locus_tag="azo0522" FT /product="superoxide dismutase" FT /function="Cu/Zn superoxide dismutase" FT /EC_number="1.15.1.1" FT /note="Superoxide dismutase [Cu-Zn]precursor (EC 1.15.1.1), FT sodC.Destroys radicals which are normally produced within FT the cells and which are toxic to biological systems. May FT function against extracytoplasmic toxic oxygen species. 45% FT SOD_CU_ZN.Copper/Zinc superoxide dismutase. Pfam: PF00080; FT sodcu; 1. TIGR:CC1579. Signal peptide: present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2T4" FT /db_xref="InterPro:IPR001424" FT /db_xref="InterPro:IPR018152" FT /db_xref="InterPro:IPR024134" FT /db_xref="InterPro:IPR024136" FT /db_xref="UniProtKB/TrEMBL:A1K2T4" FT /protein_id="CAL93139.1" FT /translation="MPFAKTVAALALAACATHALAADRATAELIDRQGKAIGTATLTEG FT PAGVLIHVSAKGLAAGPKGIHIHSVGTCEDADKGFVASKGHLNPTGKKHGLLNPEGPDA FT GDLPVIFVHADGSVEAELYTPLASIKGAGERAALLDADGAALVIHESRDDHSTQPIGGA FT GARIACGVVKGE" FT CDS 559180..560676 FT /transl_table=11 FT /gene="nifB" FT /locus_tag="azo0523" FT /product="nitrogen fixation protein" FT /function="predicted Fe-S oxidoreductases" FT /note="FeMo cofactor biosynthesis protein nifB. PROBABLY FT INVOLVED IN THE SYNTHESIS OF THE FE-MO COFACTOR." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2T5" FT /db_xref="InterPro:IPR000385" FT /db_xref="InterPro:IPR003731" FT /db_xref="InterPro:IPR005980" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="UniProtKB/TrEMBL:A1K2T5" FT /protein_id="CAL93140.1" FT /translation="MELPVISNTAPESSGGGCSSSGCGTAPDALSHLPDSIRSKVQDHP FT CYSEEAHHYFARMHVAVAPACNIQCNYCNRKYDCSNESRPGVVSEVMSPDQAVKKTLAV FT AAAIPQMTVLGIAGPGDPLANPERTFETFRRLSEEAPDIKLCVSTNGLSLPESVDELAK FT HNIDHVTITINCVDPEIGAKIYPWIFWENKRIFGVEGAKILIEQQQKGLEMLTSRGILV FT KVNSVMIPGINDEHLKEVSKIVKAKGAFLHNVMPLIAEAEHGTYFGIMGQREPTPLELE FT ALQDSCSGDMSMMRHCRQCRADAVGLLGEDRGAEFTIDKIEEMEIDYAAAMVERAKVHD FT AITSELEMKRALKAAPKFNPEAGEEKPATRPIRIAIASKGGGLVNEHFGHAHEFLVYEV FT GPTSHRFLTHRKCTPYCMGDESCGDGETVLGQIIKSLEGVEVLLASKIGFEPWADLEKA FT GIQPNGEHAMEPIEEAIRAVYDELAAAGKLDMPAEAKAAA" FT CDS 560794..561084 FT /transl_table=11 FT /locus_tag="azo0524" FT /product="conserved hypothetical ferredoxin" FT /function="Ferredoxin" FT /note="Conserved hypothetical ferredoxin. Homology to fdx FT of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are FT iron-sulfur proteins that transfer electrons in a wide FT variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin FT iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding FT domain no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2T6" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K2T6" FT /protein_id="CAL93141.1" FT /translation="MALEITEVCVGCYACEPLCPNKAISAGNPVFTIDPDKCTECLGDY FT DKPQCAEICPIEAAIVDEIGDPLNPLGSLTGIPIHLIEEYNTTGTVARPGV" FT CDS 561181..561630 FT /transl_table=11 FT /locus_tag="azo0525" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to an orf FT of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: FT arsenate reductase. Pfam: ArsC family (PF03960) no signal FT peptide. no TMHs" FT /db_xref="InterPro:IPR006503" FT /db_xref="InterPro:IPR006660" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:A1K2T7" FT /protein_id="CAL93142.1" FT /translation="MTTTMQIRFWWKPGCATNTRQIRLLKDAGCEVTVLDLLTEPWTPA FT RLAGFLARKPVAEWFNPAAPAVKSGAVVPAAFSPEAALERLVAEPILIRRPLIEIGHAR FT CSGFAPDWLAAQGVALAPEAPVPEGCSHGDAPAAFCPPPAVASPS" FT CDS 561627..562916 FT /transl_table=11 FT /gene="fprA" FT /locus_tag="azo0526" FT /product="probable type A flavoprotein" FT /function="uncharacterized flavoproteins" FT /note="Probable type A flavoprotein fprA . Homology to frpA FT of R. capsulatus of 58% (sprot|FPRA_RHOCA) Low-potential FT electron donor to a number of redox enzymes (Potential). FT InterPro: Metallo-beta-lactamase superfamily (IPR001279); FT Flavodoxin (IPR001226) Pfam: Metallo-beta-lactamase FT superfamily; Flavodoxin no singal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2T8" FT /db_xref="InterPro:IPR001226" FT /db_xref="InterPro:IPR001279" FT /db_xref="InterPro:IPR008254" FT /db_xref="InterPro:IPR016440" FT /db_xref="UniProtKB/TrEMBL:A1K2T8" FT /protein_id="CAL93143.1" FT /translation="MNTPGAVPPDKAVAVAPGVHWVGALDPDLRQFDIILRTANGTSYN FT AYAIRGTAGVAVVDTVKAEYADVFFQRLWSCCRPEEIKAIVLNHLEPDHSGALPELLRA FT APQAPLYISRPAFAMLKGILKDGLDPSRIIATEPETRVELGGRSLRFLQTPYLHWPDTQ FT CTWVEEDGFLFSGDVFGCHFCDPRLFNDKVGDFRFSFDYYYQHIMRPFREHVLTALKLV FT EPLTLRLIAPAHGPVLRDAPQTYVRRYRQLATPQLQNEAAERAKTLLVFYISAYGNTQQ FT MAHAVREGAESVDGVRVSLYDLAGGETAPFVDLIEEADGLVFGSPTINGDAVKPVWDLL FT SSLTLVNVRGKFGAAFGSYGWSGEAVGLIEDRLRGLKLRVPRPGVKVKLIPTAEELAEC FT ATLGRELAEQLTGKAGPRHIDFSALHARSA" FT CDS 562926..563213 FT /transl_table=11 FT /gene="fdxC" FT /locus_tag="azo0527" FT /product="probable ferredoxin IV" FT /function="Ferredoxin" FT /note="Ferredoxin IV (FdIV) (Ferredoxin plant-type). FT Homology to fdxC of R. capsulatus of 62% (FER4_RHOCA). FT FERREDOXINS ARE IRON-SULFUR PROTEINS THAT TRANSFER FT ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. THIS FT FERREDOXIN PROBABLY PARTICIPATES IN NITROGEN FIXATION. FT Pfam: 2Fe-2S iron-sulfur clauster binding domain no signal FT peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2T9" FT /db_xref="InterPro:IPR001041" FT /db_xref="InterPro:IPR006058" FT /db_xref="InterPro:IPR012675" FT /db_xref="UniProtKB/TrEMBL:A1K2T9" FT /protein_id="CAL93144.1" FT /translation="MPKAQVTFEDIEVTVTVPAGTRLIEVSEKIGAGITYGCREGECGT FT CMMKIVSGSEHLANPSVLEDKVLKDNFAGVANRLACQAQVLGGHVVVRPG" FT CDS 563265..563615 FT /transl_table=11 FT /gene="fdxD" FT /locus_tag="azo0528" FT /product="Ferredoxin V" FT /function="2-polyprenylphenol hydroxylase and related FT flavodoxin oxidoreductases" FT /note="Ferredoxin V (FdV) (Ferredoxin plant-type). FT FERREDOXINS ARE IRON-SULFUR PROTEINS THAT TRANSFER FT ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. THIS FT FERREDOXIN PROBABLY PARTICIPATES IN NITROGEN FIXATION. FT InterPro: Ferredoxin" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2U0" FT /db_xref="InterPro:IPR001041" FT /db_xref="InterPro:IPR006058" FT /db_xref="InterPro:IPR012675" FT /db_xref="UniProtKB/TrEMBL:A1K2U0" FT /protein_id="CAL93145.1" FT /translation="MPNITFSSPIHKDKTVYAVTGSHTNTILKVAKENHIPIDFSCEDG FT ECATCLVKVTSLTRKGKMAGPLTDKEVAVLKEHKKITAEEIERMRVEDVPTTPWRLACQ FT LVLRDEDLLVEY" FT CDS 563680..564255 FT /transl_table=11 FT /gene="nifQ" FT /locus_tag="azo0529" FT /product="putative NifQ protein" FT /note="Putative NifQ protein. Homology to nifQ of A. FT vinelandii of 33% (sprot|NIFQ_AZOVI(SRS) NifQ is involved FT in early stages of the biosynthesis of the iron-molybdenum FT cofactor (FeMo-co), which is an integral part of the active FT site of dinitrogenase [2]. The conserved C-terminal FT cysteine residues may be involved in metal binding. Pfam: FT NifQ no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2U1" FT /db_xref="InterPro:IPR006975" FT /db_xref="UniProtKB/TrEMBL:A1K2U1" FT /protein_id="CAL93146.1" FT /translation="MLAPLNHRPTPARLALHAHLMRHAAGTPNDEFIAHLIAGWTLGDG FT VLPADLGLGASRFARLMAVHFPGLAWEPKPDHGPALVLYPEFDDLVRFIGAHADPTVAG FT ADDMTLVLATACMGSDHLWQDLGLPSRRELSQLIALNFPELGALNNRDMKWKKFLYREL FT CQREGIFVCASPSCESCADYANCFGPEV" FT CDS 564301..565239 FT /transl_table=11 FT /gene="draG1" FT /locus_tag="azo0530" FT /product="probable ADP-ribosyl-[dinitrogen reductase] FT hydrolase" FT /function="ADP-ribosylglycohydrolase" FT /EC_number="3.2.2.24" FT /note="Probable ADP-ribosyl-[dinitrogen reductase] FT hydrolase. Homology to draG of R. rubrum of 44% FT (sprot|DRAG_RHORU) Involved in the regulation of the FT nitrogen fixation activity by the reversible FT ADP-ribosylation of the dinitrogenase reductase component FT of the nitrogenase enzyme complex. The FT ADP-ribosyltransferase (DraT) transfers the ADP-ribose FT group from NAD to dinitrogenase reductase. The ADP-ribose FT group is removed through the action of the FT ADP-ribosylglycohydrolase (DraG). Pfam: FT ADP-ribosylglycohydrolase no signal peptide no TMHs" FT /db_xref="GOA:A1K2U2" FT /db_xref="InterPro:IPR005502" FT /db_xref="InterPro:IPR013479" FT /db_xref="UniProtKB/TrEMBL:A1K2U2" FT /protein_id="CAL93147.1" FT /translation="MLAEAAAAAAQRVDRACGAMLGLAIGDALGATVEFMTPREISAQY FT GVHDRIRGGGWLRLPAGDVTDDTTMTFALAEAWLGAGGPPDARACADAFDAWMRAKPVD FT IGNTVRRGIVRWRLHGTAQAEPSSDAGNGATMRCLPAALATVGADTAAIEQAALVQARV FT THHNPLTDAATLCAVRMVHAAFAGAGMPGVLAEADHLVAAHGEFAFRDRRCDNPSGFIV FT DTMRAVCQALAERNGFQAVLTDVVNRGGDADTTGAIAGMIVGAVVGETGLPAAWRQAVK FT PAVRKECVRLACGLLELAPVSRGAVAGAALR" FT CDS complement(565267..566196) FT /transl_table=11 FT /locus_tag="azo0531" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT PA2778 of P.aeruginosa of 39% (trembl|Q9I065(SRS)) Has FT Signal Peptide. No TMH present. Has PF03412:Peptidase C39 FT family;Lantibiotic and non-lantibiotic bacteriocins are FT synthesised as precursor peptides containing N-terminal FT extensions (leader peptides) which are cleaved off during FT maturation. Most non-lantibiotics and also some FT lantibiotics have leader peptides of the so-called FT double-glycine type. These leader peptides share consensus FT sequences and also a common processing site with two FT conserved glycine residues in positions -1 and -2. The FT double- glycine-type leader peptides are unrelated to the FT N-terminal signal sequences which direct proteins across FT the cytoplasmic membrane via the sec pathway. Their FT processing sites are also different from typical signal FT peptidase cleavage sites, suggesting that a different FT processing enzyme is involved. Peptide bacteriocins are FT exported across the cytoplasmic membrane by a dedicated FT ATP-binding cassette (ABC) transporter. The ABC transporter FT is the maturation protease and its proteolytic domain FT resides in the N-terminal part of the protein. This FT peptidase domain is found in a wide range of ABC FT transporters, however the presumed catalytic cysteine and FT histidine are not conserved in all members of this family." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2U3" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="UniProtKB/TrEMBL:A1K2U3" FT /protein_id="CAL93148.1" FT /translation="MTSLIRCLAAAAALSAAACTTLPTADWRPPAGSDLPVRAEREDAP FT FHPQEDYQCGPAALATVLGSAGIARRPEDLTAEVYIPARQGSLQPEMMAAARRAGTVAY FT RLPPEPNALLRELAAGHPVVVLQNLRFDWAPQWHYAAAVGYDLDASRIVLRSGRERRLE FT MTLNDFDRSWAKAGRWAFVALPPDRLPASAREADYVAAAVALERVAPDAAATAYLTALQ FT AWPANLIARIGHGNAAYRQGDLPAAEGAFRQATLDHPEAGDAWNNLAQVLYERGERAAA FT RAAAERAVAIGGARLPIYQRTLDLIAGG" FT CDS complement(566198..566773) FT /transl_table=11 FT /locus_tag="azo0532" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology of the FT entire protein with the data bank. No domains predicted. No FT signal peptide. 1 TMH" FT /db_xref="UniProtKB/TrEMBL:A1K2U4" FT /protein_id="CAL93149.1" FT /translation="MGHVHGAARRRQRAVGARPRARPPARRAHASATRPLNRAGRRVAG FT VDNSDDKLAEIFPPWAASNLRARPQEKTMKKFSPRLASATLLALAVGLHTPALHAELVT FT TPQAAAQASADADRAKVQQFLEQATVKERLQAMGVDGLAAADRVAALDQDEIHALAQRI FT DTMPAGGAITTTEWILIILVAILVVVAL" FT CDS complement(566665..567276) FT /transl_table=11 FT /gene="yjdF" FT /locus_tag="azo0533" FT /product="Conserved Hypothetical protein" FT /function="predicted membrane protein" FT /note="Hypothetical protein yjdF,44% identity (56% FT similarity) to TrEMBL;Q8XDT2. SwissProt;P39270. Signal P FT reporting Signal peptide present. TMHMM2 reporting 3 TMH's FT present." FT /db_xref="InterPro:IPR014509" FT /db_xref="UniProtKB/TrEMBL:A1K2U5" FT /protein_id="CAL93150.1" FT /translation="MRLGLLILVLAALVASGVAPYDRGVWLAEVAPVLIALPVLLISAR FT RFPLTPLTCGLVAFFALILIGGGAYTYARVPIGFEVQEMFGLARNPYDRFGHFFQGVTP FT AILGRELLLRTSPLRPGKWLFALLLLACLGISAAYELVEWAAAVWWGDGSVEFLGTQGD FT PWDAQWDMFMALLGAGSAQLALGRVHDRQLAALMLPPRGR" FT CDS complement(567329..568462) FT /transl_table=11 FT /locus_tag="azo0534" FT /product="hypothetical membrane protein" FT /function="FOG: TPR repeat SEL1 subfamily" FT /note="Hypothetical membrane protein. TREMBL:Q83LX6: 27% FT identity, 42% similarity. similarity to E.coli ybeT. FT some,to yeast skt5 and s.pombe spac24b11.10c InterPro; FT IPR006597; Sel_like. InterPro; IPR001440; TPR. InterPro; FT IPR008941; TPR-like Pfam:DsbD:Cytochrome C biogenesis FT protein trans SMART:SM00671; SEL1 Signal peptide present FT (Signal P) transmembrane helices: 5 (TMHMM predicted)." FT /note="Function unclear" FT /db_xref="GOA:A1K2U6" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR006597" FT /db_xref="InterPro:IPR011990" FT /db_xref="UniProtKB/TrEMBL:A1K2U6" FT /protein_id="CAL93151.1" FT /translation="MPTFPSSRRRVLAACAALGVLLGGAAGAARADLDAGITAYERKDY FT AVAFQELQLPAVRGDAGAQFRLGRMYDEGWGVALNDALAAAWYARAAELGDASARYNLA FT LMHLEGEGIPQDREQAFTLMFDVAQGGDSAAQYVLGRMYLNAWGTAKDEGMARYWLSAA FT ADAGHEAAAKALAELPPAPPVEALPVMRTSSDTTGAGDSAEVDLFTPLLWALLATLASL FT PLIGLFGTYLLFARARTEPSSWQRRKRVFKWLLFGVQALALALVLGFTLLEGEFDESIA FT YLLLALLGLFALLDLSALWALRRSQAGADRANRLRALLFAVLALELVVFSMAAYLAFTE FT FEVLLGHLVLAAGVVYALFLHGSVRLCVHRAAPPLAA" FT CDS complement(568662..569072) FT /transl_table=11 FT /gene="dcrH1" FT /locus_tag="azo0535" FT /product="putative hemerythrin-like protein" FT /function="Hemerythrin" FT /note="DcrH: hemerythrin protein,is a transmembrane FT methyl-accepting protein probably involved in bacterial FT chemotaxis. 36% Hemerythrin. Hemerythrin family non-heme FT Pfam:PF01814; Hemerythrin; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2U7" FT /db_xref="InterPro:IPR012312" FT /db_xref="InterPro:IPR012827" FT /db_xref="UniProtKB/TrEMBL:A1K2U7" FT /protein_id="CAL93152.1" FT /translation="MAELVWDDARHTLGVAEMDATHREFVELVGRLAAADDASFPKLFA FT EFHDHTRDHFFAEDAKMKATRFNAIGEHISEHQRVLIELRSFNRNVQAGRMRFARAYVR FT ENLKEWFDLHLATMDSALAAHLKQLAAKATTG" FT CDS complement(569083..569934) FT /transl_table=11 FT /locus_tag="azo0536" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to an orf FT of Pseudomonas stutzeri of 52% (tremble:Q9EVM9). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K2U8" FT /protein_id="CAL93153.1" FT /translation="MNEAVFEQIKAGLAAGEVVPFIGAEALADVTHATKGIKIPATSDE FT LILSLNNGQPMAPRLMYEFPRAAMNVELKRGRSAVNRWLEQTYGDNGWSEAALHRWLAE FT QKLPYIVDINRDTGLQKLYAGRPHTLIVGVARIAGTAYRYKLYKYDGEKYSAAVDESAI FT DPAAPILFKPCGTPWPEGNWIASDADFVDYITELMGGFAIPGFLKTRRVGLKYLVAGMR FT LNRDTQRMLLSDIIFSAAQPSGWALIPGANDKEKRFCARLGLTVIDADLRDLAGLPLAQ FT AA" FT CDS complement(570131..570973) FT /transl_table=11 FT /gene="draT" FT /locus_tag="azo0537" FT /product="putative NAD(+)-dinitrogen-reductase FT ADP-D-ribosyltransferase" FT /EC_number="2.4.2.37" FT /note="Putative NAD(+)-dinitrogen-reductase FT ADP-D-ribosyltransferase (EC 2.4.2.37) FT (ADP-ribosyltransferase). Homology to draT of R. rubrum of FT 39% (sprot|DRAT_RHORU(SRS) Involved in the regulation of FT the nitrogen fixation activity by the reversible FT ADP-ribosylation of the dinitrogenase reductase component FT of the nitrogenase enzyme complex. The FT ADP-ribosyltransferase transfers the ADP-ribose group from FT NAD to dinitrogenase reductase. The ADP-ribose group is FT removed through the action of the ADP-ribosylglycohydrolase FT (DraG). Pfam: DRAT no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2U9" FT /db_xref="InterPro:IPR009953" FT /db_xref="UniProtKB/TrEMBL:A1K2U9" FT /protein_id="CAL93154.1" FT /translation="METPDIDPALLRTTVPAQARRAINRCNLPPDALASLAFQLGPRAL FT ELDGVLPLHRPLFDRLDELENAAERAALFQSYMTAHFLLDDAPALGLSDTARINRSKLD FT YLRLLRGWLFDSEGREGAILKAWVESRFGLLTGFHRRPLGELDTPAREAFDQEVATGLY FT TTCALEAQIDLLYAWAQYEFGRRLPGRSHLLLYRGYSGAGALPRVGELADGRVLVQLNN FT LSSFSADRERADEFGDRVLECRVPTAKVLAFSQLLPGRLQGEDEYLVIGGIAAVRWLS" FT CDS 571215..572108 FT /transl_table=11 FT /gene="nifH" FT /locus_tag="azo0538" FT /product="putative nitrogenase iron protein" FT /function="Nitrogenase subunit NifH (ATPase)" FT /EC_number="1.18.6.1" FT /note="88% NifH.IPR000392; NitrogenaseII. Pfam:PF00142; FT Fer4_NifH; 1. TIGRFAMs:TIGR02016; BchX; 1.TIGR01287; nifH; FT 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:Q9F0V9" FT /db_xref="HSSP:1G20" FT /db_xref="InterPro:IPR000392" FT /db_xref="InterPro:IPR005977" FT /db_xref="UniProtKB/TrEMBL:Q9F0V9" FT /protein_id="CAL93155.1" FT /translation="MAKLRQCAIYGKGGIGKSTTTQNLVAALAEAGKKVMIVGCDPKAD FT STRLILHSKAQTTVMHLAAEAGSVEDLELDDVLSVGFGGVKCVESGGPEPGVGCAGRGV FT ITAINFLEEEGAYDDELDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAA FT NNIAKGIVKYANSGGVRLGGLICNSRNTDREDELIEALAAAMGTQMIHFVPRDNAVQHA FT EIRRMTVIEYDPTHKQADQYRQLAQKVLNNKMLVIPTPIEMEQLEALLMEFGIMEQEDE FT SIVGQTAAELAAGAAA" FT CDS 572230..573705 FT /transl_table=11 FT /gene="nifD" FT /locus_tag="azo0539" FT /product="nitrogenase molybdenum-iron protein alpha chain" FT /function="Nitrogenase molybdenum-iron protein alpha and FT beta chains" FT /EC_number="1.18.6.1" FT /note="Nitrogenase molybdenum-iron protein alpha chain (EC FT 1.18.6.1) (Nitrogenase component I) (Dinitrogenase). The FT key enzymatic reactions in nitrogen fixation are catalyzed FT by the nitrogenase complex which has 2 components: the iron FT protein and the molybdenum-iron protein." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2V1" FT /db_xref="InterPro:IPR000318" FT /db_xref="InterPro:IPR000510" FT /db_xref="InterPro:IPR005972" FT /db_xref="InterPro:IPR010143" FT /db_xref="UniProtKB/TrEMBL:A1K2V1" FT /protein_id="CAL93156.1" FT /translation="MSNLTREETDALIQEVLEVYPEKAKKDRAKHLAVNDQSITQSKKC FT ITSNRKSLPGVMTIRGCAYAGSRGVVWGPVKDMIHISHGPVGCGQYSRGGRRNYYVGTT FT GVNTFAEMNFTSDFQEKDIVFGGDKKLAQAMAEIEQLFPLNKGISVQSECPIGLIGDDI FT EAVSKKAAAQYNKVVVPVRCEGFRGVSQSLGHHIANDAIRDYVLSNRDGKEFESTPYDV FT TIIGDYNIGGDAWASRIFLEEMGLRVIAQWSGDGTIAEMENTPKAKLNLLHCYRSMNYI FT SRHMEEKYGIPWMEYNFFGPTKIEESLRRIAAFFDDSIKAKCEEVIAKYKPMMQAVIDK FT YKPRLQGKRVMLYIGGLRPRHVIGAYEDLGMEVVGTGYEFAHNDDYDRTIQEMGNATLL FT YDDVTGFELEEFVKRIKPDLVGSGIKEKYIYQKMGIPFRQMHSWDYSGPYHGYDGFAIF FT ARDMDMTLNNPCWGKQTPPWKKTEATEDVKAAA" FT CDS 573809..575377 FT /transl_table=11 FT /gene="nifK" FT /locus_tag="azo0540" FT /product="nitrogenase molybdenum-iron protein beta chain" FT /function="Nitrogenase molybdenum-iron protein alpha and FT beta chains" FT /EC_number="1.18.6.1" FT /note="Nitrogenase molybdenum-iron protein beta chain (EC FT 1.18.6.1) (Nitrogenase component I) (Dinitrogenase). The FT key enzymatic reactions in nitrogen fixation are catalyzed FT by the nitrogenase complex which has 2 components: the iron FT protein and the molybdenum-iron protein. InterPro: FT Oxidoreductase nitrogenase component 1 araD: FT L-ribulose-5-phosphate 4-epimer" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2V2" FT /db_xref="InterPro:IPR000318" FT /db_xref="InterPro:IPR000510" FT /db_xref="InterPro:IPR005976" FT /db_xref="InterPro:IPR024564" FT /db_xref="UniProtKB/TrEMBL:A1K2V2" FT /protein_id="CAL93157.1" FT /translation="MQAVDDIKPCYPLFRDDDYKENLKRKQDLYEERVPADKIAETFEW FT TTSKEYQELNFKREAITINPAKACQPLGAVLCSLGFKNTMPYVHGSQGCVAYFRTYFNR FT HFKEPVSCVSDSMTEDAAVFGGQKNMFDGLENAKAIYKPDMIAVSTTCMAEVIGDDLNA FT FINNAKKAGHVPQEYPVPFAHTPSFVGSHTTGWDNMWEGIARFFTLNKMEGKVVGSNGK FT LNFVPGFETYLGNYRVIKRMMGQMGVDATVLSDPSEVLDTPSDGEFRMYSGGTTMDEMS FT DAPNALNTIVLQPWQLEKSKKFVETVWNHDVPKLNIPMGLDWTDEFLMKVSEITGKAIP FT EELALERGRLVDMMQDSHTWLHGKKFALYGDPDFVLGLTKILLELGAEPIHILSNNANK FT RWGKAVQKVLDGYKHGANCKVYVGNDLWHMRSLCFTEKPDFLIGNSYGKYIQRDTVFKG FT KEFEVPLIRLGFPIFDRHHLHRMTTLGYEGAMYVLTTLVNAVLERLDDETRGMGTTDYN FT YDLVR" FT CDS 575484..575708 FT /transl_table=11 FT /gene="nifT" FT /locus_tag="azo0541" FT /product="nitrogen fixation protein [nifT]" FT /note="Nitrogen fixation protein [nifT],51% identity(72% FT Similarity) to SwissProt;P09427, TrEMBL;Q93JU8,57% FT identity. Has PF06988:NifT/FixU protein(IPR009727);This FT family consists of several NifT and FixU bacterial FT proteins. The function of NifT is unknown although it is FT thought that the protein may be involved in biosynthesis of FT the FeMo cofactor of nitrogenase although perturbation of FT nifT expression in K. pneumoniae has only a limited effect FT on nitrogen fixation. No Signal peptide or TMH present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2V3" FT /db_xref="InterPro:IPR009727" FT /db_xref="InterPro:IPR024044" FT /db_xref="UniProtKB/TrEMBL:A1K2V3" FT /protein_id="CAL93158.1" FT /translation="MANIMIRKTASGGLSFYLPKRDLEDDIVSIEFDQPDKWGGALKLL FT NGGEYYVEPLEAPPKLPITVRAKRVDAPE" FT CDS 575735..575938 FT /transl_table=11 FT /gene="fdxN" FT /locus_tag="azo0542" FT /product="FdxN protein" FT /function="Ferredoxin" FT /note="Ferredoxin. Pubilication: Egner et al., 2001, J FT Bacteriol 183, 3752-3760 (trembl|Q9F0V6) Ferredoxins are FT iron-sulfur proteins that transfer electrons in a wide FT variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin FT iron-sulfur binding domain (IPR001450) Pfam: 4Fe-4S binding FT daimain no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:Q9F0V6" FT /db_xref="HSSP:1DUR" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:Q9F0V6" FT /protein_id="CAL93159.1" FT /translation="MALKIVLDECTSCGDCKPVCPTKSITDKGGIFKINKDTCTECEGD FT FDEPQCLAVCPAGDACIVPLAA" FT CDS 576021..576743 FT /transl_table=11 FT /gene="nifY1" FT /locus_tag="azo0543" FT /product="NifY protein" FT /note="NifY protein. Homology to nifY of Azoarcus sp. BH72 FT of 99% (gi|11493644|gb|AF200742.1|AF200742(NBCI ENTREZ)). FT Pfam: Dinitrogenase iron-molybdenum cofactor. This family FT contains several NIF (B, Y and X) proteins which are FT involved in the synthesis of an iron-molybdenum cofactors FT (FeMo-co) in the dinitrogenase enzyme which catalyses the FT reduction of dinitrogen to ammonium. No signal peptide FT predicted. No TMHs." FT /note="Function unclear" FT /db_xref="InterPro:IPR003731" FT /db_xref="UniProtKB/TrEMBL:A1K2V5" FT /protein_id="CAL93160.1" FT /translation="MNTASPTGSPVTREAALRIAMAARALPGVEVVAFVRALGDRLGLP FT VTDEKLARVTVEDLKALLQGDEIVDPGVESSALKAAVRFLWGEGLDDGQPTPDADVPAA FT EGALKVAVASNTGELLDGHFGSCARFLVYQVSEEGVWLIDVRSTEGTDDADDRNVARAA FT LINDCHLAYMQSIGGPAAAKIVRAGIHPVKFPVGGEARQVLAQLQGTLKRPPPWLAKVL FT GREAPSLAQFTSDEEAEA" FT CDS 576740..577012 FT /transl_table=11 FT /locus_tag="azo0544" FT /product="hypothetical protein" FT /function="function unknown" FT /note="ORF1" FT /note="Conserved hypothetical protein. Homology to orf1 of FT Azoarcus sp. BH72 of 100% (gi|11493650|gb|AAG35591.1|(NBCI FT ENTREZ)). No domains predicted. No TMHs. No signal FT peptide." FT /db_xref="UniProtKB/TrEMBL:Q9F0V4" FT /protein_id="CAL93161.1" FT /translation="MINDELLGTVAGLVKEQGASEQLVSALRVRWPNLRFTYCSDDDMP FT PRLSPALAGEGFNLYLIANGDHCLALTKDPAVAIGVVVAEVMADE" FT CDS 577211..578842 FT /transl_table=11 FT /locus_tag="azo0545" FT /product="putative methyl-accepting chemotaxis protein" FT /function="Methyl-accepting chemotaxis protein" FT /note="Putative methyl-accepting chemotaxis FT protein,Chmtaxis_transd. Pfam: PF00015; MCPsignal. SMART: FT SM00283; MA. Signal P reporting signal peptide. TMHMM FT reporting 2 transmembrane helices." FT /note="Specificity unclear" FT /db_xref="GOA:A1K2V7" FT /db_xref="InterPro:IPR004010" FT /db_xref="InterPro:IPR004089" FT /db_xref="InterPro:IPR004090" FT /db_xref="UniProtKB/TrEMBL:A1K2V7" FT /protein_id="CAL93162.1" FT /translation="MLNSLRLRTRIGLLVAAALVGLIITNLFAAMAVKRDLLEGRQLQL FT VSVMHAAKRVVVQFHDQAAKGMITEDEAKERAAAMLAGLRYGGADGMAEYFFIWDMEGR FT SVMHPFRPEWKGQSKLDLLDGDGRPLVRRTLEAAAGSGFVDVSFPRPGGTVPVPKLLHA FT SSYAPWGWVIGTGAYIDDVDAQVGSRLLTDLSFGALVIAIMIVIAVLVGRSILKQIGGE FT PAEALGLMERAAGGDLTVELRGAPKGSLLDGLGRMLQSIRDMVSQISGGAAQLKGNADN FT IVHASQQVAEAAHRQADATSSMAAAIEQMTVSINHISDSARDTESNSSSAAALAEGGEA FT KVTHATEEMQRIAGSVAEAAQKIRTLESRAGEISSIANVIKEIAAQTNLLALNAAIEAA FT RAGEQGRGFAVVADEVRGLAERTAAATVQIEQMIGAIQSETATAVAAMDHTLPQVARGV FT DLAQEAAQSLREIRGGAGMTLSRIRDVALATREQSTASNAIAQQVESIAQMVEETSASM FT QQTASSARELERIAEALHAMVGRFRH" FT CDS complement(578928..579785) FT /transl_table=11 FT /gene="nifM" FT /locus_tag="azo0546" FT /product="probable peptidylprolyl isomerase" FT /function="Parvulin-like peptidyl-prolyl isomerase" FT /EC_number="5.2.1.8" FT /note="Probable peptidylprolyl isomerase. Homology with FT nifM of A. chroococcum of 43% (sprot|NIFM_AZOCH) REQUIRED FT FOR THE ACTIVATION AND STABILIZATION OF THE IRON-COMPONENT FT (NIFH) OF NITROGENASE. PROBABLE PPIASE. InterPro: PpiC-type FT peptidyl-prolyl cis-trans isomerase (IPR000297) Pfam: FT PPIC-type PPIASE domain no signal peptide no TMHs FT hydrog_prot: hydrogenase maturation pro" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2V8" FT /db_xref="InterPro:IPR000297" FT /db_xref="InterPro:IPR008880" FT /db_xref="InterPro:IPR014282" FT /db_xref="InterPro:IPR023058" FT /db_xref="UniProtKB/TrEMBL:A1K2V8" FT /protein_id="CAL93163.1" FT /translation="MSAQVYYELKAALALFSKSPGALDDAENARVKAVARRYTEIESVV FT LASSEAQGVCLAEGAVDKAVGEIRGRYEDEGAFALELEAAGLDLPGLTAALQRDLLVEA FT VMERVGARAGSVDETEAEIFYYAHVDRFRAPERRTVRHILVTINDAYPDNRREVASRRI FT HEICKRLNNKPERFEEQAMKHSECPTALNGGLLGELPRGTLYPELDAVLFEMKAGQLSG FT VVESEIGFHLLRCDAIQPERVLSFAEVSESLRQQLTAERGRKDARRWLTELLKRTTAEA FT VATN" FT CDS complement(579782..580273) FT /transl_table=11 FT /gene="nifZ" FT /locus_tag="azo0547" FT /product="Nitrogen Fixation protein" FT /note="Nitrogen Fixation protein[nifZ], 51% identity (67% FT similarity) SwissProt;P14889,66% similarity to FT SwissProt;P23124. Has PF04319:NifZ domain;(IPR007415)This FT short protein is found in the nif (nitrogen fixation) FT operon. Its function is unknown but is probably involved in FT nitrogen fixation or regulating some component of this FT process. This 75 residue region is presumed to be a domain. FT It is found in isolation in some members and in the amino FT terminal half of the longer NifZ proteins. No Signal FT Peptide Or TMH reported Present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2V9" FT /db_xref="InterPro:IPR007415" FT /db_xref="UniProtKB/TrEMBL:A1K2V9" FT /protein_id="CAL93164.1" FT /translation="MKPEFDYGDRVRVTRNVRDDGTFPGKDVGDLLVRRGSIGTVIEIG FT TFLQDQIIYTVHFLDIDRIIGCRQEELIGADDEWNPSRFESREKVVATRSFAIDGEVVV FT PKGTIGEIIKVLRDMPGGVHYHVSFPTKFLCIPEASLEALPPGTAVPETVAAPTEAEES FT " FT CDS complement(580294..580614) FT /transl_table=11 FT /gene="nifW" FT /locus_tag="azo0548" FT /product="nitrogen fixation protein NifW" FT /note="Nitrogenase stabilizing/protective protein nifW,50% FT identity (68% similarity) to SwissProt;P14888.TrEMBL; FT Q6US88(60% similarity). Has PF03206:Nitrogen fixation FT protein NifW;(IPR004893)Nitrogenase is a complex FT metalloenzyme composed of two proteins designated the FT Fe-protein and the MoFe-protein. Apart from these two FT proteins, a number of accessory proteins are essential for FT the maturation and assembly of nitrogenase. Even though FT experimental evidence suggests that these accessory FT proteins are required for nitrogenase activity, the exact FT roles played by many of these proteins in the functions of FT nitrogenase are unclear. Using yeast two-hybrid screening FT it has been shown that NifW can interact with itself as FT well as NifZ. No Signal Peptide or TMH present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2W0" FT /db_xref="InterPro:IPR004893" FT /db_xref="UniProtKB/TrEMBL:A1K2W0" FT /protein_id="CAL93165.1" FT /translation="MDELTLEEAMEELSSAEDFLQFFEVPFEQSVVHVNRLHILQRFHD FT YISHNPAAEGSDEAAVRAHYRSFLERAYNDFVVSNSVQEKVFAVFKKAAGEAFVSLDSI FT QR" FT CDS complement(580638..581177) FT /transl_table=11 FT /locus_tag="azo0549" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to orf8 of FT Azotobacter vinelandii of 36% (tremble:Q44542). No domains FT predicted. No Signal peptide or TMH present." FT /db_xref="UniProtKB/TrEMBL:A1K2W1" FT /protein_id="CAL93166.1" FT /translation="MDLLHFDPQPLYFEDPLPEGVHDLIEEAGRHYGQPEAEALLARAA FT ALAPDHLVVLVARYRYYFYQHRIVEAQDVVWHAIGVSGAQLGLPADGAGLTVELVAAAA FT RVSMTLTRFYLSSIKAAAYVKMRLDEIPAAIALLQTLVEIDEADRMGGKVLLDIAHARQ FT NGTSDDEDELETESIL" FT CDS complement(581177..582025) FT /transl_table=11 FT /gene="nifP" FT /locus_tag="azo0550" FT /product="serine O-acetyltransferase" FT /function="Serine acetyltransferase" FT /EC_number="2.3.1.30" FT /note="Serine acetyltransferase (EC 2.3.1.30). Homology to FT nifP of A. chrooccum of 58% (pir|D43706). PROBABLE SERINE FT ACETYLTRANSFERASE REQUIRED FOR OPTIMIZING THE EXPRESSION OF FT NITROGENASE ACTIVITY. NIFP MAY BE REQUIRED TO BOOST RATES FT OF SYNTHESIS OR INTRACELLULAR CONCENTRATIONS OF CYSTEINE OR FT METHIONINE. InterPro: Bacterial transferase hexapeptide FT repeat (IPR001451) no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2W2" FT /db_xref="InterPro:IPR001451" FT /db_xref="InterPro:IPR005881" FT /db_xref="InterPro:IPR011004" FT /db_xref="InterPro:IPR018357" FT /db_xref="UniProtKB/TrEMBL:A1K2W2" FT /protein_id="CAL93167.1" FT /translation="MKTESMSMTNPVRGPGLFALLREDVRCVFGRDPAARTVWEVLTTY FT PGVHAVMSHRIAHALWRRGWRYPGRLVSFLARVFTNVDIHPGAQIGRRFFIDHGAGVVV FT GETAEIGDDVTLYHGVTLGGTTWNPGKRHPTLGDHVVVGAGAKILGAITIGSRVRVGAN FT SVVVKNVPADRTVVGIPAKVVKRESPILSATDELNLDHHVMPDPVGHTLNCLLDRIKML FT ESELATLQAEGKAALAAASAPPKPVQTVFPLINANPLDCQANTDAACPECACQPEAQEA FT R" FT CDS complement(582028..583218) FT /transl_table=11 FT /gene="nifV" FT /locus_tag="azo0551" FT /product="homocitrate synthase" FT /function="Isopropylmalate/homocitrate/citramalate FT synthases" FT /EC_number="2.3.3.14" FT /note="Homocitrate synthase is involved in the biosynthesis FT of the iron-molybdenum cofactor of nitrogenase and FT catalyzes the condensation of acetyl-CoA and FT alpha-ketoglutarate into homocitrate. Similar to FT sprot|NIFV_AZOVI (51%) and to sprot|NIV1_ANASP (42%). Pfam FT (PF00682): HMG-CoA Lyase-like family InterPro (PS00815): FT Alpha-isopropylmalate and homocitrate synthase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2W3" FT /db_xref="InterPro:IPR000891" FT /db_xref="InterPro:IPR002034" FT /db_xref="InterPro:IPR013477" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:A1K2W3" FT /protein_id="CAL93168.1" FT /translation="MSAPVTIDDTTLRDGEQSAGVAFTRAEKCGIARILAEIGVPELEI FT GIPAMGSEECGDIRAIADTLADGGHDTRLIVWGRLTSADIDACRSLPVQMLELSVPVSD FT QQIRHKLGATRDEVLARIARWVPVAREAGFDVGVGGEDASRADPAFLAEVIQAAEAAGA FT RRFRFADTLGILDPFATFEAIRALRAASKLEIEMHAHDDLGLATANTLAAVRAGASHVN FT TTVNGLGERAGNAALEEVALGLRQFHGMGEIIDFTRLLDTSEAVARASGRPVGWHKSVV FT GEGVFTHEAGIHVDGLLKDPANYQGIDPALLGRSHRMLLGKHSGGRGVAAAYAGLGIEL FT DAARTACLLARIREFTSRTKRTPQREDLLAFWEELEAGSAQCDDLLHDLLDTAAGA" FT CDS complement(583307..584530) FT /transl_table=11 FT /gene="nifS" FT /locus_tag="azo0552" FT /product="cysteine desulphurase" FT /function="Cysteine sulfinate desulfinase/cysteine FT desulfurase and related enzymes" FT /EC_number="2.8.1.7" FT /note="Cysteine desulfurase(Nitrogenase metalloclusters FT biosynthesis protein nifS). Homology to nifS of A. FT chroococcum of 71% (sprot|NIFS_AZOCH) CATALYZES THE REMOVAL FT OF ELEMENTAL SULFUR ATOMS FROM CYSTEINE TO PRODUCE ALANINE. FT SEEMS TO PARTICIPATE IN THE BIOSYNTHESIS OF THE NITROGENASE FT METALLOCLUSTERS BY PROVIDING THE INORGANIC SULFUR REQUIRED FT FOR THE FE-S CORE FORMATION. Pfam: aminotransferase class-V FT no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2W4" FT /db_xref="InterPro:IPR000192" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="InterPro:IPR016454" FT /db_xref="InterPro:IPR017772" FT /db_xref="InterPro:IPR020578" FT /db_xref="UniProtKB/TrEMBL:A1K2W4" FT /protein_id="CAL93169.1" FT /translation="MSIPNLTPIYLDNNATTRCAPEAVTAMLPYFTEQFGNPSSMHSFG FT AKVGHATKGARASLQKLLGAEFDSEIIYTAGGTEADNTAILSALKANPERKEIITSTVE FT HHAVLHLCEQLEKEGYTIHKLKVDGKGRLDLDEYAKLLTDKVAVVSVMWANNETGTYFP FT VEKMAEMAKAAGILFHTDAVQAVGKIPLNLKDSAIDMLSLSGHKLHGPKGIGALYLRRG FT ARFRPLLRGGGQERGRRAGTENVPGIIGLGVAAELALEHMEQENTYVRALRDKLQAGIL FT AAVPNAFATGDVDNRLPNTLNIAFEYVEGEAILMLLNKQGIAASSGSACTSGSLEPSHV FT MRAMGIPYTAAHGTIRFSLSRENTEAEIDRVIAAVPPIIAQLRKLSPYWGENGPVTDPE FT KAFAPTYA" FT CDS complement(584713..585603) FT /transl_table=11 FT /gene="nifU" FT /locus_tag="azo0553" FT /product="probable nitrogen fixation protein NifU" FT /function="NifU homolog involved in Fe-S cluster formation" FT /note="Probable nitrogen fixation protein NifU. Homology to FT nifU of A. vinelandii of 67% (sprot|NIFU_AZOVI). INVOLVED FT IN THE FORMATION OR REPAIR OF [FE-S] CLUSTERS PRESENT IN FT IRON-SULFUR PROTEINS. Pfam: NifU-like N-terminal domain, FT NifU-like domain no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2W5" FT /db_xref="InterPro:IPR001075" FT /db_xref="InterPro:IPR002871" FT /db_xref="InterPro:IPR007419" FT /db_xref="InterPro:IPR010238" FT /db_xref="InterPro:IPR016217" FT /db_xref="UniProtKB/TrEMBL:A1K2W5" FT /protein_id="CAL93170.1" FT /translation="MWDYSDTVKEHFYNPRNAGALADANAIGEVGSISCGDALRLMLKV FT DPANETILDASFQTFGCGSAIASSSALTEIIKGKTLEQALEVSNQDIADFLGGLPPEKM FT HCSVMGREALQAAVANYRGEEWKDDHEEGALICKCFAVDAVMIEETIRANNLCSVEQVT FT NYTKAGGGCSSCHEGIEEILAKVLAERGETFKAAPPPEKKAPGKMTTLERIRKIEQVIE FT KARPNLQRDHGDIELVDVDGKNIYVSMKGACAGCQMEAATLGGVQAQMIEALGELVKVI FT PVKATAKLAPNTLPA" FT CDS complement(585625..585948) FT /transl_table=11 FT /gene="hesB" FT /locus_tag="azo0554" FT /product="HesB/yadR/yfhF family protein" FT /function="uncharacterized conserved protein" FT /note="HesB/yadR/yfhF family protein, 45% identity to FT TrEMBL;Q9KJL2,Q6HRJ0. SwissProt;P37026(41% identity) Has FT PF01521, HesB-like domain;IPR000361, HesB_yadR_yfhF;This FT family includes HesB which may be involved in nitrogen FT fixation; the hesB gene is expressed only under nitrogen FT fixation conditions. Other members of this family include FT various hypothetical proteins of which P46847 and NP31774 FT also contains NifU-like domains NifU which is also involved FT in nitrogen fixation. In the gram-negative soil bacterium FT Rhizobium etli, the hesB-like gene iscN is required for FT nitrogen fixation." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2W6" FT /db_xref="InterPro:IPR000361" FT /db_xref="InterPro:IPR016092" FT /db_xref="InterPro:IPR017870" FT /db_xref="UniProtKB/TrEMBL:A1K2W6" FT /protein_id="CAL93171.1" FT /translation="MLNLTPTAIKAVSRFISSSADPVVGLRIHVQGGGCSGLQYGMKLE FT AEKAEDDVIVEMEGITLLVDPFSAPLLSGVTVDFVDSLTGSGFKFENPNATGGCACGQS FT FSA" FT CDS complement(586209..586601) FT /transl_table=11 FT /locus_tag="azo0555" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT Daro03002610 of Dechloromonas aromatica of 39% FT (gi|41724013|ref|ZP_00150903.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K2W7" FT /protein_id="CAL93172.1" FT /translation="MGVISLILFHKQSTSGRLRFARFADTVVAARVEVEGDPEVVTPHP FT GALVAQAAGRLGLPAGELKVEPEFRERMLAPGGTASVWIAEFASIDPPFAAVEQAGGRF FT VLLTELQGIPDTERDVMRAVYEHVLG" FT CDS complement(586611..586898) FT /transl_table=11 FT /gene="fdxB" FT /locus_tag="azo0556" FT /product="probable ferredoxin" FT /function="Ferredoxin" FT /note="Probable ferredoxin. Homology to fdxB of R. FT capsulatus of 45% (sprot|FER3_RHOCA) Ferredoxins are FT iron-sulfur proteins that transfer electrons in a wide FT variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin FT iron-sulfur binding domain (IPR001450) Pfam: 4Fe-4S binding FT domain no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K2W8" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR014283" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K2W8" FT /protein_id="CAL93173.1" FT /translation="MSDITGLTRGGATWVPQFVLTLNAKRCIGCGRCYKVCPRDVFELI FT ERESDDLDEDLDENMMVMSVANALDCIGCAACSRVCPKNCHTHGPSPVQA" FT CDS complement(587039..587254) FT /transl_table=11 FT /locus_tag="azo0557" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein Shows similarity to FT hypothetical 7.7 kDa protein in fixX 3'region (ORF1) of FT Azorhizobium caulinodans. TIGR00162: conserved hypothetical FT protein" FT /db_xref="InterPro:IPR007774" FT /db_xref="UniProtKB/TrEMBL:A1K2W9" FT /protein_id="CAL93174.1" FT /translation="MTEEEIKELEKEVKKLKRISQEWASQLHDLVEDRLPAGYEEIHGI FT SQSTYDACKAWADANKRLIAATAAAN" FT CDS complement(587265..587750) FT /transl_table=11 FT /locus_tag="azo0558" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein(Has probable FT Nif-associated protein function)41% identity(62% FT similarity) to TrEMBL;Q9KJL5. Has FT PF03270(IPR004952):Protein of unknown function, FT DUF269;Members of this family may be involved in nitrogen FT fixation, since they are found within nitrogen fixation FT operons. NO Signal Peptide or TMH present." FT /note="Family membership" FT /db_xref="InterPro:IPR004952" FT /db_xref="UniProtKB/TrEMBL:A1K2X0" FT /protein_id="CAL93175.1" FT /translation="MITIDTNTAPAPVLTPELAETDFIKEMNRQTRALDSYGTYDGWPT FT DRVLAPYILTKEQRRQIPVVGDPDDVTISRVKAFHNAIAALIEKECGLMAVPMIHISHE FT GFGRALITVGKLVVLDRTLRDVHRFGFESFSKMKDEADKHLAVALEIVGKYSEVAGL" FT CDS complement(587769..588176) FT /transl_table=11 FT /locus_tag="azo0559" FT /product="hypothetical sigma-E factor regulatory protein" FT /note="Hypothetical sigma-E factor regulatory protein,best FT similarity to SWISSPROT: sprot|Y850_HAEIN (Haemophilus FT influenzae, hypothetical protein hi0850) / sprot|RSEC_ECOLI FT (23% Escherichia coli, sigma-e factor regulatory protein FT RseC). TMHMM reporting 2 transmembrane helices." FT /db_xref="InterPro:IPR007359" FT /db_xref="UniProtKB/TrEMBL:A1K2X1" FT /protein_id="CAL93176.1" FT /translation="MMSRSGRVVAVKDDQLVVRFEGASACGSCRANKVCGSGSTTDLVL FT DGGCGSRVGDQVDVDVDAGTAFRALAVAYLLPVAGFLAGMAVASAGGLGDLGVAGISFA FT GMGLGLIASRRLGRHPSLQPVPRLAASEFND" FT CDS complement(588173..588700) FT /transl_table=11 FT /gene="nifX" FT /locus_tag="azo0560" FT /product="conserved hypothetical NifX protein" FT /note="Conserved hypothetical NifX protein. Homology to FT nifX of Azotobacter vinelandii of 47% FT (gi|128328|sp|P14887|NIFX_AZOVI(NBCI ENTREZ)). Pfam: FT Dinitrogenase iron-molybdenum cofactor. This family FT contains several NIF (B, Y and X) proteins which are FT involved in the synthesis of an iron-molybdenum cofactors FT (FeMo-co) in the dinitrogenase enzyme which catalyses the FT reduction of dinitrogen to ammonium. No signal peptide FT predicted. No TMHs." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR003731" FT /db_xref="UniProtKB/TrEMBL:A1K2X2" FT /protein_id="CAL93177.1" FT /translation="MTPSPHIDPDSSSTPNPRRRQLRLVGTEEAKPVMDGIRVAFASTD FT RSTVNQHFGSTEAFAIFEVGQNSSTLVEVTEFLDTAQDGNENKLPAKIATLAGCAAVYC FT LACGASAVKQLLAAGVQPVRVEEGSVIDNLIGDIQGELASGPSGWLAKAVKARQPVDTT FT RFDEMEAEGWQE" FT CDS complement(588618..590012) FT /transl_table=11 FT /gene="nifN" FT /locus_tag="azo0561" FT /product="probable nitrogenase iron-molybdenum cofactor FT biosynthesis protein NifN" FT /function="Nitrogenase molybdenum-iron protein alpha and FT beta chains" FT /note="Probable nitrogenase iron-molybdenum cofactor FT biosynthesis protein NifN. Homology to nifN of A. vielandii FT of 60% (sprot|NIFN_AZOVI). This protein may play a role in FT the biosynthesis of the prosthetic group of nitrogenase FT (FeMo cofactor). InterPro: Oxidoreductase nitrogenase FT component 1 (IPR000510) Pfam: Nitrogenease component 1 type FT oxidoreductase probable signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2X3" FT /db_xref="InterPro:IPR000318" FT /db_xref="InterPro:IPR000510" FT /db_xref="InterPro:IPR005975" FT /db_xref="UniProtKB/TrEMBL:A1K2X3" FT /protein_id="CAL93178.1" FT /translation="MAEIIRHPKALSVSPLKSSAPAGAALAFLGINRSMPIFHGSQGCT FT AFAKVFFVRHFREPVPLQTTAMDQVATVMNADGNVVQALATVCGKSKPSLVGLATTALS FT ETQGTDIARLVKDFRADFPEFNHIPVAAVNTPDFAGCLETGYAAAVKGILDATVPHTAG FT TGIVGKRKKQVNLLLGSHLTPGDVEAIKEWLELFGLRPLSVPDLADSLDGHLISEDTIP FT VTLGGTPVSELATLGEAVATIVVGRSLKGAADLLAERTGVPDYRFDGLVGLEACDRFTQ FT TLAEIAGVAVPEKLERHRAQLQDAMVDTHFMTGLRRVAIAADPDLLLQTATLFAGMGSE FT IVAAVSPIKTGSLTDVPGAPQVHVGDLEDLEDLARTAQAELVVANSHAAATADRLGVPL FT LRAGMPQYDLVGGYCKTWVGYRGTRQALFDIANLVLQHHDSIAPHRSRFKLDPQPAPAP FT AAAGGH" FT CDS complement(590023..591525) FT /transl_table=11 FT /gene="nifE" FT /locus_tag="azo0562" FT /product="nitrogenase iron-molybdenum cofactor biosynthesis FT protein NifE" FT /function="Nitrogenase molybdenum-iron protein alpha and FT beta chains" FT /note="Nitrogenase iron-molybdenum cofactor biosynthesis FT protein NifE. Homology to nifE of A. vielandii of 70% FT (sprot|NIFE_AZOVI). This protein may play a role in the FT biosynthesis of the prosthetic group of nitrogenase (FeMo FT cofactor). InterPro: Oxidoreductase nitrogenase component 1 FT (IPR000510) Pfam: Nitrogenease component 1 type FT oxidoreductase no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2X4" FT /db_xref="InterPro:IPR000318" FT /db_xref="InterPro:IPR000510" FT /db_xref="InterPro:IPR005973" FT /db_xref="UniProtKB/TrEMBL:A1K2X4" FT /protein_id="CAL93179.1" FT /translation="MKASEVAALLDEPACTHNKKEKSGCARPKPGASAGGCAFDGAQIA FT LLPIADVAHVVHGPIACAGNSWDNRGTKSSGPTLYKIGMTTDLSEQDIIMGKAEKRLFH FT GIKQAVERYNPPAVFVYNTCVPALIGDDIEAVCKAAAERWGVPVVPIDSAGFYGTKNLG FT NRIAGEAMVKYVIGTREPEPLPPEAIPPGIKVHNINLIGEYNIAGELWYLTPLFDELGI FT RILCTLSGDARFHEVQTMHRAEVNMLVCAKAMINVARKMEERYGIPWFEGSFYGITDTS FT AALREIARIIGDEDLIARTEAVIAREENRVRGELDVWRPRLEGKRVLLFTGGVKSWSVV FT SALQDLGMNVVASGTKKSTEEDKARILELMGDKTIMLNSEGARDLLNAVYELKADILIA FT GGRNLYTALKARLPFLDINQEREFGYAGYEGMKELVRQLALTLESPVWDAVRKPAPWTS FT KAMVIAGPELGDSPDADDGNDAHGHDHDHDHDHHHAPAGAAA" FT CDS complement(591714..592715) FT /transl_table=11 FT /locus_tag="azo0563" FT /product="probale Hypothetical protein" FT /note="Probale Hypothetical protein. Very Weak homology FT spanning the entire length of protein in the data base. No FT Significant domains,Features,TMH's or Signal Peptide FT present." FT /note="Function unclear" FT /db_xref="UniProtKB/TrEMBL:A1K2X5" FT /protein_id="CAL93180.1" FT /translation="MTDATLDTSRDTAPTAAATSQNIPPSLSETLFKLCAETLPLPGHA FT TLLDGLRKAGGPEFSPRVSRGGWFRPGRILDAEGNCVAEDALAWLEQAWLEADEDGDSF FT LERHAEAGYVLTLQQGVSHYLVAPWGKGAAEFLQLEIEELQEVSSHVLGAGGETPLTAE FT ALLDRPPRAPAPTPLGEPRYLLRRLTDIAQFVGRIQEQAGKPAPILRFLADWQASSAGQ FT QRRFCDHWVLALTEHLDRYHQTRYGATPVAAHAPVWTGIPANRGTLLARELHDFDRAAG FT YGFAWYFHMVGSRRVPRSIAPVIAADLADGMAYLPERDAALVLAWVREAYTA" FT CDS complement(592764..593639) FT /transl_table=11 FT /locus_tag="azo0564" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Has PF05484:LRV FT protein FeS4 cluster(IPR008665);This Iron sulphur cluster FT is found at the N-terminus of some proteins containing LRV FT repeats. Has 6,(IPR004830) PF01816:Leucine rich repeat FT variant;The function of this repeat is unknown. It has an FT unusual structure of two helices. One is an alpha helix,the FT other is the much rarer 3-10 helix." FT /note="Function unclear" FT /db_xref="GOA:A1K2X6" FT /db_xref="InterPro:IPR004830" FT /db_xref="InterPro:IPR008665" FT /db_xref="InterPro:IPR011989" FT /db_xref="InterPro:IPR016024" FT /db_xref="UniProtKB/TrEMBL:A1K2X6" FT /protein_id="CAL93181.1" FT /translation="MRPPSPRGRRAGAAPLLARRLRDATSFTRRAARPAALDSHDQAPA FT AAAEYTPPENPCAECELREDTLARGRCGPGDACLFVYSGRQIDRFLARNPEWAEYCLDD FT PFWERRAIAVRYAPLEAAMRLENDEDEVVRRAVAVRAHGDVLVRMARDPDREVRITVAT FT RMQPADLARLIRDPDYGVRIHVARRLPHGQLPQLLDDPDPAVRKEIARRLPAFALGKLA FT HDPDPEVRALAAERMLPDDAARMLADPEWLVRAAAVHQAPLDALQAVLDDPEPDVRQLA FT AERLAAGNAH" FT CDS 593892..597104 FT /transl_table=11 FT /gene="morA" FT /locus_tag="azo0565" FT /product="GGDEF/EAL/PAS/PAC/GAF-domain containing protein" FT /function="predicted signal transduction protein containing FT a membrane domain an EAL and a GGDEF domain" FT /note="GGDEF/EAL/PAS/PAC/GAF-domain containing protein," FT /db_xref="GOA:A1K2X7" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001633" FT /db_xref="InterPro:IPR003018" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K2X7" FT /protein_id="CAL93182.1" FT /translation="MARAVHEGLRTRLSAVVIVIVAAVILPFVLSAAAYLERQAQDEAR FT AQLVAFGTLVRDLVATHHDSVESSVARVADAMALHFDGIYARRGTRLLWQGEAVEGAGA FT ELARFGDDVAGTIAGIALRSDAGFRSVLSTSGATLPAGRVVPLPADAVSALEAGRRWRG FT TLELAGARYLLELIPARDAAGATVGMYFVGVDLVREFARLRGRLREFTIGDSGYVFVLD FT ATPGPTYGRFIVHPEQEGGNPLQDSDNAGRSVIAEMLERGDGVIAYGWRNPARGEIVSR FT PKLAAFASYPALGWVIGASSYEDEFGRGALVMRRAMLATAAVMALTLIVALYCAIGAMV FT VAPMLRLQRTLRTLSRGNETLVHSASEDELVRRICEVLVQVGDFRLACIAFDMPGQAPR FT IVATHGGGDVFRAALARADASHLAPAVGAIAERRTVLVDDLGAVPAALRAAAEAAGCRA FT LIAYPLCEGERVLGALTIGAARPGDLDQAGTALLKELAEDLAFGIATQRTAVARREAEV FT ALRLRERAIESSSDGVLIFALGDDGPRIRDVNPAAERILGMARALLVDAPAPALTVFAP FT GALAELGVALVCGRETHLEVEGERADGSPFWCECALAPVRAAGDAHVVCVVKDVTERVL FT YLRELERQAKYDGLTGLPNRYLLDDRLEQAIVAARRHERLLGVAFIDLDHFKVVNDNVG FT HRQGDELLRQAASRLAAVLRDGDTAARQGGDEFVVLLPDLGDERDAFRILGRLQAALAE FT PFRLDDRSFFVTCSIGVSLYPRDGGDGDTLLKHADIAMYQAKAAGRNVVRFFTAEMNIQ FT VRDRLQLEGALRSALENGELHLAFQPQVDGGSGQVIGAEALLRWQHPELGAVPPVRFIP FT LAEETGLIGPIGEWVLRAACRQARQWEQAGRRLRIAVNVSARQFRSPDLPARIAEILDE FT TGLPPALLELELTESMLMGDAEQAEEMLHRLKQLGVSLALDDFGTGYSSFAYLQRFPID FT TLKIDQSFVRSMVAGVRGEAIVVAIIALAHSLGMRVIAEGVETPLQQRQLFEFGCDELQ FT GYLFGRPVPAAEFPHAGRGATV" FT CDS 597165..597449 FT /transl_table=11 FT /locus_tag="azo0566" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. No signal peptide. 1 TMH" FT /db_xref="UniProtKB/TrEMBL:A1K2X8" FT /protein_id="CAL93183.1" FT /translation="MAGGSAGVLPGGVVLPGGGTLSGAVGAGGVVGVVVVGGGGGGAIS FT REVVGAGGVEGAGGVSRRSQAASNSGAASVLNSRIRAFIIAVLLGGSLS" FT CDS complement(597475..598143) FT /transl_table=11 FT /locus_tag="azo0567" FT /product="conserved hypothetical protein" FT /function="ABC-type transport system involved in resistance FT to organic solvents auxiliary component" FT /note="Similar to TREMBL:Q82SF8 (45% identity); FT TREMBL:Q7P0W9 (43% identity); TREMBL:Q8XV73 (40% FT identity)." FT /db_xref="InterPro:IPR008869" FT /db_xref="InterPro:IPR023094" FT /db_xref="UniProtKB/TrEMBL:A1K2X9" FT /protein_id="CAL93184.1" FT /translation="MTIRHPPVHAGAPPASVPRWLRQLAWLLVFATAAAHGQGAAPDEL FT VRGVTDEVLTVLRQDKDLKAGDRARAIRLIDEKIAPHFDFARMTALAVGPPWRQASPPE FT REALTREFRTLLVRTYANALTAYRDQTVHFPPSPQAQGDDVVIRSQIRQSGAAPIGLDY FT RLRRGADGWKVFDVAVDSVSLVTSYRGSFAAELAKGGPQALIDTLREQNRRYEPERPPS FT " FT CDS 598310..599704 FT /transl_table=11 FT /gene="vsrA" FT /locus_tag="azo0568" FT /product="putative sensory box histidine kinase" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.13.1" FT /note="Putative sensory box histidine kinase," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Y0" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR007891" FT /db_xref="InterPro:IPR011712" FT /db_xref="UniProtKB/TrEMBL:A1K2Y0" FT /protein_id="CAL93185.1" FT /translation="MGSTKPMAGERQLRVTHRARAALLAVGCALVVALVGASFWQAAAG FT LQALETMQLQAARTARLDSMLIQLVDAESGARGYLLSRNHDYLAPYLNSLATVEYTLDE FT IRQDVGPDPRDQDALARLTGLITLKLRVLADAVGGAGAGEEAPRRAGVSDGVRYMDTIR FT TTLAGLKSRMAAEGQALLEESTRHIGHTRAVAAVLALSALLLLGLLHAALRRELRLRAQ FT LAGLLRDENARLEALVQARTADLSALASYLTRSQERERERIARELHDELGALLTAARMD FT AAALGGDMAPAHQARHARLLRTLDGGITLKRRIIGDLRPPLLQELGLVAALRVLAEELA FT DSDGTAVSAELPDDEPALAPECALALFRIAQEALTNARRHAGARRVRLGLRVERGAVRL FT EVEDDGAGFDPAACGPGRHGLAGMRHRVQMFAGRFSVDSRAGAGTRIAAALPLDAARGA FT ELALAA" FT CDS complement(599710..600345) FT /transl_table=11 FT /gene="vsrD1" FT /locus_tag="azo0569" FT /product="DNA-binding response regulator" FT /function="Response regulator containing a CheY-like FT receiver domain and an HTH DNA-binding domain" FT /note="DNA-binding response regulator," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Y1" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:A1K2Y1" FT /protein_id="CAL93186.1" FT /translation="MLHLAIVDDHAIVRAGFREMLATETDLHIVFEAATGEDALARVAD FT TGCDLLLLDLSLPGQSGVDVLRTLRRRGDSTRVLVLTGFPEDRYAVAMIRLGADGYLCK FT NCERDELVQAIRTIAQGRRYLSARTAELLAGEIAGDGSGAAHEQLSERELQVFLRLAHG FT ESVSAIADALHLSIKTVSTYRSRVLEKLDVTSNAELATYAIRHGLIVA" FT CDS complement(600348..601409) FT /transl_table=11 FT /locus_tag="azo0570" FT /product="conserved hypothetical protein" FT /note="Similar to TREMBL:Q89KB0 (34% identity); FT TREMBL:Q8XXG5 (34% identity)." FT /db_xref="GOA:A1K2Y2" FT /db_xref="InterPro:IPR010126" FT /db_xref="UniProtKB/TrEMBL:A1K2Y2" FT /protein_id="CAL93187.1" FT /translation="MSRRTRKSPLGTAFQRTLRSLTRASVRAGTKALDQAARIAAEHAR FT PPPGQGDWIAGQALGPAGVRRYYLFRPDGITRTQRVPLMVMLHGCGQTARSFALSTRMN FT ALAARERFLVLYPEQDRRANPQGCWEWFGTATRTGHAEAATLLAAIEQVCLLYPVDRDA FT VGLTGISAGAGMAALLATLYPTRFRALVMHSGVPPGVAHSPATAMAAMHGRRTPDFATV FT GAQQWPPLLVIHGDADRIVANGNARAAVRLWAAAHGAREGETRRLQRGRRYPAVVTDYH FT AGRQLVASLYEVQGLGHAWSGGAQRQPFSDPAGPDASRLAWSFLQRQLRTAARSTPAPR FT TRARPAVLARPRS" FT tRNA complement(601691..601766) FT /gene="tRNA-Lys" FT /locus_tag="azo_tRNA_0005" FT /product="transfer RNA-Lys" FT /anticodon=(pos:601731..601733,aa:Lys) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS complement(601871..602422) FT /transl_table=11 FT /gene="ruvC" FT /locus_tag="azo0571" FT /product="crossover junction endodeoxyribonuclease" FT /function="Holliday junction resolvasome endonuclease FT subunit" FT /EC_number="3.1.22.4" FT /note="Crossover junction endodeoxyribonuclease ruvC (EC FT 3.1.22.4) (Holliday junction nuclease ruvC) (Holliday FT juction resolvase ruvC). Nuclease that resolves Holliday FT junction intermediates in genetic recombination. Cleaves FT the cruciform structure in supercoiled DNA by nicking to FT strands with the same polarity at sites symmetrically FT opposed at the junction in the homologous arms and leaves a FT 5terminal phosphate and a 3terminal hydroxyl group (By FT similarity)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Y3" FT /db_xref="InterPro:IPR002176" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR020563" FT /db_xref="UniProtKB/Swiss-Prot:A1K2Y3" FT /protein_id="CAL93188.1" FT /translation="MSSAGRIVATRILGLDPGLRITGFGVIDTLGSQLRYVASGCIKTR FT DGELPGRLKTLLDGVREVIATYQPDAVAVEKVFVNVNPQSTLLLGQARGAVICGAVSCD FT LPVAEYTALQVKQSVVGYGKAAKEQVQHMVQRLLALDASPGPDAADALACAICHAHGGQ FT GLGGQAGIGGRRRAGRILSL" FT CDS complement(602457..602777) FT /transl_table=11 FT /gene="ybjQ" FT /locus_tag="azo0572" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical protein, ybjQ, 65% identity FT to SwissProt;P75819. SwiisProt;Q8XGV2(66% identity). FT TrEMBL;Q83LS2( 65% identity) Has PF01906, Domain of unknown FT function DUF74;IPR002765; Members of this protein family FT have no known function. The domain is about 100 amino acids FT long and found in prokaryotes." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR002765" FT /db_xref="UniProtKB/Swiss-Prot:A1K2Y4" FT /protein_id="CAL93189.1" FT /translation="MLMTTTPTLEGKPVQQYLGVVTGEAIIGANIFKDLFASIRNIVGG FT RAGAYERSLADAREVAMAEMAEQALKLGANAVIGIDIDYEVLGQDNGMLMVCVSGTAVI FT TA" FT CDS complement(602808..603686) FT /transl_table=11 FT /locus_tag="azo0573" FT /product="conserved hypothetical membrane protein" FT /function="Permeases of the drug/metabolite transporter FT (DMT) superfamily" FT /note="Conserved hypothetical membrane protein. Hamology to FT PA3358 of P. aeruginosa of 56% InterPro: Integral membrane FT protein DUF6 Tigrfam: 2A78: Carboxylate/Amino Acid/Amine FT Transporter Pfam: Integral membrane protein DUF6 no signal FT peptide probable 10 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2Y5" FT /db_xref="InterPro:IPR000620" FT /db_xref="UniProtKB/TrEMBL:A1K2Y5" FT /protein_id="CAL93190.1" FT /translation="MTASSPAQRLMPLLFVVLWSTGFIGAKFGLPYAEPLTFLSTRYVL FT VVVLMAAVALATRAPWPRSPRETAHVALTGVLVHAIYLGGVFMAIHRGLPAGVTALVVG FT MQPLLTALGAGMLLGERVSARQWIGLALGFIGVALVVSNKIGAGVDADRLLHMLTPALA FT ALAGITVGTLYQKRFCPRFDLRTGAVLQFLPTLLLSALVASQTETMQIQWTGEFVFALL FT WLVVVLSVGAISLLNLLIRSGSAVNVASLFYLTPPTTALIAWAMFGETLSGLALAGMVV FT AVSGVWLARKG" FT CDS complement(603781..604506) FT /transl_table=11 FT /gene="yebC" FT /locus_tag="azo0574" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical protein,yebC,48% identity FT (63% similarity) to SwissProt;Q8FGR1,P24237,Q8XFD4. FT TrEMBL;Q9S4S9. Has PF01709, Domain of unknown function FT DUF28;IPR002876; This domain is found in bacterial and FT yeast proteins it compromises the entire length or central FT region of most of the proteins in the family, all of which FT are hypothetical with no known function. The average length FT of this domain is approximately 230 amino acids long." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR002876" FT /db_xref="InterPro:IPR017856" FT /db_xref="UniProtKB/Swiss-Prot:A1K2Y6" FT /protein_id="CAL93191.1" FT /translation="MAGHSKWANIQHRKGRQDAKRGKVFTKLIKEVTVAAKMGGGDPNA FT NPRLRLAIDKAKAESMPKDNIENAIKRGTGQLEGVTYEEARYEGYGIAGAAVMVDCLTD FT NKTRTVADVRHAFSKYGGNMGTDGCVAFQFKHCGQLMFAPGTDEDALMEAALEAGAEDV FT VANDDGSIEVITGPWEFTTVKETLEKAGFTAEFGEVTMKAQNETELSGDDAARMQKLLD FT ALESLDDVQEVYTSAVLDE" FT CDS 604637..605281 FT /transl_table=11 FT /locus_tag="azo0575" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. No TMHs. Signal peptide FT Present." FT /db_xref="UniProtKB/TrEMBL:A1K2Y7" FT /protein_id="CAL93192.1" FT /translation="MCLLRPVLLFLLLLAGSAFAADEEPIYGGCVDARGAAVVTLIDPQ FT LPSAVATATEAGRAVIRHNPDALPRLLAASRSFLYAQACARLNLGYPADGELGLAEAQR FT ADCAALATLQRSGLLANTSLPALEADLRFSDSEWAALPGPRRTIGFSACPPPSRGNLRL FT PGAEAAGSPTWNACVRACAAPLYQCQARCAAGGCADCQAAYDRCNRACDGR" FT CDS 605320..606831 FT /transl_table=11 FT /locus_tag="azo0576" FT /product="conserved hypothetical protein" FT /function="predicted ATPase" FT /note="Conserved hypothetical protein. Homology to yjgR of FT E. coli of 66% (sprot|YJGR_ECOLI). no signal peptide no FT TMHs" FT /note="Family membership" FT /db_xref="InterPro:IPR008571" FT /db_xref="UniProtKB/TrEMBL:A1K2Y8" FT /protein_id="CAL93193.1" FT /translation="MTEPLLIAKTHDKDLCLLPRLANRHGLITGATGTGKTVTLQRMAE FT SFASIGVPVFMADVKGDLSGIGAAGVASDKLMQRLAAIGITEFTPRANTTVFWDVYGAA FT GHPVRATISDMGPLLLARLLNLNDTQAGVLQLVFKIADDNGLLLLDLKDLRAMIQHVGE FT NAKSFTTEYGNVSAASIGAIQRNLLALEEQGGDVFFGEPMLDIADLMQTDADGRGVINV FT LAADKLYHSPKLYSTFLLWMLSELFEQLPEVGDLDKPKLVFFFDEAHLLFADAPKALVE FT KVEQVVRLIRSKGVGVYFVTQNPLDVPETVLGQLGNRVQHALRAFTPRDQKAVKTAAET FT MRANPAFDAATAITELGVGEALVSFLDDKGRPEVVERGFVVAPASRLGPLAPAERDAAI FT RASVLYGHYEKAVDRESAYEILRGKAAAAAQPEGAPAGNGGGAAGGAAGGIDMNDILFG FT STGPRGGKRDGLVQIAAKTITRTIGSSLGRQIVRGVLGSLLGSKR" FT CDS complement(606869..607759) FT /transl_table=11 FT /gene="gstR2" FT /locus_tag="azo0577" FT /product="probable transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="Probable transcriptional regulator, LysR family," FT /note="Family membership" FT /db_xref="GOA:A1K2Y9" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K2Y9" FT /protein_id="CAL93194.1" FT /translation="MRTINWNDWYAFATVAQSGSFTRAAEQLDLPKSSVSHAVARLERQ FT LGQRLIERSTRRLALTEQGERMLAQVLPLFERLDAVAAEAGDARDEPQGVLRIATPYEF FT GAIQLGEVVNDVLNRHPRLQIEIDVRILGAEPASGGYDVVFFATGEALPDSERVVRRVY FT SVARGLYAAPALVRRLGLPRSVAELEDWPCLSMPGEARWHFEAADGRTHSVQPRGPLRT FT TNAALRLQAAIAGHGATMLAASYCRRELEAGTLVPLLADHVPHPLKIYAHLPGRGLVPA FT RARVFMDAIERFLRD" FT CDS 607889..609352 FT /transl_table=11 FT /gene="emrY" FT /locus_tag="azo0578" FT /product="multidrug resistence transmembrane protein" FT /function="Permeases of the major facilitator superfamily" FT /note="Multidrug resistance protein B homolog. TRANSLOCASE FT THAT CONFERS RESISTANCE TO SUBSTANCES OF HIGH FT HYDROPHOBICITY (BY SIMILARITY). Presence of signal peptide FT and 14 transmembrane helices. Presence of DUF domains,CbiM, FT and bacterial cytochrome ubiquinol oxidase like domains FT efflux_EmrB: drug resistance transport" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Z0" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:A1K2Z0" FT /protein_id="CAL93195.1" FT /translation="MLLSAHPELRPLRVHAFGATLGLVAGVDFVAAILIAMAGTQVQHG FT LGVAPRDFLWALTSYAVAAVMANLMLVQLAGRVNYRRFTLASLAVFIAGALGCAAADSL FT PAFTAARLVQGLGGGGLFAAARILAQYSSQPQERLSLFWGFGVANFALVALAPWLAGWL FT VAHHGWHTLFLLQAGLALPLLPLVAWLYPRVERTPSRALGRLDWPGVLAFAGGALLLVH FT ALEHLRYLSRAELPQLAAYALLGLVLLGVVMRRFARHPDPWLDPRRLASRRYLAGLAFY FT GVFYLICGYWNFLVPAVLVDGLGFGLDTVGGLLALGGLTTLGAVVVFHLCLPYIMRKRR FT YIALGYVGLAAAFTLMAVSARPGAGVLDVLPPIVLQGAMPVLALLQVAMMTFVDMPTED FT FAHAYAFKNIVREILNALGTGLAVLQLHHGTAAAQAAMQAATPGPLQPHLAEVVHRAAV FT GTAAGQMLSGLALACLLVAAVAVWQRALR" FT CDS 609429..610385 FT /transl_table=11 FT /locus_tag="azo0579" FT /product="conserved hypothetical membrane protein" FT /function="Permeases of the drug/metabolite transporter FT (DMT) superfamily" FT /note="Conserved hypothetical membrane protein. Homology to FT RSc2187 of R. solanacerarum of 44%. Tigrfam: 2A78: FT Carboxylate/Amino Acid/Amine Transporter Pfam: Intergral FT membrane protein DUF6 no signal peptide probable 6 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K2Z1" FT /db_xref="InterPro:IPR000620" FT /db_xref="UniProtKB/TrEMBL:A1K2Z1" FT /protein_id="CAL93196.1" FT /translation="MTAASSKVAEGGGAPPVASQAVSGRALGFAFAIAGAVGFSFKAIL FT VKLAYRHQVDAETLLALRMAFSLPFFLVMGWAASRRAADRLSARDWVWMAGLGLFGYYL FT ASYLDFLGLDYISAALERLILFLYPTIVIVLSALFLGKPITRRMLAALALCYLGIALAV FT GHDLDVSGTVQEVALGCALVFASAVSYALYLMGNGQVVGRLGSSRVTAYASSFACFFSL FT GQFVLMRPLEVLLAQAWQVYAYAGLMTVFSTVAPVWMVSEAIRRLGAGPVSLTGTLAPA FT ITMLLGWIILGEQIGLFQLLGMTMVVAGVMVVARPRR" FT CDS 610477..612138 FT /transl_table=11 FT /locus_tag="azo0580" FT /product="putative methyl-accepting chemotaxis transducer" FT /function="Methyl-accepting chemotaxis protein" FT /note="Putative methyl-accepting chemotaxis FT transducer,Chmtaxis_transd. Pfam: PF00015; MCPsignal. FT SMART: SM00283; MA. Signal P reporting signal peptide. FT TMHMM reporting 1 transmembrane helices. Methyl-accepting FT chemotaxis serine transducer. CHEMOTACTIC-SIGNAL FT TRANSDUCERS RESPOND TO CHANGES IN THE CONCENTRATION OF FT ATTRACTANTS AND REPELLENTS IN THE ENVIRONMENT TRANSDUCE A FT SIGNAL FROM THE OUTSIDE TO THE INSIDE OF THE CELL AND FT FACILITATE SENSORY ADAPTATION THROUGH THE VARIATION OF THE FT LEVEL OF METHYLATION. ATTRACTANTS INCREASE THE LEVEL OF FT METHYLATION WHILE REPELLENTS DECREASE THE LEVEL OF FT METHYLATION THE METHYL GROUPS ARE ADDED BY THE FT METHYLTRANSFERASE CHER AND REMOVED BY THE METHYLESTERASE FT CHEB. recN: DNA repair protein RecN" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2Z2" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004089" FT /db_xref="InterPro:IPR004090" FT /db_xref="InterPro:IPR024478" FT /db_xref="UniProtKB/TrEMBL:A1K2Z2" FT /protein_id="CAL93197.1" FT /translation="MRIRSKLLALVACGVIGLMVSGAVSVVGMRSVGSGLQHIDRNSLP FT AILQLETINEALASIARRTLQAAIWRDESGAYGQQELGEVLALKQAAWARLDAAFAAYG FT ALPRDAAVEPLWKAFDDSFTLWRRLDAPMTELLEAMVRGMTPEAQREAFASYYEFHYDQ FT YRALEAAQASLQALVDATAAQVREDAALAVARSERSLSLQTAVSVAAILALCWMAFSVL FT RSVLRPIEALRTTVREIATRSDFTLRAPGEGKDEVGETVAAFNGLVERTRAALVDVRER FT AAQMHEAVAEVSRAALGVAARAERQNVSTSAMAASLEGLTASISQVSGHAAAARELSVA FT AGERAGAGGRVLGDTLGAMECIADRVGDAGQLIDRLVGGLREVTQVVAVIREVAEQTNL FT LALNAAIEAARAGEQGRGFAVVADEVRRLAERTGDATGNIAAIMARIEQAAAMSTQGMA FT AAVEEARQGEALAGEAGGHVQAIQQGAGRAAAAVTDISQALQAQSSAGQDIVRHVDEIA FT RMSEESRLASAEAADAARRLDELAATVGATVGRFRT" FT CDS complement(612146..613330) FT /transl_table=11 FT /gene="araJ" FT /locus_tag="azo0581" FT /product="putative transmembrane efflux precursor protein" FT /function="Arabinose efflux permease" FT /note="May be involved in either the transport or FT processing of arabinose polymers.Belongs to the major FT facilitator superfamily. 36% MFS.IPR005828; FT Sub_transporter. TMhelix:12." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Z3" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:A1K2Z3" FT /protein_id="CAL93198.1" FT /translation="MPLPLLALAIASFGIGTTEFVIMGLLPEVARDLGVDIPRAGMLVS FT GYAMGVVIGAPILAVVISRMQRRRALLGLIGMFIAGNLLCALAPDYAALMAARIATAFC FT HGAFFGLGAVVAAGLVAPERRAQAIALMFTGLTLANVLGVPLGTLLGQHAGWRATFWAV FT VAIGVAAALTLHRWLPHDLGAGSSRGLLNEVRALRRTQVLLAMLISVLSSASLFSVFTY FT IAPMLLEVTGISPRGVTLVLLLFGAGLTLGNLLGGRLADWRLMPAVIGIFVAVIAVLAL FT LPAALPVPLGAVTVVFLWGVAAFALISPLQMRVVNEAAGAPNLASTVNQGAFNLGNAIG FT AWVGGVAIRQGVGYDGIPWVGVALAILALAFSIGAHRLEARSLAAARPATEGGR" FT CDS complement(613443..614654) FT /transl_table=11 FT /locus_tag="azo0582" FT /product="putative permeases of the major facilitator FT superfamily" FT /function="Permeases of the major facilitator superfamily" FT /note="Permease,member of the Major Facilitator FT Superfamiliy (MFS)transporters. MFS are single-polypeptide FT secondary carriers capable only of transporting small FT solutes in response to chemiosmotic ion gradients. 25% FT MFS.IPR005828; Sub_transporter.IPR005829; FT Sug_transporter.InterPro: General substrate transporters FT Pfam:PF00083; sugar_tr; 1. TMHelix: 12" FT /note="Specificity unclear" FT /db_xref="GOA:A1K2Z4" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:A1K2Z4" FT /protein_id="CAL93199.1" FT /translation="MMSNIQAAHAAFVPAEAGPRPALVLLLAAGAGLSVASIYYSQPML FT GVLAGDLGADAARVGLIPTLTQLGYACGILLLAPLGDRHDRRGIIALKAALLALALLAS FT GLAPGVGLLLAASLGVGLAATLAQDIVPAAAALAPERQRGRIVGTVMTGLLLGILLSRV FT VSGFVAEQFGWRTMYFIAAFAVAAIGVVAWRGIPHIPPTTRASYLALLGSLRGLWMAHP FT ALRRAALAQGLLSVGFSAFWSTLAVMLHDSFQLGSAAAGAFGLAGAAGALAAPLAGRLA FT DRRGPQPVTVLGAALALLAFAAMWLAPLLPPSARLGLIVASAIGFDFGIQAALVAHQSI FT VYSLDAGARSRINALLITTMFVGMAAGSSLGSLALAHAGWNGVIGVAVAASAVALALRL FT GARR" FT CDS 614751..615716 FT /transl_table=11 FT /gene="lysR" FT /locus_tag="azo0583" FT /product="putative transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="Putative transcriptional regulator, LysR family," FT /note="Family membership" FT /db_xref="GOA:A1K2Z5" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K2Z5" FT /protein_id="CAL93200.1" FT /translation="MSELNLEPLAGADRVELLRTLVRIVEAGSLSAAAQQLGITQPTVS FT RRLQALERALGLKLLQRSTHGMKLTGEGERCYAHARDLIERWQAMETDLHGARDEPRGN FT LRVLVPHAFGQGQLIAPLVDYLRRYPEVAVEWLLHDRRPDFLAEGIDCAIQVGEVADPG FT VVAVRLAEVPRIVVAAPGAWGEGAPPAAPEALAAMPWLALRTYYRDEVLLVRSGDGERS FT RFPIRPRLSTDSLYALRTAALTGLGACVTSAWVVADDVAGGKLCHLLPEWEAPPLPVYL FT VYPHARHYPAKLRVFNAMMRACMPALGGMRPPTPASAGLG" FT CDS complement(615741..616574) FT /transl_table=11 FT /gene="metF" FT /locus_tag="azo0584" FT /product="5,10-methylenetetrahydrofolate reductase (FADH2" FT /function="510-methylenetetrahydrofolate reductase" FT /note="510-methylenetetrahydrofolate reductase InterPro: FT Methylenetetrahydrofolate reductase fadh2: FT 510-methylenetetrahydrofolate reductase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Z6" FT /db_xref="InterPro:IPR003171" FT /db_xref="InterPro:IPR004620" FT /db_xref="UniProtKB/TrEMBL:A1K2Z6" FT /protein_id="CAL93201.1" FT /translation="MHKTELSIEFFPPQTAEGAEKLRAVQARLAELKPTFFSVTYGAGG FT STRERTFATVKEIAASGSEAAPHLSCIGSTRDSIRAILAEYADAGVKRIVALRGDLPSG FT VVDPGEFRYANELVEFIRAETGSRFRIEVAAYPEWHPQAKTPADDLAAFKRKMDAGADS FT AITQYFYNLDAYLHFVDAVRKLGIDKPVVPGIMPIGSFSKLARFSDACGAEIPRWMRRK FT FESYGDDADAIRAFGLDVVTELCEKLLAAGVPGLHFYSMNQSALTTEICKRLGLA" FT CDS complement(616561..617238) FT /transl_table=11 FT /gene="tlyA" FT /locus_tag="azo0585" FT /product="conserved hypothetical protein" FT /function="predicted rRNA methylase" FT /note="Probable hemolysin.46% identity to TrEMBL;Q7NQ39. FT Has PF01728, FtsJ-like methyltransferase; FT IPR002877,RrmJFtsJ_mtfrase; This family consists of FtsJ FT from various bacterial and archaeal sources FtsJ is a FT methyltransferase, but actually has no effect on cell FT division. FtsJ's substrate is the 23S rRNA. The 1.5 A FT crystal structure of FtsJ in complex with its cofactor FT S-adenosylmethionine revealed that FtsJ has a FT methyltransferase fold. This family also includes the N FT terminus of flaviviral NS5 protein. It has been FT hypothesised that the N-terminal domain of NS5 is a FT methyltransferase involved in viral RNA capping." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Z7" FT /db_xref="InterPro:IPR002877" FT /db_xref="UniProtKB/TrEMBL:A1K2Z7" FT /protein_id="CAL93202.1" FT /translation="MQWNGQILKKASHSLPIDATIELVADPDDAFERYVSRGGLKLAGA FT LAASGLDPAGRVCLDVGQSTGGFTDCLLQAGATRVVGVEVGHGQLHPRLAGEPRCITLE FT GVNARHLTAADLAGHCPPGGFGLIVCDASFISLTLLLPQWPALLAADGDILALVKPQFE FT VGPQGLSKGGIVRDASRYAEVERKLRIAAAAAALDVRGWYDSPITGTDGNREFFIWMRH FT AQD" FT CDS complement(617454..617696) FT /transl_table=11 FT /locus_tag="azo0586" FT /product="Hypothetical protein" FT /note="Hypothetical protein. Weak Homology with hits in the FT Database. No domains, repeats, motifs or features could be FT predicted above threshold value." FT /db_xref="UniProtKB/TrEMBL:A1K2Z8" FT /protein_id="CAL93203.1" FT /translation="MSTRRLTNHQACLESFSLQLRRDIKENLKAWTTMDPIQARTRRAA FT YAHVVVLLKQAAAETDIPLEDLGLAGYEVPDIETT" FT CDS complement(617790..619199) FT /transl_table=11 FT /gene="acyH" FT /locus_tag="azo0587" FT /product="Adenosylhomocysteinase" FT /function="S-adenosylhomocysteine hydrolase" FT /EC_number="3.3.1.1" FT /note="Adenosylhomocysteinase. InterPro: FT S-adenosyl-L-homocysteine hydrolase ahcY: FT adenosylhomocysteinase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K2Z9" FT /db_xref="InterPro:IPR000043" FT /db_xref="InterPro:IPR015878" FT /db_xref="InterPro:IPR020082" FT /db_xref="UniProtKB/TrEMBL:A1K2Z9" FT /protein_id="CAL93204.1" FT /translation="MNTVADIKDYVIADLSLADWGRKEIRIAETEMPGLMAIREEYAAR FT QPLKGARITGSLHMTIQTAVLIETLTALGAEVRWASCNIFSTQDHAAAAIAASGVPVFA FT VKGESLEDYWDYTHRIFEWKDGGYSNMILDDGGDATLLLHLGARAEQDIAVLDKPDSEE FT ATVLFASIKAKLKTDPTWYSTRLAQIKGVTEETTTGVHRLYQMHAKGELKFPAINVNDS FT VTKSKFDNLYGCRESLVDGIKRATDVMIAGKIGVVLGYGDVGKGCAQSLRGLGATVWVT FT EIDPICALQAAMEGFRVVTMEDAAALGDIFVTTTGNVGVITHEHMKAMKNNAIVCNIGH FT FDSEIEVASLRQYEWENIKPQVDHIIFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSF FT ANQTLAQIELFTKTGDYPVGVYVLPKQLDEMVARLHLKKIGANLTVLSQAQADYIGVPV FT EGPYKPNHYRY" FT CDS 619475..620047 FT /transl_table=11 FT /locus_tag="azo0588" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT PA0776 of Pseudomonas aeruginosa of 30% FT (trembl|Q9I5G2(SRS)) No domains predicted Signal Peptide FT present. No TMH present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K300" FT /protein_id="CAL93205.1" FT /translation="MTMKTRFDVVVLVLVVGGCSAMLPKSHQETVSPWNTFEEAKAAFD FT KIELGATDREAVHQLGFNPSSTPNVQILNYSQIAHVVLPGDRLIPDGEVPTAIRKCVLA FT QERCVGYQLEESRIKRNRVGGFWGDFLNFHRETLTTGWRFNALVVLIDNHVVFKQWSGQ FT PSIREVGVSRNPLGPLQGAGERLSTFQ" FT CDS complement(620087..621253) FT /transl_table=11 FT /gene="metK" FT /locus_tag="azo0589" FT /product="methionine adenosyltransferase" FT /function="S-adenosylmethionine synthetase" FT /EC_number="2.5.1.6" FT /note="S-adenosylmethionine synthetase (EC 2.5.1.6) (AdoMet FT synthetase) (MAT). Catalyzes the formation of FT S-adenosylmethionine from methionine and ATP. The overall FT synthetic reaction is composed of two sequential steps FT AdoMet formation and the subsequent tripolyphosphate FT hydrolysis which occurs prior to release of AdoMet from the FT enzyme (By similarity). InterPro: S-adenosylmethionine FT synthetase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K301" FT /db_xref="InterPro:IPR002133" FT /db_xref="InterPro:IPR022628" FT /db_xref="InterPro:IPR022629" FT /db_xref="InterPro:IPR022630" FT /db_xref="InterPro:IPR022631" FT /db_xref="InterPro:IPR022636" FT /db_xref="UniProtKB/Swiss-Prot:A1K301" FT /protein_id="CAL93206.1" FT /translation="MANEFLFTSESVSEGHPDKVADQISDGVLDAILAEDPKARVACET FT LVSTGLVVISGEITTSAHPNYREIAQDVVRRIGYDNSDIGFDYKSCAVLAAINRQSSDI FT AQGVNEGEGLDLDQGAGDQGLMFGYATNETPSLMPLPIYYAHRIMQRQAEVRKDGRLPW FT LRPDAKSQLTVKYVDGKPVAIDTVVVSTQHNPEVSHAQISEAVIEEIIKPVLPKELMQG FT EVRYLINPTGRFVIGGPHGDCGLTGRKIIVDTYGGAAHHGGGAFSGKDPSKVDRSAAYA FT GRYVAKNVVAAGLADKCEVQVAYAIGVAKPVSLMVNTFGTGKIADDKIVDLIRAHFDLR FT PKAIIQTLDLLRPIYSRTAAYGHFGRDEPEFTWEQTDKASALRAAAGL" FT CDS 621534..622355 FT /transl_table=11 FT /gene="htrB" FT /locus_tag="azo0590" FT /product="putative lipid A biosynthesis lauroyl FT acyltransferase" FT /function="Lauroyl/myristoyl acyltransferase" FT /EC_number="2.3.1.-" FT /note="Putative lipid A biosynthesis lauroyl FT acyltransferase. Homology to htrB of E. coli of 27% FT (sprot|HTRB_ECOLI) ACYLATES THE INTERMEDIATE (KDO)2-LIPID FT IVA TO FORM (KDO)2-(LAUROYL)-LIPID IVA. HAS 10 FOLD FT SELECTIVITY FOR LAUROYL- ACP OVER MYRISTOYL-ACP. Pfam: FT Bacterial lipid A biosynthesis acyltransferase no singal FT peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K302" FT /db_xref="InterPro:IPR004960" FT /db_xref="UniProtKB/TrEMBL:A1K302" FT /protein_id="CAL93207.1" FT /translation="MPLSWLHRLGGWMGWLVYWCAPGYRRRLRRNLALATGREDRALLH FT AAVAEAGRQALELPWLWLRPLDQVVAKVVRVEGWELVEAAERAGAGILFFTPHLGCFEI FT TATCYAAHAPITVLYRPPRKVALQPLMEAGRARGNMRIAPADISGVRALVKTLRSKEAV FT GMLPDQVPAAGEGMWVPFFGRPAWTMTLGARLAEVKGVHVIYCWAERLPRGEGYVFRMF FT GPTEPLEGDLEARCATINREIERLILQCPAQYLWGYHRYKRPKGARAKEAQ" FT CDS 622384..623160 FT /transl_table=11 FT /gene="msbBa" FT /locus_tag="azo0591" FT /product="putative lipid A biosynthesis FT acyltransferase,truncated" FT /function="lipid A biosynthesis acyltransferase" FT /EC_number="2.3.1.-" FT /note="Putative Lipid A biosynthesis acyltransferase FT protein Homology to msbB of of E. coli of 27% (AAA24181). FT Homology only with the N-terminus. no signal peptide. 1 FT TMH. Tigrfam: lipid_A_htrB, lipid A biosynthesis lauroyl FT (or palmitoleoyl) acyltransferase. Pfam: FT Lip_A_acyltrans,Bacterial lipid A biosynthesis FT acyltransferase." FT /note="Family membership" FT /db_xref="GOA:A1K303" FT /db_xref="InterPro:IPR004960" FT /db_xref="UniProtKB/TrEMBL:A1K303" FT /protein_id="CAL93208.1" FT /translation="MLTRLGVAVFWLLHWLPLPLLARIGELFGLLLYLFAVPRRRVVAT FT NLRLCFPELSDGERRRLARAHFRIIGRSLLERGLLWWASPARLERLVAVEGLERLRALQ FT AEGRPVLLLTPHFLGLDMGGTRLSMLGDFVSIYARQKNKVLDRWLYHGRSRFGDQLLLS FT RQDGVRSTVKAMKAGRPFYSTCRTWTTAARTRSSCPSSACLPPPSPGCRAWRGCRAPPC FT CPASPTSCPVAAATRWRSASPGRTFPVTTWRPIPHA" FT CDS 623157..623261 FT /transl_table=11 FT /gene="msbBb" FT /locus_tag="azo0592" FT /product="putative lipid A biosynthesis FT acyltransferase,truncated" FT /function="Lauroyl/myristoyl acyltransferase" FT /EC_number="2.3.1.-" FT /note="Putative Lipid A biosynthesis acyltransferase FT protein Homology to.msbB of of E. coli of 27% (AAA24181). FT Homology only with the N-terminus. no signal peptide. 1 FT TMH. Tigrfam: lipid_A_htrB, lipid A biosynthesis lauroyl FT (or palmitoleoyl) acyltransferase. Pfam: FT Lip_A_acyltrans,Bacterial lipid A biosynthesis FT acyltransferase." FT /note="Function unclear" FT /db_xref="GOA:A1K304" FT /db_xref="InterPro:IPR004960" FT /db_xref="UniProtKB/TrEMBL:A1K304" FT /protein_id="CAL93209.1" FT /translation="MNAWIEAKVRTMPEQYYWVHRRFKTRPPGEARFY" FT CDS complement(623255..623521) FT /transl_table=11 FT /locus_tag="azo0593" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT Daro03000819 of Dechloromonas aromatica of 32% FT (gi|46140899|ref|ZP_00152594.2|(NBCI ENTREZ)). No domains FT predicted. signal peptide. 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K305" FT /protein_id="CAL93210.1" FT /translation="MQIRASSPPAAARRRIPVAAWLLGVPGLAALGAGLALLLGDFSGL FT HPILAEPGTALALIVSALALLGSAAFPLVLAHLARQDGPAPGQ" FT CDS 623683..624516 FT /transl_table=11 FT /gene="dapF" FT /locus_tag="azo0594" FT /product="DapF protein" FT /function="Diaminopimelate epimerase" FT /EC_number="5.1.1.7" FT /note="Diaminopimelate epimerase catalyzes the FT isomeriazation of L,L- to D,L-meso-diaminopimelate in the FT biosynthetic pathway leading from aspartate to lysine. This FT enzyme is a protein of about 30 kDa. Two conserved FT cysteines seem to function as the acid and base in the FT catalytic mechanism. Similar to TREMBL:Q82U84 (58%). Pfam FT (PF01678): Diaminopimelate epimerase TIGRfam (TIGR00652): FT Diaminopimelate epimerase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K306" FT /db_xref="InterPro:IPR001653" FT /db_xref="InterPro:IPR018510" FT /db_xref="UniProtKB/Swiss-Prot:A1K306" FT /protein_id="CAL93211.1" FT /translation="MHIRFTKMHGLGNDFVVIDATRTPVDLTPARVKAIADRHFGVGCD FT QLLVVEPPGSDEVDFRYRIFNADGGEVEQCGNGARCFVRFVHDKGLTDKREIRVETRAG FT VIAPALRPDGLVSVDMGVPELSPARIPFVSDSDAWVQPLQLAEDTVAITAVSMGNPHAV FT QVVADVDTAPVARQGAEIECHPRFPARVNAGFMQVVDAGHIRLRVFERGAGETLACGTG FT ACAAVVAGIGRGLLVSPVRVETRGGELEIAWAGPGTPVVMTGPAVTVFEGELELP" FT CDS 624557..625210 FT /transl_table=11 FT /locus_tag="azo0595" FT /product="3',5'-cyclic-nucleotide phosphodiesterase" FT /function="uncharacterized protein conserved in bacteria" FT /EC_number="3.1.4.17" FT /note="Conserved hypothetical protein. Coils2 Program FT reporting presence of 1 Coiled-Coil. Has SMART;SM00065,GAF FT domain;This domain is present in phytochromes and FT cGMP-specific phosphodiesterases. cGMP-dependent FT 3',5'-cyclic phosphodiesterase catalyses the conversion of FT guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. FT A phytochrome is a regulatory photoreceptor which exists in FT 2 forms that are reversibly interconvertible by light, the FT PR form that absorbs maximally in the red region of the FT spectrum, and the PFR form that absorbs maximally in the FT far-red region. This domain is also found in NifA, a FT transcriptional activator which is required for activation FT of most Nif operons which are directly involved in nitrogen FT fixation. NifA interacts with sigma-54." FT /note="Specificity unclear" FT /db_xref="GOA:A1K307" FT /db_xref="InterPro:IPR003018" FT /db_xref="InterPro:IPR007435" FT /db_xref="UniProtKB/TrEMBL:A1K307" FT /protein_id="CAL93212.1" FT /translation="MNPNDVARYLRDNPDFLAQHGELFTELTVPHPQHGGQAISLAERQ FT LYALRDKIRQLESKLAELIRFGEENDDISEKVHRLAVALLGARGYAAVRQALFNCLQED FT FAVPHVALRLWDVGGEGTGPDFDAVSEAARLHALDLRHPSCGAPGSIEIVGWFGEAAPH FT IRSMALMPLRRQGETVGVLALGSEEGERFYPEMGTLYLGRIAELCAAALLRELA" FT CDS 625290..626201 FT /transl_table=11 FT /gene="xerC" FT /locus_tag="azo0596" FT /product="site-specific recombinase" FT /function="Site-specific recombinase XerC" FT /note="Tyrosine recombinase xerC. Site-specific tyrosine FT recombinase which acts by catalyzing the cutting and FT rejoining of the recombining DNA molecules. Binds FT cooperatively to specific DNA consensus sequences that are FT separated from xerD binding sites by a short central region FT forming the heterotetrameric xerC-xerD complex that FT recombines DNA substrates. The complex is essential to FT convert dimers of the bacterial chromosome into monomers to FT permit their segregation at cell division. It also FT contributes to the segregational stability of plasmids at FT ColE1 xer (or cer) and pSC101 (or psi) sites. In the FT complex xerC specifically exchanges the top DNA strands (By FT similarity)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K308" FT /db_xref="InterPro:IPR002104" FT /db_xref="InterPro:IPR004107" FT /db_xref="InterPro:IPR010998" FT /db_xref="InterPro:IPR011010" FT /db_xref="InterPro:IPR013762" FT /db_xref="InterPro:IPR023009" FT /db_xref="InterPro:IPR023109" FT /db_xref="UniProtKB/TrEMBL:A1K308" FT /protein_id="CAL93213.1" FT /translation="MSVPREAPLAPLTDECEAYLAYLGDQRRAAPLTLENYRRDLHRLE FT RLGDGRALMTLGAADIRRFVARLHGEGLSGRSIARVLSCWRGLYRWLLRRRLIPANPVD FT GIRAPKSPRLLPRALSPDQAQALLDPPAEAALEVRDLAMFELFYSSGLRLSELAGLDVG FT GGLDPAEGMVTVLGKRGKTRSVPVGAHAWAALKAWDTVRAAIAPAAEPALFVTRSGRRM FT SPSAIRDRLARRARSVGLGVHVHPHMLRHSFASHLLQSSGDLRAVQELLGHSSIRSTQV FT YTHLDFQHLARIYDAAHPRARK" FT CDS 626345..626848 FT /transl_table=11 FT /locus_tag="azo0597" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ebA3954 FT of Azoarcus sp. EbN1 of 56% (gnl|keqq|eba:ebA3954(KEGG)). FT No domains predictied. No signal peptide. No TMHs. FT helix-turn-helix present." FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K309" FT /protein_id="CAL93214.1" FT /translation="MPNDSIPQLEPGVVGGPGAADEVADDKQRVLKRVALLLARHEVRH FT LRRWFEEFDRDILLPILLGEIALHNIGATENGKGVALGPDGDLHCPLKPCNAYSIAAAT FT GLPRETVRRKIVRLIELGWINKRHNGHLYVTSAALRHFGGVLSSRELGDLIETADHARR FT LLES" FT CDS 626914..628101 FT /transl_table=11 FT /locus_tag="azo0598" FT /product="probable SAM dependent methyl transferase" FT /function="predicted SAM-dependent methyltransferases" FT /EC_number="2.1.1.-" FT /note="Hypothetical protein yccW TREMBL:Q8Y3C9: 52% FT identity, 62% similarity. InterPro; IPR002478; PUA. FT InterPro; IPR000051; SAM_bind. Pfam:Met_1:Met-10+ FT like-protein SMART; SM00359 TIGR00095: conserved FT hypothetical protein No transmembrane helices" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K310" FT /db_xref="InterPro:IPR002478" FT /db_xref="InterPro:IPR015947" FT /db_xref="InterPro:IPR019614" FT /db_xref="UniProtKB/TrEMBL:A1K310" FT /protein_id="CAL93215.1" FT /translation="MARLFLHPGKERSLLRRHPWIFAGSVERLEGRARAGDTVDVLSAD FT GRVLGRAAWSPVSQIRARMWCFDADTTIDHAFFKRRVAAAVAARQSHPLLTGQDGLRLI FT HGESDGLPGVIADRYGDVVVVQLTSAGADKWRDAIVAALVQATGCSTVYERSDSDVRGL FT EGLEPKTGCVHGALPETLQIVEHGVRMEVDVAGGHKTGFYLDQRDNRLLTGRLARGRRV FT LNCFCYTGGFSLQALAGGAESVLSIDSSGPALATAARNLALNPQLDAARADWWEEDVFE FT ALRALRAEGRSFDLIVLDPPKFAPSAAHAERAARAYKDINLFGFRLLAPGGILMTYSCS FT GGIGLELFQKIVAGAASDAGVDARILHRLSAAPDHPIGLSVPEGEYLKGLAIQIA" FT CDS complement(628098..628448) FT /transl_table=11 FT /locus_tag="azo0599" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT ebA3957 of Azoarcus sp. EbN1 of 38% FT (gnl|keqq|eba:ebA3957(KEGG)). No domains predicted. signal FT peptide. 2 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K311" FT /protein_id="CAL93216.1" FT /translation="MRSAQVLMFCLCVIGGLFLLVQAPSFFMPDRWDPAVGRAFGPLQS FT RLLGAALLAIAWLGLDYLRNRYYSETRQLPGVPQQRRYFAVLVLALVLLSAAFNLAPPG FT PNPDYRPPASAR" FT CDS complement(628448..628666) FT /transl_table=11 FT /locus_tag="azo0600" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. no homology of the FT entire protein to the data bank. no domains predicted. FT signal peptide. no TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K312" FT /protein_id="CAL93217.1" FT /translation="MLVPLLLGLLALALLAVLATRGRATQSRRRAAHGTDGAGATTSAT FT GDSDGNDGACDGGGDGGSGGDGGGGGD" FT CDS complement(628671..629729) FT /transl_table=11 FT /gene="ruvB" FT /locus_tag="azo0601" FT /product="holliday junction DNA helicase" FT /function="Holliday junction resolvasome helicase subunit" FT /note="Holliday junction DNA helicase ruvB. The ruvA-ruvB FT complex in the presence of ATP renatures cruciform FT structure in supercoiled DNA with palindromic sequence FT indicating that it may promote strand exchange reactions in FT homologous recombination. RuvAB is an helicase that FT mediates the Holliday junction migration by localized FT denaturation and reanneling (By similarity). InterPro: FT Holliday junction DNA helicase RuvB" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K313" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR004605" FT /db_xref="InterPro:IPR008823" FT /db_xref="InterPro:IPR008824" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/Swiss-Prot:A1K313" FT /protein_id="CAL93218.1" FT /translation="MIETDKLRAAAPERLISPQPADRQEDAVERALRPKRLAEYVGQAK FT IREQLEIFIHAAKKRSEALDHVLLFGPPGLGKTTLAHIVAAEMGVNLRQTSGPVLERAG FT DLAALLTNLEPHDVLFIDEIHRLSPVVEEILYPALEDFQIDIMIGEGPAARSVKLDLPP FT FTLVGATTRAGMLTNPLRDRFGIVSRLEFYTPDELGFIVSRSARLLNVEIDDDGALEIA FT RRARGTPRIANRLLRRVRDYAEVKAGGHITRAVADAALRMLDVDSLGLDLMDRKMLSAM FT LEKFGGGPVGLDNLAAAIGESTDTIEDVIEPYLIQQGYLQRTPRGRMATHSIWQHFGLA FT PPRPGGTDLFGG" FT CDS complement(629785..630384) FT /transl_table=11 FT /gene="ruvA" FT /locus_tag="azo0602" FT /product="holliday junction DNA helicase" FT /function="Holliday junction resolvasome DNA-binding FT subunit" FT /note="Holliday junction DNA helicase ruvA. The ruvA-ruvB FT complex in the presence of ATP renatures cruciform FT structure in supercoiled DNA with palindromic sequence FT indicating that it may promote strand exchange reactions in FT homologous recombination. RuvAB is an helicase that FT mediates the Holliday junction migration by localized FT denaturation and reanneling. RuvA stimulates in the FT presence of DNA the weak ATPase activity of ruvB (By FT similarity). InterPro: Bacterial DNA recombination protein FT RuvA" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K314" FT /db_xref="InterPro:IPR000085" FT /db_xref="InterPro:IPR003583" FT /db_xref="InterPro:IPR010994" FT /db_xref="InterPro:IPR011114" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR013849" FT /db_xref="InterPro:IPR016027" FT /db_xref="UniProtKB/Swiss-Prot:A1K314" FT /protein_id="CAL93219.1" FT /translation="MIGRISGLLLEKNPPQILVDAHGVGYELEVPMSTFYGLPATGTQV FT SLHTHLAIREDGHFLYGFATDEERTAFRQLLKVSGIGARTALAVLSGLSVSDLAQAVAL FT QEAGRLVKIPGIGKKTAERLLLELRDKLGKALPQVAGARLAAVAGGAPDAKSDILNALL FT ALGYNEKEALGAMKGLAEDTGVSDGIRQALKLLSKA" FT CDS 630563..631267 FT /transl_table=11 FT /locus_tag="azo0603" FT /product="conserved hypothetical membrane protein" FT /function="predicted branched-chain amino acid permease FT (azaleucine resistance)" FT /note="Conserved hypothetical membrane protein. Homology to FT BP3397 of B. pertussis of 41% (bpe:BP3397(KEGG)). Tigrfam: FT azlC: azlC protein (azlC). 6 TMHs no signal peptide" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR011606" FT /db_xref="UniProtKB/TrEMBL:A1K315" FT /protein_id="CAL93220.1" FT /translation="MNPAFRDGAREGIRDFMPMSVGLLPWAVVTGIAMVSAGLSPLQAA FT GMNLIVYAGTAQLGTLPLLASGAPLWLIVLTALALNLRFVIFSAALAPAFHDYGLARRL FT ASSYLLVDGVFAMCTERLLKADDPHWRWGYYLGPSLWVWTLWQLFTLAGVLGAGIVPQG FT WSLEFMATIALLVMMLPMSRTRPMLVAALAGGIATVLLRGLPLRLGLIAGIAVGILAGF FT AAEHGLQKRGAR" FT CDS 631264..631590 FT /transl_table=11 FT /locus_tag="azo0604" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT RS04896 of Ralstonia solanacearum o 43% (trembl|Q8Y1W8) Has FT PF06063, Domain of unknown function FT (DUF931);IPR010337;Family of transmembrane proteins with FT undetermined function. singal peptide. 2 THMs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR008407" FT /db_xref="UniProtKB/TrEMBL:A1K316" FT /protein_id="CAL93221.1" FT /translation="MSGDALLWLTFCLIGMTTVATRGSFILLGERARLPPVVQRLLRYA FT PAAALACLVMPDLLLDDGALDPLNPKLAAGLVVVLVATRWRNPWLPFVCGMGVLLLLRR FT GLGW" FT CDS complement(631597..631851) FT /transl_table=11 FT /locus_tag="azo0605" FT /product="conserved hypothetical protein" FT /note="Hypothetical protein. Homology to Daro03002672 of FT Dechloromonas aromatica of 51% FT (gi|41723577|ref|ZP_00150487.1|(NBCI ENTREZ)). Has PF04023, FT FeoA domain;IPR007167; This family includes FeoA a small FT protein, probably involved in Fe2+ transport. This presumed FT short domain is also found at the C-terminus of a variety FT of metal dependent transcriptional regulators. This FT suggests that this domain may be metal-binding. In most FT cases this is likely to be either iron or manganese. no FT signal peptide. no TMHs" FT /db_xref="GOA:A1K317" FT /db_xref="InterPro:IPR007167" FT /db_xref="InterPro:IPR008988" FT /db_xref="UniProtKB/TrEMBL:A1K317" FT /protein_id="CAL93222.1" FT /translation="MNAPASPAHERIRLTGTPVGRQARIADFGDGIDPLQREQLHAYGL FT SAPHQVTVLQQQPMTVVLCDHVELALEHEVARNIWVEAD" FT CDS complement(631860..633851) FT /transl_table=11 FT /gene="feoB" FT /locus_tag="azo0606" FT /product="putative ferrous iron transport protein B" FT /function="Fe2+ transport system protein B" FT /note="Ferrous iron transport protein B, FeoB.Probable FT GTP-driven transporter of ferrous ion.Invovled in iron II FT uptake. 29% FeoB.IPR005289; GTP-bindding_dom.IPR005225; FT Small_GTP. Pfam:PF02421; FeoB; 1.TIGRFAMs TIGR00437; feoB; FT 1.TIGR00650; MG442; 1. TIGR00231; small_GTP; 1. TMHelix:12 FT Siganl pepetide present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K318" FT /db_xref="InterPro:IPR003373" FT /db_xref="InterPro:IPR006073" FT /db_xref="InterPro:IPR011619" FT /db_xref="InterPro:IPR011640" FT /db_xref="InterPro:IPR011642" FT /db_xref="UniProtKB/TrEMBL:A1K318" FT /protein_id="CAL93223.1" FT /translation="MSHRHNSPSDPAMTLAATAASPARTFALVGHPNVGKSVLFHRLTG FT TYVNVSNYPGTTVEVARATPRFDREASLLDTPGVLALPSRSDDERATMRALLQEDMRTL FT IQVGDAKNLRRTLNLTALLAELGVPMVMALNMTDEASARGVTVDSAALAEALGVPVVAT FT VATGGEGVAPLTDALPRACAPAPLLRYDADTEAAIERIAALITAHAPHPRLAARGLAIL FT LLGHDSEVVRWIDEHAGDKAALIHQALIAASNIGKEPLAARLARERGRAAEALARTVSH FT QAAGKERTLSLLVGQLAVHPLWGWPMLLGVLFLVYLFVGDFGAGTLVGLLEEDFFGGVL FT NPAFTEFVQQHISAPWLADLLVGEYGLWTMGMTYALALILPIVTTFFLAFGVLEDSGYF FT SRLSVIANRSFAAIGLNGRAVLPMVLGLGCVTMATLTTRILHTPRERLITTFLMALAIP FT CSAQLGVVLGLLGGISLGALTIWGITIACVLLFTGWLAGKLVKGRRIPLVTELPPMRMP FT VLGNVLKKTGGRLKWYLIEVIPLFLIGTFIMFVLDRLGILPWIIKAGEPVVTGWLGLPP FT EASAAFVMGFLRRDFGATGLFALSHELSMVQAVVGMVTITLFVPCIASVMMIVKEQGLR FT TAALMLAMIMPTAFLIGGILNHVLRLFF" FT CDS 634049..636247 FT /transl_table=11 FT /locus_tag="azo0607" FT /product="putative TonB-dependent receptor" FT /function="Outer membrane receptor for monomeric catechols" FT /note="Outer membrane TonB-dependent, hydroxamate-type FT ferrisiderophore receptor. Probably involved in iron FT transport. 30% TONB_C.IPR000531; TonB_receptor.IPR010105; FT TonB_siderophor. InterPro: TonB-dependent receptor protein FT Pfam:PF00593; TonB_dep_Rec; 1. TIGRFAMs:TIGR01783; FT TonB-siderophor; 1. Signal peptide present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K319" FT /db_xref="InterPro:IPR000531" FT /db_xref="InterPro:IPR010105" FT /db_xref="InterPro:IPR012910" FT /db_xref="UniProtKB/TrEMBL:A1K319" FT /protein_id="CAL93224.1" FT /translation="MKKKLARKPAAQAAAAPAQPVRLLPLGAALMAGGLSLSAMAQDTA FT TPAPKEKALSAVTVNATTEAPPEDGYRATATRVGKTLQDPHDVPQAITTVTRSLMEEQQ FT VGSLKEALRNVSGLTFNAAEGGRSGDNMMLRGFYTYGDIYLDGIRDTAQYNRETFNLEQ FT VDVLRGAAAMLFGRGQAGGVINQVSKTPMLVDRNRVTGSVGTDDYRELTGDFNKVLGDT FT TAVRLNVMKRDEGSWRSNPATGTEPEIHREGAAASIGFGLFTDNELIVSHQYLRTDDNP FT DYGISFDNATHKPTKRFDESDFWGIDQNFDESETNISTVTHTYRFTGKTQLRTQLRYSN FT YKRAYWASAPSNTVAPSDRGNAPKTRKSDTDNLVLQSDFSTEFNALGMKHELVTGIEYL FT HEDSVRWGLLNLGTNARPYYSSSVVNRASASKYEGDTYSVYAQDSIEFVKDWKVVLGAR FT RDFMDAEYSAVRSPELKFNENSYRAGLSWQPSEYAHYYLSWSDSFSPTADLYQLSGGEF FT PPERSDVVELGAKFMFFEGDLAFRTALYRATKDWERNNDLESTASILTRKRRTDGLEFE FT LAGRITDKWEVFAGLALMDSEILKVAVNRNATTGVVTSANPNFKGERARNTPTYTFNFW FT STYALGNGWKVGGGAEGKGERYGYNPSAGGTAAFNPNKAPAYVRWDAMVAYEQPKWAVR FT LNLRNLFDEVYYDAIYDNGGFTVPGTRRSAILTTEFKF" FT CDS 636324..637007 FT /transl_table=11 FT /gene="ybiX" FT /locus_tag="azo0608" FT /product="putative PKHD-type hydroxylase" FT /function="uncharacterized iron-regulated protein" FT /EC_number="1.14.11.2" FT /note="Putative PKHD-type hydroxylase protein, 69% FT Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% FT identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase FT alpha subunit homologues: IPR006620; Pro_4_hyd_alph; FT Mammalian enzymes catalyse hydroxylation of collagen, for FT example. Prokaryotic enzymes might catalyse hydroxylation FT of antibiotic peptides. These are 2-oxoglutarate-dependent FT dioxygenases, requiring 2-oxoglutarate and dioxygen as FT cosubstrates and ferrous iron as a cofactor. Has FT PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This FT family contains members of the 2-oxoglutarate (2OG) and FT Fe(II)-dependent oxygenase superfamily. This family FT includes the C-terminal of prolyl 4-hydroxylase alpha FT subunit. The holoenzyme has the activity catalysing the FT reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> FT procollagen trans- 4-hydroxy-L-proline + succinate + CO2. FT The full enzyme consists of a alpha2 beta2 complex with the FT alpha subunit contributing most of the parts of the active FT site. The family also includes lysyl FT hydrolases,isopenicillin synthases and AlkB." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K320" FT /db_xref="InterPro:IPR005123" FT /db_xref="InterPro:IPR006620" FT /db_xref="InterPro:IPR023550" FT /db_xref="UniProtKB/Swiss-Prot:A1K320" FT /protein_id="CAL93225.1" FT /translation="MLITIDDVLSPEELAQARKLIAASRWVSGHVTAGPQALHSKNNEQ FT LPEDAEHLPALRRLILGALNRNPLFFAAALPLRVLTPFFNRYAGDSNHYGYHTDNAMRL FT APEGGYVRADVSATVFLSDPEEYEGGVLTIADTFGTHGVKLKAGSAVVYPSSSIHQVTP FT VTAGARVACFMFMQSMVRDAHQRRLLFDMDMALLQLRQSVGEDNDAVVRLTGTYHNLLR FT LWADA" FT CDS 637000..638121 FT /transl_table=11 FT /gene="gox" FT /locus_tag="azo0609" FT /product="probable (S)-2-hydroxy-acid oxidase" FT /function="L-lactate dehydrogenase (FMN-dependent) and FT related alpha-hydroxy acid dehydrogenases" FT /EC_number="1.1.3.15" FT /note="Probable (S)-2-hydroxy-acid oxidase. Homology to gox FT of S. oleracea (spinach) of 42% (sprot|GOX_SPIOL). FT CATALYTIC ACTIVITY: (S)-2-hydroxy-acid + O(2) = 2-oxo acid FT + H(2)O(2). InterPro: FMN-dependent alpha-hydroxy acid FT dehydrogenases (IPR000262); Protein binding FMN and related FT compounds core region (IPR003009) Pfam: FMN-dependent FT dehydrogenase no signal peptide no TMHs guaA_Cterm: GMP FT synthase C-terminal d" FT /note="Family membership" FT /db_xref="GOA:A1K321" FT /db_xref="InterPro:IPR000262" FT /db_xref="InterPro:IPR012133" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:A1K321" FT /protein_id="CAL93226.1" FT /translation="MPEAGKPAQRLAAIPREIAAVADYERFSRASLDDNAWAYLHSAAA FT DELSWRWNREAYDRLRILPRVLRDVTAGHTRCSLPGLELAHPILLAPVAWQKLFHPDGE FT RASAYAAAALDTGLVLSTLSSYTLEEVAAVGAGPRWFQLYLQPDRGVSRALVERAERAG FT YSGIVFTIDAPLNGVRNREHRAGFQLPPGVDSANLRGAPAPVRPALGEHDSAVFQGLMR FT EAPTWRDVEWLSGITRLPVILKGVLHPEDARIAADLGAAGLIVSNHGGRTLDTLPPALE FT MLPAMADAVGDRVALLLDGGIRRGSDVFKAIALGARAVLVGRGYIHALAAAGPLGVAHV FT IRLLRDELEVAMALAGCATLADIGPQALLAAPR" FT CDS complement(638132..639553) FT /transl_table=11 FT /gene="oprM2" FT /locus_tag="azo0610" FT /product="putative outer membrane efflux protein" FT /function="Outer membrane protein" FT /note="Putative outer membrane efflux protein. Homology to FT orpM in P. aeruginosa of 36%. Component of an efflux system FT that confers multidrug or multible antibiotic resistence. FT Interpro: Outer membran efflux protein Pfam: Outer membran FT efflux protein signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K322" FT /db_xref="InterPro:IPR003423" FT /db_xref="InterPro:IPR010131" FT /db_xref="UniProtKB/TrEMBL:A1K322" FT /protein_id="CAL93227.1" FT /translation="MTASVARLRLAPVLLAALVAGCAFTEPVARPDQPLPAQWTEQPGP FT AAATPLPDTWWQSFGSPALDALVAEALVASPDLQVQAERVLQAELALRQTRASLFPWLT FT LDADSGWRRADAGDRGASTVTETKTTSLGLSASYEVDLWGRVAANVGSARASLNATRYD FT RDSVRLSLAASVATTYFQLLTLQERLEIARQNLAIAERVLRVVEARYRNGAASALEVSQ FT QRTTVLTQRAAIEPLEVSVRQTRSALAILLGRNPQDAAPEFERLEALAIPTVTPGLPVE FT LLLRRPDLASVEASLAAASADIAAARAALLPSISLSAGGGVASSLLLSLADPGTTVSLS FT ASLVQTIFDGGRLQAAVDIARSRQRELLESYRSAIITALKEVEDALGNASRDANQEAAQ FT REILAEAQRALRLAELRYREGAADLLTVLDAQRTLFSAQDQLAQLRQARLTDAVGLYKA FT LGGGWRAENSMAAGG" FT CDS complement(639568..641538) FT /transl_table=11 FT /gene="macB" FT /locus_tag="azo0611" FT /product="ATP-binding/permease fusion ABC transporter" FT /function="ABC-type antimicrobial peptide transport system FT permease component" FT /note="Putative efflux transporter for macrolide FT antibiotics, TREMBL:Q92NU9 (57% identity); TREMBL:Q884D4 FT (49% identity). Pfam (PF00005): ABC transporter. Pfam FT (DUF214): Predicted permease. TMHMM reporting four FT transmembrane helices. TC (3.A.1.122): The Macrolide FT Exporter Family." FT /note="Specificity unclear" FT /db_xref="GOA:A1K323" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003838" FT /db_xref="InterPro:IPR017871" FT /db_xref="InterPro:IPR017911" FT /db_xref="UniProtKB/Swiss-Prot:A1K323" FT /protein_id="CAL93228.1" FT /translation="MKREAFSPSASSTGAGTPLIELAGITRSFRNGEIETRVLHGIDLT FT IYPGEFVAIVGASGSGKSTLMNILGCLDRPSSGTYRFMGEDVAGFDRDELARLRREAFG FT FVFQSYNLLGGASARENVEVPAVYSGMPPAERHARAEQLLASLGLGERSHHRPSQLSGG FT QQQRVSIARALMNGGRIILADEPTGALDSRSGEEVMKLLRQLSAEGHTIILITHAREVA FT EMAQRIIEIRDGHIVADPGPSKPQGPEPDFAPHVDRTSSMSDLVEATRTALRALRANLF FT RSALTLLGIVIGVASVIAMLAIGDGAKAKVVDQISAMGTNLLTVRPGAPNQRGRETTAT FT LVIEDVRAIAELPNVLASVPEQSASVTLRADNTDQRTTANATSWNYGVARNWPVASGTF FT FSAEDEARYATVAVLGQTTAGALFPGVDPIGQYVLVNNIPFQVIGVMSPKGATPWGQDQ FT DDIVFVPFTTGSLRVTGQRYLRNVTVAVEDVSRIDATQNEVSQLLLARHGVEDFQIRNM FT ASVIDTVSATQNTLTILLGTVAAISLLVGGIGVMNIMLVSVTERTREIGIRMATGARMK FT NILQQFLIEALVVSALGGLIGVAVGLGTAAVIALFDTPIKYSLLPVVLAFGCAFATGLV FT FGYLPARKAARLDPVVALASE" FT CDS complement(641535..642686) FT /transl_table=11 FT /gene="macA" FT /locus_tag="azo0612" FT /product="periplasmic component of efflux system" FT /function="Membrane-fusion protein" FT /note="Macrolide-specific efflux protein macA precursor. FT Efflux transporter for macrolide antibiotics (By FT similarity). Membrane Fusion Protein (MFP) family." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K324" FT /db_xref="InterPro:IPR006143" FT /db_xref="UniProtKB/TrEMBL:A1K324" FT /protein_id="CAL93229.1" FT /translation="MFGNGDPTALYQFATVSRGDIEDVVTATGTLQPREYVDVGAQVSG FT QLKKIHVEVGSLVKNGDLLGEIDSTVYLSKVDASRAQLRNLRAQLKEREAQVALAQVQF FT KRQTALMAEDATTTETLQTAEATLKSAEAQLEALRAQIEQYESTLRGDEANLQYARIMS FT PMTGTVVSITARQGQTLNTNQSAPTILRVADLTTMTVQTQVSEADVSRLKLGMAAYFTT FT LGGHGKRWYGKLDKIEPTPTVTNNVVLYNALFDVPNDDNLLMTQMTAQVFFIVAQAKDV FT LQIPLAAVSQGARGPRAGAQPAAGGAPAGAARGNGPRRATVKVLRADNTLEEREVQIGV FT SNRVQAQVLDGLQEGERVVTGLLSAPAPAASTTSNRQGPPPRL" FT CDS complement(642997..643413) FT /transl_table=11 FT /gene="exbD3" FT /locus_tag="azo0613" FT /product="probable biopolymer transport protein ExbD" FT /function="Biopolymer transport protein" FT /note="Probable fiopolymer transport protein ExbD. Homology FT to exbD1 of X. campestris of 43%. ExbD is part of the FT TonB-dependent transduction complex. The TonB complex uses FT the proton gradient across the inner bacterial membrane to FT transport large molecules across the outer bacterial FT membrane. InterPro: Biopolymer transport protein ExbD/TolR FT Pfam: Biopolymer transport protein ExbD/TolR no signal FT peptide probable 1 TMH" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K325" FT /db_xref="InterPro:IPR003400" FT /db_xref="UniProtKB/TrEMBL:A1K325" FT /protein_id="CAL93230.1" FT /translation="MAFGGFHQGGERQPTSDINMVPLIDVMLVLLIVFMITAPLLTHSV FT KIDLPKAASQPNVEKPETVTLALDGDGKLFWNNEPLPDDQLATRLTEAAGRTPQPELHL FT RADQNTRYQKLAEVMSEAREAGIEKMGFITVPER" FT CDS complement(643413..644174) FT /transl_table=11 FT /gene="exbB2" FT /locus_tag="azo0614" FT /product="probable biopolymer transport protein ExbB" FT /function="Biopolymer transport proteins" FT /note="Probable biopolymer transport protein ExbB. Homology FT to exbB of B. pertussis of 50% ExbB is part of the FT TonB-dependent transduction complex. The TonB complex uses FT the proton gradient across the inner bacterial membrane to FT transport large molecules across the outer bacterial FT membrane. InterPro: MotA/TolQ/ExbB proton channel family FT Pfam: MotA/TolQ/ExbB proton channel family no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K326" FT /db_xref="InterPro:IPR002898" FT /db_xref="UniProtKB/TrEMBL:A1K326" FT /protein_id="CAL93231.1" FT /translation="MEGTQAFGFAHLWGQSDAIIRTVAILLLAMSVTSWYLILVRALRQ FT LRARRSIDAVDAFWAASDLSQGLKRLQDQAPDSPFDDLARQGAAAADHVRRHTHQETLG FT GKLDADEFITRALRKSISLSTARLEAGLTMLASIGSTAPFVGLFGTVWGIYHALVNISA FT SGMATLDKVAGPVGEALIMTAFGLFVAIPAVLAYNAFTRANRVELSELDAFAHDLHAWF FT STGARIAPLPGQGAETATKAGATRLAAAGAA" FT CDS complement(644177..644926) FT /transl_table=11 FT /gene="tonB1" FT /locus_tag="azo0615" FT /product="putative TonB protein" FT /function="Periplasmic protein TonB links inner and outer FT membranes" FT /note="Putative TonB protein. Homology to tonb2 of P. FT aeruginosa of 39% (TREMBL:Q9RMT3). To complete transport of FT bound iron across the inner membrane, a second receptor FT complex is needed. The major component of this is tonB, a FT 27kDa protein that facilitates energy transfer from the FT proton motive force to outer receptors Pfam: Gram-negative FT bacterial TonB protein no signal peptide 1 TMH" FT /note="Function unclear" FT /db_xref="GOA:A1K327" FT /db_xref="InterPro:IPR006260" FT /db_xref="UniProtKB/TrEMBL:A1K327" FT /protein_id="CAL93232.1" FT /translation="MTVPSPATPTVRPVARPVAVAVAPRQRRPRAPERLGLGVLVVAAH FT AAGLLALAYVRSPEPPPEIRPIEIAFIPLEAPPQPEPVKPEPVKQAPQPKKPAEVRPKP FT PKPTPQPVAEKTTASPNALSAEPAPPAPAQPAAPAVATPAPPAPPAPPPVVAARFDADY FT LNNPKPAYPPLSTRLREEGTVMLRVQVTAEGLPGQIEINRSSGFERLDSAARAAVARWR FT FVPARQGDRAIEAWVLVPLVFKLTEGR" FT CDS complement(645213..645689) FT /transl_table=11 FT /gene="bfr2" FT /locus_tag="azo0616" FT /product="putative bacterioferritin" FT /function="Bacterioferritin (cytochrome b1)" FT /note="Bacterioferritin (BFR)(Cytochrome B-1)(Cytochrome FT B-557).May perform analogous functions in iron FT detoxification and storage to that of animal ferritins.Key FT role in iron homeostasis. 71% Bacterioferritin.IPR008331; FT Ferritin_Dps.IPR009040; Ferritin_like. Pfam:PF00210; FT ferritin; 1. TIGRFAMs:TIGR00754; bfr; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K328" FT /db_xref="InterPro:IPR002024" FT /db_xref="InterPro:IPR008331" FT /db_xref="InterPro:IPR009040" FT /db_xref="InterPro:IPR009078" FT /db_xref="InterPro:IPR012347" FT /db_xref="UniProtKB/TrEMBL:A1K328" FT /protein_id="CAL93233.1" FT /translation="MKGDKKVIQLLNKQLTNELTAINQYFLHARMYKNWGLGQLGKHEY FT EESIEEMKHADKLIERVLFLEGLPNLQNLNKLMIGENVPECIQGDLALESASRTDLVEA FT IAYCESCKDYVSRELLEDILEDTEEHIDYLETQLELIGSVGLQNYLQSQLETHS" FT CDS complement(645686..645928) FT /transl_table=11 FT /gene="bfd" FT /locus_tag="azo0617" FT /product="conserved hypothetical FT bacterioferritin-associated ferredoxin" FT /function="NAD(P)H-nitrite reductase" FT /note="Bacterioferritin-associated ferredoxin. Homology to FT psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO FT ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR FT REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE FT MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE FT RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN FT (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding FT domain no signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007419" FT /db_xref="UniProtKB/TrEMBL:A1K329" FT /protein_id="CAL93234.1" FT /translation="MYVCVCNAVTERHINEAVREGVSTLRHLRKELGVTAECGRCAVCA FT RDCLRSALAEKTQRPAAAPVHIGVAPSFSLAAEAS" FT CDS complement(645969..646178) FT /transl_table=11 FT /locus_tag="azo0618" FT /product="putative hemin uptake protein" FT /function="Hemin uptake protein" FT /note="47% DUF1008. Pfam:PF06228; DUF1008; 1." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR016060" FT /db_xref="InterPro:IPR019600" FT /db_xref="UniProtKB/TrEMBL:A1K330" FT /protein_id="CAL93235.1" FT /translation="MATESSDPCSPAVAAPRPERAVAEAPADEQGPAISSAQLLAGRPC FT VTIDHQGVNYVLRATRAGKLILTK" FT CDS 646348..647070 FT /transl_table=11 FT /locus_tag="azo0619" FT /product="conserved hypothetical protein" FT /note="Similar to TREMBL:Q8Y2F3 (57% identity); FT TREMBL:Q7VVV4 (55% identity); TREMBL:Q9I111 (53% identity). FT Pfam (FAA_hydrolase): Fumarylacetoacetate (FAA) hydrolase FT family." FT /db_xref="GOA:A1K331" FT /db_xref="InterPro:IPR002529" FT /db_xref="InterPro:IPR011234" FT /db_xref="UniProtKB/TrEMBL:A1K331" FT /protein_id="CAL93236.1" FT /translation="MSEKHEAFHVIPPAPQPVVPVLGGGVFPVRRIFCVARNYAAHARE FT MGGDPAREAPFFFTKPADAVLPVGEGECGRMSYPVATSDLHHELELVVALAAGGSGLTP FT EQAAGCIYGYAVGLDMTRRDLQAAAKAARRPWDAGKAFDHSAPISPIRPLAEVLAAGEI FT VLDVNGVRRQAGDLADMIWNVPETLAFLSRYFELRAGDLVFTGTPEGVGAVAAGDRLHG FT RIARVGELRLEIVAPQHA" FT CDS complement(647080..647529) FT /transl_table=11 FT /locus_tag="azo0620" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT an orf of G. sulfurreducens of 34% FT (tremblnew|AAR35905(SRS)). No domains predicted. Signal FT peptide. No TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K332" FT /protein_id="CAL93237.1" FT /translation="MSRSDPPPVASCWRHAVALLAALMLSGSAWAELVLVAARSGPIPA FT LSREEAEQLYLGRRTTLADGTPVSLVDLPAGAARDSFYQELTGKNPSQTRAYWSRLVFT FT GRALPPREAATVAEARDWIATRPGTIGYLPVGSPDDRLRVLLRLP" FT CDS complement(647516..648724) FT /transl_table=11 FT /locus_tag="azo0621" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT ebA1833 of Azoarcus sp. EbN1 of 48% FT (gnl|keqq|eba:ebA1833(KEGG)). No domains predicted. Signal FT peptide Present. No TMH present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K333" FT /protein_id="CAL93238.1" FT /translation="MKPAIPILCLALLLGLAPPARADAPEIRWSAFGTVGAVVTDDEDV FT RFIRSGIDHPGAESPDFGPDSVLGVQGNINLSEQAGAVLQVISRENPEGDYTPRVTLAF FT LSYALAPTLTARIGRMRVPFFMLSDSLDINYANPWVRPPIEVYGLNPFSDLDGVDLLYR FT TRIGNTDLEIHPYAGSSYIPIHRRGNARLRELYGINLALTHDHLSLYLGHAEARVALHW FT DDNEYNTMTAQLRSFGLGSVVAQLSGNDGYAAFSSAGVQWDDGRWLLIGEYARRENRSY FT ANSAHGWYVTVGRRVGATLPYLSFARHTQDRPTSGSSAVPAGSPFQPFIEGFDKSRNIA FT QHSTTAGVRWDFTRNAAFKAELSHIRTDPDAWGSLFPRGNPAFARMGDRSYNVLSVSVD FT VAF" FT CDS complement(648721..651168) FT /transl_table=11 FT /locus_tag="azo0622" FT /product="conserved hypothetical signaling protein" FT /function="predicted signal transduction protein containing FT a membrane domain an EAL and a GGDEF domain" FT /note="Conserved hypothetical signaling protein. Homology FT to ebA1830 of Azoarcus sp. EbN1 of 63% FT (gnl|keqq|eba:ebA1830(KEGG)). Pfam: PF00990 GGDEF domain. FT PF00989 PAS domain. PF00785 PAC motif. PF00563 EAL domain. FT PF00672 HAMP. TIGRFAM:TIGR00229 PAS domain S-box. TIGR00254 FT putative diguanylate cyclase (GGDEF) domain. TMHMM FT reporting 2 transmembrane helices of which one is in the FT signal peptide. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K334" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001633" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR013655" FT /db_xref="UniProtKB/TrEMBL:A1K334" FT /protein_id="CAL93239.1" FT /translation="MRLPFRHSSIRFRLLLASTAVQVVLLTLLLANSVRLMNDAASASL FT ATLTTQNASMLHAMATAYGEQGRYRTLQDVLGELLTDSTEGLVYVRIGGPDGQLLVSAG FT LPAMTTLPPPTPDMAQALGSLIDRPIIHVRRPLLLERNEVGFLQFGVSVSVLAAARQAI FT IQQGTLIALAEILLTFILLSGIGYLLTHNLGRLLAGSRAIAEGHLDHRLPEKGEDELAR FT LARNFNVMAATLQQRVGELQRTALQLRTSEERYALALRGANDGLWDWDLPTGQVYFSER FT FCEIVGRDMSGFSNAQDALASYLHPDELETYREVMRAHLRGESAQFMLEHRIRQGDGKV FT RWVMTRGVAQRDAGGRATRMAGSISDIDLRKRAEQQLVHDALHDGLTGLPNRALFIEHV FT QQALGHQRRDENARFAVLAINIERFSLINDSFGHAAGDELLRRVAEHIVASMRAGDVAA FT RVGGDQFALLLNGIDGSTEALRVAESLVELPGLSAPAAGRPLHLRCRIGVAVSDIERDD FT AEALLRDADNALHKARRDQADPVEFFHASMHTQAVRALQLEADLRTALRIGGLTVHYQP FT IVALGDRRLTSFEALVRWRHPTHGLLPPLEFIPLAETLDLIHDVGMRVLTLVCRDLLEW FT GIAYPGRALPSVSVNLSARQLSRPNLADELLDVIESHGVPISCLRFEVTESVLADPDGP FT AKPVLHQLREAGASVLIDDFGTGYSALSYLHTIPCDIVKLDGTFVRSITQDSRLRDIVR FT RSIQLAHDLGIAVVAECIEHEDQASVLYGMDCDYGQGYLYSRPLEADDARRLLAPSNPG FT TPQ" FT CDS complement(651269..652651) FT /transl_table=11 FT /gene="matA" FT /locus_tag="azo0623" FT /product="putative malonyl-CoA decarboxylase" FT /function="malonyl-CoA decarboxylase" FT /EC_number="4.1.1.9" FT /note="Catalyzes the conversion of malonyl-CoA to FT acetyl-CoA. In the fatty acid biosynthesis MCD selectively FT removes malonyl-CoA and thus assures that FT methyl-malonyl-CoA is the only chain elongating substrate FT for fatty acid synthase and that fatty acids with multiple FT methyl side chains are produced. 40% Malonyl_CoA_deC. FT Pfam:PF05292; MCD; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K335" FT /db_xref="InterPro:IPR007956" FT /db_xref="UniProtKB/TrEMBL:A1K335" FT /protein_id="CAL93240.1" FT /translation="MSATGLISKSLSRVRAMVAEAAGRNREPSVRTLERIRQQLRECAE FT GRGGEVSTRQRAARLADTYLSLDDGGRLAFLRIIALEFGPDPAKVASAHKAYQAAIGTD FT RQWDSEAALRAAMRSQRLRILTQFNAIPQGVKFLVDLRADLLRFLADEPLLKPLDRELE FT ARLAAWFDVGFLELARITWNSPAALLEKLVQYEAVHEIRSWRDLKNRLDSDRRCYAFFH FT PRMPLEPLIFVEVALVEELADNVQKLLDENAPVADPARASAAIFYSISNTQAGLRGVSF FT GNFLLKRVVEDLQRDYPRLHTFATLSPIPGLVGWMRRHPEQLAEAFTPNDWKRLAALGI FT EGPDAPALRALLSAPREAMADTQLQRALREPLLRVAAYYLLNAARDGKPVDPVARFHLG FT NGARVERLNWLADTADKGHEQSWGMMVNYLYDPDRIEANLESFASEGRVDASASVRRLA FT RR" FT CDS 652780..653454 FT /transl_table=11 FT /locus_tag="azo0624" FT /product="PAS/PAC-domain containing protein" FT /function="FOG: PAS/PAC domain" FT /note="PAS/PAC-domain containing protein, shows good FT similarity only to parts of other proteins (mostly sensor FT kinases). This suggests that there normally should be a FT kinase domain and therefore the protein is not complete. FT Also the downstream response regulator gives a hint for FT this suggestion. InterPro: IPR000014 PAS_domain. IPR001610 FT PAC motif. TIGRFAM: TIGR00229 PAS domain S-box. Signal P FT reporting signal peptide. TMHMM reporting 2 transmembrane FT helices." FT /db_xref="GOA:A1K336" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR013655" FT /db_xref="UniProtKB/TrEMBL:A1K336" FT /protein_id="CAL93241.1" FT /translation="MPNSPLPVLPSPAMLALPVALIYAAFAVAWIVYSDQVIGIWVRDP FT DRLTDVQTLKGIVFVVGTALMLWAMVRRGYARQAELQEVLLRREARLRIALRATGLGLW FT DYLVESREVEYDEEAARMLGRPPAAFREPAEVWLGRLHPDDREPFRQRFRDYLEGRSEQ FT YASEFRLAMPNGEFRWFSSVGQIVDRDAQGLPLRLIGTYLDITGRRRSSGSNGVLSVEH FT TT" FT CDS 653521..653943 FT /transl_table=11 FT /locus_tag="azo0625" FT /product="hypothetical two-component system response FT regulator" FT /function="Response regulator containing a CheY-like FT receiver domain and an HTH DNA-binding domain" FT /note="Hypothetical two-component system response FT regulator, very low similarity to a part of YehT: FT SWISSPROT: sprot|YEHT_ECOLI (16% Escherichia coli, YehT) FT Pfam: PF00072 Response_reg." FT /db_xref="GOA:A1K337" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="UniProtKB/TrEMBL:A1K337" FT /protein_id="CAL93242.1" FT /translation="MILMQKMYLPDDLAAVPLRVMLAMPEPLCCAHVTQYLGEATEIEV FT VGRTAAESEAMQLFFRLRPDVTVLDWRIAMHEPARLVGMLKRVAPGACVVSVVPALDSM FT PARAARALGADEVVTCDSLPQCLSTLAEHLERVRHH" FT CDS complement(653963..654760) FT /transl_table=11 FT /gene="lgt" FT /locus_tag="azo0626" FT /product="probable prolipoprotein diacylglyceryl FT transferase" FT /function="Prolipoprotein diacylglyceryltransferase" FT /EC_number="2.4.99.-" FT /note="Probable prolipoprotein diacylglyceryl transferase. FT Homology to lgt of E. coli of 47% (sprot|LGT_ECOLI) FT TRANSFERS THE N-ACYL DIGLYCERIDE GROUP ON WHAT WILL BECOME FT THE N-TERMINAL CYSTEINE OF MEMBRANE LIPOPROTEINS. InterPro: FT Prolipoprotein diacylglyceryl transferase (IPR001640) FT Tigrfam: lgt: prolipoprotein diacylglyceryl transferase FT Pfam: Prolipoprotein diacylglyceryl transferase no signal FT peptide 7 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K338" FT /db_xref="InterPro:IPR001640" FT /db_xref="UniProtKB/Swiss-Prot:A1K338" FT /protein_id="CAL93243.1" FT /translation="MLVHPQFDPVAIAVGPVAVRWYGLMYLLAFVLFVVLGRAHARRRP FT ELGWNAQAIDDLLLYGVLGVIIGGRLGEVLFYQPGYYLSHPAEILAVWKGGMSFHGGFL FT GVLVAMWLYGQRSGRGFWQITDFIAPLVPTGLAAGRIGNFINGELWGRPASPDLPWAMI FT FPWVDALPRHPSQLYQAAGEGLLLFAIVWVFAAKPRPLRAVSAVFLIGYGSLRFVAEFF FT RTPDPGIFSDLVPGLSTAQWLCVPMVVVGLALLKHAAHARARG" FT CDS complement(654774..655454) FT /transl_table=11 FT /gene="yceH" FT /locus_tag="azo0627" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein, 47% identity (59% FT similarity)to TrEMBL;Q8FIR0.TrEMBL;Q83LI7 Has FT PF04337,Protein of unknown function, DUF480;IPR007432;This FT family consists of several proteins of uncharacterised FT function. Coils2 program reporting presence of FT Coiled-Coil." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR007432" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/Swiss-Prot:A1K339" FT /protein_id="CAL93244.1" FT /translation="MDTTPAAPDASFDLDPAEIRVLGVLVEKAFLTPDAYPLSVNALVA FT GCNQLTAREPVMALSEGEVQAAIDSLLARRLVSRRDQAGGRVAKYEHQLRLRHSLPPAE FT QAVLALLMLRGPQTPGELRSRSERMHRFDDIAAVEAVLEHLGEKYPPMAAALPRAPGTK FT EIRHMHLLGGAEALEAAAEGLASAAAGGTGRGRLAELEEEVQRLRSEVAELRAAFDTFR FT QQFD" FT CDS 655581..657689 FT /transl_table=11 FT /locus_tag="azo0628" FT /product="putative adenylate/guanylate cyclase" FT /function="predicted transmembrane sensor domain" FT /note="Putative adenylate/guanylate cyclase," FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K340" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR007890" FT /db_xref="UniProtKB/TrEMBL:A1K340" FT /protein_id="CAL93245.1" FT /translation="MRRFLFLLVLALSVAAAAAAHLLQPGMAKTLRYAVFDQYQRWFPR FT PPSAVPDVVVVDIDDESLSRLGQWPWPRTRFAVLQRRLAEAGAVAVGYDILFAERDRSS FT PAVLARDLALPGALARELDALPDHDEVFAASLGAPPAVLGFAVDRENGGGTTGVKWPFR FT IVTRGVDALPVTAEAHAAVMPLPGLAAAAAGLGSISFAADGDGVVRRVPMMMRLADGWV FT PALDAELLRLAGGGHNLVLEGEGGQLAALRVGARRLPVTSAGEAWLHYAAAPEQPFLPA FT WRVLSADAPLASLQGRIVLVGSSAKGLLDLRFSPLGEVVPGIEIHAQALRQALAGRFPV FT RPQWAEAFELLMLLAGSLGGVLVALRLAALPAALLAGGAALAMLGAGAAAFAGGRLLLD FT PALPVLATLVASVMAGLVRYRHQESRQRWLRQAFARYLSPNLVDYLVRHPQALKLGGER FT CVCSFVFTDLAGYTRLIESLAPERAVGLLNDYLEGMVAIAFRHQGTLDRIVGDAVAVLF FT SAPLAQPDHARRALACALEMHAFSERYAEGVRAQGIAFGHTRIGVHSGEVIVGNFGGQT FT MFDYRALGDPVNTAARLESANKWLGTRICISAAVREACPDVAARAVGTVRLQGKNSALA FT VFEPLPGAGQPDSAYDVAFDLLDRAPDAAQAAFARLAAERPADGLVAFHLQRLRAGHRG FT TLIEMGYK" FT CDS complement(657725..658321) FT /transl_table=11 FT /locus_tag="azo0629" FT /product="conserved hypothetical secreted protein" FT /function="Outer membrane protein and related FT peptidoglycan-associated (lipo)proteins" FT /note="Conserved hypothetical secreted protein. Homology to FT Daro03000403 of Dechloromonas aromatica of 37% FT (gi|46140621|ref|ZP_00152222.2|(NBCI ENTREZ)). InterPro: FT Bacterial outer membrane protein (IPR006664). Pfam: OmpA FT family. signal peptide. no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K341" FT /db_xref="InterPro:IPR006664" FT /db_xref="InterPro:IPR006665" FT /db_xref="UniProtKB/TrEMBL:A1K341" FT /protein_id="CAL93246.1" FT /translation="MRRHARAASIALLLATLLSGCAPRSYLVLLENTDGSTGKVIVEGS FT DGRRQVVERAGDGVSLAASPAPVATTQETLSSDFGPAMAALPPPPTSFLLYFETAAARL FT TPESRNQLPRVLAQVRSRPAPDISIIGHTDTVGSNADNEALGLVRARTVLKLLEAAGVT FT AREITVTSHGERNLLVPTADNTDEARNRRVEVTVR" FT CDS complement(658318..658761) FT /transl_table=11 FT /locus_tag="azo0630" FT /product="conserved hypothetical secreted protein" FT /function="function unclear" FT /note="Conserved hypothetical secreted protein. Homology to FT PJS6w01004783 of Polaromonas sp. JS666 of 45% FT (gi|54028512|ref|ZP_00360661.1|(NBCI ENTREZ)). No domains FT predicted. signal peptide. TMH in signal peptide." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR006860" FT /db_xref="UniProtKB/TrEMBL:A1K342" FT /protein_id="CAL93247.1" FT /translation="MNLRQTISICALCAASFGAFAQAAPIGYVKTLSGDAVIVGSSGEQ FT AADVGSAVFAGDRIRTRANGSLGLTLKDNTMMAIGPDTEISVDEFAYAPASEQLRLGAR FT IMRGTLQFVSGIIAKLRPEAVTISTPTATIGVRGTRFLVKVAE" FT CDS 658869..661868 FT /transl_table=11 FT /locus_tag="azo0631" FT /product="HD-domain containing protein" FT /function="HD-GYP domain" FT /note="HD-domain containing protein," FT /db_xref="GOA:A1K343" FT /db_xref="InterPro:IPR003018" FT /db_xref="InterPro:IPR003607" FT /db_xref="InterPro:IPR023279" FT /db_xref="UniProtKB/TrEMBL:A1K343" FT /protein_id="CAL93248.1" FT /translation="MPAWRGLRVRFHYVATALLVVLVIALMSVFLLSVLHRFEEMAREH FT ARAVFAQVADRNALKLQETLARAGRVVGAHAAFEAPAYRAALSRLDADAPLAGLFAELR FT VNPQVYGFYVGFDDGAFLQLVGVRGNAGVIAALSAPASTWFALRSITADGARRVETWRF FT YDEAAHELGRRSADAVYLPQSRPWYSAAMQRAGLQATDPYVFQSSGELGVTLSQALAGG FT QGVFGADLALGELAAFVGASLGEWPGGVAVLDGAQRLLLYHASGGLGASRPPTLQPLTS FT ADDPFLGTLRADGLPPASGSVTAVLGRDFVFAGQEVTVAADTTFQVVAFAPVDAFAGAI FT ERARDDLVRVSALVLCISLPIAFFAARHASRTLGLLARDSERVMQMDFSGAVEVRSMFY FT EIDTLSEAHRTMKASIQARTRALNEALDKLESLVDNGLRLSAERDHERLLAHILGVGKR FT LCNADAASLLMVTPEGSLRFALRSRNDPLPQMEIPLHDPHTGAPNEHFVAVWVALHRQT FT VRIDDTATETRFDVSGARGMDSATGYRTVSMLTVPMTSSGGEVIGVLQFLNATDPETGA FT PVAFPAQLVPYVEALASQSAVALDNHNLLDSQQKLMDALVRLVAGAIDAKSPYTGGHCE FT RVPELAVMLAEAACEADSGPLAAFRFDSEEEWREFRIGAWLHDCGKVTTPEYVVDKATK FT LETIYNRIHEVRTRFEVLLRDAEIERLQRLLQGEDAEAANTAFAARKARLQDEFRFVAE FT CNIGGEAMEQGHQARLRDIGGQTWLRHFDDRLGLSQDELRRRADLPAAGLPAVETLLAD FT HPWQVVPRPAAQRFDPRYGFRVRVPENLYNFGELYNLSVTRGTLTEEERFKINEHIMQT FT IIMLDALPLPRQLARVPEYAGTHHETLTGSGYPKGLAQEELSIPARIMAVADIFEALTA FT ADRPYKKAKPLSEAIAILARLARQRHVDPDVFALFLRSGVYLRYAQRFLDPAQIDDVDI FT DHYLAEVCTA" FT CDS 661937..663787 FT /transl_table=11 FT /gene="ilvD" FT /locus_tag="azo0632" FT /product="dihydroxy-acid dehydratase" FT /function="Dihydroxyacid dehydratase/phosphogluconate FT dehydratase" FT /EC_number="4.2.1.9" FT /note="Dihydroxy-acid dehydratase catalyzes the fourth step FT in the biosynthesis of isoleucine and valine, the FT dehydratation of 2,3-dihydroxy-isovaleic acid into FT alpha-ketoisovaleric acid. Similar to sprot|ILVD_PSEAE FT (74%) and sprot|ILVD_ECOL6 (72%). TIGRfam (TIGR00110): FT Dihydroxy-acid dehydratase Pfam (PF00920): Dihydroxy-acid FT and 6-phosphogluconate dehydratase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K344" FT /db_xref="InterPro:IPR000581" FT /db_xref="InterPro:IPR004404" FT /db_xref="InterPro:IPR015928" FT /db_xref="InterPro:IPR020558" FT /db_xref="UniProtKB/Swiss-Prot:A1K344" FT /protein_id="CAL93249.1" FT /translation="MPQYRSRTSTAGRNMAGARALWRATGMKDGDFEKPIIAIANSFTQ FT FVPGHVHLKDLGQLVAREIEAAGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRDLIADSV FT EYMVNAHTADALVCISNCDKITPGMLMAALRLNIPTIFVSGGPMEAGKVKWEAKIIPLD FT LVDAMVKAADKNCSDEEVDAIERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGTTL FT ATHADREKLFREAGRRIVDLAKRYYEKDDATVLPRAIASFAAFENAISLDVAMGGSTNT FT VLHLLAAAKEAGVDFTMKDIDRISRHVPCLCKVAPAVPDVHIEDVHRAGGIMSILGELD FT RAGLLNRDVPTVHSKTLGEALGRWDIMQAHDKAVFDFFLAAPGGVPTQVAFSQNRRWNE FT LDMDRAKGVIRNKANAFSQDGGLAVLYGNIAEKGCIVKTAGVDESIWQFTGKARVYESQ FT EDAVEGILGEQVQAGDVVVIRYEGPKGGPGMQEMLYPTSYLKSRGLGKECALLTDGRFS FT GGTSGLSIGHASPEAAMGGAIALVEDGDTIEIDIPNRRIALAVSDEELARRRAAMEAKG FT AAAWKPANRERVVSAALQAYAALTTSADTGAVRDITQVQR" FT CDS 663873..664067 FT /transl_table=11 FT /locus_tag="azo0633" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT Mflag03001107 of Methylobacillus flagellatus of 42% FT (gi|53759956|ref|ZP_00350342.1|(NBCI ENTREZ)). No Signal FT peptide or TMH present. No domains predicted." FT /db_xref="UniProtKB/TrEMBL:A1K345" FT /protein_id="CAL93250.1" FT /translation="MDADLTHLEAQLEQLISLYTGLKAENRDLRARVVKLESDNRALAD FT KVSYATSKIEAVLEQLPEA" FT CDS 664076..664372 FT /transl_table=11 FT /locus_tag="azo0634" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to NE1890 FT of N.europaea of 35% (tremble:Q82TJ7) Has PF05164, Family FT of unknown function (DUF710);IPR007838;Family of FT eubacterial hypothetical proteins. No signal peptid. No FT TMHs" FT /db_xref="GOA:A1K346" FT /db_xref="InterPro:IPR007838" FT /db_xref="UniProtKB/TrEMBL:A1K346" FT /protein_id="CAL93251.1" FT /translation="MDALDITLLGKEYRVSCAPENRDALLAAAAFVDGKLVELAEKTHS FT SGERLAIMTALNIAHEFLQFQRGNGFDMPAAKRRIELMKARLDGVLAQQEKLF" FT CDS 664722..665201 FT /transl_table=11 FT /locus_tag="azo0635" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Hypothetical protein, 72% identity(81% similarity) FT to TrEMBL;Q82TJ8. TrEMBL;Q8XWR7(62% identity). Has PF04543, FT Family of unknown function (DUF589);IPR007628 ;Family of FT uncharacterised proteins" FT /note="Function unclear" FT /db_xref="InterPro:IPR002740" FT /db_xref="InterPro:IPR015947" FT /db_xref="UniProtKB/TrEMBL:A1K347" FT /protein_id="CAL93252.1" FT /translation="MRYWLMKSEPDDCSIDDLARRPGSTVPWYGVRNYQARNLMRDQMQ FT VGDAVFFYHSSCPQPGIAGIARVSSPAYPDATQFDPASPYHDPKSTPEAPRWLNVDVQF FT VRKTPLVPLAELRSHTELANMRVLARANRLSITPVDPAEWRFITRELMGLDNDGI" FT CDS 665191..665997 FT /transl_table=11 FT /locus_tag="azo0636" FT /product="conserved hypothetical membrane protein" FT /function="predicted permeases" FT /note="Conserved hypothetical membrane protein. FT TREMBL:Q82TJ9: 43% identity, 59% similarity FT InterPro:IPR002781; DUF81. Pfam:PF01925; DUF81 no signal FT peptide. 8 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K348" FT /db_xref="InterPro:IPR002781" FT /db_xref="UniProtKB/TrEMBL:A1K348" FT /protein_id="CAL93253.1" FT /translation="MAFDLWWLAYPLLGAVVGFFAGLLGIGGGGIMVPMLTTLFIAQGF FT PLAQVVHLALGTSMAAIVLTSISSLRTHHRHGAVRWEVVRGITPGILLGTFGGTFIAAH FT ADTVPLAIFFAVFMAYVSTQMLINVKPKPSRELPGTLGLGAAGLGIGGVSALVAIGGGS FT LSVPFMTWCNVKVQHAIGTSAAIGLPIALAGTLGYLINGWGEAGLPPLSLGFVYLPALV FT LVSGVSYFTAPVGAALAHRLPVATLKKIFAGVLILLCVKMLYSIFS" FT CDS 666063..666431 FT /transl_table=11 FT /locus_tag="azo0637" FT /product="Hypothetical protein" FT /note="Hypothetical protein Extremely poor homology with FT hits in the DB. NO features/signal Peptide/Domains FT present." FT /db_xref="UniProtKB/TrEMBL:A1K349" FT /protein_id="CAL93254.1" FT /translation="MNDTPHDQLEALAADILTLTEEVDAEGLARSRLTRGETIKRLRRM FT AAIAAALPDEARAALPEMDWARWLALGEDLAADRVGPLALWTAAREFTTDTLQWLRVYR FT EANPNWYRPAPDSGATLS" FT CDS 666529..667926 FT /transl_table=11 FT /locus_tag="azo0638" FT /product="conserved hypothetical protein" FT /function="Fe-S oxidoreductases" FT /note="Conserved hypothtecial protein. Homology to FT Avin02002811 of Azotobacter vinelandii of 50% FT (gi|23103464|ref|ZP_00089946.1|(NBCI ENTREZ)). InterPro: FT Domain of unknown function DUF224 (IPR004017). no signal FT peptide. no TMHs" FT /db_xref="GOA:A1K350" FT /db_xref="InterPro:IPR009051" FT /db_xref="InterPro:IPR012285" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K350" FT /protein_id="CAL93255.1" FT /translation="METKLDWSAYDNTGMGDPFGADPFGAGSFGGDAFGAAAAPVAGGA FT FGKAVALCTGNRACLRTDSPGVMCPSFRATEDPLHSTRGRIEALNAALAGADDAVDFSD FT PRLAEAMALCLSCKGCKRECPNGVDMALLRAEYLAQRNAREGVPAQARLLASFTDHLAA FT YPALRWLVALRNRVAPLAALGERWWGIAGDRRLPAPAARPFKEASPASVPAEGPQVALL FT VDSFCRHFEPGVAEAALAVLRAAGYRVTVLAPAADDANPTRPLCCGRSKLSFGLVDDAR FT AEARRMMAALAPALAARIPVVGLEPSCLFMLKDEYFSLGLGPDVGRLAGQVFLFEEFLA FT REHAAGRLRLALKPLDLPPALVHGHCHQKAYGAMPAVSTVLGLIPGFSFGMIDSGCCGM FT AGSFGLQARNQAVSRKLAEAALLPAVRAAEPEAPVVADGFSCRHQIRDGAGRRPVHVAE FT LLQRALA" FT CDS 668039..668347 FT /transl_table=11 FT /locus_tag="azo0639" FT /product="Hypothetical protein" FT /note="Hypothetical protein. 22% identity to FT SwissProt;P45905 No domains, repeats, motifs or features FT present." FT /db_xref="UniProtKB/TrEMBL:A1K351" FT /protein_id="CAL93256.1" FT /translation="MLANAPCAEKTLNAEDRLSVVVQCMQEGDCPAACVAYGDFRATLR FT ETLQDADLGGVLRDALAAFSQSLGAADIARCSGLAGRLREQLRASFPSQADRLLRFC" FT CDS complement(668355..669284) FT /transl_table=11 FT /gene="mntC1" FT /locus_tag="azo0640" FT /product="putative manganese transport system, FT periplasmic-binding protein" FT /function="ABC-type metal ion transport system periplasmic FT component/surface adhesin" FT /note="Part of the ABC transporter complex mntABC involved FT in manganese uptake. 41% Similar to the putative FT periplasmic-binding protein MntC precursor in E.coli. The FT MntC protein is also involved in the resistance to FT oxidative stress in N gonorrhoaeae. TREMBL E.coli:Q9F4F6. FT InterPro:IPR006128; Lipoprotein_4.IPR006127; SBP_bac_9. FT Pfam:PF01297; SBP_bac_9; 1. Signal peptide FT present.TMHelix:1 This operon probably is also involved in FT other cations uptake like Fe,Cu and Zn." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K352" FT /db_xref="InterPro:IPR006127" FT /db_xref="InterPro:IPR006128" FT /db_xref="InterPro:IPR006129" FT /db_xref="UniProtKB/TrEMBL:A1K352" FT /protein_id="CAL93257.1" FT /translation="MLPAFVARPLRALLLCIVAAPAAALAAPLEVVTSFSILADFVRQV FT GGERVSVHALVGEDGDTHAFQPRPSDARRVGSAALVVANGLGFDDWVARLARSAGYRGE FT VVLAAQGVATLEMTDHAHDDGKGPDQHAVDPHAWQDTRNAERYVDNIAEALARTDPAGA FT AIYRANAARYRAQLRELDAELRALVATLPATRRKVVSSHDAFGYLAHAYGLRFLAPVGV FT SNNAEPTAQGVARLIRQLKAEQVPAVFLENIADPRLIERIRSESGARVGGTLYSDALSA FT AGGPAPDYLALMRHNVRTLVAALAAPAR" FT CDS complement(669287..670171) FT /transl_table=11 FT /gene="mntB1" FT /locus_tag="azo0641" FT /product="putative manganese transport system, permease FT protein" FT /function="ABC-type Mn2+/Zn2+ transport systems permease FT components" FT /note="Part of the ABC transporter complex mntABC involved FT in manganese import. Probably responsible for the FT translocation of the substrate across the membrane. Similar FT to the permease protein, MntB in Synechocystis 6803. 30% FT IPR001626; ABC_transpt3. Pfam; PF00950; ABC-3; 1. This FT operon probably is also involved in other cations uptake FT like Fe,Cu and Zn." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K353" FT /db_xref="InterPro:IPR001626" FT /db_xref="UniProtKB/TrEMBL:A1K353" FT /protein_id="CAL93258.1" FT /translation="MNLLSVVIDYLVTPFADFGFMRRALAGCLALSLGATPVGAFLLLR FT RMSLMGDAMSHAILPGAALGYLAFGLSLGAMTVGGIVAGLVVVFAAGAVTRASVLKEDA FT SLAAFYLLSLAAGVMIVSLRGRNLDLLHVLFGSVLALDDRSLVLIASIASATAFGLALL FT FRPLVLECLDPAFLRAVGRWSPVAHYGFLVLVVLNLVAGFHALGTLMAVGIMILPAAAA FT RLWARRLSAMLALAVAIAFGSSVGGLLLSFHADVPAGPAIVLLCGLAYFASLLAAPGGL FT LAGRLPVRRHLES" FT CDS complement(670168..670938) FT /transl_table=11 FT /gene="mntA1" FT /locus_tag="azo0642" FT /product="putative manganese transport system, ATP-asa FT protein" FT /function="ABC-type Mn/Zn transport systems ATPase FT component" FT /EC_number="3.6.3.35" FT /note="Manganese transport system ATP-binding protein mntA. FT This protein is probably a component of a manganese FT permease a binding protein-dependent ATP-driven transport FT system (mntABC). Probably responsible for energy coupling FT to the transport system. 36% AAA_ATPase.IPR003439,AAA FT ATPase superfamily; ABC_transporter. Pfam: PF00005; FT ABC_tran; 1. This operon probably is also involved in other FT cations uptake like Fe,Cu and Zn." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K354" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K354" FT /protein_id="CAL93259.1" FT /translation="MHSVKPPAIHIDNLTLGYERHPAVHHLSVEIAPGALVAVVGPNGA FT GKSTLLKGLAGELRPIGGHIRLADAGRADVAYMPQRSEMDHSFPLSVFEMVAMGLWHEV FT GAFGRVGAAHARRIEAALTAVGLGGFEARAIGSLSGGQLQRARFARLILQDAPLILLDE FT PFAAIDARTVGDLVRLILDWHAQGRTVLTVVHDYDQVRRHFPHCLLLARELVAYGPTAE FT VLTAERLARARRLSEAFDDYAPECHVEEAAEARR" FT CDS complement(670947..671174) FT /transl_table=11 FT /locus_tag="azo0643" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT ebA1811 of Azoarcus sp. EbN1 of 38% FT (gi|56476415|ref|YP_158004.1|(NBCI ENTREZ)). no domains FT predicted. no signal peptide. 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K355" FT /protein_id="CAL93260.1" FT /translation="MTPRPRPETPAADTAPMSASHPHPHPHTHAAPHAHAHAPRIAMPR FT SALLAGLGARIAWAAGATALLWLCVAWALG" FT CDS complement(671152..671676) FT /transl_table=11 FT /locus_tag="azo0644" FT /product="putative regulatory protein" FT /function="Fe2+/Zn2+ uptake regulation proteins" FT /note="Putative regulator protein, probably involved in the FT regulation of cation uptake systems. 32% FUR.IPR009058; FT Wing_hlx_DNA_bnd. Pfam:PF01475; FUR; 1.Fur family protein FT 30%" FT /note="Function unclear" FT /db_xref="GOA:A1K356" FT /db_xref="InterPro:IPR002481" FT /db_xref="UniProtKB/TrEMBL:A1K356" FT /protein_id="CAL93261.1" FT /translation="MLQLQRTATRVRASHPTAKLSSTASSTGDSAARRLIVDHGGRVTR FT TRVAVIEALQGSAHPLSHDELGHALAARAVPHDRVTLYRALDWLVEQGIARRIAGSDRA FT WRFEIRARGAHHHAHFHCDRCGQVVCLEDLQPSLAAALPAGFQLDRAELVLHGACAACG FT RSAEDDTPPAP" FT CDS complement(671714..672076) FT /transl_table=11 FT /locus_tag="azo0645" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT PSPTO4639 of P.syringae of 41% (tremble:Q87WB4) No domains FT predicted. No TMHs. No signal peptide" FT /db_xref="GOA:A1K357" FT /db_xref="InterPro:IPR009875" FT /db_xref="UniProtKB/TrEMBL:A1K357" FT /protein_id="CAL93262.1" FT /translation="MSVEHRHFSRIRFQTGAHLLIDGREIACEVCDLSLKGALIEAPDP FT ATLPPPGERCLLELQLDSDALVRMEGDVAHVEGRRLGLVCREIDLDSITHLRRLIELNL FT GDAALLQREFGALIGA" FT CDS 672312..674498 FT /transl_table=11 FT /locus_tag="azo0646" FT /product="toxin secretion ABC transporter permease and FT ATP-binding protein" FT /function="ABC-type bacteriocin/lantibiotic exporters FT contain an N-terminal double-glycine peptidase domain" FT /note="HlyB-family protein. Similar to TREMBL:Q7WBM7 (50% FT identity); TREMBL:Q9KKL9 (41% identity); SWISSPROT:P18770 FT (28% identity). Pfam (PF00005): ABC transporter. Pfam FT (PF00664): ABC transporter transmembrane region. TMHMM FT reporting four transmembrane helices. TC (3.A.1.109.3): FT LapA adhesin protein exporter, LapB." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K358" FT /db_xref="InterPro:IPR001140" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005074" FT /db_xref="InterPro:IPR011527" FT /db_xref="InterPro:IPR017750" FT /db_xref="InterPro:IPR017940" FT /db_xref="UniProtKB/TrEMBL:A1K358" FT /protein_id="CAL93263.1" FT /translation="MAEGLVSDYAPGSDGVAAAARGSGAHHALVDCLLLVARAHGVAVT FT RDAVLAGLPVGDEGLPPSLFERAARRAGLSSRIVSLPLERLNDALAPTVLLLREDSACV FT LTGWNADRSVARVVFPELGDAVVELARDDLAARYIGRAIYVRPRQHFDARTPVVRQQRG FT HHWFWGVIGESRSLYRDVLLAAFMINVFALGMPLFTMNVYDRVVPNNATETLWVLAVGV FT VVVLVADLVLRTLRGYFIDLAGNRADVKISSHIMERVLGMRMEERPPSAGSFAANLRAF FT ESVRDFIGSATVVSFIDLPFALVFLVVIGWIAWPLLLPFFIGVAIVLLYALSVQGRMHE FT LSEMTYRAGAQRNATLVEGLVGLETLKALGAEAPLQRKWEKSAALLARVAAQLRLLSAT FT ATNGTSVVQQVVNVVIIVAGVYLIGRNELSMGGLIACYMLASRAMAPIGQVAGLLIQYH FT NASTALESLDQMMQREVERPEGSTFISRGSFEGEIEFRDVGFRYPGQQTEALRGVSFRI FT RAGERVGVLGRVGSGKTTLEKLILGLYRPTSGAVLIDGIDMRQLDPAELRRHIGYVQQD FT VTLFYGSLRENLTMGAPLAEDADVIRAAEVAGIADFVNAHPQGFEMLIGERGESLSGGQ FT RQGVAIARAVINDPPILLLDEPTASMDHSSEEGVKRRLGEYAKNKTMIVITHRTSLLDL FT VDRVIVVDGGRIVADGPKAQVVEALRQGRIGRVG" FT CDS 674498..675913 FT /transl_table=11 FT /gene="hylD" FT /locus_tag="azo0647" FT /product="putatice HlyD family secretion protein" FT /function="Membrane-fusion protein" FT /note="Putative HylD family secretion protein. Homology to FT hylD of E. coli of 24% (sprot|HLY4_ECOLI) Involved in the FT transport of hemolysin A. InterPro: HlyD family secretion FT protein; Gram-negative bacteril RTX secretion protein D FT Pfam: HylD family secretion protein no signal peptide no FT TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K359" FT /db_xref="InterPro:IPR003997" FT /db_xref="InterPro:IPR006143" FT /db_xref="InterPro:IPR006144" FT /db_xref="InterPro:IPR010129" FT /db_xref="UniProtKB/TrEMBL:A1K359" FT /protein_id="CAL93264.1" FT /translation="MAAFGQDVFRRFGTVTERFSGTGGKLFGGLLARLSSVERDDSLDW FT ASDADWARLQQEPLRARAVLKVSAIALLVLLGWAAVAHVDEVTKGDGKVIPSSQLQIIQ FT SVDGGVVESIAVREGEVVEAGQLLLKVDPTRFMSSLLENRAEFLALEIKRRRLEALTQG FT TPFSVPAELEKEAADIAAHERRLYESSRAEMDAQQSIARDQLRQREQELNEVRARSENA FT ARAYELVQQELKVTKPLAASGAVSEVELLRLERDVSRLRGEREQSAAQISRIQSAIAES FT TRKIQEIELTVRNQLRNELSDTMARLGSLTQGSRMLADRVKHAEIRAPMRGTVKRILVN FT TVGGVVQPGKEVAEIVPLDDALILEAQVKPSDIAFLRPGQSALVKFSAYDFSIYGGLEA FT VVDQISADTVVDAKGSAFYVVRVRTLHSSLGENLPIIPGMVAEVDILTGKKTILSYLLK FT PVLRAKANALSER" FT CDS 675910..676521 FT /transl_table=11 FT /locus_tag="azo0648" FT /product="putative DNA-binding response regulator, LuxR FT family" FT /function="Response regulator containing a CheY-like FT receiver domain and an HTH DNA-binding domain" FT /note="Putative DNA-binding response regulator, LuxR FT family," FT /note="Function unclear" FT /db_xref="GOA:A1K360" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:A1K360" FT /protein_id="CAL93265.1" FT /translation="MSRHFFLTRNGFSSPRWTEAFPHAVVAANADGVAPAAGDRVWLCA FT ELPDWRSRIGTLAAAGVIVVVLSLQPDESEGLAALELGARGYAHGLATAALLQEIDTVV FT SHGGLWVGETLMGRLLTALRPRLPATRTDVLAGLSPREAEVARAVAAGMTNKEVARTLG FT VTERTVKAHLGAIFEKLGVRDRLQLVLRVGASQAAAATAP" FT CDS 676646..679489 FT /transl_table=11 FT /locus_tag="azo0649" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to ebA1795 FT of Azoarcus sp. EbN1 of 46% (gnl|keqq|eba:ebA1795(KEGG)). FT No domains predicted. No TMHs." FT /db_xref="UniProtKB/TrEMBL:A1K361" FT /protein_id="CAL93266.1" FT /translation="MANATPVATVVAVTGNVFARDAEGKTRALKAGDVLREGETIVTAA FT GGRVELAMEDGSRLDIPEKQTVAVRADMDETTRPQGQDAQLAGGEIDRVIQALNQGGDL FT DAALEAPAAGLGGGGGGEGNNFVRLLRIAEGVTPLEFEFSALAQDDIPLILPADVEESP FT TVLVTLPTEPVTETVTVTLTETVTITETVTLPVTGTVTGIITDTVTGIVTQTVTGTAVT FT ETVTVVTQTVEVPTVIETVTTGTQTIEVPTTTETVTIGTQTVEVPTTIETVTIGTETVT FT VPALTETVTVGTQTVLVPTTIDTVTVGTQTVEVPTTTETVTIGTQTVDVPTMIETVTVG FT TETVDVPTTTATVLIGTETVDVPTAVDTVTVGTETVDVPTTTATVVIGTETVSVPTQVA FT TTTVGTETVGVPTVTETVTTGTATVTVPTTIDTVTIGTQTVNVTTTTPTVTSTSYTATT FT AVTSTEFSTQGLAIKAGGPGGSYYVTVNGLTILFTSTTGQINEKNGYLGVDQPHMQNGE FT KLLVTFLDANGQPTSVSNVSLNIDVINGPANFTWTSSANTSGTGASVAADGNFVVGGQY FT QWLEISATGGKFSIGALIGVALQVTHTETVTVTETGTTATPTVTAGTETVTVATTTETV FT TTGTQTVAVPTTTDTVTVGTQTVEVPTMTDTVTVGTQTVEVPTVTETVTVGTHTIEVPT FT TIATTTVGTQTVEVPTVTETVTVGTQTIDVPTMIETFTVVTETVDVPTTTATVISGTET FT VDVPTTIDTVTTGTETVNVPTVTETVTIGTETVEVSTMTETITTGTETVTVPALTETVT FT TGTETVSGTALAETVTTGTETVTAATMTETVTEATETVTQFTETVTVTQFTETVTSVGT FT DTVTDTATVTDTATSTVQGETVLGDALPAGDVLGQSDSLIEGGDSGSGGGGSTDPLASF FT QTDPVNSLLTTTTPSVD" FT CDS 679569..680795 FT /transl_table=11 FT /locus_tag="azo0650" FT /product="conserved hypothetical glycosyltransferase" FT /function="predicted glycosyltransferases" FT /EC_number="2.4.1.-" FT /note="Conserved hypothetical glycosyltransferase. Homology FT to gsu0991 of G. sulfurreducens of 30% (tremblnew|AAR34318) FT Pfam: Glycosyl transferase group 1 no signal peptide no FT TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K362" FT /db_xref="InterPro:IPR001296" FT /db_xref="InterPro:IPR022623" FT /db_xref="UniProtKB/TrEMBL:A1K362" FT /protein_id="CAL93267.1" FT /translation="MRVLFVHEGLGQFQTLHEHLNAEGLAHSWFLCSTGVYNANKDRIP FT NLVPFALAEENPKSYFYTKNLEARMQRSFLIKQAVNELLKKTGIDLIVAHGSGGFPLQL FT FDEFDIPIITYIEFPSFGHHGHDPKYPQPDYATYRDKVFEMTSYHQALKSELVIVPSAY FT AKSMFPSCLHERIHPQMEGFNITRKPSTFVKEEGVFHIGFSARDLSSAKGFEQFVMIAK FT EILKVRPQVRFVFCGSPKVLYSYEEAFLQQAFPAAESRPESFMQYVLQREGITLGEGSS FT FQHVKFAGYDEFASYVEAMDMFLYPLQFGSANWGLFELLFRGKKIIASDRCFVPEVIRH FT GYNGLLCKYDDMASWVRNATDIIDAPQDFDHLSANALADAHERFSVSSVARRYLAIFET FT AIHQHKLRK" FT CDS 680822..681160 FT /transl_table=11 FT /locus_tag="azo0651" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ebB52 FT Azoarcus sp. EbN1 of 40% (gnl|keqq|eba:ebB52(KEGG)). No FT domains predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K363" FT /protein_id="CAL93268.1" FT /translation="MPFVERDASGNITAVALEQSAAAREWLEPGDPAVAAFARRLGSHP FT GEALAALESSDIGLIRVIEDLIDTLLAKDVIRFTDLPLPAQNRLLQRRSLRQSLNSDSL FT LDDDAGLL" FT CDS complement(681161..683074) FT /transl_table=11 FT /locus_tag="azo0652" FT /product="conserved hypothetical GGDEF domain protein" FT /note="Conserved hypothetical GGDF domain protein. Homology FT to CV0310 of Chromobacterium violaceum of 34% FT (trembl|Q7P1A3). Has IPR003660_HAMP,SMART;SM00304:This FT domain is known as the HAMP domain for histidine FT kinases,adenylyl cyclases, methyl binding proteins and FT phosphatases. It is found in bacterial sensor and FT chemotaxis proteins and in eukaryotic histidine kinases. FT The bacterial proteins are usually integral membrane FT proteins and part of a two-component signal transduction FT pathway. Has IPR000160_GGDEF(SMART;SM00267);This domain is FT found linked to a wide range of non-homologous domains in a FT variety of bacteria. The function of this domain is FT unknown, however it has been shown to be homologous to the FT adenylyl cyclase catalytic domain. This prediction FT correlates with the functional information available on two FT GGDEF-containing proteins, namely diguanylate cyclase and FT phosphodiesterase A of Acetobacter xylinum, both of which FT regulate the turnover of cyclic diguanosine monophosphate. FT Has DUF2: This domain is found in diverse bacterial FT signaling proteins. It is called EAL after its conserved FT residues. The EAL domain is a good candidate for a FT diguanylate phosphodiesterase function. The domain contains FT many conserved acidic residues that could participate in FT metal binding and might form the phosphodiesterase active FT site. It often but not always occurs along with PAS FT IPR000014 and DUF9 IPR000160 domains that are also found in FT many signalling proteins. signal peptide 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K364" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001633" FT /db_xref="InterPro:IPR003660" FT /db_xref="UniProtKB/TrEMBL:A1K364" FT /protein_id="CAL93269.1" FT /translation="MSLIKQLWIAIALVTVLSLGGSFVVSTLAARHYLQQELAVKNMDN FT AASLALSLSQMPKDPVTVELQVAAQFDTGHYRLIRLTGASGEVLVERSFDGAEASAPAW FT FMALVPIETQPGVAQVQDGWHQFGTLSVETHSRYAYDSLWQATRQLLMWFVGGGLLTGL FT VGTLALKFITRPLDRMVEQAEAIGGRRFVTTPEPRTLEFRSVVRAMNALSDRVRSMLAE FT ESQRLEALRRQTQQDELTGLFNRAQLLRQLDAALSGEASADGVMLIARVADLAALNQRL FT GRLAVDNTLRTLAGALGGFTAAHPGWDCGRLNATDFALIAPGAVDAAALADELAHTLDT FT ALTPVSEIHRLHLAATPYAAQEARSAVLTRLDGVLAASELHGDRAVRVGIADGAEAGPQ FT GAGEWRRLLDAALAAGHIELARFPVIDRDGALLHDEAPVRLALDGNWYAAGRFMPWAAR FT LGMMVAVDTAVARTALAALAADGAATLAINLSVEALRDAGFRDALYHLLESDPAAARRL FT WIDVPEHAALQYQVEFRALCLALRPLGCRVGLKHAGPAFSRIAELHDLGLDYIKVAAAF FT VRDIDNSPGNMAFVRGLCTIAHSIGLQTIAEGVSTEAERDALPDLGLDGMTGPAIRRPQ FT AA" FT CDS complement(683109..683831) FT /transl_table=11 FT /locus_tag="azo0653" FT /product="conserved hypothetical secreted protein" FT /function="predicted periplasmic protein" FT /note="Conserved hypothetical secreted protein. Homology to FT BB1185 of Bordetella bronchiseptica of 49% FT (trembl|Q7WN55(SRS)) Signal peptide present. No TMHs Has FT PF06035, Bacterial protein of unknown function FT (DUF920);IPR010319; This family consists of several FT hypothetical bacterial proteins of unknown function." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR010319" FT /db_xref="UniProtKB/TrEMBL:A1K365" FT /protein_id="CAL93270.1" FT /translation="MPVLFPRLVPVMSQRSRALAAALRSLCAAAAVALAWLCAAAPDLD FT RMQSQAAERFGSTAAELVAAWRRLLGESAAETDADKLARVNTFFNRRLLFEDDSVVWRQ FT NDYWATPLETMGRGAGDCEDFAIAKYMTLRLLGVPADKLRLIYVRAQIGGPGSTASQAH FT MVLGYFAAPTDEPLVLDNLISEIRPAARRPDLFPVFSFNDEGLWVAGASTSSADPTARL FT SRWRDALDRMRREGLTLP" FT CDS 684035..685477 FT /transl_table=11 FT /gene="aggA" FT /locus_tag="azo0654" FT /product="putative outer membrane efflux protein" FT /function="Outer membrane protein" FT /note="Putative outer membrane efflux protein. Homology to FT aggA from P. putida of 35%. The OEP family (outer membrane FT efflux protein) allow export of a variety of substrates in FT Gram negative bacteria. InterPro: Outer membrane efflux FT protein Pfam: Outer membrane efflux protein signal peptide FT no TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K366" FT /db_xref="InterPro:IPR003423" FT /db_xref="InterPro:IPR010130" FT /db_xref="UniProtKB/TrEMBL:A1K366" FT /protein_id="CAL93271.1" FT /translation="MKKVRTLVCLAVLSTLQVAPAIAATPEPLRDAVRKAVVSNPEVQA FT RWHAFQGATADQDAARGGYYPQVDLNAAIGRERIDRPTTGTNDYTHRGATLSLTQMVYD FT GFFTQSEVARMGYAKLARYYELIETSESAALEVVRAYGDVLRYRELVRLAKANYVEHKL FT ISDQIAQRAGAGVGRRVDQEQASGRLALAESNLLTEVSNLHDVTARYQRLVGDTPPEAL FT PDLGETLTAMPLPANPRDALREAFNTSPAINAAVENVRAGQALVESRRSAYHPRVELQA FT YKSIDRNLDGVDGRSSDSVVQLVFNYNLFRGGADQARLRSAAESLNQSKDLREKACRDL FT RQTLAIAYNDTQRLTEQLRYLDQHQLSIEKAREAYRRQFDIGQRTLLDLLDTENEYFQA FT RRAYANARYDQVIAQARTLNGLGKLMSALEVAREDLPAAKDIGQDRAGIDPETMCPPEA FT PSPLQVDKAQLLSDAMRDAGRR" FT CDS 685558..689061 FT /transl_table=11 FT /locus_tag="azo0655" FT /product="putative two-component sensor histidine kinase FT protein" FT /note="Putative two-component sensor histidine kinase FT protein. TrEMBL; Q87XU6( 47% identity, 64% FT similarity),Q6F9J5(43% identity,61% similarity),Q6NAD6(44% FT Identity,61% similarity). TMHMM2 reporting 2 TMH's present. FT No Signal peptide Present. Has PF02133;Permease for FT cytosine/purines, uracil, thiamine, allantoin: FT IPR001248;Cyt_pur_permease:The Nucleobase Cation FT Symporter-1 (NCS1) family consists of bacterial and yeast FT transporters for nucleobases including purines and FT pyrimidines. Members of this family possess twelve putative FT transmembrane a-helical spanners (TMSs). At least some of FT them have been shown to function in uptake by substrate:H+ FT symport mechanism. Has PF07578:Lipid A Biosynthesis FT N-terminal domain;This family is found at the N-terminus of FT a group of Chlamydial Lipid A biosynthesis proteins. It is FT also found by itself in a family of proteins of unknown FT function. Has SMART;SM00388:(IPR003661)Dimerisation and FT phosphoacceptor domain of histidine kinases.The histidine FT kinase A (phosphoacceptor) N-terminal domain is a FT dimerisation and phosphoacceptor domain of histidine FT kinases. It has been found in bacterial sensor FT protein/histidine kinases. FT IPR003594;ATPbind_ATPase;(SM00387)This domain is found in FT several ATP-binding proteins for example: histidine kinase, FT DNA gyrase B, topoisomerases, heat shock protein HSP90, FT phytochrome-like ATPases and DNA mismatch repair proteins. FT SM00448;IPR001789;Response_reg:This domain receives the FT signal from the sensor partner in bacterial two-component FT systems. It is usually found N-terminal to a DNA binding FT effector domain." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K367" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="InterPro:IPR011006" FT /db_xref="UniProtKB/TrEMBL:A1K367" FT /protein_id="CAL93272.1" FT /translation="MERHPAAAALFPLTMNAADSDARLASSARAAGAPAAEHEPVQRVV FT KIRRDYNTWVANETLEDYALRFTPRSFRKWTEFRVGNTAFGAASFLVLEAVGATMLVSY FT GFINSFWAILALGLIIFLTGLPISLYAARHGVDMDLLTRGSGFGYIGSTLSSLVYASFT FT FILFALEAAIMAYALELALGIPPAWGYLVCALVVIPLVTHGITVISKLQTLTQPLWLFL FT LALPFFFLLREDPAALAGLWQYPGEKGEPGVFDLHLFAAAMTVGAALITQMGEQADYLR FT FMPARTAQNRWRWLAGVVLGGPGWVLIGVVKMLGGALLAWLLLREGMPAEKAVDPNQMY FT LLGFSGVFDSALWAVVVTALFVIVSQLKINVTNAYAGSLAWSNFFSRLTHSHPGRVVWV FT VFNILIGLLLMEMNVFQALGQVLGLYSNVAISWMVAVVADLVINKPMGWSPPGIEFKRS FT HLYDINPVGVGAMLVASILSVSTFVGVFGPAWQPFAPFVALVAALVTSPLIAWATKGRY FT YLARPPEPVATAGRAWVATRRCAICGQDFEPEDTSHCPAYQGTICSLCCSLDARCGDLC FT KPHARLSAQWSALVRRLVPGGLQPYIDGGLGHYLLLMGGVTGFLVLLLGTLYYHEVLAL FT GPDVARGALQGVLVKTFAALVLVSGIGVWWMVLTHKSRHVAQEESNRQTQLLMQEIESH FT RRTDEQLQNARRVAEQANQAKSRYVTSISHELRTPLNSILGYAQILDGDEAIPPHRRQA FT VSVIKKSGEHLLSLIEGTLDIARIESGKFALDMRPLAFPAFVHQLVGMFEPQARDKGLD FT FVFETVGTLPEVVRADEKRLRQILINIIGNAIKFTPRGRVGVKLTYRREMALIEVEDSG FT PGIAAGELQQIFEPFARGSSARTTTGTGLGLTISKMLTDLMGGELSVDSVPGEGSTFRI FT RLFLPQVHGAQAEAVQPRTQRIGYQGVRRRILTVDNERVDRELLASLLEPLGFEIGQAA FT SGYECLEMVPAFRPHLVFMDLAMPGIDGWETIRRLRDAGFDEVPVAIISANAFDKGLDN FT DVGIAPEDFILKPIRVEELLDWIGRRLQLDWVWAERVEPAAPQPVPAPAPHLVRPPADA FT VQELEQLIDLGYLRGILAKLAEIERLAPDYAEFVRVQRELARQFQFDAMHEILRRSEAP FT Q" FT CDS 689058..690014 FT /transl_table=11 FT /locus_tag="azo0656" FT /product="putative transcriptional regulator, LuxR family" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="Putative transcriptional regulator, LuxR FT family,Response_reg. IPR000792; HTH_LuxR. Pfam: PF00072; FT response_reg. PF00196; GerE. SMART: SM00448; REC. SM00421; FT HTH_LUXR. HTH reporting reporting nucleic acid binding FT motif." FT /note="Family membership" FT /db_xref="GOA:A1K368" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:A1K368" FT /protein_id="CAL93273.1" FT /translation="MSPSPATVAVPQSAGIVLIVDDVPENLSLLHDALDEAGYTVLVAT FT NGESALARARQSLPDVVLLDAVMPGMDGFEVARRLKADFVTRAIPLIFMTGLTETEHVV FT AAFAAGGADYVTKPIKPAEVLARIAAHVQNARQMKQARSALDAFGQATVAVRATDGKLV FT WQTPLARQLIRNWFDIGADETTPPRLIEWILAAELARRERREVAPLVMADGARRLLASF FT HDHTGEEEWLVVLREENDASAIEALIAAFRLTTREAEVLYWVTRGKTNRDIGDILGSSP FT RTVHKHLEHVFEKLGVETRTAAASMALAKIRGAGEGG" FT CDS 691405..692367 FT /transl_table=11 FT /locus_tag="azo0657" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT Raeut03005995 of Ralstonia eutropha of 34% FT (gi|53760601|ref|ZP_00350538.1|(NBCI ENTREZ)). No domains FT predicted. No signal peptide. 10 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR018677" FT /db_xref="UniProtKB/TrEMBL:A1K369" FT /protein_id="CAL93274.1" FT /translation="MNPRLSLYELAARHRLDAGASARLLELAGLDREPALLRRLAVRSV FT AVLAAALGGFGLILWVAANWAVFGRFGRFGLLIGAVVAMGLGAALRPRLRAPLALLAFL FT ATGGLFAYFGQTYQTGADPWQLFALWAALGLPLALGVRSDVVWAPWALVAGSALSLWLY FT AYNGHGAWRAGELGVHLVSWLLWLGLAASLSAPLRRWTGAGPWSARLALTLATAAISAS FT ALVGLFDDSPMLYLLGLLALAAAAALFAAPRAFDVYCVSAVGLGLNVLLVCGLARLLLA FT GHSEVGGLLVLGVAAAALLAGTVAMILALVRRADDGART" FT CDS 692364..693995 FT /transl_table=11 FT /locus_tag="azo0658" FT /product="hypothetical membrane protein" FT /function="uncharacterized membrane-anchored protein" FT /note="Hypothetical membrane protein. No homology of the FT entire protein to the data bank. No domains predicted. No FT signal peptide. 12 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K370" FT /protein_id="CAL93275.1" FT /translation="MNRAQWQRLLEDAAAAGLIPAGEAAAPGGGRPWPVVLLTGLGAWL FT AALPLLGFVALATDLVDSGVGAIVVGSLLLAAAVMVLRGRGVSLFIEQLAVPGLLAGAG FT LIALGLLDSSSERVAAGVMAVLALGVAAGVPQAWLRALLGAAAAVLIWLVITDLAYDGL FT GFLVPPAAVLHLQLLVWIAALQGQQRALAEGRAGVAAALEAIGGGWLAAVLAAFALWSG FT TTFLLGANLGAAAAVELAEALADGPRAGGAGLAGGWAALSAVLALGAGVWLARRWPGLR FT QAWCAGVVLVLAGLALFLPALGAVLLAAAICAAGRRAVLALTALVAAAWIIGAFYYQLA FT WPLATKAGVLVGAAAVLGTLAAWGARVRQAKPAVAGVPAHAGRGAAWVIALGTVAVVLV FT AVGAIVQKEQLIAHGRTVFVPLAPVDPRSLMQGDYMALNFLAWAERPGEDPDPFVLDTP FT RLALRLDARGVVTARRPDDGSALQADEVVIRLVPRAGRWMLVTDAFYFPEGEGERWAAA FT RFGEFRVDADGKALLVGLRGEDLAPL" FT CDS complement(694005..695342) FT /transl_table=11 FT /gene="gor" FT /locus_tag="azo0659" FT /product="probable glutathione-disulfide reductase" FT /function="Pyruvate/2-oxoglutarate dehydrogenase complex FT dihydrolipoamide dehydrogenase (E3) component and related FT enzymes" FT /EC_number="1.8.1.7" FT /note="Probable glutathione-disulfide reductase. Homology FT to gor of E. coli of 53% (sprot|GSHR_ECOLI). Maintain high FT levels of reduced glutathione in the cytosol. InterPro: FT FAD-dependent pyridine nucleotide-disulphide oxidoreductase FT (IPR001327); NAD binding site (IPR000205); Pyridine FT nuclotide-disulfide oxidoreductase dimerisation doamin FT (IPR004099); Pyridine nucleotide-disulphide oxidoreductase, FT class I (IPR001100) Pfam: Pyridine nuccleotide-dusulfphide FT oxidoreductase; Pyridine nucleotide-disulphide FT oxidoreductase dimerisation domain no signal peptide no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K371" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR004099" FT /db_xref="InterPro:IPR006322" FT /db_xref="InterPro:IPR012999" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR016156" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K371" FT /protein_id="CAL93276.1" FT /translation="MTHFDYLVIGGGSGGVATARRAAEYGARVLLIESARLGGTCVNAG FT CVPKKLMWHAAGIGHALHDAAAFGFRVDGLRFDWAALKRGRDDFVAYLNGVYASLLDKA FT GVSVVRGHARFVDAHTVEVGGQRYSAPHIVIATGGEPRVPDSPGAALGITSDGFFALDH FT LPARTIVVGGGYIAVELAGVLAALGSEVTMLVRGEHLLRPFDAMVRDELALQMRDAGIR FT IVTGSEAGAVRRADDGALRAACGSAEFEGDTLIWAIGRQARTAGLNLAAAGLGTEKDGS FT IATDAWQDTAVPGIHAIGDVTGRVELTPVAIAAGRRLAARLFGGQPEARLDYENVPSVV FT FSHPPIGTVGLTEEAARARHADVRVYHTRFTAMYHALKTQRPKTAMKLVCAGPQEQVVG FT CHIIGEGADEMLQGFAVAIRMGATKADFDDTVAIHPTSAEELVTMR" FT CDS 695491..697395 FT /transl_table=11 FT /locus_tag="azo0660" FT /product="ABC transporter permease and ATP-binding protein" FT /function="ABC-type multidrug transport system ATPase and FT permease components" FT /note="ATP-binding cassette (ABC) transporters form a large FT family of proteins responsible for translocation of a FT variety of compounds across biological membranes. They are FT composed of two transmembrane domains responsible for FT binding and transport and two nucleotide-binding domains FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the TMDs. Similar to FT TREMBL:Q87G83 (52% identity); TREMBL:Q9K1A3 (61% identity); FT SWISSPROT:Q57180 (60% identity). Pfam (PF00005): ABC FT transporter. TMHMM reporting five transmembrane helices. TC FT (3.A.1): The ATP-binding Cassette (ABC) Superfamily." FT /note="Specificity unclear" FT /db_xref="GOA:A1K372" FT /db_xref="InterPro:IPR001140" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR011527" FT /db_xref="InterPro:IPR017871" FT /db_xref="InterPro:IPR017940" FT /db_xref="UniProtKB/TrEMBL:A1K372" FT /protein_id="CAL93277.1" FT /translation="MSRLFRLFENLVDPYPEALPRTPPRGFLAFLWAGTEGVRPYILGM FT TALTATIGAFEALLFAMLGRIVDWLSAIAPAHLWADEGGTLLALGAVIVGSIALVALQT FT MLKHQTLAGNFPMRLRWNFHRLMLGQSMAFYQDEFAGRVAAKVMQTALAVRDTCLILTD FT ILVFVVIYFVTLAAVVGSFDAWLLLPFLGWIGCYLTALRWFVPRLSAVSRAQADARALM FT TGRITDAYTNIATVKLFSHAGREASYARAAMKEFMVTVHGQMRLVSGIEVINHSLSMGL FT ILSTAGVALWLWTQGQVGIGAVAAATAMALRLNGMSHWVMWELASLFEHVGTVQDGINT FT LARPHVVVDRPDARPLQVSRGEIRFESLSFSYGERDPQARKVIDALDLVIRPGEKIGLV FT GRSGAGKSTIVNLLLRFYDVDQGRILIDGQDIAGVTQDSLRAQIGMVTQDTSLLHRSVR FT DNILYGRPDASDEDMIAAARRAEAHEFVQGLGDPQGRRGYDAHVGERGVKLSGGQRQRI FT AIARVMLKDAPILLLDEATSALDSEVEAAIQASLYRLMEGKTVVAIAHRLSTIAAMDRL FT IVLDRGRIVEEGDHRSLLARGGLYARLWAHQSGGFLGEEADDELSPPAGGVSRLAEPV" FT CDS 697403..697951 FT /transl_table=11 FT /locus_tag="azo0661" FT /product="conserved hypothetical protein" FT /function="predicted metal-dependent hydrolase" FT /note="Hypothetical protein ygjP. TREMBL:Q83JJ6: 60% FT identity,74% similarity (probable metal dependent FT hydrolase) Members of this family are found in some FT archaebacteria, as well as Helicobacter pylori. The FT proteins are 190-240 amino acids long, with the C terminus FT being the most conserved region, containing three conserved FT histidines InterPro:IPR002725; DUF45. Pfam:PF01863; DUF45 FT Non secretory protein with probability of signal peptide FT being 0.243 No transmembrane helices gmhA: phosphoheptose FT isomerase" FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR002725" FT /db_xref="UniProtKB/TrEMBL:A1K373" FT /protein_id="CAL93278.1" FT /translation="MSMMKYLAGYPAPLVAQVSALMEEGRLAAMLAGRYRTAHAVRTDA FT ALYDYVAGLKAEFMRKAEPLSRVQYDNTLHVVRHALGTHTAISRVQGSKLKAKREIRIA FT SLFREVPDEFLRMIVVHELAHLKEREHDKAFYQLCTHMEPAYHQYEFDLRVYLCHLEAG FT GARLWGAGGTAPAAAGAGD" FT CDS complement(697992..698543) FT /transl_table=11 FT /locus_tag="azo0662" FT /product="conserved hypothetical secreted protein" FT /note="conserved hypothetical secreted protein. Homology to FT bA4595 of Azoarcus sp. EbN1 of 52% FT (gnl|keqq|eba:ebA4595(KEGG)) . No domains predicted. No FT TMHs. Signal Peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR009642" FT /db_xref="UniProtKB/TrEMBL:A1K374" FT /protein_id="CAL93279.1" FT /translation="MRPGTSLKAGVLAALTTGILAATPALAEKPDWAGGGHGGGKHEQR FT DKGRGGPDRDDRRGDDRRGERDYRDDRRAPSVSVDVHFHDRQRTVIREYYHREFSGGHC FT PPGLAKKHNGCMPPGQAKKWSRGRPLPRDVVYYDLPPALVVEIGVPPPGYKYVRVASDI FT LMIAIGTSMVVDAIEDLSRM" FT CDS 698767..699378 FT /transl_table=11 FT /locus_tag="azo0663" FT /product="probable CDP-alcohol phosphatidyltransferase FT family protein." FT /function="Phosphatidylglycerophosphate synthase" FT /note="Catalysis of the reaction: CDP + alcohol = CMP + FT phosphatidyl alcohol. Entry name Q8PQ18 Primary accession FT number: Q8PQ18 InterPro IPR000462; CDP-OH_P_trans. Pfam FT PF01066; CDP-OH_P_transf; 1. Identities = 114/203 FT (56%),Prediction: Signal peptide Signal peptide FT probability: 0.988 Number of predicted TMHs: 3" FT /note="Family membership" FT /db_xref="GOA:A1K375" FT /db_xref="InterPro:IPR000462" FT /db_xref="UniProtKB/TrEMBL:A1K375" FT /protein_id="CAL93280.1" FT /translation="MSSIYLLKSRFQSLLRPLVRRLAAAGVTANQVTLAAAAVSIALGA FT LLFFVPRPALFLLLPGWMFLRMALNAIDGMLAREFGQKSALGAYLNELADVIADAALFL FT PFALVPPFGWESVGAVILLASWSEMAGALGPMVGAPRCYDGPMGKSDRAFLFGALGLWL FT GLAGTLPGWLAWVMPAAAAAIALNLINRVRSGVRQASSSR" FT CDS 699386..701152 FT /transl_table=11 FT /locus_tag="azo0664" FT /product="conserved hypothetical protein" FT /note="Similar to TREMBL:Q87TY0 (64% identity); FT TREMBL:Q8PQ17 (61% identity); SWISSPROT:P76092 (55% FT identity)." FT /db_xref="InterPro:IPR022742" FT /db_xref="InterPro:IPR022744" FT /db_xref="UniProtKB/TrEMBL:A1K376" FT /protein_id="CAL93281.1" FT /translation="MTTTRPVQQHHFTTHDGVALFYRYWPATAPRRGCVVMFHRGHEHS FT GRMAHLADELALPEFDIFAWDARGHGMSPGARGDSPSLGSSVRDVQTFIEHIRDTWGIA FT EQDMAVLAQSVGAVLVSTWAHDYAPRVRCLVLASPAFKVKLYVPFARAGLALMRRLRGN FT FFVNSYVKSKFLTHDPARQASYDADPLIARAISVNILLALYEAGERVVADAQAITVPTQ FT LLISGADWVVHHAPQHAFFDRLGSAVKEKHVLPGFFHDTLGERDRTLAIDKVRDFILRQ FT FAAAPQRVGLLESHRQGPSFEEARALAAPLPALSPRGLYWKAYRAGLRVGGWLSAGVRL FT GHDTGFDSGSTLDYVYRNTPTGRGPLAPLGRLVDRQYLDAIGWRGIRQRKLNVEELLQK FT ALALLQRDGRPVRVLDIAAGHGRYVLEGLARAPQRVEAILLRDFSEINVRDGSALIAAK FT GLSDIARFERGDAFDEASVATVRPRPTIGIVSGLYELFPDNDAVRRSLAGMAAAVEPGG FT YLIYTGQPWHPQLEMIARALTSHRGGAAWVMRRRSQAEMDQLVEAAGFDKLEQRVDEWG FT IFTVSLARRRAA" FT CDS 701149..702507 FT /transl_table=11 FT /locus_tag="azo0665" FT /product="conserved hypothetical protein" FT /function="Membrane-associated phospholipid phosphatase" FT /note="Entry name:- Q9I0U5 Primary accession number:-Q9I0U5 FT InterPro:- IPR008934; AcPase_VanPerase. IPR000340; FT DS_phosphatase. IPR000326; PA_PTPase. Number of predicted FT TMHs: 8 Prediction: Non-secretory protein Signal peptide FT probability: 0.061 IPR000387; TYR_phosphatase. Pfam FT PF00782; DSPc; 1. PF01569; PAP2; 1. Identity:- 58%" FT /db_xref="GOA:A1K377" FT /db_xref="InterPro:IPR000326" FT /db_xref="InterPro:IPR000340" FT /db_xref="InterPro:IPR000387" FT /db_xref="UniProtKB/TrEMBL:A1K377" FT /protein_id="CAL93282.1" FT /translation="MSRPVPALALPLTDGRIHWLRSIGWLVLLGPFFFLSYGYANSMAA FT ARGVTDALFFEWERAIPFVPWSIVPYWSIDLLYGLSFLCCRSAQAVDRQAYRLLAAQCV FT SVACFLLFPLRFAFERPAADGLPGTLFTLLAGFDQPYNQAPSLHISLLVIIWACFARAV FT PGRWRGVVHVWALAIGLSVLTTYQHHFIDVPTGAAVGLLCLWLWPERGPSPLAGWRRRA FT SRGRLRLAFAYLAGAALLAAAALAVGGVALWLAWPALALALVAFCYAGPGAAGFQKDAT FT GHSIAARCLLAPYMLGAWLNSRAWTRRQPRPDAVCDGVWVGRMPDAAAMRAGGFAALFD FT LSAELPAPRGPWRYATLPWLDLVAPESSALIAAARGIEAERRAANGPLLVCCALGYSRS FT AAAVAAWLLLSGRAADVDQAVAMVARARPRVVLGDDLRAALAGCAAQTGSADD" FT CDS 702500..702943 FT /transl_table=11 FT /locus_tag="azo0666" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT PA2538 of Pseudomonas aeruginosa of 36% (trembl|Q9I0U6). No FT domains predicted. No signal peptide. 3 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K378" FT /protein_id="CAL93283.1" FT /translation="MTERERVDAAARAAACADLLALGRPLGRASAALALFALAVLLLGR FT EIPALPLWASLLLALPAQYHALRVAYDERVFRRWSGLWLHDPAAAPADTMAAFDCALGL FT APAGRSLADRCRGARRLLQRQLIATVLQLACLVAAALYIRWPY" FT CDS 702973..703596 FT /transl_table=11 FT /locus_tag="azo0667" FT /product="putative acyltransferase" FT /function="1-acyl-sn-glycerol-3-phosphate acyltransferase" FT /EC_number="2.3.1.51" FT /note="FUNCTION: Converts lysophosphatidic acid (LPA) into FT phosphatidic acid by incorporating an acyl moiety at the 2 FT position. This enzyme can utilize either acyl-CoA or FT acyl-acyl carrier protein as the fatty acyl donor. FT CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol FT 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. FT Entry name:-SWISSPROT:PLSC_ECOLI Prim. accession # P26647 FT InterPro:-IPR002123; Acyltransferase. IPR004552; FT AGP_acyltrn. Pfam:-PF01553; Acyltransferase; 1. Identities FT = 42/127 (33%) Prediction: Non-secretory protein Signal FT peptide probability: 0.014 Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K379" FT /db_xref="InterPro:IPR002123" FT /db_xref="UniProtKB/TrEMBL:A1K379" FT /protein_id="CAL93284.1" FT /translation="MGLERLTGSALCGFAKLITGMRATWRDNAPDARQRVYFANHRSHG FT DFLLIWASLPPALRQSTRPVAGADYWLTDRLRRYIAERVFRGVLIDRSAASRQADPVAQ FT MSAALAAGDSLIVFPEGTRNLGDGLLPFKSGIYHLARANPAVEFVPVWIENLGRVMPKG FT SYVPVPLLCSLSFGGALQWQAGEAKTDFLARARTALLDLAPALD" FT CDS 703602..704546 FT /transl_table=11 FT /locus_tag="azo0668" FT /product="conserved hypothetical phosphatidate FT cytidylyltransferase" FT /function="predicted CDP-diglyceride FT synthetase/phosphatidate cytidylyltransferase" FT /EC_number="2.7.7.41" FT /note="Conserved hypothetical phoshpatidate FT cytidyltransferase. Homology to pa2536 of P. aeruginosa FT (trembl|Q9I0U8). Phosphatidate cytidylyltransferase is the FT enzyme that catalyzes the synthesis of CDP-diacylglycerol FT from CTP and phosphatidate (PA): CTP + phosphatidate = FT diphosphate + CDP-diacylglycerol Pfam: Phospatidate FT cytidyltransferase signal peptide 7 TMHs InterPro: FT Phosphatidate cytidylyltransferase stp: serine transporter" FT /note="Family membership" FT /db_xref="GOA:A1K380" FT /db_xref="InterPro:IPR000374" FT /db_xref="UniProtKB/TrEMBL:A1K380" FT /protein_id="CAL93285.1" FT /translation="MNLSETLVAVFGGVFAVLAAASLVGAVLKFRLAPARPHAVIDNLN FT ARLKAWWVMIGLIALAIWAGDGGVIGLFAFISFQCLREFVSLTHTRRGDHRALLWSFFV FT LLPLQYYLIAIGWYGLFSILIPVYGFLLLPISAALGSDTTRFLERAAKVQWGLMICVYC FT LSHVPALLTLQIPGYEGKGALLIVFLVLVVQSSDVFQYVWGKLCGRHKLNPAVSPSKTV FT EGLLGGVASSTAVGAAMWWITPFSPLQAAAVALVVNVLGFFGGFVLSAIKRDRGVKDWG FT SLIEGHGGMLDRVDSISFSAPVFFHIVRYWWVP" FT CDS complement(704566..705237) FT /transl_table=11 FT /gene="napC1" FT /locus_tag="azo0669" FT /product="probable cytochrome C-type protein NapC" FT /function="Nitrate/TMAO reductases membrane-bound tetraheme FT cytochrome c subunit" FT /note="Probable cytochrome c-type protein NapC. Homology to FT napC of r. sphaeroides of 67% (sprot|NAPC_RHOSH). MEDIATES FT ELECTRON FLOW FROM QUINONES TO THE NAPAB COMPLEX. signal FT peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K381" FT /db_xref="InterPro:IPR005126" FT /db_xref="InterPro:IPR011031" FT /db_xref="InterPro:IPR011885" FT /db_xref="InterPro:IPR024717" FT /db_xref="UniProtKB/TrEMBL:A1K381" FT /protein_id="CAL93286.1" FT /translation="MFGLLKRYWRVIRRPSTHYSLGLLVIGGFVGGVLFWGGFNTALEA FT TNTEPFCTSCHEMYDNVYQELQPTIHFTNRSGVRATCPDCHVPHRWTAKIARKMQASKE FT VWGKVFGTISTREKFEGMRLALAVNEWRRLKANNSLECRNCHQFNSMDFTRQSPRAQHA FT HSTSLAKGERTCIDCHIGIAHRLPNLEGVDRLVEAHGGRNVLPALVSGGLQEDMAPPAP FT R" FT CDS complement(705250..705717) FT /transl_table=11 FT /gene="napB1" FT /locus_tag="azo0670" FT /product="probable diheme cytochrome C" FT /function="Nitrate reductase cytochrome c-type subunit" FT /note="probable diheme cytochrome c. Homology to napB of A. FT eutrophus of 51% (sprot|NAPB_ALCEU). SMALL SUBUNIT OF THE FT PERIPLASMIC NITRATE REDUCTASE (NAP). ONLY EXPRESSED AT HIGH FT LEVELS DURING AEROBIC GROWTH. NAPAB COMPLEX RECEIVES FT ELECTRONS FROM THE MEMBRANE-ANCHORED TETRAHEME NAPC PROTEIN FT THUS ALLOWING ELECTRON FLOW BETWEEN MEMBRANE AND PERIPLASM. FT ESSENTIAL FUNCTION FOR NITRATE ASSIMILATION AND MAY HAVE A FT ROLE IN ANAEROBIC METABOLISM. signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR005591" FT /db_xref="UniProtKB/TrEMBL:A1K382" FT /protein_id="CAL93287.1" FT /translation="MRILLPFALAAAFAGAALAQHVDNARGPTPLMEERTPPPLQNPDN FT SDVRRQRAYAMQPPIIPHKIEGYQLDRNVNRCMMCHARTRTEQSQAPMISVSHFTDRDG FT NFLAELSPRRYFCLQCHVPQVPVNPIVENRFIDVETMLRRGGSASTLPEQR" FT CDS complement(705728..708220) FT /transl_table=11 FT /gene="napA1" FT /locus_tag="azo0671" FT /product="nitrate reductase" FT /function="Anaerobic dehydrogenases typically FT selenocysteine-containing" FT /EC_number="1.7.99.4" FT /note="Nitrate reductase large subunit. Homology to napA of FT a. eutrophus of 76% (sprot|NAPA_ALCEU). ONLY EXPRESSED AT FT HIGH LEVELS DURING AEROBIC GROWTH. NAPAB COMPLEX RECEIVES FT ELECTRONS FROM THE MEMBRANE-ANCHORED TETRAHEME NAPC PROTEIN FT THUS ALLOWING ELECTRON FLOW BETWEEN MEMBRANE AND PERIPLASM. FT ESSENTIAL FUNCTION FOR NITRATE ASSIMILATION AND MAY HAVE A FT ROLE IN ANAEROBIC METABOLISM. InterPro: Prokaryotic FT molybdopterin oxidoreductases (IPR006655) Pfam: FT Molybdopterin oxidoreductase; Molydopterin dinucleotide FT binding domain signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K383" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR006655" FT /db_xref="InterPro:IPR006656" FT /db_xref="InterPro:IPR006657" FT /db_xref="InterPro:IPR006963" FT /db_xref="InterPro:IPR009010" FT /db_xref="InterPro:IPR010051" FT /db_xref="UniProtKB/TrEMBL:A1K383" FT /protein_id="CAL93288.1" FT /translation="MKLTRRAFIKQSAALSTAAAAGIPAETLGANIVTDAALTKLAWHK FT APCRFCGVGCGVNVAVRDNRVVATHGDINAEVNRGINCVKGYFLSKIMYGADRLTEPLL FT RQTNGQYDKNGELQPVSWERAFDVMAEQFKKALREKGPSGVGMFGSGQWTIWEGYAAAK FT LYKAGFRSNNIDPNARHCMASAVAGFMRTFGMDEPMGCYDDFEQADAFVLWGANMAEMH FT PILWTRLTDRRLSAPQSRVAVLSVFEHRCYDLADLTLTFRPQTDLAILNYIANYIIQRG FT AVNRDFINRHTRFMTGNTDIGYGLRPEHPLQKAKNVAAPGGGQPSTFDEYAAFVAKYDV FT DTVARLSNVPKDRLEQLAQLYADPKVKVMSLFTMGFNQHTRGTWCSHLLYNLHLLTGKI FT SSPGNGPFSLTGQPSACGTAREVGTFSHRLPADMVVTNPQHRETAERIWKLPAGTIPDK FT PGYHAVLQNRMLKDGQLQAYWVMCNNNMQAAPNIAQEAWPGYRNPSNFVVVSDAYPTMT FT TVAADLVLPTAMWVEKEGAYGNAERRTQFWHQLVQAPGQARSDLWQLMEFSKRFRMEEV FT WPAELLAKAPQYRGKTLFDVLFRNGEVDKFPATQVEAGYANDEARAFGFYPQKGLFEEY FT AQFGRGHGHDLAPFDTYHQVRGLRWPVVNGQETRWRYREGLDPYVKAGEDVKFYGMPDG FT KAVIYALPYEPAAEEPDKEYPFWLCTGRVLEHWHSGSMTQRVPELHRAFPNAVCFMHPD FT DTRKLGLRRGDEIEVVSRRGVMRTRVETRGRNKPPPGLVFVPWFDASQLINKVTLDATC FT PISLQTDFKKCAVNIRKV" FT CDS complement(708192..708494) FT /transl_table=11 FT /gene="napD1" FT /locus_tag="azo0672" FT /product="putative NapD protein" FT /function="uncharacterized protein involved in formation of FT periplasmic nitrate reductase" FT /note="Putative NapD protein, component of of periplasmic FT nitrate reductase system. Plays a role in the correct FT assembly of subunits of the periplasmic napAB enzyme. FT Homology to napD of Rhodobacter sphaeroides of 26% FT (gi|3345484|dbj|AB016290.1|). InterPro:IPR005623; NapD. FT Pfam:PF03927; NapD; 1. no signal peptide. No TMHs." FT /note="Function unclear" FT /db_xref="GOA:A1K384" FT /db_xref="InterPro:IPR005623" FT /db_xref="InterPro:IPR019887" FT /db_xref="UniProtKB/TrEMBL:A1K384" FT /protein_id="CAL93289.1" FT /translation="MLEDIEVHVTGVLVQALPDHVQAVCVAVANFPEAEVCAVSETGKL FT VVVCECASADETLALLDRIRDLAGVANVALVYQHTETGAEMDEEINDEADPPRVH" FT CDS complement(708506..708664) FT /transl_table=11 FT /gene="napE" FT /locus_tag="azo0673" FT /product="putative periplasmic nitrate reductase accessory FT protein NapE" FT /note="Putative periplasmic nitrate reductase accessory FT protein NapE. Homology to napE of R. sphaeroides of 36% FT (trembl|O88159). Pfam: Periplasmic nitrate reductase FT protein NapE (PF06796) This family consists of several FT bacterial periplasmic nitrate reductase NapE proteins. NapE FT is thought to be a transmembrane protein of the reductase. FT Interpro: Periplasmic nitrate reductase protein NapE FT (IPR010649) no signal peptide 1 TMH" FT /note="Family membership" FT /db_xref="InterPro:IPR004448" FT /db_xref="InterPro:IPR010649" FT /db_xref="UniProtKB/TrEMBL:A1K385" FT /protein_id="CAL93290.1" FT /translation="MSQEPPSTRQEELRSFLFLAFVTAPVLAVLIVAGYGFAVWMFQLL FT SGQLPTS" FT CDS 709010..710266 FT /transl_table=11 FT /gene="amiC2" FT /locus_tag="azo0674" FT /product="putative aliphatic amidase expression-regulating FT protein" FT /function="ABC-type branched-chain amino acid transport FT systems periplasmic component" FT /note="AmiC regulates the expression of the inducible FT aliphatic amidase activity in Pseudomonas aeruginosa. FT Similar to trembl|Q87VQ0 (80%) and to sprot|AMIC_PSEAE FT (27%). Pfam (PF01094): Receptor family ligand binding FT region SignalP reporting Signal peptide." FT /note="Specificity unclear" FT /db_xref="GOA:A1K386" FT /db_xref="InterPro:IPR000709" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR017777" FT /db_xref="UniProtKB/TrEMBL:A1K386" FT /protein_id="CAL93291.1" FT /translation="MQTRRSFIKALALSASIAAIGAPFGAHAADTIKVGILHSLSGTMA FT ISETALKNVALMTIEEINAKGGVMGKKLEPVVVDPASNWPLFAEKARQLVAQDKVAAVF FT GCWTSVSRKSVNPVFKELNGLLFYPVQYEGEELEKNVFYTGAAPNQQAIPAVEYLMSAE FT GGSAKRFVLLGTDYVYPRTTNKILRAFLKSKGVADADIMEDYTPFGHSDYQTIIANIKK FT FASEGKKTAVISTINGDSNVPFYKELGNAGLKATDVPVVAFSVGEEELRGVDTKPLVGH FT LAAWNYFMTVKNPENTAFIKKYKDWAKKNGVPNADTVVTNDPMEATYVGIYMWKQAVEK FT AKSTDTDKVIAALGGQTFKAPSGFTLTMDKTNHHLHKPVFIGEVRADGQFDVVWKTKEP FT IRAQPWSPFIPGNEGKQGL" FT CDS 710535..712166 FT /transl_table=11 FT /locus_tag="azo0675" FT /product="ABC transporter permease protein" FT /function="Branched-chain amino acid ABC-type transport FT system permease components" FT /note="Branched-chain amino acid transport system typically FT composed of a periplasmic substrate-binding protein, one or FT two reciprocally homologous integral inner-membrane FT proteins and one or two peripheral membrane ATP-binding FT proteins that couple energy to the active transport FT system.The integral inner-membrane proteins translocate the FT substrate across the membrane. Similar to trembl|Q87VP9 FT (50%)and to pir|AB0146 (48%). Pfam (PF02653): FT Binding-system dependent bacterial transporters (araH, FT livH/limM families) TMHMM reporting nine Tmhelix. SignalP FT reporting Signal peptide." FT /note="Specificity unclear" FT /db_xref="GOA:A1K387" FT /db_xref="InterPro:IPR001851" FT /db_xref="InterPro:IPR016024" FT /db_xref="InterPro:IPR017779" FT /db_xref="UniProtKB/TrEMBL:A1K387" FT /protein_id="CAL93292.1" FT /translation="MEPAMNRLLLRLALLFASLACLALPARAALDPALVAGFAGDFNSR FT VAAIEALGVEGSAEARALLDAVEAGNLGVAADKVVVIDGDAVKDAASGEALQIPADEVE FT TITVNNRIRRALATAHAALALSAESAADRLAAANTLTENTSESLLPLFERTLAGEKDEA FT VRGVLSRAVARVNLGSADAAKRLKAAEALGESSDPAVKNMLAALLEKRGEGKDASWAEP FT DAEVRAAAEASIKAIDRRIATAQAVGTVFSGLSLGSILLLAALGLAITYGVMGIINMAH FT GELLMVGAYATFLVQGLFRSYLPAYLDWYVVAAIPVAFFAAALVGVAMERLVLRHLYGR FT PLESLLATWGLSLVLIQAARVVFGPQNLELANPGWMSGGMELAAGVVLPYNRIVIIGFA FT VFVLVLIWLMMQKTRLGMFVRAVTQNRPMAGCVGVPTARVDTLAFAIGSGVAGLGGLAL FT SQIANVGPAMGQGYIVDAFMVVVLGGVGQLAGAVWAALGLGIVAKFLEGWAGAVIAKIL FT VLVFIIVFIQKRPQGIFALKGRFADS" FT CDS 712360..713553 FT /transl_table=11 FT /gene="urtC" FT /locus_tag="azo0676" FT /product="probable ABC transporter, membrane spanning FT protein" FT /function="ABC-type branched-chain amino acid transport FT system permease component" FT /note="Probable ABC transporter, membrane spanning protein. FT Homology to urtC of Anabaena sp. of 41% (involved in urea FT transport). Part of the binding-protein-dependent transport FT system. Probably responsible for the translocation of the FT substrates across the membrane. InterPro: Binding-system FT dependent bacterial transporters (araH livH/limM families) FT Pfam: Branched-chain amino acid transport system signal FT peptide probable 9 TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K388" FT /db_xref="InterPro:IPR001851" FT /db_xref="InterPro:IPR017778" FT /db_xref="UniProtKB/TrEMBL:A1K388" FT /protein_id="CAL93293.1" FT /translation="MRTPFTVRLFQSMPKTGWVALAIFAVVACVGVPVAHLALPEGHAL FT HLSAYTVSLLGKILCYMVVAVAMDLIWGYAGILSLGHGLFFALGGYAFGMYLMRQIGRD FT GSYQSDLPDFMVFLDWKELPWYWAGSDSFLWALFLAMALPGLVAFVFGYFAFRSRIKGV FT YFSIITQALTYAAMLLFFRNETGFGGNNGFTDFKRILGYSITSPEMRATLFALSALLLI FT ACLVLGRYLVSSRFGRVLAAIRDAESRVMFIGYNPLHYKLFMWTLSAVLCGLAGALYVP FT QVGIINPSEMSPANSIEIAVWVAVGGRGTLVGAVLGAGIVNLAKSFFTVTVPEYWPFFL FT GFLFIAVTLYLPDGVVGLWRKLRARKGPDSAAAAPAATAAPVGEAAPETTVAKGATA" FT CDS 713550..714407 FT /transl_table=11 FT /gene="urtD" FT /locus_tag="azo0677" FT /product="conserved hypothetical ABC transporter, ATP FT binding protein" FT /function="uncharacterized ABC-type transport system ATPase FT component" FT /note="Conserved hypothetical ABC transporter, ATP binding FT protein. Homology to pp4844 of P. putida of 70% FT (trembl|Q88DI1). Probable component of a branched-chain FT amino-acid transport system. Pfam: ABC-Transporter no FT signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K389" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017781" FT /db_xref="UniProtKB/TrEMBL:A1K389" FT /protein_id="CAL93294.1" FT /translation="MTETTELERRARAFAEAGGRENWEGAAATGHVATGELDLSHNVIL FT YLDDITVSFDGFRALNKLSLTIDAGELRCIIGPNGAGKTTMMDVITGKTRPDEGKAFFG FT QTLDLTRMTEPEIAHAGIGRKFQKPTIFENHSAFENLELAMKADKRVRRTLFASLFDDE FT RDRIADVLKQIRLDKFADRSAGLLSHGQKQWLEIGMLLMQEPKLLLLDEPVAGMTDDET FT ERTAELFVSLAGKHSLMVVEHDMAFVEALGGKVTVLCEGSVLAEGDLATVQADSRVIEV FT YLGR" FT CDS 714834..715526 FT /transl_table=11 FT /gene="urtE" FT /locus_tag="azo0678" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems ATPase component" FT /note="ATP-binding cassette (ABC) transporters are FT multidomain membrane proteins, responsible for the FT controlled efflux and influx of substances (allocrites) FT across cellular membranes. ATP-binding protein is for FT coupling the energy of ATP hydrolysis to conformational FT changes in the transmembrane domains. Similar to FT trembl|Q88DI0 (59%) and to sprot|BRAG_PSEAE (35%). Pfam: FT ABC transporter Smart: AAA ATPases" FT /note="Specificity unclear" FT /db_xref="GOA:A1K390" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017780" FT /db_xref="UniProtKB/TrEMBL:A1K390" FT /protein_id="CAL93295.1" FT /translation="MLKVDNLNQYYGGSHILRGLSFEVPVGKVTTLLGRNGVGKTTLLK FT TLMGLVPAASGTIHFGAQDITRAPSYNRVRAGIGYVPQGREIFPRLSVEENLLMGLATQ FT PRGSSIPQRIFDMFPVLKQMMGRRGGDLSGGQQQQLAIGRALAFGPKLLILDEPTEGIQ FT PSIIKDIERAIRSLAATGEMAILLVEQYYDFARALSDQYLVMERGEIVMRGEGANMDAD FT GVREALAV" FT CDS 715560..716513 FT /transl_table=11 FT /gene="nodD" FT /locus_tag="azo0679" FT /product="probable nodulation protein" FT /function="Transcriptional regulator" FT /note="Probable nodulation protein," FT /note="Function unclear" FT /db_xref="GOA:A1K391" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K391" FT /protein_id="CAL93296.1" FT /translation="MANGCTWDSLDAHLLRVLHVLLTEGSVSRAARRLNQSQPAVSTAL FT KRLRDITGDKLLVRSRTGMTPTERGAELLEPVRIALEQMERIAAGPEGFEPANSRRVFN FT IATPDYLNALMLGDIVADIHRQAPGAQVAFHSMTQTFDYPRALESGELDLVIGNWPNPP FT EHLRTAPLFEDRMVVMMRTGHPLAGAPLTLSAWLAAEHVVPTSYSVGQRGVVDVYLARE FT RLRRNVVAHVPYFHMAPYMVLQSDLVFTAPARFASHYADFLPMAVVDAPAELPRMAYYL FT LWHDRSQHSAECRWLRERIIRAARPDPAPAPLRRVA" FT CDS complement(716527..717309) FT /transl_table=11 FT /gene="caiD" FT /locus_tag="azo0680" FT /product="putative Carnitinyl-CoA dehydratase" FT /function="Enoyl-CoA hydratase/carnithine racemase" FT /EC_number="4.2.1.-" FT /note="Function: Catalyzes the reversible dehydration of FT L-carnitinyl-CoA to crotobetainyl-CoA. Entry name FT CAID_ECO57 Primary accession number Q8XA35 InterPro FT IPR001753; EnCoA_hydrtse. Pfam PF00378; ECH; 1. Identities FT = 30% Prediction: Non-secretory protein Signal peptide FT probability: 0.003 Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K392" FT /db_xref="InterPro:IPR001753" FT /db_xref="UniProtKB/TrEMBL:A1K392" FT /protein_id="CAL93297.1" FT /translation="MNGQILVDRGDAVATVSLSNPGKLNAVNAGMWRQLRAAFAELGAD FT PGVRCIVLRGAGDEAFAAGGDIEEFRTVRATVDDALHYHEELVAAALNAIRDCPVPTVA FT AIRGACVGGGLEIAGCCDLRIAGASSRFGAPINKLGFSMYPGEMAGLLALVGPAVVLEI FT LLEGRILDAAEALQKGLLSRVVDDANVFDEAAACAARIAAGAPLVARWHKQWAKRLQRP FT EPLSEAERRAAFDFLATEDYREGLEAFLAKRKPVFKGR" FT CDS 717556..717876 FT /transl_table=11 FT /locus_tag="azo0681" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT PP2796 of P. putida of 44% (trembl|Q88J53) PF04341,Protein FT of unknown function, DUF485;IPR007436;This family includes FT several putative integral membrane proteins. signal peptide FT 1 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007436" FT /db_xref="UniProtKB/TrEMBL:A1K393" FT /protein_id="CAL93298.1" FT /translation="MSSSVYAHIRRNPRFAELVAKRTRFATLLAAIVLVVFYGFVLVVA FT FAPQIVGQRLSEGSNLTIGIVAGLFQFIFFWVLTFVYVRRANGEFDAINTEIVRAAWQE FT EK" FT CDS 717876..719555 FT /transl_table=11 FT /locus_tag="azo0682" FT /product="conserved hypothetical sodium:solute symporter" FT /function="predicted symporter" FT /note="conserved hypothetical sodium:solute symporter: FT Homology to an orf of P. aeruginosa of 72% (trembl|Q9APX1). FT Sodium/substrate symport (or co-transport) is a widespread FT mechanism of solute transport across cytoplasmic membranes FT of pro- and eukaryotic cells. Thereby the energy stored in FT an inwardly directed electrochemical sodium gradient FT (sodium motive force, SMF) is used to drive solute FT accumulation against a concentration gradient. The solutes FT transported may be sugars, amino acids, nucleosides, FT inositols, vitamins,urea or anions, depending on the FT system. InterPro: Sodium:solute symporter family FT (IPR001734) Tigrfam: sss: SSS sodium solute transporter FT superfamily Pfam: Sodim:solute symporter family signal FT peptide 13 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K394" FT /db_xref="InterPro:IPR001734" FT /db_xref="InterPro:IPR018212" FT /db_xref="InterPro:IPR019900" FT /db_xref="UniProtKB/TrEMBL:A1K394" FT /protein_id="CAL93299.1" FT /translation="MNASRLSRLALGLASLPLSAAALAAGPAMEAAQKQPLNLHAIGMF FT FVFVLMTLGITYWAASRTKSASDFYTAGGGITGFQNGLAIAGDYMSAATLLGLTAMMYA FT QGVDAYIYMIAFFVGWPIILFLMAERLRNLGKFTFADITAYRLDQGKVRTMAAVSSLTV FT VCFYLVAQMVGAGQLIKLLFGLDYTVALFVVGALMMVYVTFGGMVATTWVQIIKACMLL FT LGGTTVMLLALSQFGFSFEALATRAMEVHKLGPKLFNPGSLLADPVTAISLGLGLMFGT FT AGLPHILMRFFTVTDAKEARKSVLYASGIIAYFFNVIALMGLAAILIVGQNPQYFEGGD FT LAGKIVGGGNMVAMHLAHAVGGNLLLGFLSAVAFATILAVVAGLALAGASAISHDIYAR FT VIMKGRASETTEIRVSKFATIGLGVVAVLLGIVFEKMNVAFMVALAFGVAASANFPVLI FT LSMYWKGLTTRGALAGGYLGLFSAVTFVVLSKSVWVDVLGNAAPIFPWTQPALFSMPLA FT FLATIVVSLLDSSHKARSEREAFEDQYVRAQTGVGAASAAAH" FT CDS 719709..721004 FT /transl_table=11 FT /gene="ytfL1" FT /locus_tag="azo0683" FT /product="probable hemolysin" FT /function="Hemolysins and related proteins containing CBS FT domains" FT /note="Hypothetical protein ytfL. TREMBL:Q7NQ98: 61% FT identity, 78% similarity InterPro IPR002550; CBS. FT IPR000644; CBS_domain. IPR005170; CorC_transpt-asc. Pfam: FT PF00571; CBS; 2. PF03471; CorC_HlyC; PF01595; DUF21; gntP: FT gluconate transporter Signal peptide present (Signal P FT predicted) Transmembrane helices 4 (TMHMM predicted)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K395" FT /db_xref="InterPro:IPR000644" FT /db_xref="InterPro:IPR002550" FT /db_xref="InterPro:IPR005170" FT /db_xref="InterPro:IPR016169" FT /db_xref="UniProtKB/TrEMBL:A1K395" FT /protein_id="CAL93300.1" FT /translation="MALLNHLLLILLLIAVSAFFSLAEISLAAARKIKLQQLAEEGVAD FT ARRVLALQESPGSFFTVVQIALNAVAILGGIVGEQALSPYVESALRPFYDGPALGTVSF FT VIAFVFVTSMFVLLADLMPKRLAMVKPEAVAMRVVRPIQASMWLFAPLVWLFNSLADRL FT FGLFGVPSARADDITSDDILAMAEAGTRAGALLEQEQNLIRNVFELDARIVPSAMTSRD FT SVVYFTLGEAEDSIRRKMAAHPHGKFPVCESGIDDVIGYVDAKDLFRRILQGQDLSLRT FT QPIVRKVLMLPDTLTLFEALERFRDAKEDFALVISEYALVVGLLTLQDVMNTVMGELGS FT PYQEELIVRRDDCSWLIDGVTPIEDVMQALEIEVFEGFENYETIAGFLMYRLRKVPKRT FT DFVVYAGYKFEVVDIDNYRIDQVLVTREPAAA" FT CDS complement(721389..722060) FT /transl_table=11 FT /gene="mdcY" FT /locus_tag="azo0684" FT /product="transcriptional regulator, GntR-family" FT /function="Transcriptional regulators" FT /note="Transcriptional regulator, GntR-family," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K396" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K396" FT /protein_id="CAL93301.1" FT /translation="MTASRIAPLALYQEVAERLRERIFSHELPPGTWVDEQALAEQYGI FT SRTPLREALKVLASEGLVTLKPRRGCYVTEISERDLDEVFNIIALLEGECARASVARAS FT DADLARLRDIHATLEAAAAAQDIDRFFEANQAFHHVLQQIADNRWLLQVIEDLRKVIKL FT SRHHSLFSEGRLEQSLAEHREILEAVLARDPDAAETRMRRHIHSGRAALSRIAEARNRA FT A" FT CDS 722387..724552 FT /transl_table=11 FT /gene="mutB" FT /locus_tag="azo0685" FT /product="probable Methylmalonyl-CoA mutase large subunit" FT /function="Methylmalonyl-CoA mutase N-terminal FT domain/subunit" FT /EC_number="5.4.99.2" FT /note="FUNCTION: Catalyzes the isomerization of FT succinyl-CoA to methylmalonyl-CoA during synthesis of FT propionate from tricarboxylic acid-cycle intermediates (By FT similarity). ACtivity:- (R)-2-Methylmalonyl-CoA = FT succinyl-CoA Entry name :- MUTB_PORGI Primary accession FT number :-Q59677 Identities = 467/679 (68%) InterPro :- FT IPR006159; Acid_CoA_mut_C. IPR006158; B12-binding. FT IPR006099; MMCoA_mutase. IPR006098; MMCoA_mutase_N. FT IPR006100; MMCoA_mutase_sub. Pfam PF02310; B12-binding; 1. FT PF01642; MM_CoA_mutase; 1. Prediction: Non-secretory FT protein Signal peptide probability: 0.000 Number of FT predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K397" FT /db_xref="InterPro:IPR006098" FT /db_xref="InterPro:IPR006099" FT /db_xref="InterPro:IPR006158" FT /db_xref="InterPro:IPR006159" FT /db_xref="InterPro:IPR014348" FT /db_xref="InterPro:IPR016176" FT /db_xref="UniProtKB/TrEMBL:A1K397" FT /protein_id="CAL93302.1" FT /translation="MSNANLPAYPQPDLEAWNKAAAKQAPDGQLDKLNWITPEGLTVKP FT LYTKADTADLPHADTLPGFEPFLRGPQPTMYAVKPWTIRQYAGFSTAEESNAFYRKALA FT AGGQGVSVAFDLATHRGYDSDNPRVLGDVGKAGVAIDSVEDMKILFDGIPLDKISVSMT FT MNGAVLPILAGYIVAAEEQGVAQDKLSGTIQNDILKEFMVRNTYIYPPTPSMKIIADIF FT QYTSSHMPKFNSISISGYHIQEAGANQAIELAFTLADGLEYVRTGIAAGMDVDTFAGRL FT SFFWAVGMNFYLEIAKMRAARLLWWRIMKQFNPKSPKSMMLRTHSQTSGWSLTEQDPYN FT NVVRTTIEAMAAVFGGTQSLHTNALDEAIALPTEFSARIARNTQIIIQEETHICNVVDP FT WAGSYMMEKLTQDMADKAWALIEEIEAMGGMTKAVESGWAKMKVEECAADKQARIDSGK FT DVIVGVNKYKLAKEDPIEILDIDNHAVREAQIARLTKIRATRDSAAVQAALDALTQCAE FT SGEGNLLDLAVKAVRLRASVGEISDALEKVFGRYRANPQAVSGVYGAVVEDDADWKELK FT AEIEAFIAEEGRRPRIMIAKLGQDGHDRGAKVVASAFADLGFDIDIGPLFQTPEEAARH FT AVENDVHAVGCSSLAAGHKTLVPAIIAELKRLGAEDIITFVGGVIPAQDYDALYAAGAK FT GIFGPGTPIPKAAREVLKQIRAAKVAA" FT CDS 724619..725632 FT /transl_table=11 FT /gene="argK" FT /locus_tag="azo0686" FT /product="putative LAO/AO transport system kinase" FT /function="Putative periplasmic protein kinase ArgK and FT related GTPases of G3E family" FT /EC_number="2.7.-.-" FT /note="Putative LAO/AO transport system kinase. Homology to FT argK of E. coli (sprot|ARGK_ECOLI). In Escherichia coli FT K-12, the arginine-ornithine transport system requires an FT arginine-ornithine-binding protein and the FT lysine-arginine-ornithine (LAO) transport system includes a FT LAO-binding protein. Both periplasmic proteins can be FT phosphorylated by a single kinase, ArgK resulting in FT reduced levels of transport activity of the periplasmic FT transport systems that include each of the binding FT proteins. The ArgK protein acts as an ATPase enzyme and as FT a kinase. no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K398" FT /db_xref="InterPro:IPR005129" FT /db_xref="UniProtKB/TrEMBL:A1K398" FT /protein_id="CAL93303.1" FT /translation="MAMNMPESLPVLDDADLALVEGVRARQLRPLAKTITLIESQREDH FT KARARAVLEALLPHTGGAMRVGISGVPGVGKSTFIEALGLYLIEQGLRVAVLAVDPSSS FT LTGGSILGDKTRMELLSQNPAAFIRPSPSAGSLGGVAEKTRETLLVCEAAGFDVIIVET FT VGVGQSETAVAGMTDIFCLLQLPNAGDDLQAIKKGIMEIADLIVINKADIDAGAAMRAK FT SQMKTALHMLRPASPNWTVPVLTLSALKKDGIAEFWNAVQDYRGAMTKSGEFEAKRRHQ FT ALAWMWELIDTGLRSRFRNHPGVRDALPLLAAAVEAGGTTPSAAAQRLLGCLNRTN" FT CDS 725698..727233 FT /transl_table=11 FT /gene="pccB" FT /locus_tag="azo0687" FT /product="probable propionyl-coa carboxylase beta subunit." FT /function="Acetyl-CoA carboxylase carboxyltransferase FT component (subunits alpha and beta)" FT /EC_number="6.4.1.3" FT /note="Activity:- ATP + propanoyl-CoA + HCO3- = ADP + FT phosphate + (S)-methylmalonyl-CoA Entry name:-TREMBL:Q8U9Y9 FT Prim. accession # Q8U9Y9 InterPro:-IPR000438; FT ACoACC_transB. IPR000022; Carboxyl_trans. Pfam:- PF01039; FT Carboxyl_trans; 1. Identities = 363/511 (71%) Number of FT predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K399" FT /db_xref="InterPro:IPR000022" FT /db_xref="InterPro:IPR011762" FT /db_xref="InterPro:IPR011763" FT /db_xref="UniProtKB/TrEMBL:A1K399" FT /protein_id="CAL93304.1" FT /translation="MHDIIRQLDEKRAAARLGGGQKRIDSQHAKGKLTARERIELLLDP FT DSFEEWDMFKEHRCVDFGMDKAEKTPGDGVVTGYGTINGRLVFVFSQDFTVFGGSLSET FT HAEKICKVMDHAMKVGAPVIGLNDSGGARIQEGVASLGGYADVFQRNVMASGVIPQISM FT IMGPCAGGAVYSPSMTDFIFMVKDSSYMFVTGPEVVKTVTHEDVTAEELGGAVTHTSKS FT GVADLAFENDVEALTMLRRFMNYLPSSNREKPPVQPTNDPADRQDFSLDTLVPDNPNKP FT YDMKELIIKVVDDCDFFELQPDYAKNIIIGMARMDGQPVGIVANQPLVLAGCLDIKSAI FT KAARFVRFCDAFNIPVVTFVDVPGFMPGTAQEYGGIIKHGAKLLYAYAECTVPKVTVIT FT RKAYGGAYDVMASKHLRGDVNLAWPSAEIAVMGPKGAVEIIFREEKNNPEKLAEREAEY FT KAKFANPFVAASRGFIDDVVMPHNTRKRICRSLAMLADKQLDNPWRKHGNIPL" FT CDS 727372..729378 FT /transl_table=11 FT /gene="pccA" FT /locus_tag="azo0688" FT /product="probable propionyl-CoA carboxylase alpha chain" FT /function="Acetyl/propionyl-CoA carboxylase alpha subunit" FT /EC_number="6.4.1.3" FT /note="Activity:- ATP + propanoyl-CoA + HCO3- = ADP + FT phosphate + (S)-methylmalonyl-CoA Entry name :- Q8U9Z4 FT Primary accession number:- Q8U9Z4 InterPro:- IPR001882; FT Biotin_BS. IPR005482; Biotin_carb_C. IPR000089; FT Biotin_lipoyl. IPR005481; CPase_L_N. IPR005479; FT Cphp_synth_L_D2. Pfam:- PF02785; Biotin_carb_C; 1. PF00364; FT Biotin_lipoyl; 1. PF00289; CPSase_L_chain; 1. PF02786; FT CPSase_L_D2; 1. Identities = 400/673 (59%) Prediction: FT Non-secretory protein Signal peptide probability: 0.000 FT Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K3A0" FT /db_xref="InterPro:IPR000089" FT /db_xref="InterPro:IPR001882" FT /db_xref="InterPro:IPR004549" FT /db_xref="InterPro:IPR005479" FT /db_xref="InterPro:IPR005481" FT /db_xref="InterPro:IPR005482" FT /db_xref="InterPro:IPR011053" FT /db_xref="InterPro:IPR011054" FT /db_xref="InterPro:IPR011761" FT /db_xref="InterPro:IPR011764" FT /db_xref="InterPro:IPR013815" FT /db_xref="InterPro:IPR013816" FT /db_xref="InterPro:IPR013817" FT /db_xref="InterPro:IPR016185" FT /db_xref="UniProtKB/TrEMBL:A1K3A0" FT /protein_id="CAL93305.1" FT /translation="MFTKILIANRGEIACRVIKTARKMGIKTVAVYSEADKDALHVDLA FT DEAVCIGPAPSKDSYLVMDRIIAACKQTGAEAVHPGYGFLSENAEFSRRLEEEGIKFIG FT PKHYSVAKMGDKIESKKLAIEAKVNTIPGYNDAIAGPAEAVEIAKKIGYPVMIKASAGG FT GGKGLRVAYNDEQAFEGFSSCVNEARNSFGDDRVFIEKYVLEPRHIEIQVLGDSHGNYV FT YLNERDCSIQRRHQKVIEEAPSPFVDAEMRKAMGEQAVALARAVNYESAGTVEFVVSGA FT TKEFYFLEMNTRLQVEHPVTELITGLDLVEQMIRVAAGEKLPLSQADVKINGWAMECRI FT NAEDPFRGFLPSTGRLVRFQPPAEVDGQVRVDTGVYDGGEISMFYDSMIAKLIVHGATR FT DQAIGRMRDALNAFVIRGISSNIPFQAALMQHPRFCSGNFNTGFIAEEFPKGFDASMVP FT HDDPALLAAVAAYVHRSYIDRAARVSGQLPGHERAVGNEWVVIRLGTDNQNELLPVTAT FT PVAGGYAVTLNGETYTIKSDWQLGQALFNGTCNGNEFTLQVERHKMRYRLFHWGTQADF FT LVMSKRAAELQSLMPVKLPPDLSKFLLSPMPGLLREVSVSEGQEVKAGEKLAVIEAMKM FT ENLLKAEQDGKVKKVVIKPGASLAVDDVIIEFE" FT CDS 729561..732017 FT /transl_table=11 FT /locus_tag="azo0689" FT /product="GGEF/EAL/PAS/PAC-domain containing protein" FT /function="predicted signal transduction protein containing FT a membrane domain an EAL and a GGDEF domain" FT /note="GGEF/EAL/PAS/PAC-domain containing protein, sym; FT pNGR234a) / TREMBL: trembl|Q7NYX4 (40% Chromobacterium FT violaceum, cv1148) InterPro: IPR000160 GGDEF. IPR000014 FT PAS. IPR000700 PAS-assoc_C. IPR001633 EAL. Pfam: PF00990 FT GGDEF domain. PF00989 PAS domain. PF00785 PAC motif. FT PF00563 EAL domain. TIGRFAM:TIGR00229 PAS domain S-box. FT TIGR00254 putative diguanylate cyclase (GGDEF) domain." FT /db_xref="GOA:A1K3A1" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001633" FT /db_xref="InterPro:IPR013655" FT /db_xref="InterPro:IPR013656" FT /db_xref="InterPro:IPR013767" FT /db_xref="UniProtKB/TrEMBL:A1K3A1" FT /protein_id="CAL93306.1" FT /translation="MEPTLPVDLETVADEGEDSLLRALIDVIPDLVFFKDEAGRYLGCN FT RAFEAYTGRREAELIGYTDRDLFDLSTADSYRGYDNAVLASGRSSRNEEWIVYPDGRRV FT LVDTLKTPFRDAASGRRGVVGISRDVTVFRETAEALRRSQENLERAQAVARTGSWYVDF FT VSGQMDWSAETCRLFGQAPGCVPSYELFLSVVHPEDQALVEAAWRQAVARGDYDLTHRV FT IVGGEVRWVHERAEFRRAADGAALAGIGTVQDITDRKLAEQSLRQAATVFENTGEGVII FT ADAKNRIIAVNRAFTVITGYGPEEVIGRSPNLLRSGRHDAAYYDAMWRGVHEAGHWQGE FT IWNRRKNGEIFPELLTLSVVRDHNGKVSHYVGVFSDISRMKETEARLQRLAHYDALTDL FT PNRVLLNLRLAHGVERVQRSGEMLAVLFLDIDRFKNVNDSLGHPVGDELLIEIARRLRS FT RIRAEDTLARLGGDEFVILLDRIRSANDVADFAQEIIDLLNQSFQLASGQEVFVGASIG FT ISLYPLDTDDATQLISNADAALYQAKEAGRNVYRFYTADLTRAAHERLGLEAALRRGLE FT RGEFVLHFQPVVALDKGEVVGAEALVRWNHPTEGMIAPLRFIPLAEETGLIVPLGEWVL FT ESACRQGREWLDCGRPLTIAVNLSTRQFRAGDLTATVRDILDRTGFPAALLELEITEST FT VMEDADRAVATLAALKGLGVRLSIDDFGTGYSSLAYLKRFAVDALKIDRSFVRDIADDE FT NDRMIVATVVAMAHQMRLGVIAEGVETAEQLAFLRSLGCEAYQGYLVGRPQAAADFLGA FT VERAGI" FT CDS 732026..733909 FT /transl_table=11 FT /locus_tag="azo0690" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to PA4929 FT of P.aeruginosa of 32% (trembl|Q9HUN5(SRS)). Signal P FT reporting presence of signal peptide. 7 TMHs Has PF07696: FT 7TMR-DISM extracellular 2; This entry represents one of two FT distinct types of extracellular domain found in the FT 7TM-DISM (7TM Receptors with Diverse Intracellular FT Signalling Modules) bacterial transmembrane proteins. It is FT possible that this domain adopts a jelly roll fold and acts FT as a receptor for carbohydrates and their derivatives. Has FT PF07695:7TM diverse intracellular signalling domain;This FT entry represents the transmembrane region of the 7TM-DISM FT (7TM Receptors with Diverse Intracellular Signalling FT Modules). Has IPR000160;GGDEF:(SM00267)This domain is found FT linked to a wide range of non-homologous domains. The FT function of this domain is unknown This domain is found in FT proteins which contain bacterial signaling domains. Has FT PF07696:7TMR-DISM extracellular 2 domain;This entry FT represents one of two distinct types of extracellular FT domain found in the 7TM-DISM (7TM Receptors with Diverse FT Intracellular Signalling Modules) bacterial transmembrane FT proteins. It is possible that this domain adopts a jelly FT roll fold and acts as a receptor for carbohydrates and FT their derivatives." FT /db_xref="GOA:A1K3A2" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR011622" FT /db_xref="InterPro:IPR011623" FT /db_xref="UniProtKB/TrEMBL:A1K3A2" FT /protein_id="CAL93307.1" FT /translation="MTSVRQWAARLIWAMLAWALAIAAGGARADDIALDPAHGEVDLAR FT RVSVLVDDGRSLSLEAAKAAFARGEGAPAEPARGGELNFGYRAADIWLHFSVAAAAPDD FT ARWLLEVGFPSLDRVEFHAFGPGGEAHQVAGDRIAFHARPWQHRSPVFPLPQLAPGERL FT EVYVKVASEGSLTVPLRLWTQTALGARDQRAYSEDALYFGMLTALALYNLLLWVALREQ FT VFLRYVGFVASLAVGFAGQTGAGGEFLWPAWPTWSHLSFPVGMALTGFFGTLFTRSFLD FT TRNTVPRLDRCLAVAAWVFLAAVAAHLVVGYRFAAMLTSLAGIGFAPIAALAGVRGAVR FT GHPGARVFLLAWALLLVGVVVMAMRNFGWLPTVWLTTHAMQIGSALEMLLLSFAMADRI FT NVMRREREAARQALVDTLQEAGQRLEQRVAERTAELQAANRRLRDNELALQQLAFHDPL FT TGLYNRVMLEERIRHAMLRADRQDTQLAVLLLDLDGFKAVNDGYGHAVGDAVLAAAATR FT MKAQVRASDTVARLGGDEFVVVLEPFSGEDQAVRVAAKLVAALAEPVVESGVAHQIGAS FT IGIALYPADGRDVDQLILAADRAMYRVKAAGKGGWRRNSPEQAAHPAGLRP" FT CDS 734005..734865 FT /transl_table=11 FT /locus_tag="azo0691" FT /product="conserved hypothetical metallopeptidase" FT /function="predicted metalloprotease" FT /EC_number="3.4.-.-" FT /note="Conserved hypothetical metallopeptidase. Homology to FT bpp2257 of B. parapertussis of 63% (trembl|Q7W887). Members FT of this family of bacterial proteins are described as FT hypothetical proteins or zinc metallopeptidases. The FT majority have a HExxH zinc-binding motif characteristic of FT neutral zinc metallopeptidases, however there is no FT evidence to support their function as metallopeptidases. FT Pfam: putaive neutral zinc metallopeptidase no signal FT peptide 1 TMH" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3A3" FT /db_xref="InterPro:IPR007343" FT /db_xref="UniProtKB/TrEMBL:A1K3A3" FT /protein_id="CAL93308.1" FT /translation="MRFDHGRESDNIEDRRGEGGGGFRLGGGGKLGLGGIVLTLVALYF FT GVDPALLLQTAEVVRPPAAVERPASRPQDEAGRFVSMVLADTEDTWSDIFSGAGRTYQA FT PRLVLFSGVTGTACGTGQAAMGPFYCPADQKVYIDLSFYDDLQQRFRAPGDFAQAYVIA FT HEIGHHVQNLLGVSERAQRARARLSPRESNALSVRLELQADCFAGVWAHHADRSRQVLE FT AGDVEEALTAAAAIGDDRLQKQAQGYAVPDSFTHGSAEQRVRWFRTGLQHGSLQACDTF FT AARSP" FT CDS complement(734887..735363) FT /transl_table=11 FT /gene="gloA1" FT /locus_tag="azo0692" FT /product="probable lactoylglutathione lyase" FT /EC_number="4.4.1.5" FT /note="Glyoxalase I (lactoylglutathione lyase) catalyzes FT the first step of the glyoxal pathway in the following FT reaction: glutathione + methylglyoxal = FT (R)-S-lactoylglutathione," FT /note="Function unclear" FT /db_xref="GOA:A1K3A4" FT /db_xref="UniProtKB/TrEMBL:A1K3A4" FT /protein_id="CAL93309.1" FT /translation="MSQRPFKILGVQQIAIGGPSKEKLKTFWVDMLGLEVTGNFVSERE FT NVDEDICAMGKGPFKVEVDLMQPLDPEKKPAVHATPLNHIGLWVDDLPVAVEWLTAQGV FT RFAPGGIRRGAAGYDITFLHPKGNEEFPIGGEGVLVELVQAPPEVVEAFARLAG" FT CDS complement(735949..736680) FT /transl_table=11 FT /gene="virG" FT /locus_tag="azo0693" FT /product="probable DNA-binding response regulator" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="Probable DNA-binding response FT regulator,Response_reg. IPR001867; Trans_reg_C. Pfam: FT PF00072; response_reg. PF00486; trans_reg_C. SMART: FT SM00448; REC." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3A5" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:A1K3A5" FT /protein_id="CAL93310.1" FT /translation="MSATRPEASPPTIFVLEDEPDIARLICSSLTEYGFRCEHLTTGRQ FT LLQRARQQTPDLCIVDLGLPDMDGMQVVRELQDGSPCAVLILTGRNDVTDRVLGLELGA FT DDYIVKPFEPRELVARVRSILRRYQRSAPPETSAAEKTVARFAGWTFDGGRLTMTAPDG FT REVNLSAAEASLLAVLLRRPNKIFSREQLLGERDVDPFDRSIDVRISRLRRKLDDDPQN FT PRLIKTVYGAGYLFAAQVSWE" FT CDS complement(736677..738734) FT /transl_table=11 FT /locus_tag="azo0694" FT /product="putative hybrid sensor and regulator protein" FT /function="Signal transduction histidine kinase" FT /note="Putative hybrid sensor and regulator protein," FT /note="Specificity unclear" FT /db_xref="GOA:A1K3A6" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K3A6" FT /protein_id="CAL93311.1" FT /translation="MAKPADHSPTPEQRRRYDLLLAGLDLLDQAIAVFDAAPKLVTWNK FT ALLRLLDFPESMVRVGTPFEDFVRFNAERGEYGDGDLERLVNERMAAARSFQPHYAERA FT RPNGKILAIRGVPIPNLGFVSLWTDITEQRRYETVIQEQNSRLEDRVRARTAELEEANA FT HLARAKADIDDIAGALSKSEERLRLILDSIPALIAHVDASQRYLFANRSYAQWFGTTKE FT EIVGRSIAEVFGARAYAAISPHLENATHGERVTYEYSRKNADGQTVHARSVVVPDVSAE FT GGFQGYFVLSIDITEQKAHQAALVQAQKMEAVGQLTGGLAHDFNNLLTIIIGNLSALQT FT QLGDGPGAEYVAPALQASRRGAELIKRLLSFSRRQPLEPSAVEVGALVQNMSHLLERSL FT SETITVRLALPAEPLHALVDPHQLENALLNLALNARDAMPEGGQLTITVTRREIDLDIA FT RLVEVPAGSYVQIDVTDTGSGIDPALLPRLFEPFFTTKPFGIGSGLGLSMVYGFVRQSG FT GNIRILSTPGEGTNVRFVLPMTQPAPPPSPESAPAAAAPQLRSGPVLLVEDEPAVRQVI FT RMQLTALGYPVIEAENGVEALSLLENVEDIAILVSDTVMPGGIGGRELAARARRLRPDL FT PILLITGYASSSGNPTPPPADIPVLRKPFDQAALAAALQNIHPPQEHEPS" FT CDS complement(738888..739898) FT /transl_table=11 FT /gene="oruR1" FT /locus_tag="azo0695" FT /product="putative ornithine utilization regulator" FT /function="AraC-type DNA-binding domain-containing FT proteins" FT /note="Putative ornithine utilization regulator," FT /note="Specificity unclear" FT /db_xref="GOA:A1K3A7" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR018060" FT /db_xref="UniProtKB/TrEMBL:A1K3A7" FT /protein_id="CAL93312.1" FT /translation="MTGMLAGLQRRGLDAAPLLAVAGVGLADSASRIPVDRYAALYNLI FT VRELDDEGFALFAARMPVGSFEFLCRGMLGAASLAEALDRAARFLRIVLPDLAVTVVRE FT PGAGHAELRIAETRPLAADTDDPARVFAFEWLLRLLHGVACWFVGRGLALDAVRFPYAR FT PAHADDYALVYTEHSSFGGDALVARFQANLLDLPLRRDDAALAAFLDGAPGKITMLYRR FT DREMVFRVRDILRDALPENLSLDEVADRLHQSPRTLARRLEEEGSGFRTIKDATRRDIA FT LARLTKTRQPIAQLAADLGYADTSAFYRAFVAWTGVSPERFRGRLGERAAPAQGG" FT CDS 740204..743470 FT /transl_table=11 FT /locus_tag="azo0696" FT /product="probable methylmalonyl-coa mutase protein" FT /function="Methylmalonyl-CoA mutase N-terminal FT domain/subunit" FT /EC_number="5.4.99.2" FT /note="Methylmalonyl-CoA mutase mitochondrial precursor (EC FT 5.4.99.2) (MCM). INVOLVED IN MAN IN THE DEGRADATION OF FT SEVERAL AMINO ACIDS ODD-CHAIN FATTY ACIDS AND CHOLESTEROL FT VIA PROPIONYL-COA TO THE TRICARBOXYLIC ACID CYCLE. MCM HAS FT DIFFERENT FUNCTIONS IN OTHER SPECIES. Activity:- FT (R)-2-Methylmalonyl-CoA = succinyl-CoA Entry name FT :-TREMBL:Q8Y2U5 Prim. accession # Q8Y2U5 Identities = FT 797/1103 (72%) InterPro:- IPR006159; Acid_CoA_mut_C. FT IPR005129; ArgK. IPR006158; B12-binding. IPR006099; FT MMCoA_mutase. IPR006098; MMCoA_mutase_N. Pfam:- PF03308; FT ArgK; 1. PF02310; B12-binding; 1. PF01642; MM_CoA_mutase; FT 1. Prediction: Non-secretory protein Signal peptide FT probability: 0.005 Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K3A8" FT /db_xref="InterPro:IPR005129" FT /db_xref="InterPro:IPR006098" FT /db_xref="InterPro:IPR006099" FT /db_xref="InterPro:IPR006158" FT /db_xref="InterPro:IPR014348" FT /db_xref="InterPro:IPR016176" FT /db_xref="UniProtKB/TrEMBL:A1K3A8" FT /protein_id="CAL93313.1" FT /translation="MTDLSIAKKLSPYKPKNKVRFVTAAALFDGHDASINIMRRILQST FT GAEVIHLGHNRSVGEIVKAALQEDVQGIAITSYQGGHVEFFKYMIDLLKANGGENIKVF FT GGGGGVIVPSEIKELHDYGVTRIYSPEDGATIGLQGMINDVVERSDVDLTHVAPKSADE FT MLKRLASGDRRALAQIITALENGACGDDVKQAIKDAAAKCKTPTLGITGTGGAGKSSLT FT DELVRRFRLDHNDTLRIAIVSIDPSRKRTGGALLGDRIRMNAIEHEHIFMRSLATRDTG FT SEVSAALPEVIAACKLSGFDLVIVETSGIGQGDAAIVPFVDLSLYVMTPEFGAASQLEK FT IDMLDFADFVAINKFDRKGAEDALRDVRKQYQRNRELFTQPTDDMPVFGTMAARFNDDG FT VTALYQAIFPRLVEKGLKAKGGKLPLVTVKASSKGRAIVPAERTRYLAEIADTVRDYHK FT HVLQQARVARERQSLKTAKALFEQCGKDVGSFDELINWKDGELTPVAKKLLEQWPTEKA FT LYAADEYVVKIRDKEIRTKLTYESLSGSKIRKVALPNFDDDGETLKFLMKENVPGSFPY FT TAGVFAFKREGEDPTRMFAGEGDAFRTNRRFKKVSEGMPAHRLSTAFDSVTLYGCDPDL FT RPDIYGKIGNSGVSIATLDDMKVLYDGFDLCCPTTSVSMTINGPAPIILAFFFNTALEQ FT QLAKFKADNGRDPTEDEYAKIRAWTLSSVRGTVQADILKEDQGQNTCIFSTEFALKMMG FT DIQEFFVRNKVQNFYSVSISGYHIAEAGANPISQLAFTLANGFTYVESYLARGMHIDDF FT APNLSFFFSNGMDPEYTVIGRVARRIWAVAMKNKYGANERSQKLKYHVQTSGRSLHAQE FT MDFNDIRTTLQALIAIYDNCNSLHTNAYDEAITTPTEESVRRAMAIQLIINREWGLAKN FT ENPNQGSFIVEELTDLVEEAVLKEFEAIASRGGVLGAMETGYQRGKIQEESLYYEHKKH FT DGSYPIIGVNTFLNPKGQAQQEIELARSTEEEKQSQLARLKDFHARNKAEAPKWQAKLQ FT QTVIENGNVFEVLVDAVRYCSLGQITEALYKVGGQYRRSM" FT CDS complement(743567..743848) FT /transl_table=11 FT /locus_tag="azo0697" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. no homology to the FT data bank. no domains predicted. signal peptide. no TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K3A9" FT /protein_id="CAL93314.1" FT /translation="MSFFGFIPVRRGRSCGQAVGPVRSALSAMAFFALHKNVASAPAPY FT AGRISAACPRPRAVDKRVRRGFPRPQRPLSTPPVDHAVDKLWAARGDA" FT CDS complement(743845..745224) FT /transl_table=11 FT /gene="fumC" FT /locus_tag="azo0698" FT /product="fumarate hydratase" FT /function="Fumarase" FT /EC_number="4.2.1.2" FT /note="Fumarate hydratase. Homology to fumCo f P. FT aerunigosa of 76% (sprot|FMC1_PSEAE). Catalyzes the FT reversible hydration of fumarate to L-malate. Tigrfam: FT aspA: aspartate ammonia-lyase Pfam: Lyase no signal peptide FT no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3B0" FT /db_xref="InterPro:IPR000362" FT /db_xref="InterPro:IPR003031" FT /db_xref="InterPro:IPR005677" FT /db_xref="InterPro:IPR008948" FT /db_xref="InterPro:IPR018951" FT /db_xref="InterPro:IPR020557" FT /db_xref="InterPro:IPR022761" FT /db_xref="InterPro:IPR024083" FT /db_xref="UniProtKB/TrEMBL:A1K3B0" FT /protein_id="CAL93315.1" FT /translation="MDPSTRIERDSMGEMAVPLAALYGAQTQRAVLNFPISGQRLPPAF FT IRALLLVKLAAARANVELGQLPAPTGEAIAQACEQLLAGEFMQHFPVDVFQTGSGTSSN FT MNANEVVATVASRILGAPVSPNDDVNHGQSSNDTVPSAIHIAAAIALAGELLPALRYLA FT HTIRDKARTVHHHVKTGRTHLMDAMPVRMSQVLNGWAQQLDTDIEHLRALQPSVQSLAQ FT GGTAVGTGINAHPQFAACFCAELGRLTGLGFTPAHDYFALMGAQDVAVALSGQLKTTAV FT SLMKIANDLRWMNSGPLAGLGEIELEALQPGSSIMPGKVNPVIPEATCMVAAQVIGNDA FT AITVAGQSGNFELNVMLPLIAHNLLGSLHLLTTTSRLLADRAIAGFRVNDARLKEALAR FT NPILVTALNPVIGYAKAAEIAKQAYREGRPIIDVAAEQTGIDRAELERLLDPEKLTAGG FT L" FT CDS complement(745304..746044) FT /transl_table=11 FT /locus_tag="azo0699" FT /product="hypothetical secreted protein" FT /function="function unknown" FT /note="Hypothetical secreted protein. No significant FT homology to the data bank. no domains pedicted. signal FT peptide. TMH in signal peptide" FT /db_xref="InterPro:IPR013424" FT /db_xref="UniProtKB/TrEMBL:A1K3B1" FT /protein_id="CAL93316.1" FT /translation="MTKRSLLLPALFAAASCLPGAASAALYTTALGSQIASLSDCDDCY FT SGPYGFGAGHSLSYFGGSYNGLYVGSNGYVTLGEGVSDFVTRPLDTQDLAPMIAALFTD FT LDSRADDASRVYVNTAQAGQIIVTWSQMGHYDTTYSVRSTFQLVIRSDQFAYAKGEGQV FT GFFYDTITDDAIASAGFGDGYFPSIPGEVALFLGPASAQSGAAPRWFVLRDGIPDVVGQ FT VPEPGALGLAALGLLGLGLRRRRG" FT CDS complement(746188..747486) FT /transl_table=11 FT /locus_tag="azo0700" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Hypothetical protein, 52% identity to TrEMBL;Q8XYG9. FT Has PF03781, Domain of unknown function (DUF323);IPR005532 FT ;This presumed domain is found in bacterial proteins. In FT some cases these proteins also contain a protein kinase FT domain. The function of this domain is unknown. The domain FT has also been found in a eukaryotic protein, required for FT post-translational sulphatase modification." FT /note="Function unclear" FT /db_xref="GOA:A1K3B2" FT /db_xref="InterPro:IPR005532" FT /db_xref="InterPro:IPR016187" FT /db_xref="InterPro:IPR017806" FT /db_xref="InterPro:IPR024775" FT /db_xref="UniProtKB/TrEMBL:A1K3B2" FT /protein_id="CAL93317.1" FT /translation="MNTLLHTADRGDELDRAAWAQRYRRVRDASTDLCAPLAVEDYVIQ FT ACEEASPAKWHLAHVSWFFETFILTEYLPGYSEFHPRYRQLFNSYYQQIGEVFPRAARG FT TLARPTVDEVLRYRAHVDAGMLALLAERADLPWAEILQRLEIGLNHEQQHQELLLTDIK FT RNFAANPLRPAYRLDLPHPAQRPRAPLEWVSFEGGVYEIGAPALGEHFSYDNETPRHRV FT YLQPFRLASRLVTNGEFLAFIESGGYSNPALWLADGWTQVRSAGWSAPLYWERIGGEWW FT HYTLGGMAPLAPDEPVCHVSHYEAAAYAAWAGRRLPTEAEWEVAAATQPVAGNLRETGL FT LRPTVAPAGAGPAQLYGDVWEHTGSAYLPYPGYHAAEGAIGEYNGKFMCNQMVLRGGSC FT VTPADHLRATYRNFFYPQERWQFQGFRLAEDAT" FT CDS complement(747598..748953) FT /transl_table=11 FT /gene="nagZ1" FT /locus_tag="azo0701" FT /product="putative beta-hexosaminidase" FT /function="Beta-glucosidase-related glycosidases" FT /EC_number="3.2.1.52" FT /note="(N-acetyl-beta-glucosaminidase)(Beta-N- FT acetylhexosaminidase). Cleaves GlcNAc linked beta-1,4 to FT MurNAc tripeptides (By similarity). Hydrolyzes rapidly FT p-nitrophenyl-N-acetyl-beta-D-glucosaminide FT (PNP-beta-GlcNAc) and 4-methylumbelliferyl-beta-GlcNAc, and FT slightly active on p-nitrophenyl-beta-GalNAc. May play a FT role in signal transduction between host and organism. 34% FT Glyco_hydro_3N. Pfam:PF00933; Glyco_hydro_3; 1. TMhelix:2." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3B3" FT /db_xref="InterPro:IPR001764" FT /db_xref="InterPro:IPR017853" FT /db_xref="UniProtKB/TrEMBL:A1K3B3" FT /protein_id="CAL93318.1" FT /translation="MRAGARLLRWGSAALALLLAHDPHTPYLLAVRGVIVPALVVAGVL FT GAAWAGRAACRRRLAWREAAALAAAGITVATLALADAHRFAAARLEVLAAGASDPQLRR FT LGAHFMIGYRDADEVAALAERGLIGGIYLGRHNVRGRSVEAVRAEIDRLQALRARNALP FT PLIVAADQEGGSVAHMSPPLAPQPALASVLAGDDAGLEMRARDYGRLQGAGLAALGVTL FT NFGPVVDLRPAHGGPLFDTHTRIGERAIDGDPARVARVARAYAEGLADAGVQATLKHFP FT GLGGVMRDTHHFAARLDTPGAALAAHDWQAFRGAAPASAAIMVGHVVLPELDADRPASL FT SPAVVQGLLRRGWGYQGLLVTDDLNMGAVYRRGTCRAAVEALEAGIDLVLISYDPAQFY FT RALLCARRAFDEGRLQPALLAAGRRRLAAAAHLSTAAGGQAVREMWTQAASP" FT CDS complement(748950..750281) FT /transl_table=11 FT /gene="creD" FT /locus_tag="azo0702" FT /product="inner membrane protein CreD" FT /function="Inner membrane protein involved in colicin E2 FT resistance" FT /note="CreD confers tolerance to colicin E2. Similar to FT SWISSPROT:P08369 (35% identity). TMHMM reporting six FT transmembrane helices." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR010364" FT /db_xref="UniProtKB/TrEMBL:A1K3B4" FT /protein_id="CAL93319.1" FT /translation="MQRKLFAKLGIIVLLSIILLIPLAMIEAQIAARSERQDEVVEDIA FT ASAAGPQTLVGPVLSVRYRERVTLRQRDAAGKETVQREIVERVLVLPPAVLGIDGDASV FT ETRQRGLYRANLFHLAAHLQGHFEVPPRLGLDEGRELVDARAALVLGLGDSRGVGNDPE FT VKVNGRAHRFTPGGGGALDGAALQVDLGALALDGQRLEFAFPLALTGSSRLAIAPAGDA FT TTVTLRSPWPHPSFQGRFLPLSRSVSARGFEAQWQVSHLARSFDRVLATAAGEDRGRPE FT ALVVGFIEPVNVYLKAERAVKYGVLFVVLTFAAFFLTEVLRRLPIHPLQYLLVGLALAV FT FFLLLVALSEHLAFGLAYALSAAACVALIGSYLAGALGSARRGAAYGGGIAALYGVLYG FT VLLSEDNALLMGALLLFAALAASMLATRRIDWYRLGATAPGEAA" FT CDS complement(750394..751824) FT /transl_table=11 FT /gene="creC" FT /locus_tag="azo0703" FT /product="catabolite repression sensor kinase for PhoB" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.13.1" FT /note="Sensor protein creC," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3B5" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="UniProtKB/TrEMBL:A1K3B5" FT /protein_id="CAL93320.1" FT /translation="MNIAIRFFIGYFLIVGLAAWFVLNIFAREVEPGLRQATEDTLVDA FT ANLLAEFAAEHLGPGDGGFERDRFATAVRRAQARVPRADIYGVPKTAVDFRVYLTDARG FT IVLFDSEGSAEGADYSQWRDVARVLRGEYGARSTRDDPADPNSSVMYVAAPVLLDGRLA FT GVVSVAKPAAALLPYADQARDRVRRAGWLLLGSSALIGLAFTLWLTWSLNRLRDYARAV FT ARGDKAVAPTGGGGQLSELARALAEMRARLDGKQYVEHYVQSLAHELKSPLTAVRGAAE FT LLAEAPSADDRARFVGHIGEQAERMQLIIDRLLALARVEQLQAPEALAEIALGELAAEV FT VASRQPQLAARGLQVDIGGEGERRVRGDRFLLQQALANLVDNAIDFSPPGARIGLTLGG FT DASHHVITVRDHGPGAPEFALPQLFERFYSLPRPATGRKSTGLGLAFVREVARVHGGDA FT DFANAPEGGAQARIVLPR" FT CDS complement(751848..752555) FT /transl_table=11 FT /gene="creB" FT /locus_tag="azo0704" FT /product="two-component system regulatory protein" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="transcriptional regulatory protein FT creB,Response_reg. IPR001867; Trans_reg_C. Pfam:PF00072; FT response_reg. PF00486; trans_reg_C. SMART:SM00448; REC. FT Transcriptional regulatory protein creB. MEMBER OF THE FT TWO-COMPONENT REGULATORY SYSTEM CREC/CREB INVOLVED IN FT CATABOLIC REGULATION." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3B6" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K3B6" FT /protein_id="CAL93321.1" FT /translation="MSRRILIVDDEPAIADMLAYALRTEGYEPDCVGLGGDALAALRGG FT ADYALVILDVGLPDQSGFDVCRALRRESDVPVIFLTARSDEVDRIVGLELGADDYVPKP FT FSPREVASRVRAILRRARPQPAAVAPAPAAETCSAPFHHDAAGARIAYHGVWLSLTRYE FT YRLLATLLDRPGRVQSRAQLMADVWRDAEDSLERTVDAHIKTLRAKLRAVREDEDPIET FT HRGLGYSLRPAQR" FT CDS complement(752570..754012) FT /transl_table=11 FT /gene="mgtE" FT /locus_tag="azo0705" FT /product="putative magnesium transport protein" FT /function="Mg/Co/Ni transporter MgtE (contains CBS domain)" FT /note="Probable magnesium transporter, MgtE. Members of FT this family probably transport Mg2+ or other divalent FT cations into the cell. 26% CBS_domain.IPR006667; FT MgtE_integrmembr. Pfam:PF00571; CBS; 2.PF01769; MgtE; 1. FT TMHleix: 3." FT /note="Function unclear" FT /db_xref="GOA:A1K3B7" FT /db_xref="InterPro:IPR000644" FT /db_xref="InterPro:IPR006667" FT /db_xref="InterPro:IPR006668" FT /db_xref="InterPro:IPR006669" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:A1K3B7" FT /protein_id="CAL93322.1" FT /translation="MTPEEELHPDDVQHHLREVQELLARQKLVEDLVHRQDMPRHELVE FT SLVHKQHVAELRSKLDSLHPADIAYILEALPLEERLFVWDLVKAERDGEILLEVSDAVR FT ESLIETMAPEELKAAAETLDADELADLAPDLPPEVIQDVFQSLDHEGREQLRAAMSYPE FT DSVGALMDFDLMTVREDVTLEVVLRYLRRFDELPDHTDKLFVVDREDRLKGILSLESLL FT LNDPESLVADVMRKEVMISFEPADDADDAAQAFERYDLVSAPVIGPDKRLIGRLTVADV FT VDYIREESEAEILSHAGLREEEDIFASVWDSVKNRWSWLAVNLVTAFVASRVIGAFEGS FT IEKLVALAALMPIVAGIGGNSGNQTVTMIVRAIAIGQVEQSAMQRLLKKEISVALINGL FT VWGGLLGILSWWLYHSAALGVVMTAAMTLNLLLAATAGVAIPMLRQRLGADPAIGGSVM FT ITALTDSGGFFIFLGLATLFLL" FT CDS complement(754167..754862) FT /transl_table=11 FT /gene="mtgA" FT /locus_tag="azo0706" FT /product="probable monofunctional biosynthetic FT peptidoglycan transglycosylase" FT /function="Membrane carboxypeptidase (penicillin-binding FT protein)" FT /EC_number="2.4.2.-" FT /note="Probable monofunctional biosynthetic peptidoglycan FT transglycosylase. Homology to mtgA of N. gonorrhoeae of 43% FT (sprot|MTGA_NEIGO) Cell wall formation (By similarity). The FT transglycosylase domain catalyses the polymerisation of FT murein glycan chains. Pfam: Transglycosylase signal peptide FT no TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K3B8" FT /db_xref="InterPro:IPR001264" FT /db_xref="InterPro:IPR011812" FT /db_xref="UniProtKB/Swiss-Prot:A1K3B8" FT /protein_id="CAL93323.1" FT /translation="MKTLWRWLGRALLAAFALLLLWQVWLFAQVAWWRTHNPDSTSFMR FT LRLDALQEKKPDARLRHTWVPYEQISIHLKRAVVAAEDDGFVDHEGFDWDGIQRALEKN FT ERKGRPVSGGSTISQQLAKNLFLSPSRSYFRKAQEAVITVMIEQLWSKRRILEVYLNVV FT EWGNGIFGAEAAARRYYGLPASRLGPAEAARLAVMLPNPRKYERSFGPRLAAHADRIRG FT RMAWAEVPP" FT CDS complement(754859..755704) FT /transl_table=11 FT /gene="aroE" FT /locus_tag="azo0707" FT /product="AroE protein" FT /function="Shikimate 5-dehydrogenase" FT /EC_number="1.1.1.25" FT /note="Shikimate 5-dehydrogenase catalyses the conversion FT of shikimate to 5-dehydroshikimate. This reaction is part FT of the shikimate pathway which is involved in the FT biosynthesis of aromatic amino acids. Similar to FT sprot|AROE_ECOL6 (51%), to trembl|Q7W3V3 (45%) and to FT sprot|AROE_PSEAE (43%). TIGRFAM: aroE, shikimate FT 5-dehydrogenase Pfam: Shikimate / quinate 5-dehydrogenase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3B9" FT /db_xref="InterPro:IPR006151" FT /db_xref="InterPro:IPR011342" FT /db_xref="InterPro:IPR013708" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR022893" FT /db_xref="UniProtKB/Swiss-Prot:A1K3B9" FT /protein_id="CAL93324.1" FT /translation="MDRYAVVGNPIAHSKSPQIHAAFAHQTGEALGYEAILAPLDGFVD FT TVLAFRAVGGRGMNVTVPFKLEAHALATRLTPRAAAAGAVNTLAFGGPETPDDILGDNT FT DGAGLVRDLTVNLGCPLHGRRVLLLGAGGAARGALLPLLEQAPAALTIANRTAAKAVEL FT AAGFAAGHPGVAIDGGGFDALAGRRFDVVINATAASLADQAPPLPAGIYAEGALAYDMM FT YGRGDTPFLAAARADGAGRLADGLGMLVEQAAESFLLWRGVRPDTAPVLADLRARLAAA FT " FT CDS complement(755718..756620) FT /transl_table=11 FT /locus_tag="azo0708" FT /product="conserved hypothetical secreted protein" FT /function="Periplasmic protein TonB links inner and outer FT membranes" FT /note="Conserved hypothetical secreted protein. Homology to FT ne1626 of N. europaea of 46% (trembl|Q82U75) no domains FT predicted signal peptide TMH in signal peptide" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3C0" FT /db_xref="InterPro:IPR006260" FT /db_xref="UniProtKB/TrEMBL:A1K3C0" FT /protein_id="CAL93325.1" FT /translation="MSPTLPPTRRAGRSATLGAIARGTPLLVLAFALSGLLHATLLAVH FT FVSPPPKPTRDRGLEVVLVNARHARAPDQAQVLAQANLDGGGTSDKAVTPKSPLPPQDA FT RREGTALTEARRKVQQQERTQQELLTRVKQAPAVASTREHAEQPAPTPQASGLDLLDSA FT AAIARIEAQIDRNLEEYAKRPRKKFIGARAREYRFAQYVEDWRLKIERIGTLNYPDAAR FT GKLYGSLLLSVSIRADGSVASVEVTRSSGHKVLDEAAMRIVNMSAPYAPFPPDISRDTD FT IIEIVRTWTFTNTDQVRAN" FT CDS complement(756666..758567) FT /transl_table=11 FT /locus_tag="azo0709" FT /product="putative exoribonuclease II" FT /function="Exoribonuclease R" FT /note="Putative exoribonuclease II (EC: 3.1.13.1), RNase R FT / VacB protein) / TREMBL: trembl|Q7P1X0 (50% FT Chromobacterium violaceum, probable ribonuclease ll,cv0092) FT InterPro: IPR001900 Ribonuclease_II. Pfam: PF00773 RNB-like FT protein." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3C1" FT /db_xref="InterPro:IPR001900" FT /db_xref="UniProtKB/TrEMBL:A1K3C1" FT /protein_id="CAL93326.1" FT /translation="MFVLFEEDGAFKAGTILAENDASLQVENTHGKRVKIKRANVLLNF FT REPSPADLLARAEAAAEALDTEFLWEVCGDDEFGFAEFAAEYHGHAPSAVEAATVLLRL FT HSAPIWFHRKGRGRFRKAPTEILQAALAGLEKKRQQALAIEEMRAELVEGRMPAAFAGM FT LPQILYRPDRNRIEVKALEAACVDTGLSAPRLLLKCGALASSFDYHFNRFLFEYFPEGL FT AFPDFEPPVVPADLPRADVAAFSIDDATTTEIDDAFSVTPRPGGGWRVGIHIAAPGLGC FT ERGSTLDTIARRRLSTVYMPGNKITMLPDQMVQAYTLAEGRDCPAVSLYLDVTADLAIL FT GQESRLEIVPIVANLRHHDIEPVFNDETVHEGVPDFPWKRELMLLWDLATVLEAGRGKP FT AANQNQVDHRFYVDWQTETADGPGYITIGKRLRGSPMDKLVAELMILANSTWGKLLDEA FT GVPGLYRVQSGGKVRMTTTAGPHEGLGVDCYAWSSSPLRRYVDLVNQWQIISVLQGRPP FT AFAPKSAELMAALRDFELTYAAYAEFQRQMERYWCVRWLRQHGAGPVDGIVLRDNVVRL FT EAVPLVFKVPSMPLQMPGSRVRLVVEGSDLLDVEVEARFQQILSEPDPEDYAEFEGP" FT CDS complement(758634..759479) FT /transl_table=11 FT /locus_tag="azo0710" FT /product="putative methyltransferase" FT /function="SAM-dependent methyltransferases" FT /note="Similar to TREMBL:Q8KNG7 (29% identity); FT TREMBL:Q8UEX8 (27% identity). Pfam (PF01209): ubiE/COQ5 FT methyltransferase family." FT /note="Function unclear" FT /db_xref="GOA:A1K3C2" FT /db_xref="InterPro:IPR013216" FT /db_xref="UniProtKB/TrEMBL:A1K3C2" FT /protein_id="CAL93327.1" FT /translation="MTQDAPFDPRRFKAQERAGFNRIAARYAGGAPLRAALAEAVLNAA FT RLEPGLRVLDLASGPGLLALPAATQVAPHGWVLATDIAETMLAEAARRSDDTAPLLFAA FT ADAEHLCVPDASIDRVLAGLALFLFPDPARALAEVGRVLAPGGRVVLSVWGPRAEVPLL FT HRAQDAIATALGPPRVARPSVFRLGEAGALAQLLDAAGFTDIRVEPCSFSCPFDDADAY FT WQAFLDLAGGVAEAMAQVPESRLAAVRAAVADAIAPHRLPAGGYRLPATALVAVARRPD FT " FT CDS complement(759510..760103) FT /transl_table=11 FT /locus_tag="azo0711" FT /product="conserved hypothetical protein" FT /function="predicted esterase" FT /note="Conserrved hypothetical protein. Homology to rsc2781 FT of R. solanacearum of 51% (trembl|Q8XVP9) Pfam: UPF0227 FT Despite being classed as uncharacterised proteins,the FT members of this family are almost certainly enzymes that FT are distantly related to the Abhydrolase_1. no signal FT peptide no TMHs" FT /db_xref="InterPro:IPR008886" FT /db_xref="UniProtKB/TrEMBL:A1K3C3" FT /protein_id="CAL93328.1" FT /translation="MSAPAPMIVYLHGFRSAPASVKAQALRARMAARGLGEAFWCEQLP FT VSPWAAVGLASAQIERSLANGGTPTVVGSSLGGYYATWLAEKYRLRAVLVNPAVVAPLS FT LEAYVGEQTNLYTGERFQFTQRHIDELRALEIPRITRPERYWLLVETGDEVLDYRHAVQ FT RYAGAHQTVLEGGDHGFSRWNDYLDDVIAFAGPV" FT CDS complement(760137..760961) FT /transl_table=11 FT /gene="uppP" FT /locus_tag="azo0712" FT /product="undecaprenol kinase" FT /function="uncharacterized bacitracin resistance protein" FT /EC_number="2.7.1.66" FT /note="Bacitracin resistance protein, may confer resistance FT to bacitracin by phosphorylation of undecaprenol, FT SWISSPROT:Q88IY7 (47% identity); TREMBL:Q82Y49. InterPro FT (IPR003824): Bacitracin resistance protein BacA. Pfam FT (PF02673): Bacitracin resistance protein BacA. TIGRFAM FT (TIGR00753): Undecaprenol kinase,putative. TMHMM reporting FT seven transmembrane helices." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3C4" FT /db_xref="InterPro:IPR003824" FT /db_xref="UniProtKB/Swiss-Prot:A1K3C4" FT /protein_id="CAL93329.1" FT /translation="MDITLLLTALILGIVEGLTEFLPVSSTGHLIILGDLLGYNDEASK FT VFKIVIQLAAILAVCWDYRERLIKVAVGVPSDRSAQRFVGLLLLGFLPAAVLGFLFHST FT IKNVLFNPLVVATALVVGGLIILYVEKRAYHPRVTSVDEMRWGDALKVGFAQALAMIPG FT TSRSGATIMGGLIFGLSRKTAAEFSFFLAIPTMLAATVYDVYKNWTLLRVEDLPVFAVG FT FVASFFAAMWAVKSFIRFISNHTFVVFAWYRIVFGIVVLATWQFDLVSWSTP" FT CDS complement(761053..761304) FT /transl_table=11 FT /locus_tag="azo0713" FT /product="conserved hypothetical protein" FT /function="predicted Fe-S-cluster oxidoreductase" FT /note="Hypothetical protein PA1578.1. TREMBL:Q7W9P0:69% FT identity, 78% similarity TREMBL: Q8PDJ2: 69% identity, 74% FT similarity (predicted proteinase inhibitor)) Probable Fe-S FT cluster bearing oxidoreductase function. FT InterPro:IPR005358; UPF0153. Pfam:PF03692; UPF0153" FT /note="High confidence in function and specificity" FT /db_xref="UniProtKB/TrEMBL:A1K3C5" FT /protein_id="CAL93330.1" FT /translation="MDCRPGCAACCIAPSISSPIPGLPAGKPAGVRCPQLDDADRCRLF FT GNPTRPRVCGSLQPSAEMCGDSRAHALAWLTRLESLTA" FT CDS complement(761309..761842) FT /transl_table=11 FT /locus_tag="azo0714" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to RPA1001 FT of R.palustris of 37% (tremble:Q6NB29). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="InterPro:IPR018912" FT /db_xref="UniProtKB/TrEMBL:A1K3C6" FT /protein_id="CAL93331.1" FT /translation="MTAQTSSPLPIAAILYTPQDNIEMILMEAAAALGERGVRLGGVIQ FT HDIGISANDPCAMELEDLSSGARFSLSQELGRGSEACRLDPDALARASMIVRNGLDQGA FT DLVIFNKFGAQEAAGAGLRTEMGLAALAGTPLLTAVGHRFLPEWNDFTGGEGSLLQPTV FT ASVLAWWNSLRGDA" FT CDS complement(761844..762548) FT /transl_table=11 FT /locus_tag="azo0715" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to DP0001 FT of Desulfotalea psychrophila of 43% FT (gnl|keqq|dps:DP0001(KEGG)). No domains predicted. No FT signal peptide. No TMHs." FT /db_xref="UniProtKB/TrEMBL:A1K3C7" FT /protein_id="CAL93332.1" FT /translation="MSVPPQPCPLCLAAAAPFHLREARRRMPARDYHRCPVCALVFVPA FT PFHLDPAAERAEYDLHRNDPADTGYRRFLGRLVTPLAAMLPAGARGLDYGCGPTPALQL FT LLHESGFDCATYDPHYQPDPSVLDARYDFITCTEVAEHFAAPRQEFDLLHALLAEGGVL FT ALMTRRPDEHTDFANWHYSRDPTHIAFYAADTLRWIGRHYGMALTLADNDIALLHKRGV FT SATIPAPRPGAR" FT CDS 762691..766773 FT /transl_table=11 FT /gene="hrpA" FT /locus_tag="azo0716" FT /product="putative ATP-dependent helicase" FT /function="HrpA-like helicases" FT /EC_number="3.-.-.-" FT /note="ATP-dependent helicase hrpA. Not yet known. FT InterPro: DEAD/DEAH box helicase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3C8" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR007502" FT /db_xref="InterPro:IPR010222" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR011709" FT /db_xref="InterPro:IPR014001" FT /db_xref="InterPro:IPR024590" FT /db_xref="UniProtKB/TrEMBL:A1K3C8" FT /protein_id="CAL93333.1" FT /translation="MKQMQQAGRGAAIEHFDDCLSVDRPRLRRLARDIGRQRGERRDKL FT VADLAALRERSRAALAARRAALPVPSFPAELPVSARRDEIAAALEAHQVIIVCGETGSG FT KTTQLPKICLSLGRGAAGLIGHTQPRRLAARATASRIAQELNSELGRAVGYKIRFTDRL FT SADSHIKLMTDGILLAETQTDPLLAAYDTIIIDEAHERSLNIDFLLGYLKTLLPRRPDL FT KLIVTSATLDADRFARHFASADDKPAPVIEVSGRLYPIEMRYRPVEEADEAPAGDKSGP FT RRQKGKELLDALVDAVDEAQSCGPGDVLVFLPGEREIREAAEALRKAHHAAGTEILPLF FT ARQSAQEQARVFASGKGRRVVLATNVAETSLTVPGIRYVVDTGQARVKRYSPRNKVEQL FT QIENIAQSAARQRAGRCGRVMDGICFRLYAEDDFNRRPAHTDPEILRSSLAGVILRMKA FT LKLGAVEEFPFIDPPGGRLIADGYQLLTELGAVSDDEQRELTPIGVELAKLPLDPKIGR FT MILAARDRGCLKELLVIAAALSVQDPRERPPESTGAADQAHAKFRGGEQDQRSEFLWYL FT RLWQAWEEVQRHESGNQQKQWCKKHFLSWLRMREWRDVYTQLHSLCAEHGWKENELPAN FT YEAIHKALLAGLLGHIGCKTEEDQGAKGPQAGAYLGARGIKFWPHPGSALAKKAGKWIM FT GAELVDTSRLFARCLARIEPEWVEEVGAHLLKRHVFEPHWSKTAGSVRAWERGTVHGLV FT LYGRRGVNYRDIDPALCRELFIREGLVAGEIAEGPARAMAFLAHNRKLVAEIERLEHKS FT RRPDVLVDEALIEAFYDAKIPAEVVDLAGFEHWRKAAEKREPKLLYLSREQLMRHEAEG FT ITTERFPTQLEVLGQKLKLGYLHQPGEADDGVTLTVPLAMLNQVPAARCEWLVPGLLEE FT KVTALLKTVPQKHRHRLQPMSESAAAFMEQFESGEFDTGEPLLKALQRFVEERVQLKLP FT LESFRPENLNPHCFMNFRVIDEHGRPLAQSRNLADLRARYREQIAERFRGARLSGAADA FT TASAAAAPAATSAPQRKASTAAGGNDGATYAGHTAWTFPPLPELLEVKVGGRDVIGFPA FT LHDDGASVSLRPYDTQEEAAQVHRRGLARLFALNLRDQVKAIERLPGLRELALQYLSFG FT TEAELRQRLIDATLARTCLLEPLPTDAAAFERRIAEAKPRITLVAQEFARLTGQILADY FT AVVQKRVSGLKTFPDVVADVQAQLAALLPKDFLVALPWERLAQLPRYLKAVAVRIDKLR FT NNTARDAQSMAEWKTLAAAYERERAARSRAGVLDPVLEEFRWLLEELRVGLFAQELKTP FT MPVSVKRLQKIWEARPR" FT CDS complement(766798..767121) FT /transl_table=11 FT /locus_tag="azo0717" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT ebA3912 of Azoarcus sp. EbN1 of 45% FT (gi|56477657|ref|YP_159246.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K3C9" FT /protein_id="CAL93334.1" FT /translation="MKPTTLRYLAPILLCGGLLAALPAQAHGDRYDRGDRAEWRHRHWG FT HPHKHHFHGRETVVRERVIIRERPRYYEEEVRYYERPAYRAYRHDPAVVIGVQIPPLVI FT PLR" FT CDS 767369..767752 FT /transl_table=11 FT /gene="rpsF" FT /locus_tag="azo0718" FT /product="RpsF protein" FT /function="Ribosomal protein S6" FT /note="30S ribosomal protein S6. Binds together with S18 to FT 16S ribosomal RNA" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3D0" FT /db_xref="InterPro:IPR000529" FT /db_xref="InterPro:IPR014717" FT /db_xref="InterPro:IPR020814" FT /db_xref="UniProtKB/Swiss-Prot:A1K3D0" FT /protein_id="CAL93335.1" FT /translation="MRHYEIVFIVHPDQSEQVPAMIDRYKSIVTARNGQIHRLEDWGRR FT QLAYPIQKVHKAHYVLMNIECDGEALGELEHAFKFNDAVLRHLTIKMKKAVTTPSPMMK FT EEKSRSLTPAAGDEGKPAEAAEA" FT CDS 767768..768079 FT /transl_table=11 FT /gene="priB" FT /locus_tag="azo0719" FT /product="putative primosomal replication proteinN" FT /note="Putative primosomal replication protein N Homology FT to priB of E. coli of 31% (sprot|PRIB_ECOLI) Component of FT the preprimosomal complex composed of priA, priB, priC,dnaB FT and dnaT. Upon transient interaction with dnaG it forms the FT primosome. Binds single-stranded DNA. Pfam: Single-stranded FT binding protein family (PF00436) Interpro: Single stranded FT binding (IPR010913) no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3D1" FT /db_xref="InterPro:IPR000424" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR023646" FT /db_xref="UniProtKB/TrEMBL:A1K3D1" FT /protein_id="CAL93336.1" FT /translation="MESGLNELRLEATVAELLPLRRTPAGTAVASCTLTHESKQVEAGL FT ERSVRVELQAVAVGELASILATVVPGTRVVTTGFLAAKSMRSRLPVLHLNKIEFVEGN" FT CDS 768081..768356 FT /transl_table=11 FT /gene="rpsR" FT /locus_tag="azo0720" FT /product="30S ribosomal protein S18" FT /function="Ribosomal protein S18" FT /note="30S ribosomal protein S18. Binds as a heterodimer FT with protein S6 to the central domain of the 16S rRNA where FT it helps stabilize the platform of the 30S subunit (By FT similarity). InterPro: Ribosomal protein S18 S18: ribosomal FT protein S18" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3D2" FT /db_xref="InterPro:IPR001648" FT /db_xref="InterPro:IPR018275" FT /db_xref="UniProtKB/TrEMBL:A1K3D2" FT /protein_id="CAL93337.1" FT /translation="MAFKPKSKFKKKDDRGGRGLFKRRKFCRFTAEKIEEVDYKDVDIL FT KDFITENAKIMPARITGTKAGYQRQLSVAVKRARFLALMPYTDLHQ" FT CDS 768375..768830 FT /transl_table=11 FT /gene="rplI" FT /locus_tag="azo0721" FT /product="50S ribosomal protein L9" FT /function="Ribosomal protein L9" FT /note="50S ribosomal protein L9. Binds to the 23S rRNA" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3D3" FT /db_xref="InterPro:IPR000244" FT /db_xref="InterPro:IPR009027" FT /db_xref="InterPro:IPR020069" FT /db_xref="InterPro:IPR020070" FT /db_xref="InterPro:IPR020594" FT /db_xref="UniProtKB/Swiss-Prot:A1K3D3" FT /protein_id="CAL93338.1" FT /translation="MQIILLEKVVNLGNLGDVVKVKDGYARNFLIPQGKAKRANQANLA FT EFEARRAELERQQAEKLAAAQEVGAKLEGLMVQIARKAGMDGRLFGSVTNADVAEALAA FT QGFEIERSTVRMPDGPLKQIGDTQLEVALHSDVVVSITVSVLGEQQQ" FT CDS 768968..770377 FT /transl_table=11 FT /gene="dnaB" FT /locus_tag="azo0722" FT /product="DnaB protein" FT /function="Replicative DNA helicase" FT /EC_number="3.6.1.-" FT /note="Replicative DNA helicase (EC 3.6.1.-). PARTICIPATES FT IN INITIATION AND ELONGATION DURING CHROMOSOME REPLICATION; FT IT EXHIBITS DNA-DEPENDENT ATPASE ACTIVITY AND CONTAINS FT DISTINCT ACTIVE SITES FOR ATP BINDING DNA BINDING AND FT INTERACTION WITH DNAC PROTEIN PRIMASE AND OTHER PREPRIMING FT PROTEINS. InterPro: DnaB helicase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3D4" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR007692" FT /db_xref="InterPro:IPR007693" FT /db_xref="InterPro:IPR007694" FT /db_xref="InterPro:IPR016136" FT /db_xref="UniProtKB/TrEMBL:A1K3D4" FT /protein_id="CAL93339.1" FT /translation="MSSTSRRFQDGPHDPEMASIKLPPHSLEAEQSLIGGILIDNAAWE FT RIADLVNEADFYRDDHRRIYRHITRLIDLGKPADVVTVFESLEKNGEAEQAGGLVYLAE FT IANNTPSAANIRRYAEIVRERAILRKLVAVGDEIAASALTPSGKDAKSLLDEAEAKVFE FT IAEAGARHASGFISIQPILKQVVDRVQELYDRDSPSEVTGIPSGFVDLDDKTSGLQPSD FT MLIVAGRPAMGKTTFALNVAEHVAVEARLPVAIFSMEMPGTQLATRFISSVGRIDMQKI FT RSGRLTDEDWQRLTVAMGKLYDAPLYIDETPGLNPIDLRARARRLARQCGKLGLIVIDY FT LQLMTGSKDSDNRAAELSEISRSIKALAKELHVPIIALSQLNRSLEQRPNKRPVMSDLR FT ESGAIEQDADIIMFIYRDEVYNPDSPDKGTAELIIGKHRNGPTGVIRMTFLGQYTRFEN FT FAGGGFYTADE" FT rRNA 770728..772261 FT /locus_tag="azo_rrn7" FT tRNA 772335..772411 FT /gene="tRNA-Ile" FT /locus_tag="azo_tRNA_0006" FT /product="transfer RNA-Ile" FT /anticodon=(pos:772369..772371,aa:Ile) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA 772439..772514 FT /gene="tRNA-Ala" FT /locus_tag="azo_tRNA_0007" FT /product="transfer RNA-Ala" FT /anticodon=(pos:772472..772474,aa:Ala) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT rRNA 772779..775665 FT /locus_tag="azo_rrn8" FT CDS 776049..777212 FT /transl_table=11 FT /locus_tag="azo0723" FT /product="putative monooxygenase" FT /function="2-polyprenyl-6-methoxyphenol hydroxylase and FT related FAD-dependent oxidoreductases" FT /note="Putative monoxygenase. Pfam: Monoxygenase InterPro: FT Aromatic-ring hydroxylase (flavoprotein monoxygenase)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3D5" FT /db_xref="InterPro:IPR002938" FT /db_xref="InterPro:IPR003042" FT /db_xref="InterPro:IPR010971" FT /db_xref="UniProtKB/TrEMBL:A1K3D5" FT /protein_id="CAL93340.1" FT /translation="MNFDVVVVGGGLAGAALTVALRASSLRVAVVDAGLPTPSQGWDSR FT IYAYSPASADFLGTLGVWQHLDADRLCPVHSMDVRGDDGGRLRFDAAGCGLRELAWIGE FT SSLVHRELWESLKRQHNVTVFAPARPTALTVSGNDAALELEDGRLLHTRLLVGADGRDS FT WVRSQTAIKASSVNYEETAVVANFSCERPHRNEALQWFTDEGVVAWLPLPGRMMSLVWS FT APAALAETLMAMTPEQFTRRVQERGGAAWGRLSVVTPPAAFPLRFMRLDRVVASRVALI FT GDAAHAIHPLSGHGINLGFQDARVLSQRLLSAPAWADPGDERLLRSYARERAEEPFLVQ FT YVTHGINRLFAARNPLAAFVRNLGLNLTDRLPVVRSALTRYAVHGKF" FT CDS 777226..777951 FT /transl_table=11 FT /gene="dsbC" FT /locus_tag="azo0724" FT /product="putative protein disulfide-isomerase" FT /function="Protein-disulfide isomerase" FT /EC_number="5.3.4.1" FT /note="Putative protein disulfide-isomerase. Homology to FT dsbC of E. coli of 29% (sprot|DSBC_ECOLI) REQUIRED FOR FT DISULFIDE BOND FORMATION IN SOME PERIPLASMIC PROTEINS. ACTS FT BY TRANSFERRING ITS DISULFIDE BOND TO OTHER PROTEINS AND IS FT REDUCED IN THE PROCESS. DSBC IS REOXIDIZED BY A YET FT UNCHARACTERIZED PROTEIN. ALSO ACTS AS A DISULFIDE FT ISOMERASE. signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3D6" FT /db_xref="InterPro:IPR009094" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR017937" FT /db_xref="InterPro:IPR018950" FT /db_xref="UniProtKB/TrEMBL:A1K3D6" FT /protein_id="CAL93341.1" FT /translation="MVALKSAGRFALVIAFGLLPTLVAAGEEDVRKGVDAFIGSAAVES FT VTRTPYAGLYEVVLKSGEIIYTDDKTSFIMDGRVIDTRTRRDLTQAKLNQLSSIDFSTL FT PLDQAVKQVKGNGKRVIATFEDPNCGYCKRLAKELAQMPDVTIYTFLYPILSQDSTAKS FT RSIWCSKDRAKAWNDWIVSGKAPSGDDCNSAVVDRNVELGQKLRINGTPTIFLSDGTRI FT GGFVQLPELEKALARVTPR" FT CDS complement(777974..779038) FT /transl_table=11 FT /gene="mltA" FT /locus_tag="azo0725" FT /product="putative membrane-bound transglycolase" FT /function="Murein-degrading enzyme. May play a role in FT recycling of muropeptides during cell elongation and/or FT cell division." FT /EC_number="3.2.1.-" FT /note="Membrane-bound lytic murein transglycosylase A FT precursor (EC 3.2.1.-) (Murein hydrolase A) (Mlt38). FT MUREIN-DEGRADING ENZYME. MAY PLAY A ROLE IN RECYCLING OF FT MUROPEPTIDES DURING CELL ELONGATION AND/OR CELL DIVISION. FT OPTIMAL ACTIVITY IS BETWEEN PH 4.0 AND 4.5; LOSES ITS FT ACTIVITY RAPIDLY AT TEMPERATURES ABOVE 30 DEGREES CELSIUS. FT DEGRADES MUREIN GLYCAN STRANDS AND INSOLUBLE HIGH-MOLECULAR FT WEIGHT MUREIN SACCULI. ssl1: transcription factor ssl1" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3D7" FT /db_xref="InterPro:IPR005300" FT /db_xref="InterPro:IPR010611" FT /db_xref="InterPro:IPR014733" FT /db_xref="UniProtKB/TrEMBL:A1K3D7" FT /protein_id="CAL93342.1" FT /translation="MAEVPPHRAASWTEIDGWRDDDPSEAWSAFRKSCNVLEKQAPWQA FT SCKAARQLGEAPGPAQARAFFERHFSPWQLVNPDGSEQGLITGYYEPLIKASRTPDALY FT RWPVHGTPGDLLTIDLASVYPELKGYRLRGRLVGNKVLPYWKRDELGDQGSRLPAPVLL FT WAADPIDLFFMQVQGSGRAELPDGSVLRLGYADQNGHPYQSIGRWLVQQGQLSLDKASM FT DGIRDWARRHPQRLEEMLNSNPSYVFFRELPSSAEGPIGAQGAPLTANRSIAIDSRFVA FT LGAPVFLATTQPNSDTPLKRLMIAQDTGGAIKGAVRADYFWGFGPQAGAMAGRMRQQGR FT MWVLLPNGMKPAAN" FT CDS 779280..779393 FT /transl_table=11 FT /locus_tag="azo0726" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. No signal peptide. 1 TMH" FT /db_xref="UniProtKB/TrEMBL:A1K3D8" FT /protein_id="CAL93343.1" FT /translation="MWVIFLEVGIALALVGVVVWATWPRGRNQLEDKNDDD" FT CDS 779386..780249 FT /transl_table=11 FT /locus_tag="azo0727" FT /product="conserved hypothetical ATPase family protein" FT /function="predicted ATPase (AAA+ superfamily)" FT /note="Conserved hypothetical ATPase family protein. FT Homology to bb4427 of B. bronchiseptica of 65% FT (trembl|Q7WF53). Pfam: ATPase family associated with FT various cellular activities This large family has the key FT feature that they share a conserved region of about 220 FT amino acids that contains an ATP-binding site. no signal FT peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR008533" FT /db_xref="UniProtKB/TrEMBL:A1K3D9" FT /protein_id="CAL93344.1" FT /translation="MTDLNGFLQRAEALLDRLDALLPAPAPEPDWTAAKAFRWQRRNGR FT GALVPVKLVDRIRLEDLKDVDSQKERIDRNTRQFLAGRSANNVLLTGARGTGKSSLIKG FT LLNAYADQGLRLIEVDKSDLVALPEIVDLVAGRPERFILYCDDLSFEEGEDAYKALKSV FT LDGSIAAMSANVLVYATSNRRHLMPEYHDENLQVRHAGGELHPGEAVEEKVSLSDRFGL FT WVSFYPFNQDEYLEIVEHWLGVFRVPKRRIAAARQEALQWALMRGARSGRVAWQFARDY FT AGREDG" FT CDS 780242..781198 FT /transl_table=11 FT /locus_tag="azo0728" FT /product="bifunctional FT DGTP-pyrophosphohydrolase/Thiamine-phosphate FT diphosphorylase" FT /function="Thiamine monophosphate synthase" FT /EC_number="3.6.1.-" FT /note="NUDIX hydrolase/thiamine phosphate synthase FT Condenses 4-methyl-5-(beta-hydroxyethyl)-thiazole FT monophosphate (THZ-P) and 4-amino-5-hydroxymethyl FT pyrimidine pyrophosphate (HMP-PP) to form thiamine FT monophosphate (TMP) (By similarity). InterPro: NUDIX FT hydrolase TIGRFAM: mutt: mutator mutT protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3E0" FT /db_xref="InterPro:IPR000086" FT /db_xref="InterPro:IPR003733" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR015797" FT /db_xref="InterPro:IPR020084" FT /db_xref="InterPro:IPR020476" FT /db_xref="InterPro:IPR022998" FT /db_xref="UniProtKB/TrEMBL:A1K3E0" FT /protein_id="CAL93345.1" FT /translation="MAEVGARKIVNVAAGVILERGRVLLGQRAPDTFYPGYWEFPGGKV FT EPGESAADALKRELAEELGIVVPHVRPWLTREHDYEHAHVRLHFFEVPAWSGAPVAHVH FT AALRWAEPELIATACAPMLPANGPILKALQLPRRMGITQAAERGVARQLDELEQALGAG FT LRLVQVREAALPRRQQIEFAQEVVRRVAAAGGIVVINGDLDLARAVGAPGVHLPSAALL FT DCTVRPAFEWVGASCHSEEELRAAAALGLDYAVLGPVRPTASHPGQAALGWARFGELAG FT TLPFPVFALGGLGWGDMDCARDHGAHGVAAIRGAWGA" FT CDS complement(781195..781395) FT /transl_table=11 FT /locus_tag="azo0729" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to RSc2830 FT of Ralstonia solanacearum of 53% (trembl:Q8XVK0). Has FT PF03884, Domain of unknown function (DUF329);IPR005584;The FT function of this short domain is unknown it contains four FT conserved cysteines and may therefore be involved in zinc FT binding. no TMHs. No signal peptide." FT /db_xref="GOA:A1K3E1" FT /db_xref="InterPro:IPR005584" FT /db_xref="InterPro:IPR013088" FT /db_xref="UniProtKB/TrEMBL:A1K3E1" FT /protein_id="CAL93346.1" FT /translation="MVDHAPRIVKCPTCGAQVPWVPESRYRPFCSARCRQIDLGAWASE FT EYKVPTSPPDDTDAAETGSGR" FT CDS complement(781398..782153) FT /transl_table=11 FT /gene="yacF" FT /locus_tag="azo0730" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Hypothetical protein, yacF, 32% identitcal to FT SwissProt;P36680,Q8FL56. Has PF07072, Protein of unknown FT function (DUF1342);IPR009777 ;This family consists of FT several hypothetical bacterial proteins of around 250 FT residues in length. Members of this family are often known FT as YacF after the Escherichia coli protein P36680. The FT function of this family is unknown. cobA: cob(I)alamin FT adenosyltransferase" FT /db_xref="InterPro:IPR009777" FT /db_xref="UniProtKB/Swiss-Prot:A1K3E2" FT /protein_id="CAL93347.1" FT /translation="MISYEYPLSERIRTLLRLEDLFRKVAHFGGSEAPLDHHVALLTIF FT EILEVASRADLKVDLVQELERQRQILLSFRNNPEISEEALAGALYEIEQASTALLSMAG FT KIGQYLRENEWLMGIRSRAAIPGGVCQFDLPSYHFWLNRDAAERRHDLDAWIMPMTPIR FT DGIEIVMRLLRSSGRPEQQRARAGTYQLTMAGRVAQMLRVRIPRSEAVVPEISANKYAL FT NIRFMLPETVARPRVAEREITFELTFCTL" FT CDS complement(782235..782855) FT /transl_table=11 FT /gene="coaE" FT /locus_tag="azo0731" FT /product="CoaE protein" FT /function="Dephospho-CoA kinase" FT /EC_number="2.7.1.24" FT /note="Dephospho-CoA kinase (EC 2.7.1.24) FT (Dephosphocoenzyme A kinase). Catalyzes the phosphorylation FT of the 3-hydroxyl group of dephosphocoenzyme A to form FT coenzyme A (By similarity). InterPro: Uncharacterized FT protein family UPF0038 TIGRFAM: TIGR00152: kinase putative" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3E3" FT /db_xref="InterPro:IPR001977" FT /db_xref="UniProtKB/TrEMBL:A1K3E3" FT /protein_id="CAL93348.1" FT /translation="MKRPYVVGLSGGIGSGKSAAADRFAHLGATLVDTDAIAHALTGPG FT GAAMPQIAAHFGSACITADGRMDREAMRALVFSRPAARRELEAILHPMIRTESDRQVAA FT APSPYVILAIPLLVESGTARARCDRICIVDCPEALQIERVRARSGLEEAQILAIMQAQA FT SRAERLAVADDVIDNSTTLSALHAQVDILHARYLALAGDTTKV" FT CDS complement(782852..783562) FT /transl_table=11 FT /locus_tag="azo0732" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT rs03277 of R. solanacearum of 30% (TrEMBL:Q8Y2M5). No FT domains predicted. signal peptide. no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007730" FT /db_xref="UniProtKB/TrEMBL:A1K3E4" FT /protein_id="CAL93349.1" FT /translation="MVWTRFALILLLILNGLALAAIAGWFGAPASVGEPERVANQLHPE FT RVRFIGEQAPSASAAVSAAPAATADNTTAANEAPTPSAPPAEPPPASTLACASWSGLSA FT EEAERLAARIAEAGLTVRRHSGEAPASWWVRLPPQGSRDQAERKVRELKALGVTDYFIV FT QDAGPNQFAISLGLFKSEAAAHQQLAQLRSRGVRTAGVAPRLAVTQAVDAIATEEQLRR FT VATGLPAANATCTP" FT CDS complement(783572..784363) FT /transl_table=11 FT /gene="baf" FT /locus_tag="azo0733" FT /product="probable Bvg accessory factor" FT /function="Putative transcriptional regulator homolog of FT Bvg accessory factor" FT /note="Bvg accessory factor. Activates transcription of the FT pertussis toxin operon in a bvgAS-dependent manner. May FT interact with the alpha subunit of RNA polymerase. Similar FT to SWISSPROT: sprot|BAF_BORPE (29% Bordetella pertussis, FT bvg accessory factor baf or bp0097) InterPro: IPR004619 FT Baf. TIGRFAM: TIGR00671 transcriptional activator, FT putative, Baf family." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3E5" FT /db_xref="InterPro:IPR004619" FT /db_xref="UniProtKB/Swiss-Prot:A1K3E5" FT /protein_id="CAL93350.1" FT /translation="MILLLDVGNTRIKWRVVQAAGTPAMAEGALGHAEVHGLQAIVAGF FT PALRRMVGSNVAGASLGAALDGMLTTAGIAGRWVQAARDEHGVRNGYDRPAQLGTDRWA FT ALIGARRLHGGPCLVVSAGTATTVDHLDADGQFQGGLILPGIDLMRQSLASNTSGLRLE FT DGHVTPHPRNTADAIESGCAMAQAGAVERMFAQLVPQEDALCVLTGGAAPRFADLLSVR FT THPVPNLVLDGLAVIAAADAADSCPPHPTGTRAWPGDGRIR" FT CDS complement(784360..785088) FT /transl_table=11 FT /gene="birA" FT /locus_tag="azo0734" FT /product="biotin--[acetyl-CoA-carboxylase] ligase" FT /function="Biotin-(acetyl-CoA carboxylase) ligase" FT /EC_number="6.3.4.15" FT /note="BirA bifunctional protein [Includes: Biotin operon FT repressor; Biotin--[acetyl-CoA-carboxylase] synthetase (EC FT 6.3.4.15) (Biotin--protein ligase)]. birA acts both as a FT biotin-operon repressor and as the enzyme that synthesizes FT the corepressor, acetyl-coa:carbon- dioxide ligase. this FT protein also activates biotin to form biotinyl-5'-adenylate FT and transfers the biotin moiety to biotin-accepting FT proteins. InterPro: Biotin--acetyl-CoA-carboxylase ligase FT birA_ligase: biotin--acetyl-CoA-carboxyla" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3E6" FT /db_xref="InterPro:IPR003142" FT /db_xref="InterPro:IPR004143" FT /db_xref="InterPro:IPR004408" FT /db_xref="InterPro:IPR008988" FT /db_xref="UniProtKB/TrEMBL:A1K3E6" FT /protein_id="CAL93351.1" FT /translation="MRCIARCGSTNSELLNATPPDDDRVHVLVADEQTGGRGRRGRQWL FT SWPEGSLTFSSLWRFAPGAPVPAGLSLVAGLALARALEKLGLEGIQLKWPNDLLVHGCK FT LAGILVELLPGRGRTPAAIIGIGLNLRLPPEADIPEQGGVTDLHTEIPALPPREQLLAA FT ILRELHAALDLYAMAGFGALRGAWQQRNAFADLPVRIFGEGSEIVGICTGVDEDGALLV FT RTDAGVVRVLSGEVSLRAAP" FT CDS complement(785250..786680) FT /transl_table=11 FT /gene="ntrC" FT /locus_tag="azo0735" FT /product="nitrogen regulation protein NR(I)" FT /function="Response regulator containing CheY-like receiver FT AAA-type ATPase and DNA-binding domains" FT /note="Nitrogen regulation protein NR(I)," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3E7" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR002078" FT /db_xref="InterPro:IPR002197" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR010114" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR020441" FT /db_xref="UniProtKB/TrEMBL:A1K3E7" FT /protein_id="CAL93352.1" FT /translation="MNTVWIVDDDRSIRWVLEKALSREEIPHRSFTSANEALAELESTA FT HPPKVLVSDIRMPGESGLTLLQRVKNLHPHLPVIIMTAYSDLESAVAAFQGGAFEYLPK FT PFDVDQAVALVRRAIDQSAHQEGAQEETALAPEILGQAPSMQEVFRAIGRLSQSHATVL FT INGESGTGKELVARALHRHSPRRDAPFIAINTAAIPRDLLESELFGHERGAFTGAAAQR FT RGRFEQAENGTLFLDEIGDMPSELQTRLLRVLSDGNFYRVGGHQPIKANVRVIAATHQD FT LEERVRLGLFREDLFHRLNVIRLRLPPLRERREDVPILVRHFLQRSAQELGVESKRISE FT GAIKYLQALPFPGNVRQLENLCHWLTVMAPGQVVEVADLPPEMRDQPTREAPVNWVDGL FT GLEADRMIAANPGEVFDKLTREFERTLIRRALTATGGRRIEAAQLLGIGRNTITRKIQE FT LGMDDDHRPAAGEGEHED" FT CDS complement(786724..787797) FT /transl_table=11 FT /gene="ntrB" FT /locus_tag="azo0736" FT /product="nitrogen regulation protein NR(II)" FT /function="Signal transduction histidine kinase nitrogen FT specific" FT /EC_number="2.7.13.1" FT /note="Nitrogen regulation protein NR(II)," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3E8" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K3E8" FT /protein_id="CAL93353.1" FT /translation="MARSSSSQPIAAESFNGLDLLSSAVVMIDERRVIRYINPGAENLF FT AISQRKLLGAPLARLLGEPAGLGTALDNVLRTNWSYTGQDLTIARPASEAIHVDCTVSP FT VDIAGVKLLLEFRPIDAQLRVAREEQLLQQQQANRELIRNLAHEIKNPLGGIRGSAQLL FT ERELADPQLREYTEVIIAEADRLQDLMNRLLTSHSMMRPAQLNIHDVLERVRRLILAEF FT PDVVIRRDYDTSLPELTADREQLIQAILNIARNAAQALGGKGEIRLRTRVARQVTLAKR FT RYKLALELQVIDNGPGIPDEIRDKIFYPLVSGRDGGSGLGLSLAQSFVEQHQGMIDVDS FT RPGRTCFCILLPITDRT" FT CDS complement(787859..788335) FT /transl_table=11 FT /locus_tag="azo0737" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT cv3590 of C. violaceum of 39% (trembl|Q7NS37(SRS)) no FT domains predicted signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K3E9" FT /protein_id="CAL93354.1" FT /translation="MPKLRILPFAFMLLAAPLAHAEVYKCVDADGRVTYTNDRNVGRGC FT KQLSQDQSVSTMPPPARSPASPGAAASPTFPRVTPDAQRARDDSRRQVLEKELATEEAA FT LAEARKSLGEQEAVRLGDERNYQRVLDRLQPFKDKVDLHERNIEALKREIANLR" FT CDS complement(788464..789873) FT /transl_table=11 FT /gene="glnA" FT /locus_tag="azo0738" FT /product="glutamine synthetase I" FT /function="Glutamine synthetase" FT /EC_number="6.3.1.2" FT /note="Glutamine synthetase I (GS) plays an essential role FT in the metabolism of nitrogen by catalyzing the FT condensation of glutamate and ammonia to form glutamine. FT Similar to pir|G83005 (70%) and to pir|AJECQ (66%). Pfam FT (PF00120): Glutamine synthetase, catalytic domain Pfam FT (PF03951): Glutamine synthetase, beta-Grasp domain" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3F0" FT /db_xref="InterPro:IPR001637" FT /db_xref="InterPro:IPR004809" FT /db_xref="InterPro:IPR008146" FT /db_xref="InterPro:IPR008147" FT /db_xref="InterPro:IPR014746" FT /db_xref="UniProtKB/TrEMBL:A1K3F0" FT /protein_id="CAL93355.1" FT /translation="MNAQDVMKMIQENEVRFVDLRFTDTRGKEQHVGLPVSAFEEDHFE FT HGHPFDGSSIAGWKGIQASDMILMPDAASAYIDPFFDETTLVLACDVIEPSDGKGYDRD FT PRSIAKRAEAYLKSTGIGDTAFFGPEPEFFIFDAVEWSVDMSGVYSKIISEEAAWSTAD FT KFEGGNTGHRPKVKGGYFPVPPVDSLNDIRAAMVLALEAAGIPVEVHHHEVANAGQCEI FT GTKFSTLTKRADWTQTLKYIVHNVAHQYGKTATFMPKPIVGDNGSGMHVHQSIWKDGQN FT LFAGNGYAGLSETALYYIGGIIKHARALNAITNPATNSYKRLVPHYEAPTKLAYSARNR FT SASIRIPYVANPKGRRIESRFPDPAANPYLCFAALLMAGLDGIQNKIHPGDPADKNLYD FT LPPEEDALIPTVCTSLDQALEYLDKDREFLTRGGVFSNDFIDAYIELKMEEVNRLRVTT FT HPVEFDLYYSL" FT CDS complement(790055..791269) FT /transl_table=11 FT /gene="czcD1" FT /locus_tag="azo0739" FT /product="putative cobalt-zinc-cadmium resistance protein" FT /function="predicted Co/Zn/Cd cation transporters" FT /note="CzcD: Members of this family (TC 2.A.4) are integral FT membrane proteins that are found to increase tolerance to FT divalent metal ions such as cadmium, zinc,and cobalt. These FT proteins are thought to be efflux pumps that remove these FT ions from cells. (Slc30a subfamily). Similar to the FT cobalt-zinc-cadmium resistance protein CzcD (cation efflux FT system protein) from Alcaligenes eutrophus (Ralstonia FT eutropha). SWISSPROT:CZCD_ALCEU.P13512. InterPro:IPR002524; FT Cation_efflux.InterPro: Cation efflux family. Pfam:PF01545; FT Cation_efflux; 1. TIGRFAMs:TIGR01297; CDF; 1. TMHelix: 4." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3F1" FT /db_xref="InterPro:IPR002524" FT /db_xref="UniProtKB/TrEMBL:A1K3F1" FT /protein_id="CAL93356.1" FT /translation="MREPPSIPVPLSMHAPPPSAPTLAPAEAATRAAGIQRAALAAICT FT NALLVVSQVVIGLLSNAFSLVADAMHTLSDLVTDILVLFAGRRGAEPADHNHPYGHGRI FT ETFVSLLLGVALGAVGAGFLWASGMRLQHMDAAPTLHPVALGMALFTLLAKEVLFRYTL FT AAARRLQAPLLEANAWHARSDAASSLVVAVGIGGSLAGFPFLEPLAAALVGFLIAHTGW FT RVVAGAVRELIDTALPDEEVARLRTTIRATPGVAGLHDLRTRRMANRVLCDAHVQVEPR FT ITVSEGHRISDAVYYRVRAQHPEVQDILVHVDPEHDGPLHGTATHPLPERSDILPVVHE FT LLGDTAPPPSRVQLHYLGHRIEVEVLLPRNGAEIDAEALKQRTDAWLRSHPQFRSITFF FT APIAP" FT CDS 791287..791739 FT /transl_table=11 FT /locus_tag="azo0740" FT /product="conserved hypothetical sulphurtransferase FT protein" FT /function="Rhodanese-related sulfurtransferase" FT /EC_number="2.8.1.1" FT /note="Similar to Rhodanese domain protein, a FT sulphurtransferase involved in cyanide detoxification. FT InterPro: Rhodanese/cdc25 fold" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3F2" FT /db_xref="InterPro:IPR001763" FT /db_xref="UniProtKB/TrEMBL:A1K3F2" FT /protein_id="CAL93357.1" FT /translation="MATLSELLDLARERATAMNLPYEGALTPAEAHQVWGLAPGARLVD FT VRTRAEWDWVGRVPNAVEIEWLSWPGSQPNPAFLNQLRQQVDPEALVMFMCRSGARSDA FT AARAAKSAGFTNCYNVLEGFEGDKDANGQRNRIGGWRHAGLPWHQG" FT CDS 791814..792914 FT /transl_table=11 FT /gene="nadA" FT /locus_tag="azo0741" FT /product="quinolinate synthetase" FT /function="Quinolinate synthase" FT /EC_number="4.1.99.-" FT /note="Quinolinate synthetase A. Catalyzes the condensation FT of iminoaspartate with dihydroxyacetone phosphate to form FT quinolinate. InterPro: Quinolinate synthetase A protein FT TIGRFAM: nadA: quinolinate synthetase complex" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3F3" FT /db_xref="InterPro:IPR003473" FT /db_xref="InterPro:IPR023515" FT /db_xref="UniProtKB/TrEMBL:A1K3F3" FT /protein_id="CAL93358.1" FT /translation="MQVATISFDRFNALQDTEAQERIRAARARLGDRAVLLCHHYQRAD FT VYQHADLTGDSLKLARLASQTDAEYIVFCGVHFMAEVADILSKPSQIAILPDLAAGCSM FT ADMANLAKVERCWRELGEVLDTPDDLITPVTYINSAADLKAFCGEHGGIVCTSTNAPTI FT LDWAFAQREKVLFFPDQHLGRWTGYKKGIPLEQMVVWDPDLEYGGLTPEQIRNAKVLLW FT KGHCSVHQMFQESHIRRWRMQHPDGLVISHPESSLEVCQNSDFVGSTEYIIKTIAAAPA FT NTRWLVGTELNLVNRLAEEMKPEGKIVQFMAPTVCMCSTMQRIDPQHLAWTLENLAEGN FT VVNRIQVPAHEAELARVALDRMLAVS" FT CDS 792936..793685 FT /transl_table=11 FT /locus_tag="azo0742" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to rs04427 FT of R. solanacearum of 55% (trembl|Q8Y267). Pfam: FT Endonuclease/Exonuclease/phosphatase family (PF03372). FT Interpro: Endonuclease/Exonuclease/phosphatase family FT (IPR005135). no signal peptide. no TMHs" FT /db_xref="InterPro:IPR005135" FT /db_xref="UniProtKB/TrEMBL:A1K3F4" FT /protein_id="CAL93359.1" FT /translation="MGLRICTYNIHKGFSQFNRRMVVHDLRERLRSLDVDLVFLQEVQG FT LHLRHSRRHADWPAHPQYEFLAEDVWHQTAYGGNAVYDHGHHGNAILSRHAILSSDNQD FT VSDHRFERRGLLHCEVQLPGEDTVVHCVCVHLGLMAGSRRRQMEALAERMERLAPDGAP FT LIIAGDFNDWRNHADSVLCRRLGLVEAFGAGSVRPPRSFPSALPLFRLDRIYVRGFQVR FT RAEVHYGEPWSRISDHAALTADLELVH" FT CDS 793682..794839 FT /transl_table=11 FT /gene="cls1" FT /locus_tag="azo0743" FT /product="putative cardiolipin synthetase" FT /function="Phosphatidylserine/phosphatidylglycerophosphate/ FT cardiolipin synthases and related enzymes" FT /EC_number="2.7.8.-" FT /note="Catalyzes the reversible phosphatidyl group transfer FT from one phosphatidylglycerol molecule to another to form FT cardiolipin (CL) (diphosphatidylglycerol) and glycerol. FT Affects resistance to the gyrase inhibitor novobiocin. FT Entry name: CLS_ECOLI Primary accession number P31071 FT InterPro IPR001736; PLD. Pfam PF00614; PLDc; 2 Identity:- FT 28% Prediction: Non-secretory protein Signal peptide FT probability: 0.000 Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K3F5" FT /db_xref="InterPro:IPR001736" FT /db_xref="UniProtKB/TrEMBL:A1K3F5" FT /protein_id="CAL93360.1" FT /translation="MTVLVEGNAIALLENGLQYFPALEAEIDSARHEIFLETYIFSRDV FT VGRRIAAALVRAAARGVRVRVLVDGFGGREFVRDLMPGLLADGVEVLIFRRELRLTSLR FT RHRLRRMHRKIALIDARVAFVGGINITDDFELSGPPHPRYDYAVRVEGPLLAEIAEAVH FT RLWRLVSWASLQRRLQEAMRLPRRGPPAGGLRAAFLVRDNLRHRRDIEDAYLAAIGRAR FT EEIVIANAYFFPGRQFRQALLEAAARGVRVTLVLQGLADHPVLAHATRALYPHFLQRGI FT RLFEYHRSYLHAKVAVVDRRWATVGSSNIDPFSLWLAREANVVVEDAGFAGSLHRSLES FT AVQEGARELHREDWRRQRTLRRVASWLAYQAVRLAIGIAGYGGRH" FT CDS complement(794846..795355) FT /transl_table=11 FT /locus_tag="azo0744" FT /product="conserved hypothetical protein" FT /function="predicted CoA-binding protein" FT /note="Protein yccU. TREMBL:Q982W3: 50% identity, 70% FT similarity. This domain has a Rossmann fold and is found in FT a number of proteins including succinyl CoA synthetases, FT malate and ATP-citrate ligases. InterPro:IPR003781; FT CoA_binding. Pfam: PF02629; CoA_binding FRU: PTS enzyme-IIB FT fructose permease No signal peptide. No transmembrane FT helices present." FT /note="Function unclear" FT /db_xref="GOA:A1K3F6" FT /db_xref="InterPro:IPR003781" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K3F6" FT /protein_id="CAL93361.1" FT /translation="MPATPQGQFIDDIAGLRRVLQQTRSIAVVGLSANWNRPSYFAAKY FT MQTRGYRIIPVNPAYEEVLGEKCYPSLRAIPEPVDMVDVFRRPEEVPAIVDDAIAIGAR FT TLWLQLGVIHPEAAAKAQAGGLDVVMDRCVKIEFARLFGGLNWVGVNTGVISAKRAGRS FT LPRPGA" FT CDS complement(795366..796367) FT /transl_table=11 FT /locus_tag="azo0745" FT /product="Glutamate-tRNA ligase" FT /function="Glutamyl- and glutaminyl-tRNA synthetases" FT /EC_number="6.1.1.17" FT /note="Putative glutamyl-tRNA synthetase-related FT protein,58% identity to TrEMBl; Q5P2J9,47% identity to FT TrEMBL; Q7NSJ1. Has PF00749, tRNA synthetases class I (E FT and Q),catalytic domain.Other tRNA synthetase sub-families FT are too dis" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3F7" FT /db_xref="InterPro:IPR000924" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR020058" FT /db_xref="InterPro:IPR022380" FT /db_xref="UniProtKB/TrEMBL:A1K3F7" FT /protein_id="CAL93362.1" FT /translation="MRRQPGARSTRAPPSAGRLPMTAADTAPVPRPVPPAPARYVGRFA FT PSPTGPLHFGSLVAAAASWLEAQAHDGRWLLRIEDVDAPRCVPGAAADILATLDRFGFR FT WDGEVVYQSTRTAAYEAALEHLRSSEHAFPCGCTRAELAAAPLARDGSRRYPGTCRNGL FT APGRGARAWRVRAEGVVRFEDGVQGWQEEDLARDCGDYVVRRADGLFAYQLAVVVDDAA FT AGVTHVVRGADLLDSTARQIHLHRLLGSAAPAHAHVPVATNAAGEKLSKQTHALALDPA FT APAPALLAALAFLGQNPPPELARATPAEVWAWARMHWHLAGVPRQRHAPAPA" FT CDS 796481..798106 FT /transl_table=11 FT /locus_tag="azo0746" FT /product="hypothetical membrane protein" FT /function="4-amino-4-deoxy-L-arabinose transferase and FT related glycosyltransferases of PMT family" FT /note="Hypothetical membrane protein. Homology to la0834 of FT L. interrogans of 25% (trembl|Q8F7U9). InterPro: FT Dolichyl-phosphate-mannose-protein mannosyltransferase FT (IPR003342). Dolichyl-phosphate-mannose-protein FT mannosyltransferase proteins belong to the FT glycosyltransferase family 39 and are responsible for FT O-linked glycosylation of proteins. They catalyse the FT reaction: Dolichyl phosphate D-mannose + protein -> FT dolichyl phosphate + O-D-mannosyl-protein. Pfam: FT Dolichyl-phosphate-mannose-protein mannosyltransferase. FT signal peptide. 10 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K3F8" FT /protein_id="CAL93363.1" FT /translation="MRLDSRSVLACYLLLAVAYVGGLMVPLMNNDSAHHAGIALHMHLS FT GDYLSLVTQGENYLDKPHLLFWLAALGFKVFGVNTFAYKLPSLLFSVLAVYSTARLAAL FT LYSPAAGRLAGLVLASALAFVLANNDVRMDALLTGAIAFSIWQLAEFVACPRWRNLALA FT ALGLALGFSTKGMIGVAMPLIAVFLHLLYRRDWQRLFDPRWLVLGVLTLLPASPVLYAY FT HHQFGADGVRFILWSQNFERLAGERFGNAGAQDPLFFVHTFLWAFLPWSLLALAALWAH FT GRRVVAARLRPQAGGELITLGTLVVLFAIISASRFKLPHYLNILLPLFAVQLAGWLAPR FT LDAEAGRGLRLAQWVAAALLVAIALALNGWVFPLTSPVVALGAAAIATAGAVLTFRRRG FT VARVVVATVAVAAVFNFLLNFNFYPRLLGYQAGNQLAAAAHELALPVDQIAYLDGYGRA FT NSFDFYTARLTPSVPLAQLQRGEGPRYLYTSAGGRDALTAAGVRYDVLASNPDFRITRL FT NAQFLDPARRPKTLTEHVLLKVGE" FT CDS 798162..799442 FT /transl_table=11 FT /locus_tag="azo0747" FT /product="conserved hypothetical secreted protein" FT /function="predicted neuraminidase (sialidase)" FT /EC_number="3.2.1.-" FT /note="40% GH_BNR. Pfam:PF02012; BNR; 2. TMHelix:1. Signal FT peptide: present." FT /note="Function unclear" FT /db_xref="GOA:A1K3F9" FT /db_xref="InterPro:IPR011040" FT /db_xref="UniProtKB/TrEMBL:A1K3F9" FT /protein_id="CAL93364.1" FT /translation="MISVRRFGFIAIAALTAWAALPGFNPAPAPRFVAPPAAAMAASPG FT ASPLFASAIVNLPDPPRVHAASVAVLPDGRLFATWFGGEREGGTEVKVYAATRNPGEAG FT WGRQHAIATPEQTSADVGRLVRKMGNPVAFVTPRGELWVVYVSVTLGGWATSHLNLLRS FT PDLGTTWLPARRLAATPFFNLSTLVKGFPVFFDNGDVGLPVYHEMAGKFAELLVLSDEG FT EVRHKVRMDHGRRSLQPVVLVEDEQRAVALMRYGGEHGPFRAWRSETADGGRSWSAVEP FT TTLANPNSALAALRLDDGRLLAVANDTEDERLRLSLLVSEDGGRNWRSIHRFEDKQDFA FT GHEAGGEVFRARLEADVADLGPGPAAADLVRVAERNLCRNQGACGWQYDYPYLVRAADG FT DFHLVYTWNRSFVRHIQFNRAWLEGKL" FT CDS complement(799936..800856) FT /transl_table=11 FT /locus_tag="azo0748" FT /product="cellobiose phosphorylase" FT /function="uncharacterized protein conserved in bacteria" FT /EC_number="2.4.1.20" FT /note="Probable cellobiose phosphorylase, 31% identity to FT TrEMBL;Q7NYW4. Has PF04794, YdjC-like protein;IPR006879; FT Family of YdjC-like proteins. This region is possibly FT involved in the the cleavage of cellobiose-phosphate." FT /note="Function unclear" FT /db_xref="GOA:A1K3G0" FT /db_xref="InterPro:IPR002509" FT /db_xref="InterPro:IPR006879" FT /db_xref="UniProtKB/TrEMBL:A1K3G0" FT /protein_id="CAL93365.1" FT /translation="MTAFFDFHPVVVCADDYGIAAGVSTAIAQLIEAGRLSATSCMSTL FT PDWRRAAPELRAVVARQAADVGLHLTLTDHHAATPARGLADHGRLPPLGRVLRQSLAGG FT LPRAAVRDELRAQLDAFEDAWGAPPDYIDGHQHVHLFAGVREAVVDEVARRYPLGRVWV FT RDCVEAPARCVRRGVATPKALFLASLGRPLRRLLRTAGIPANDGFSGLHDFASPQPFGA FT KMRRFLALPGPRPLVHVHPGRVDAELRACDSLTTPREAELAYLASAAFPADLAEAGLRI FT ARYAEFAAMESSANSPPSASSGSIR" FT CDS 800954..801982 FT /transl_table=11 FT /locus_tag="azo0749" FT /product="conserved hypothetical glycosyl transferase" FT /note="Conserved hypothetical glycosyl transferase. FT Homology to cc2889 of. C. crescentus (trembl|Q9A4E5). Pfam: FT Glycosyl transferase family 2(PF00535). Diverse family, FT transferring sugar from UDP-glucose, FT UDP-N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to FT a range of substrates including cellulose, dolichol FT phosphate and teichoic acids. Interpro: Glycosyl FT transferase family 2 (IPR001173). no signal peptide. 2 FT TMHs." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3G1" FT /db_xref="InterPro:IPR001173" FT /db_xref="UniProtKB/TrEMBL:A1K3G1" FT /protein_id="CAL93366.1" FT /translation="MSRPDLHLALAQPAAVEPAPARGRIAVLSIVIPLYNESGSLGLLH FT QRLGAVLDTLGLSVERRELVFVDDGSRDTTFAEVAMLRAVDPCVRAIRFARNFGKEAAM FT AAGLRAATGDVVILMDGDLQHPPELIPEMVRRWQQGADMVTAVRRSRDTDPWLRRQLSQ FT AFYGLFKRVSEVALAEGGGDFRLFDRKVVAAINSLPERTRFMKGITSWVGFRQVEVDFD FT PEERAAGASAWSMLRLLRYAVDGLSTFSTLPLRVWSLVGMAMAAISGLYGTWLVVRTAI FT WGIDVPGYASIMVAVLFLSGIQLISLGVLGEYVGRIFTEVKARPLFLVAERIGFDEPAE FT RG" FT CDS 802057..803655 FT /transl_table=11 FT /locus_tag="azo0750" FT /product="conserved hypothetical membrane protein" FT /function="predicted ATPase (AAA+ superfamily)" FT /note="Conserved hypothetical membrane protein. FT TREMBL:Q89QQ8: 34% identity This is a subfamily of FT bacterial binding-protein-dependent transport systems FT family, and includes transport system permease proteins FT involved in the transport across the membrane of several FT compounds. This entry contains the inner components of this FT multicomponent transport system InterPro: IPR000522; FecD. FT Pfam: PF01032; FecCD ncs1: NCS1 nucleoside transporter fam FT Nonsecretory protein with signal peptide probability 0.203 FT (Signal P predicted). TMHMM predicted 9 transmembrane FT helices." FT /note="Function unclear" FT /db_xref="UniProtKB/TrEMBL:A1K3G2" FT /protein_id="CAL93367.1" FT /translation="MLSVALFGVLVAYVLASCRQHGISNDEEVQHVYGRLLVDFYGSGF FT ADRSAFAYKNLYLYGGLFDLIAAGLERVVPMNVWDLRHLLSAAFGILGMAGTWLLTRRL FT AALAFGPEDARAEWAGFLALLLLSLTGAWSGALFTHTKDVPFATAMVWSLYFTVVVLQQ FT LPRPGLATLVGLGVAFGCAFGLRVGAVFAVFYLGTGMLLAAWLAAPDVRGRSVFLLRSL FT RRLLPAVVLAVALMGLFWPWSVMAPGNLYTAMTTFSHFSFQLDTILAGVVMQNGDAPAT FT YLSRYLLVRLPELFLLGLALALLAGLRTVPRLSESGSYRRAAVPWLPVVLAALFPLGYT FT LLAAPPLYNGIRHFTFLLPPFAVVAAIGLVSAWMRAARWPRARLAGAVACAVMAAAHLT FT TLARLHPYEYVAYNGLAGGLRGTVERWEQDYWALSLRELTTDLEALVSAEGRAPAHPYR FT VAVCAESLQAAAWLDERFEVTRDWRAADFFLSPTHMDCDTASKGPVVAEVVREGVVLGV FT LRDRRMLVGEERAPR" FT CDS 803652..804053 FT /transl_table=11 FT /locus_tag="azo0751" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT PA4820 of P. aeruginosa of 38% (trembl|Q9HUZ0(SRS)) Has FT PF04138, GtrA-like protein;IPR007267;Members of this family FT are predicted to be integral membrane proteins with three FT or four transmembrane spans. They are involved in the FT synthesis of cell surface polysaccharides. The GtrA family FT are a subset of this family. GtrA is predicted to be an FT integral membrane protein with 4 transmembrane spans. It is FT involved is in O antigen modification by Shigella flexneri FT bacteriophage X (SfX), but does not determine the FT specificity of glucosylation. Its function remains unknown, FT but it may play a role in translocation of undecaprenyl FT phosphate linked glucose (UndP-Glc) across the cytoplasmic FT membrane. no signal peptide 4 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3G3" FT /db_xref="InterPro:IPR007267" FT /db_xref="UniProtKB/TrEMBL:A1K3G3" FT /protein_id="CAL93368.1" FT /translation="MSAVHFARFVRFATVGAVGTLAHYSLLLALVEGGGADPVVGSVAG FT FVLGALVNYGLNRKLVFASERAHTEALPRFFAVAGLGLVWNALLMRLLVHALGMQYLLA FT QVLTTALLMIWHYGANALWTFGARPPAGE" FT CDS complement(804105..805196) FT /transl_table=11 FT /gene="ychF" FT /locus_tag="azo0752" FT /product="conserved hypothetical protein" FT /function="predicted GTPase probable translation factor" FT /note="Probable GTP-binding protein ychF (ORF-3). InterPro: FT Conserved hypothetical protein 92 TIGR00092: conserved FT hypothetical prote" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3G4" FT /db_xref="InterPro:IPR004396" FT /db_xref="InterPro:IPR006073" FT /db_xref="InterPro:IPR012675" FT /db_xref="InterPro:IPR012676" FT /db_xref="InterPro:IPR013029" FT /db_xref="InterPro:IPR023192" FT /db_xref="UniProtKB/TrEMBL:A1K3G4" FT /protein_id="CAL93369.1" FT /translation="MSLKCGIVGLPNVGKSTLFNALTKAGIEAANYPFCTIEPNVGIVE FT VPDPRLAALSEIVKPQKIQPAIVEFVDIAGLVAGASKGEGLGNQFLANIRETDAIVHVV FT RCFADDNVVHVSGSVDPIRDIEVIDTELALADMATVEKALNRYKRPAAAGDKDAKVLVA FT VLEKCFAQLDTGKPVRALDLSREELASIKQFCLITQKPVLYAANVAEDGFENNPHLDAV FT RAHAAAEGAEVVALCAAIEAEIADLDDADKKDFLESMGLEEPGLDRLIRAGYKLLGLQT FT YFTAGVKEVRAWTIHVGDTAPQAAGVIHTDFERGFIRAQTIAFDDFIAFKGEAGAKEAG FT KMRAEGKDYVVKDGDVLNFLFNV" FT CDS complement(805193..805849) FT /transl_table=11 FT /gene="pth" FT /locus_tag="azo0753" FT /product="Pth protein" FT /function="Peptidyl-tRNA hydrolase" FT /EC_number="3.1.1.29" FT /note="Peptidyl-tRNA hydrolase (EC 3.1.1.29) . The natural FT substrate for this enzyme may be peptidyl- tRNAS which drop FT off the ribosome during protein synthesis." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3G5" FT /db_xref="InterPro:IPR001328" FT /db_xref="InterPro:IPR018171" FT /db_xref="UniProtKB/Swiss-Prot:A1K3G5" FT /protein_id="CAL93370.1" FT /translation="MSAAPPRLVVGLGNPGAEYSETRHNAGFWFCERLADTLGVRFSHE FT SRFHGLVANAREAGVWLLMPQTYMNRSGQAIGALARFYRIAPAEILVVHDELDIPPGQL FT RLKFGGGLGGHNGLKDTSAHLGTNDYWRLRVGIGHPGDRNEVVNFVLKPARREEQTLID FT ESLDRALAAWPTLAKGDWNTATQRLNARPAPPKPPKAPKAPQPAAADQPKDESQP" FT CDS complement(805889..806491) FT /transl_table=11 FT /gene="rplY" FT /locus_tag="azo0754" FT /product="50S ribosomal protein L25" FT /function="Ribosomal protein L25 (general stress protein FT Ctc)" FT /note="50S ribosomal protein L25. BINDS TO THE 5S RRNA" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3G6" FT /db_xref="InterPro:IPR001021" FT /db_xref="InterPro:IPR011035" FT /db_xref="InterPro:IPR020055" FT /db_xref="InterPro:IPR020056" FT /db_xref="InterPro:IPR020057" FT /db_xref="UniProtKB/Swiss-Prot:A1K3G6" FT /protein_id="CAL93371.1" FT /translation="MTIEFNATKREGQGSSASRRLRRAAQVPGIIYGAGKDAQPITLDH FT NELYHLLKKEAFHASVLSINVEGAKETVVLRDTQWHAYKQQVLHIDFQRVDASQKLHLK FT VPLHFVNGDNAPAVKLGGNIIAHVMTELDVQCLPSSLPEFIEVDLAALEAGQSIHVSQL FT KLPAGVEAVHHGEGDPVVASAQTTRGAAAAEGEGEAA" FT CDS complement(806573..807523) FT /transl_table=11 FT /gene="prsA" FT /locus_tag="azo0755" FT /product="Ribose-phosphate diphosphokinase" FT /EC_number="2.7.6.1" FT /note="Ribose-phosphate pyrophosphokinase (RPPK) FT (Phosphoribosyl pyrophosphate synthetase) (P-Rib-PP FT synthetase) (PRPP synthetase)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3G7" FT /db_xref="InterPro:IPR000836" FT /db_xref="InterPro:IPR000842" FT /db_xref="InterPro:IPR005946" FT /db_xref="UniProtKB/TrEMBL:A1K3G7" FT /protein_id="CAL93372.1" FT /translation="MPYGSLMVFTGNANPKLAADVARRLGISLGSVTVGRFSDGEVNVE FT LLENVRGKDVFILQPTCAPTNENLMELLVLVDALKRASAGRITAAIPYFGYARQDRRPR FT SARVPITAKVVANMLQAVGVQRVLTMDLHADQIQGFFDIPVDNVYAAPVLLADLDKQKY FT DDLMVVSPDVGGVVRARAFAKRMECDLAIIDKRRPKANVSEVMNIIGEVDGRTCVIMDD FT IVDTAGTLCKAASALKEHGAKRVLAYCTHAVLSGAAVSRINDSELDELVVTDTIPLRDD FT AKASSRIRQVSVASLLADTVLRISNEESVSSLFME" FT tRNA complement(807603..807679) FT /gene="tRNA-Gln" FT /locus_tag="azo_tRNA_0008" FT /product="transfer RNA-Gln" FT /anticodon=(pos:807643..807645,aa:Gln) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS complement(807698..808546) FT /transl_table=11 FT /gene="ispE" FT /locus_tag="azo0756" FT /product="probable FT 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase" FT /function="4-diphosphocytidyl-2C-methyl-D-erythritol FT 2-phosphate synthase" FT /EC_number="2.7.1.148" FT /note="FUNCTION: Catalyzes the phosphorylation of the FT position 2 hydroxy group of FT 4-diphosphocytidyl-2C-methyl-D-erythritol. Phosphorylates FT isopentenyl phosphate at low rates. Also acts on FT isopentenol, and, much less efficiently, dimethylallyl FT alcohol. Dimethylallyl monophosphate does not serve as a FT substrate. CATALYTIC ACTIVITY: ATP + FT 4-(cytidine5'-diphospho)-2-C-methyl-D-erythritol = ADP + FT 2-phospho-4-(cytidine FT 5'-diphospho)-2-C-methyl-D-erythritol. Entry name FT SWISSPROT:ISPE_ECOLI Prim. accession # P24209 Identities = FT 133/274 (48%) InterPro IPR006204; GHMP_kinase. IPR004424; FT IspE. Pfam PF00288; GHMP_kinases; 1. Prediction: FT Non-secretory protein Signal peptide probability: 0.006 FT Number of predicted TMHs: 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3G8" FT /db_xref="InterPro:IPR004424" FT /db_xref="InterPro:IPR006204" FT /db_xref="InterPro:IPR013750" FT /db_xref="InterPro:IPR014721" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/Swiss-Prot:A1K3G8" FT /protein_id="CAL93373.1" FT /translation="MTISGVLAGCPAPAKLNLFLHVVGRRDDGYHLLQTAFRLLDWGDR FT LDFRVRDDGLIRRTNQVAGVAEDDDLVVRAARRLQQATGTPLGADITLHKVLPMGGGVG FT GGSSDAATTLIALNHLWQTGLTRADLQQLGLALGADVPFFIYGRDAFAEGVGEAFQPLA FT LPAAVYVVLSPEVSVPTAEIFSAKGLTRDTPPIRIADFAASPTRNDLQATACSRYPEVA FT RAINWLEHYAPARMTGSGACVFAEVASEIEADEIVSLCPARWKAWKAKSLARHPLYGLL FT D" FT CDS complement(808543..809124) FT /transl_table=11 FT /gene="lolB" FT /locus_tag="azo0757" FT /product="conserved hypothetical outer membrane FT lipoprotein" FT /function="Outer membrane lipoprotein involved in outer FT membrane biogenesis" FT /note="conserved hypothetical outer-membrane lipoprotein. FT Homology to lolB of C. violaceum of 32% (sprot|LOLB_CHRVO) FT Plays a critical role in the incorporation of lipoproteins FT in the outer membrane after they are released by the lolA FT protein (By similarity). Tigrfam: lolB: outer membrane FT lipoprotein LolB Pfam: outer membrane lipoprotein LolB FT signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3G9" FT /db_xref="InterPro:IPR004565" FT /db_xref="UniProtKB/Swiss-Prot:A1K3G9" FT /protein_id="CAL93374.1" FT /translation="MRPARRFLAALACVAGALLSACATPTPRAERAVLREVSAQFFLGG FT RMSASDGNQGASGRIEWQHDTAGDEVTVYSPLGQIAARLISSPTGAELLTSDGQRYQAE FT NAEALMPRVFGFGVPVSRLAHWVQAAPPPGAEVRELDAAGRPALVIDQGWRVDYLEYPD FT TRARTLPTRVEVSRGDARIRLIIDQWELLQ" FT CDS complement(809121..810836) FT /transl_table=11 FT /locus_tag="azo0758" FT /product="conserved hypothetical secreted protein" FT /function="FOG: TPR repeat" FT /note="Conserved hypothetical secreted protein. Homology to FT cv4061 of C. violaceum of 37% (trembl|Q7NQS6). InterPro: FT TPR repeat (IPR001440) signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3H0" FT /db_xref="InterPro:IPR011717" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="InterPro:IPR019734" FT /db_xref="UniProtKB/TrEMBL:A1K3H0" FT /protein_id="CAL93375.1" FT /translation="MKCSPSRFAASAALAVAATLFGALPASAQAPARDSRESLPNQELS FT PNVLYQFLLAEIAGARGQIGLSTQLYLELARSTRDPRIARRATEIALFSRNAEAATQAA FT RLWAEISPQSEEARRILDTVATGRESRLDEIQIQLARALAQNPEHLAQNLMGLNRALTR FT VQDKQLTRDLVWRLTEPYLEQPEAHFARAQAAILADNAMEAAAEIDRALNLRADWEPGI FT LFKAQLLQQAGAHEEAAALLARQLERTPDSTSLRLAHARALVGARQFEAARGEFRRLLD FT AAPDDRDLMYANALLAQQLDDDAAAEALFSRALEAGHPEADAIRINLGQLADKRGDPAG FT ARRWYEQVGPGRHFGEARIRLAQALAKDGKLDEARRILREEGGDEDARRRFILAEAQLL FT RDADRSAEALQVVDQALRSAPDDTDLLYESAMLAERLDRMEVMEGRLRKVIALAPDHAH FT AYNALGYSLADRGQRLEEAQQLIERALELSPEDPFILDSLGWVRFRQGHLQDAATHLQR FT AYGIRADPEIAAHLGEVLWRLDRREDANRLFDEALRAHPDNTVLRDTAARLRKP" FT CDS 810989..811807 FT /transl_table=11 FT /gene="mutM" FT /locus_tag="azo0759" FT /product="MutM protein" FT /function="Formamidopyrimidine-DNA glycosylase" FT /EC_number="3.2.2.23" FT /note="Formamidopyrimidine-DNA glycosylase (EC 3.2.2.23) FT (Fapy-DNA glycosylase). This enzyme may play a significant FT role in processes leading to recovery from mutagenesis FT and/or cell death by alkylating agents. Also involved in FT the go system responsible for removing an oxidatively FT damaged form of guanine (78-dihydro-8- oxoguanine = 7-OxoG) FT from DNA. Can also nick DNA at apurinic/apyrimidinic sites FT (AP sites) (By similarity). InterPro: FT Formamidopyrimidine-DNA glycolase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3H1" FT /db_xref="InterPro:IPR000191" FT /db_xref="InterPro:IPR000214" FT /db_xref="InterPro:IPR010663" FT /db_xref="InterPro:IPR010979" FT /db_xref="InterPro:IPR012319" FT /db_xref="InterPro:IPR015886" FT /db_xref="InterPro:IPR015887" FT /db_xref="InterPro:IPR020629" FT /db_xref="UniProtKB/TrEMBL:A1K3H1" FT /protein_id="CAL93376.1" FT /translation="MPELPEVETTCRGVRPHVEGRRLSAVVVRNPRLRVPVPDNLAQLA FT AGQVLASVSRRAKYLLLDFDRGGLVVHLGMSGSLRVVAAGEPAGKHDHLDLVFGETSLR FT LRDPRRFGMVLWQEGGAVAHPLLAGLGPEPLDDAFDARYWVAATRGLRAPIKHVLMDGR FT RVVGVGNIYASESLFRSRIHPLEPAGAIGPQRAARLVLAVKETLTEAIAAGGSTLRDFV FT GGDGRPGYFQQQYFAYDREGEACRVCGSVIRRFVSGQRATFFCPRCQRRA" FT CDS 811931..813898 FT /transl_table=11 FT /locus_tag="azo0760" FT /product="conserved hypothetical protein" FT /function="predicted GTPases (dynamin-related)" FT /note="TREMBL:Q8Y2D6:42% identity, 59% similarity FT Hypothetical protein in xynA 3region (ORF6) (Fragment). FT Pfam:dynamin_2 :Dynamin central region; FH2:Formin Homology FT 2 Domain surE: stationary-phase survival prote No FT transmembrane helices(TMHMM predicted)" FT /note="Function unclear" FT /db_xref="GOA:A1K3H2" FT /db_xref="InterPro:IPR001401" FT /db_xref="UniProtKB/TrEMBL:A1K3H2" FT /protein_id="CAL93377.1" FT /translation="MNLVDQFSAYSRWRTGASDAISRLRSWLTRNEVGDAHGDLRLQYL FT LDRLRDDRLTVAFVAEFSRGKSELINAIFFSDFGDRILPSSAGRTTMCPTELQWQAGAR FT PELRLLPIRTRALQAPVGELKRADDHWSITPLKADSATELQEALARVGETERVGQAEAE FT QLGFKVDPSGEEGLKPGGDGLVEIPRWRHAVIQFPHPLLEQGLVVLDTPGLNAIGAEPE FT LTLSMLPNAHAVLFILAADTGVTHSDLAVWRHYVHAGAGGQKGRLVVLNKIDGLWDGLR FT DQARIDAELDRQVANVAETLEIEPATVFPVSAQKGLVARVTRDAALLERSRLPLLERAL FT TEDLLPTKQDIVRDNTLGETTELVDQTRALLQARLDGVREQLQELTDLRGKNQSVIEYM FT MRKIRAEKDEFEEGLQKYYAVRSVFSTMTNTLLAHLGLDTLRDETRRTREAMLESTFSR FT GLSEAMEGFFANLRANLQRSTEDIGEISRMLEAMYKRFSVEHGLKLNAPEAFSTLRYEQ FT ELDRLEKGFNRQINNTFTLVTTEKHTLTQKFFETVALQARRTFELANRDVEQWLRAVMS FT PLETQVREYQLQLKRRLDSVKRIHQATDTLEDRVEELRQAEAGVQALMDELAGIEAGIA FT DALGVPLRQAPAPQALERVA" FT CDS complement(813966..814223) FT /transl_table=11 FT /gene="fdx1" FT /locus_tag="azo0761" FT /product="probable ferredoxin" FT /function="Ferredoxin" FT /note="Probable ferredoxin. Homology to fdx of C. vinosum FT of 67% (sprot|FER_CHRVI). Ferredons are iron-sulfur FT proteins that transfer electrons in a wide variety of FT metabolic reactions. Pfam: 4Fe-4S binding domain no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3H3" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K3H3" FT /protein_id="CAL93378.1" FT /translation="MSLIITDECINCDVCEPECPNGAISQGDEIYQIDPNKCTECVGHF FT DEPQCQQVCPVDCIPHDPDHQETKDQLMQKFLKLSAAAKA" FT CDS complement(814240..814731) FT /transl_table=11 FT /gene="coaD" FT /locus_tag="azo0762" FT /product="Pantetheine-phosphate adenylyltransferase" FT /function="Phosphopantetheine adenylyltransferase" FT /EC_number="2.7.7.3" FT /note="Pantetheine- phosphate adenylyltransferas (PPAT) FT reversibly transfers an adenylyl group from ATP to FT 4-phosphopantetheine yielding dephospho-CoA (dPCoA) and FT pyrophosphate (By similarity)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3H4" FT /db_xref="InterPro:IPR001980" FT /db_xref="InterPro:IPR004820" FT /db_xref="InterPro:IPR004821" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/Swiss-Prot:A1K3H4" FT /protein_id="CAL93379.1" FT /translation="MRDGVAIYPGTFDPFTRGHEDLVRRASLLFDQVVVGVAESRGKAP FT IFTLEERVEIAREVVKPFPNVRVAGFDGLLMDFLRAQNGRVILRGLRAVSDFEYEFQMA FT GMNRKLFPDVETVFLTPAEEYMFISATMVREIARLGGDVSKFVQPSVLTQLQQKVSSKR FT " FT CDS complement(814728..815249) FT /transl_table=11 FT /locus_tag="azo0763" FT /product="putative methylase" FT /function="N6-adenine-specific methylase" FT /EC_number="2.1.1.-" FT /note="Putative methylase" FT /note="Family membership" FT /db_xref="GOA:A1K3H5" FT /db_xref="InterPro:IPR002052" FT /db_xref="InterPro:IPR004398" FT /db_xref="UniProtKB/TrEMBL:A1K3H5" FT /protein_id="CAL93380.1" FT /translation="MGGTWRSRLLDVAAVEGLRPTPDRVRETLFNWLGQRLDGLRCLDL FT FAGTGILGFEAASRGAEAVTLVEQNPRALDALHKAAITLQASQVEIVRGDAVKFLQNTT FT ARFDVVFLDPPYHQGWLDRLEPWLDRVLDKDGWLYAEAETPLDRLGKWQTLKQGHAGLV FT HYHLMQRADE" FT CDS complement(815264..816616) FT /transl_table=11 FT /locus_tag="azo0764" FT /product="probable Zn dependent peptidase" FT /function="predicted Zn-dependent peptidases" FT /note="Hypothetical zinc protease-like protein y4wB. FT TREMBL:Q8Y2E8: 43% identity; 57% similarity. InterPro: FT Insulinase family (Peptidase family M16) FT InterPro:IPR001431; Peptidase_M16. IPR007863: FT Peptidase_M16_C. Pfam:PF00675; Peptidase_M16 (Insulinase); FT homoserine_dh; aldehyde dehydrogenase; FT PF05193:Peptidase_M16_C; precor6x_red: precorrin-6x FT reductase TIGRFAM:folate/biopterin transporter SignalP FT predicted signal peptide and TMHMM predicted transmembrane FT helix" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3H6" FT /db_xref="InterPro:IPR007863" FT /db_xref="InterPro:IPR011237" FT /db_xref="InterPro:IPR011249" FT /db_xref="InterPro:IPR011765" FT /db_xref="UniProtKB/TrEMBL:A1K3H6" FT /protein_id="CAL93381.1" FT /translation="MTTTLPRPLPRPFAFLLGVLLLAVAHTALAAPRIEQWNTAAGARV FT LFVENHALPMVDVQIDFAAGSAADPAAKAGLASLVRSLLDAGTATLDEQAIADRSADIG FT AQIGGSTDLDRSSLSVRSLSSARERDAAVALAAELLARPVFPAQVLERERARAIAGLRE FT SLTRPATLAARRFNAAVYPNHPYGTNVTEESLAAVSREDLVAFHRRYYAATGASIAIVG FT DVDRATAEQIALRLTEGLPRTAPPAPLPPPALPTAGETHIPHPSAQAHILVGQPGMSRQ FT DPDYFPLLVGNYTLGGGGFVSRLTSEVREKRGFAYSVYSYFVPQQVAGIFQIGLQTRGS FT QAGEALDVVRRTLAGFIAEGPTAAELKSAKDNLINGFGLRLDSNRKILDHVAMIGFYRL FT PLDWLDTYPRKVEAVTAEQVRDAFARRVRPEHMVTVVAGGDGDTQAKAAAR" FT CDS complement(816645..818111) FT /transl_table=11 FT /locus_tag="azo0765" FT /product="probable Zn dependent peptidase" FT /function="predicted Zn-dependent peptidases" FT /note="TREMBL:Q8Y2E9: 55% identity, 68% similarity. FT Hypothetical zinc protease y4wA. InterPro:IPR001431; FT Peptidase_M16. IPR007863: Peptidase_M16_C. cofactor:binds 1 FT zinc ion per subunit (by similarity). belongs to peptidase FT family m16. similarity:to y4wb. Pfam:PF00675; FT Peptidase_M16; 1. PF05193:Peptidase_M16_C TIGRFAM: uxuA FT SignalP predicted signal peptide and TMHMM predicted FT transmembrane helices menD: FT 2-succinyl-6-hydroxy-24-cyclohex" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3H7" FT /db_xref="InterPro:IPR001431" FT /db_xref="InterPro:IPR007863" FT /db_xref="InterPro:IPR011237" FT /db_xref="InterPro:IPR011249" FT /db_xref="InterPro:IPR011765" FT /db_xref="UniProtKB/TrEMBL:A1K3H7" FT /protein_id="CAL93382.1" FT /translation="MRLPGGRVGSALEKRREFYQMQDIPMFRLTFPRTLLFAAVLLGGA FT VQAASAPDANTFETTLPNGMKVIVKEDRRAPSAVHMVWYRSGSMDEPDGVSGVAHVLEH FT MMFKGTKKVGPGEFNKRVAELGGRDNAFTSKDYTAYFQQIPPSHLDAVMALEADRMRNL FT VITDAEFGREVEVVKEERRLRTDDQPRALVHEQLMATAFQAHPYRRPIIGWMSDLDGMT FT ASDARAWYKRWYAPNNAYLVVVGDVSHEAVFRQAREHYGVIPARQLPPRRVPAEPEQRG FT TRHATVKAPAELPYLALAWHAPALRNPAADRDAYALQVLAAVLDGYDGARLTRRLVRDS FT RVAVSAGAGYDATGRGPALFYLDGVPAPGKTMDDLEAALRAEIQRIRDEGVGEDELARV FT KTQAVAAQVYKRDSLVGQAMEIGFLEASNLSWRDDERLLDGLRSVTAEEVRSVAQRYFG FT DDTLTAARLFPLPMDNNAPRPAAAPAALRH" FT CDS 818232..819365 FT /transl_table=11 FT /gene="FtsY" FT /locus_tag="azo0766" FT /product="probable signal recognition particle-docing FT protein FtsY" FT /note="Probable signal recognition particle-docing protein FT FtsY Homology to ftsY of C. violaceum of 65% FT (trembl|Q7NQD7) In E.coli, ftsY is an essential gene FT located in an operon with cell division genes ftsE and FT ftsX, but its apparent function is as the signal FT recognition particle docking protein. Pfam: SRP54-type FT protein, helical bundle domain (PF02881); SRP54-type FT protein, GTPase domain Tigrfam: ftsY: signal recognition FT particale-docking protein FtsY no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3H8" FT /db_xref="InterPro:IPR000897" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR004390" FT /db_xref="InterPro:IPR013822" FT /db_xref="UniProtKB/TrEMBL:A1K3H8" FT /protein_id="CAL93383.1" FT /translation="MFGFFKKSGKPEPAGRDPQPASPSAEQAPAIAADAPVAAPAPISP FT VPAQPVTAPAEPAAAPKLSWGERLKAGLARTRQQLGGGLANLFGRRKIDEDLLEELETT FT LLMADCGVDATQYLLDELRLRWKRDRLETADQLQAALADALHKIIAPLEQPLDVSGHKP FT YIIMIAGVNGSGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLMTWGERNNVTVI FT AQDGGDAAAVIFDAINAARARGIDIVLADTAGRLPTQLHLMEEIAKVRRVIAKADASGP FT HEVVLVLDANIGQNALAQVKAFDAAIGVTGLVVTKLDGTAKGGVVAAIARQCPKPLRFI FT GVGEGIDDLQPFKAREFIDALFEPAPAGATKRGDASA" FT CDS 819362..820021 FT /transl_table=11 FT /gene="FtsE" FT /locus_tag="azo0767" FT /product="probable cell division ATP-binding protein FtsE" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3H9" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K3H9" FT /protein_id="CAL93384.1" FT /translation="MIAFEQVAKRYAGGYTALAGVSFEIARGELVVLSGHSGAGKSTLL FT KLIPVIERPTAGTVRINGEDVSRLPRRAIPYLRRNLGLVLQESRLLFDRNVFDNVMLPL FT VITGHPPRDAAKRATAALERVGLAGREKEMPAGLSGGEQQRVAIARAVVNRPSILIADE FT PTAHLDPASAAGIAALFKSFHSAGVTVLVSTHDASLFAENAPRRLMLSKGLLAEAA" FT CDS 820018..820914 FT /transl_table=11 FT /gene="FtsX" FT /locus_tag="azo0768" FT /product="putative cell division protein FtsX" FT /function="Cell division protein" FT /note="Putative cell division protein FtsX. Homology to FT ftsX of E. coli of 33% (sprot|FTSX_ECOLI). FtsX is an FT integral membrane protein encoded in the same operon as FT signal recognition particle docking protein FtsY and FtsE. FT Might be a permease. Tigrfam: ftsX: cell division ABC FT transporter protein probable signal peptide probable 4 FT TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3I0" FT /db_xref="InterPro:IPR003838" FT /db_xref="UniProtKB/TrEMBL:A1K3I0" FT /protein_id="CAL93385.1" FT /translation="MIHWLYLHLRAIAHALRRLASQPLGTLLSALVVGIALSLPAGGYL FT LLDNVSSLVRGVSGTPEISVFMAPGAGAAQVAAVDRNLKAEAALASYRYVSRDEALKQL FT ERSGLGDVLGGLAANPLPDAFIVSPRGEDPALFDRLATQMKGWPAVAHVQVDSAWVKRL FT HALLGLGRSAVLMLAALLGLALVIVTFNTIRLQIMTQRAEIEVSRLLGATDPFIRRPFY FT WFGSLQGALGGLVALGTVWLGVKALERPVAALAESYGAVFALSGPGAVESAVVVAFAAV FT LGWMGAAISVRRHLAGA" FT CDS 821109..821672 FT /transl_table=11 FT /gene="ahpC" FT /locus_tag="azo0769" FT /product="alkyl hydroperoxide reductase subunit C" FT /function="Peroxiredoxin" FT /EC_number="1.6.99.3" FT /note="Alkyl hydroperoxide reductase subunit C. Homology to FT aphC of X. campestris of 84% (trembl|O06464). Directly FT reduces organic hydroperoxides in its reduced dithiol form. FT InterPro: Alkyl hydroperoxide reductase/ Thiol specific FT antioxidant/ Mal allergen (IPR000866) Pfam: AhpC/TSA family FT no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3I1" FT /db_xref="InterPro:IPR000866" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR017559" FT /db_xref="InterPro:IPR019479" FT /db_xref="InterPro:IPR024706" FT /db_xref="UniProtKB/TrEMBL:A1K3I1" FT /protein_id="CAL93386.1" FT /translation="MSLINTQVQPFKAQAYKNGKFIEVTDADLKGKWSVLIFMPAAFTF FT NCPTEIEDAAEHYAEFEKAGAEVYIVTTDTHFSHKVWHETSPAVGKAKFALVGDPTHAL FT TNAFDVHIAEEGLALRGTFIINPEGVIKTMEVHDNAIARDVTETVRKLKAAQYVASHPN FT EVCPAKWKEGEKTLAPSIDLVGKI" FT CDS 821802..823355 FT /transl_table=11 FT /gene="ahpF" FT /locus_tag="azo0770" FT /product="alkyl hydroperoxide reductase subunit F" FT /function="Alkyl hydroperoxide reductase large subunit" FT /EC_number="1.6.99.3" FT /note="Alkyl hydroperoxide reductase subunit F. Homology to FT aphF of X. campestris of 71% (sprot|AHPF_XANCH) Serves to FT protect the cell against DNA damage by alkyl FT hydroperoxides. It can use either NADH or NADPH as electron FT donor for direct reduction of redox dyes or of alkyl FT hydroperoxides when combined with the AHPC protein. Pfam: FT Pyridine nucleotide-disulphide oxidareductase no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3I2" FT /db_xref="InterPro:IPR000103" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR002109" FT /db_xref="InterPro:IPR008255" FT /db_xref="InterPro:IPR012081" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K3I2" FT /protein_id="CAL93387.1" FT /translation="MLDANIKTQLKAYLERVTQPIEIVASLDDGAKSREMQELLADVAE FT QSHLITVIERRDDNERKPSFSVGPKGGEARVRFAGLPMGHEFTSLILALLQSAGYPPKV FT EADVIEQIKALEGEFNFETYISLSCHNCPDVVQALNLLSILNPNIRHTMIDGGVFQEEV FT EKRQIMAVPTVYLNGQEFGAGRMELGEILAKIDTGAAKRDAAKLSAKDVFDVLVVGGGP FT AGAAAAIYAARKGIRTGVLAERFGGQVMDTLAIENFISVKETEGPKLAMALEEHVKQYE FT VDVMNLQRATALVPGDIHEVRLENGGTLKAKTVILATGARWREMNVPGEKEYRGKGVAY FT CPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVAHVTLLEFADTLRADAVLQKKLASL FT PNVTVIKSAQTTEVTGAEKVNGLVYKDRVSGEEKRLELEGIFVQIGLLPNTDFLKGTVE FT LTRFGEIIVDAKGQTSVPGVFAAGDCTTVPYKQIIIAMGEGSKASLAAFDHLIRTSVPA FT " FT CDS complement(824754..826058) FT /transl_table=11 FT /locus_tag="azo0771" FT /product="probable C-5 cytosine-specific DNA methylase" FT /note="Probable C-5 cytosine-specific DNA methylase FT InterPro: C-5 cytosine-specific DNA methylase" FT /db_xref="GOA:A1K3I3" FT /db_xref="InterPro:IPR001525" FT /db_xref="InterPro:IPR018117" FT /db_xref="UniProtKB/TrEMBL:A1K3I3" FT /protein_id="CAL93388.1" FT /translation="MGLDLGLDRTGRYEIVACVEKEKVFCNTIRQNSAAGRINPNLKVF FT EGDINDLDPAQVLDSVNLKPGEVDLLVGGPPCQSFSTAGKRGTVQDPRGTLLWQYLRFV FT EYIQPKFFLMENVRGLVSAALRHRPIAERPEHGGAPLTDNEKPGSVLRRFSEDLQAIPN FT AAYHFDVFEVNSVNYGAPQIRERVIFIGNRFNMEVDFPNPTHGPIAAAKAQDDLFSAPA FT AQPWATLRDAIGDLNETNPVVLDFSPRKKSFLSLIPPGSNWRSLPENLQQESMGKAWFA FT KGGRSGWWRRLTFDLPCPTLVTMPNHASTALCHPTETRALSLREYARIQEFPDDWQFSG FT TVSEQYRQVGNAVPTRLGKIAGEVIASCLDTMKGRNWQPFPTPPDAFRIIYIQSHVRTR FT QWFKGGKTVIWEDGEQNETAAYDRPQTLRKTSVIG" FT CDS complement(826594..827043) FT /transl_table=11 FT /gene="rnhA1" FT /locus_tag="azo0772" FT /product="RnhA1 protein" FT /function="Ribonuclease HI" FT /EC_number="3.1.26.4" FT /note="Ribonuclease H (EC 3.1.26.4) (RNase H). This enzyme FT is an endonuclease that degrades the RNA of RNA-DNA hybrids FT specifically (By similarity). InterPro: RNase H" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3I4" FT /db_xref="InterPro:IPR002156" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR022892" FT /db_xref="UniProtKB/TrEMBL:A1K3I4" FT /protein_id="CAL93389.1" FT /translation="MIEPPVTIYTDGACRGNPGPGGWGVILSRGRQYKELYGGEPETTN FT NRMELTAAIKALEALKRPLPVILYTDSKYLVQGMTQWLPKWKAKGWRKADGKPVENADL FT WKVLDEAASVHDVQWHWVRGHNGNPGNERADTLANLGIDTIHAAP" FT CDS complement(827040..827819) FT /transl_table=11 FT /locus_tag="azo0773" FT /product="Hypothetical protein" FT /note="Hypothetical protein , 32% identity to TrEMBL;Q8NZP4 FT No domains, repeats, motifs or features present." FT /db_xref="InterPro:IPR013557" FT /db_xref="UniProtKB/TrEMBL:A1K3I5" FT /protein_id="CAL93390.1" FT /translation="MTLGFTEEQAQRMMNTRRVLPIVENRKAPCMDARKLWERIGEPHG FT RFDKWVEYHIKPLLNHDNGFAEVSAKVTQGKTGRPRIDYTLSRNIAAHLAMMANTPEGR FT DVRDYFLDMEDLALRLTKRLPVRVATLVSTDNDLTHHCYRKAAEEAKRGQFPVWRFKAV FT ASEWEKAIKSIVAEVLTGHPARHWRQAIGGNRGIRDILNDEDLILYSRCYDTAVTLFRA FT GFTDMDKLKAILLESFGGRINPADYGFAANDAIEEAA" FT CDS complement(828127..828822) FT /transl_table=11 FT /locus_tag="azo0774" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K3I6" FT /inference="nucleotide motif:Gismo" FT /protein_id="CAL93391.1" FT /translation="MHLIDATQEVPLQPIQVGVDLLDLTETQAFLSAAYSLRPTFGRGV FT RIHWETPGHPLFDAASVLWRSGYKDVEKGAMRHLKGCPSAVWKVRVSGRGYPFRHFLDT FT EGVLWVIKKARHRDIEPDLNDPYSVGDYAEERNERRDQFLERFQSMLNTGILDRYDELM FT RTEATSAERQVCQHWIEEHKIHSNNLRLQPGGLFSPEGMKNFELYSRASFAGDVLQGGP FT RFALRDVWA" FT CDS complement(829733..830302) FT /transl_table=11 FT /locus_tag="azo0775" FT /product="putative resolvase" FT /function="Site-specific recombinases DNA invertase Pin FT homologs" FT /note="Putative DNA-invertase from lambdoid prophage Rac. FT InterPro: Site-specific recombinase Pfam: Resolvase" FT /note="Family membership" FT /db_xref="GOA:A1K3I7" FT /db_xref="InterPro:IPR006118" FT /db_xref="InterPro:IPR006119" FT /db_xref="UniProtKB/TrEMBL:A1K3I7" FT /protein_id="CAL93392.1" FT /translation="MSATIAYLRVSTDDQTTENQRRAIEARYNISKWFVEEGVSGTIPA FT AQRPAMASLLNYVREDDTVVVVAIDRLGRNTIDVLTTVEALKAKGVSVVSMREGFDLAT FT PAGKLMLTMLAAVAELERENIKARQIAGIVRARAEGKNLGREKTIDDAAVAKWRAENSA FT SIKATAEHFGISPASVKRACAAKTSA" FT CDS complement(830685..832355) FT /transl_table=11 FT /locus_tag="azo0776" FT /product="putative integrase" FT /function="Integrase" FT /note="Family membership" FT /db_xref="GOA:A1K3I8" FT /db_xref="InterPro:IPR002104" FT /db_xref="InterPro:IPR011010" FT /db_xref="InterPro:IPR013762" FT /db_xref="UniProtKB/TrEMBL:A1K3I8" FT /protein_id="CAL93393.1" FT /translation="MDKKVPKPWCDPASGIYYTNFRVPTDLVPLVGRPLIQKSLRTKER FT RTAERKNCEIWLTYQREFERLRRERALDAPLSEEFIPHLVEEWLHQTLKADEDGRIMGA FT VPRTQEGMGEVYYGMIDELAEGSLTGKHPDFLIRAAAAFLDEKGISYDSRSLAFAKFVE FT ELSPRYARYLGTLASRDEGQKVSTPAPPRQQLIPLSQLIREFIESRPKGKATALTKDAA FT CMTKFLEIVGDKPMPSLRQQDIREFFHVAQRLPSQRGGPKKPEGITWREWADDTVTMSP FT DTFKNNYVAPVRHFLKWAKSAYHDQGFPVGLTTDAIEYQGTRERGEDKQRAFRTDELQR FT LFLGEEMQSFATAPDQAERYWLPLLGLHTGARINELCQINPAEDWITPDGIHCLHITTE FT TEAGEDVTKSIKTGTPRIVPIHPKLIELGFLGYLEHTKATGVGRLFPAFKPKMGNAGER FT AREWFASLIVKAGLRDDTPFAKITGFHAFRHTLITYAANHDDPSMEAAIDQITGHVSHG FT SAVKRGYISNRSARKAYETIRKVDFGLGFFKPVLSGDQD" FT tRNA complement(832451..832527) FT /gene="tRNA-Met" FT /locus_tag="azo_tRNA_0009" FT /product="transfer RNA-Met" FT /anticodon=(pos:832491..832493,aa:Met) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 832729..833076 FT /transl_table=11 FT /locus_tag="azo0777" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. No TMHs. Signal peptide FT present." FT /db_xref="UniProtKB/TrEMBL:A1K3I9" FT /protein_id="CAL93394.1" FT /translation="MRALRSLFVVLLLLPLAAGGVLASLTRSFPPDAQRVVMVFAGAGT FT VKIKAGSFFKSDRVLTLSPGAQIRDTDNRIVMPTAIAGEYKVRAQIDNAGQVHRVWVLT FT PAEIAVVDPKQ" FT CDS 833091..834440 FT /transl_table=11 FT /locus_tag="azo0778" FT /product="Conserved Hypothetical protein" FT /function="2-methylthioadenine synthetase" FT /note="Conserved Hypothetical protein, 72% idetity (82% FT similarity) to TrEMBL;Q7NQI8.TrEMBL;Q8Y206(71% Identity). FT Has Elp3, Elongator protein 3, MiaB family, Radical FT SAM;This superfamily contains MoaA, NifB, FT PqqE,coproporphyrinogen III oxidase, biotin synthase and FT MiaB families, and includes a representative in the FT eukaryotic elongator subunit, Elp-3. Some members of the FT family are methyltransferases.SMART;SM00729. Has PF01938, FT TRAM domain;IPR002792; This small domain has no known FT function. However it may perform a nucleic acid binding FT role. Has PF00919; Uncharacterized protein family FT UPF0004;IPR005839;This family is the N terminal half of the FT Prosite family. The C-terminal half has been shown to be FT related to MiaB proteins. This domain is a nearly always FT found in conjunction with Radical_SAM and TRAM although its FT function is uncertain." FT /note="Family membership" FT /db_xref="GOA:A1K3J0" FT /db_xref="InterPro:IPR002792" FT /db_xref="InterPro:IPR005839" FT /db_xref="InterPro:IPR006463" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR013848" FT /db_xref="InterPro:IPR020612" FT /db_xref="InterPro:IPR023404" FT /db_xref="InterPro:IPR023970" FT /db_xref="UniProtKB/Swiss-Prot:A1K3J0" FT /protein_id="CAL93395.1" FT /translation="MKKLYIRTFGCQMNEYDSEKMADVLGAGEGIAKTDNPEEADVILF FT NTCSVREKAQEKVFHDLGRVKHLKQLKPDLIIGVGGCVASQEGDAIVARAPYVDVVFGP FT QTLHRLPALIAARKQSGRSQVDISFPEIEKFDAMPPARVEGASAFVSIMEGCSKYCTFC FT VVPYTRGEEISRPLEDVLAEIAGLAEQGVKEVTLLGQNVNAWRGEIVRDAGEEGDFAFL FT LECVAEIPGIERIRYTTSHPREMTQRLFDAYVKIPKLVSQLHLPVQSGSDRILAAMKRG FT YSVLEFKSIVRKLRAARPDLSLSSDFIVGFPGETEEDFEKTMKLIDEVGFDGSFSFVYS FT ARPGTPAADLEDPVPQETKLAWLARLQKRIDEQAQAVSQSMVGSAQRILVEGVSRKSAE FT ELMGRTDNNRVVNFPAPSPHRDRLVGQFIEVRITSALPHSLRGEILTRES" FT CDS 834440..835423 FT /transl_table=11 FT /gene="ybeZ" FT /locus_tag="azo0779" FT /product="PhoH-like protein" FT /function="Phosphate starvation-inducible protein PhoH FT predicted ATPase" FT /note="PhoH-like protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3J1" FT /db_xref="InterPro:IPR003714" FT /db_xref="UniProtKB/TrEMBL:A1K3J1" FT /protein_id="CAL93396.1" FT /translation="MAKILEVFFEPVDNLRLARLCGVLDENLRQIENAFDITVTRRGEQ FT FTLHGHPAQVLRGEMALKHFYERAEKDLTVDDVQLGLIEIANRGENPLPAPALLTRRSE FT LHGRTPRQVEYLRHIQDHDITFGIGPAGTGKTYLAVASAVDAFERDLVERIILTRPAVE FT AGERLGFLPGDLAQKVDPYLRPLYDALYDLMGFDRVAKLFERGSIEIAPLAFMRGRTLN FT NAFIILDEAQNTTPEQMKMFLTRIGFGAKAVVTGDLTQVDLPRATRSGLREAREVLAGV FT RGIAFTEFKKEDVVRHPLVARIVEAYDNQAARQADAHKKDAGEEHA" FT CDS 835416..836174 FT /transl_table=11 FT /locus_tag="azo0780" FT /product="conserved hypothetical protein" FT /function="predicted metal-dependent hydrolase" FT /note="Conserved hypothetical protein. Homology to rso4939 FT of R. solanacearum of 40% (rso:RS04939). Pfam: FT Uncharacterized protein family UPF005 Tigrfam: TIGR00043: FT conserved hypothetical protein no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3J2" FT /db_xref="InterPro:IPR002036" FT /db_xref="InterPro:IPR023091" FT /db_xref="UniProtKB/Swiss-Prot:A1K3J2" FT /protein_id="CAL93397.1" FT /translation="MPKQADGVRIVAVDAAGKTSRIKAERLEIDYGDGRRLTLTLPNDG FT WAHLDIEADVAGDDDGDLPVITIQPSACNAVALRVEVVQQPQVADIDLPVAAKLPVLTL FT EVQKALDGGDKAAAPKKHQIRRWAQAALRTDAEVTVRLVGETEGRALNLGYRGKDYATN FT VLTFVYGEEGGAPAVEGMPLMGDLVLCVPVVVREAAEQGKALDAHFAHLVVHGMLHLQG FT LDHEDDAEAEAMETAETNILRGLGYANPYA" FT CDS 836270..837115 FT /transl_table=11 FT /gene="corC" FT /locus_tag="azo0781" FT /product="putative magnesium and cobalt efflux protein" FT /function="Putative Mg2+ and Co2+ transporter CorC" FT /note="Magnesium and cobalt efflux protein corC. Plays a FT role in the transport of magnesium and cobalt ions. Also FT mediates transport of cobalt and nickel. 43% FT CBS_domain.IPR005170; CorC_transpt-asc. Pfam:PF00571; CBS; FT 2.PF03471; CorC_HlyC; 1. Belongs to the UPF0053 FT family.Contains 2 cbs domains." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3J3" FT /db_xref="InterPro:IPR000644" FT /db_xref="InterPro:IPR005170" FT /db_xref="InterPro:IPR016169" FT /db_xref="UniProtKB/TrEMBL:A1K3J3" FT /protein_id="CAL93398.1" FT /translation="MDSVPSKPTLLERLSSMLSREPEDRDELLVLLHAALERGLLDADA FT FSIIEGALQVSELQVRDVMVSRSRMDVIRLADPMERIAEFVIDTAHSRFPAVGESKDDV FT VGILLAKDLLRYFAGREFNLREMLRPAVFVPESKRLNVLLREFRVSHNHMAIVVDEYGG FT VSGLITIEDVLEQIVGDIEDEYDFDEIGARIRLDHKGRYRVQASTEIEDFNAAFGTRCH FT EEDVDTIGGLILRRLGRLPVRGEVIDVDGLRVQVLRADSRRIHTLLVERLPQVSDVTAN FT " FT CDS 837115..838629 FT /transl_table=11 FT /gene="lnt" FT /locus_tag="azo0782" FT /product="putative apolipoprotein N-acyltransferase" FT /function="Apolipoprotein N-acyltransferase" FT /EC_number="2.3.1.-" FT /note="Putative apolipoprotein N-acyltransferase. Homology FT to cutE of E. coli of 36% (sprot|LNT_ECOLI). Transfers the FT fatty acyl group on membrane lipoproteins. InterPro: FT Apolipoprotein N-acyltransferase (IPR004563); FT Carbon-nitrogen hydrolase (IPR003010) Tigrfam: lnt: FT apolipoprotein N-acyltransferase Pfam: Carbon-nitrogen FT hydrolase signal peptide 6 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3J4" FT /db_xref="InterPro:IPR003010" FT /db_xref="InterPro:IPR004563" FT /db_xref="UniProtKB/TrEMBL:A1K3J4" FT /protein_id="CAL93399.1" FT /translation="MRRLVLAALAGATLTPALAPFELFPLALVSLAGLVFLLAGEARAR FT AGFLLGFGWGLGAFGSGVSWLYVALARFGGMPPPLAVLAVALFCAFLALYPALVAAAFV FT RLRRTAPSGSVVLSGLLFAGLWVGAEWLRGVLFTGFPWLAVGYSQTPPSPLAGLMPVVG FT VYGVGGVMAWMAAALALAARGGRDRATWRPALAVAAIPWIAGALLGRVQWTAPEGAPLS FT VALVQTNVEQHLKWRPEHFAAVLQTNARLVRDASAQLVVLPETTLPALAEQLPNGYLEL FT LGDYVRANGGSLVLGVFSRDAGQRIYNAALSFGEQPGQFYAKRHLVPFGEYSPPLFGWF FT YRLVNIPMSDQTRGPEHQAPMVFGEHRVALNICYEDLFGAEIVRSLPEATLLLNLSNLA FT WYGDSLAQPQHLQIARVRALESGRPMLRATNTGMTAVVQPDGMVSAVLPAFEQGVLRAE FT VRGYSGLTPYARWGDGAALALAALALVLGIAGAALRVRPLARSVGR" FT CDS 838754..839893 FT /transl_table=11 FT /locus_tag="azo0783" FT /product="membrane fusion protein" FT /function="Membrane-fusion protein" FT /note="HlyD family secretion protein. The secretion of a FT number of proteins/molecules require the help of members FT belonging to the ABC transporter family and a membrane FT fusion protein belonging to the HlyD family, TREMBL:Q7NHP0 FT (27% identity); SignalP predicting signal peptide. TC FT (8.A.1): The Membrane Fusion Protein (MFP) Family." FT /note="Family membership" FT /db_xref="GOA:A1K3J5" FT /db_xref="InterPro:IPR006143" FT /db_xref="InterPro:IPR006311" FT /db_xref="UniProtKB/TrEMBL:A1K3J5" FT /protein_id="CAL93400.1" FT /translation="MKKPISRRALVLAALAATLVLAIAVLRPPAGDAVAERPPAAPRPA FT LTVTTTTPESRPLPLRIAANGDIAAWQEASIGAGVGDQRLLEVLVNVGDRVRAGQLLAR FT FDEDTLRADVAQARAALLEAEAAAAEAQANAERARNLRSGGAMSEQQVVQYLTAERTTQ FT ARIAAARATLAAQEVRLAHARVVAPDHGVISSRSATVGAVVGAGAELFRMIRQGRLEWR FT AELTAAEMARVRVGTPVRLTLPDGSEAGGKVRMLAPTVDPRTRSGLAYVDLAAAESAQA FT GAGPRAGMFARGEFELGASTGLTLPQQAVVVREAFSYVFRVGEDDRVSQIKIQTGRRVG FT DRVEVVDGLPADARVVVAGAGFLNEGDLVRVAEAPADPR" FT CDS 839904..842957 FT /transl_table=11 FT /locus_tag="azo0784" FT /product="RND efflux transporter, permease protein" FT /function="Cation/multidrug efflux pump" FT /note="AcrB/AcrD/AcrF family protein. Members of this FT family are integral membrane proteins. Some are involved in FT drug resistance. AcrB cooperates with a membrane fusion FT protein, AcrA, and an outer membrane channel TolC. The FT structure shows the AcrB forms a homotrimer, TREMBL:Q9A3K6 FT (38% identity); TREMBL:Q89XF8 (40% identity). InterPro FT (IPR001036): Acriflavin resistance protein. Pfam (PF00873): FT AcrB/AcrD/AcrF family. TIGRFAM (TIGR00914): Heavy metal FT efflux pump, CzcA family. TIGRFAM (TIGR00915): FT Hydrophobe/Amphiphile Efflux-1 (HAE1) Family protein. TMHMM FT predicting 12 transmembrane helices. TC (2.A.6.2): The FT (Largely Gram-negative Bacterial) Hydrophobe/Amphiphile FT Efflux-1 (HAE1) Family." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3J6" FT /db_xref="InterPro:IPR001036" FT /db_xref="UniProtKB/TrEMBL:A1K3J6" FT /protein_id="CAL93401.1" FT /translation="MNVSAWSIRNPIPAGMLFVLLSFAGLLSFAGMKVQNFPDIDLPTV FT TVTASLPGATPSQLENDVARKIENAIATLQGLKHIYTKVQDGSVVITVEFRLEKPVQEA FT VDDVRSAVARVKADLPGDLRDPIVNKVDLAGQPVLAFTIRSARMDDEALSWFVDDTVSR FT RLLAVRGVGAVTRVGGVTRELRVTLDPLRLQALGATAAAISHQLRQVQTESAGGRADLG FT GGEQPVRTLATVASAAELADLELALSDGRSIRLSQVASITDTFAEPRSAALLNGQPVVG FT FEVARSRGESEVEVGAAVQGALDELRAAHPDIEITEAFNFVAPVQEEYDGSLQLLYEGA FT LLAVLVVWLFLRDWRATFVSAVALPLSVIPAFIGMYLLGFSVNVITLLALSLVVGILVD FT DAIVEVENIVRHLRMGKTPYEAAMEAADEIGLAVIATTFTLIAVFLPTAFMSGVAGKFF FT KQFGWTAALAVFASLVVARVLTPMMAAYILKPVVGTHREPRWLAWYERWAERCLRHRAL FT TMLAAAAFFIGSLMLVPLLPTGFIPPDDNSQTQVYLELPPGATLATTRAVAEEARLALT FT RVDHVVSVYTTIGAGSAGGDPFAPKGEGEVRKATLTVQLSPRGERPRKQDIENRIRAAL FT EPLPGVRSKVGLGGSGEKYVLVLTGEDPRALQATALAVERDLRTIPGLGSVASTASLIR FT PEIAVRPDFARAADLGVTSSAIGETLRVATLGDYDMSLAKLNLSQRQVPILVRLDESAR FT QDLALLERLAVPGAEGPVMLRQVATLEVAGGPAVIDRYDRSRNINFEIELSGLPLGDVT FT AAVAELPSVKNLPPGIRVVPVGDAEVMGELFASFGLAMLTGVLCIYIVLVLLFKDLLHP FT VTILMALPLSLGGAFVGLLIAQKSFSMPSLIGLIMLMGIATKNSILLVEYAIVARRDHG FT MSRSEALLDACRKRARPIVMTTIAMGAGMMPIAIGAGAADTSFRSPMAIAVIGGLITST FT VLSLLVVPVVFTYVDSFKNRFLALFGRG" FT CDS 843084..844010 FT /transl_table=11 FT /locus_tag="azo0785" FT /product="Glycyl-tRNA synthetase alpha chain" FT /function="Glycyl-tRNA synthetase alpha subunit" FT /EC_number="6.1.1.14" FT /note="Glycyl-tRNA synthetase alpha chain (EC 6.1.1.14) FT (Glycine--tRNA ligase alpha chain) (GlyRS)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3J7" FT /db_xref="InterPro:IPR002310" FT /db_xref="InterPro:IPR006194" FT /db_xref="UniProtKB/TrEMBL:A1K3J7" FT /protein_id="CAL93402.1" FT /translation="MSPAHAKPTFQQVILTLQQFWGERGCVLLQPYDLEVGAGTSHTAT FT FLRAIGPEPWNAAYVQPSRRPKDGRYGENPNRLQHYYQYQVVLKPSPLNIQELYLDSLR FT ALGIDPNAHDIRFVEDDWENPTLGAWGLGWEVWLDGMEVTQFTYFQQVGGLDCKPVLGE FT ITYGLERLAMYLQGVENVYDLTWAVYPDGSKVTYGDVYHQNEVEQSKYNFEHSNVDFLF FT SLFNNYESEAKRLMDAGLALPAYEMVLKAAHNFNMLDARGAISVTERAAYIGRIRNLSR FT AVAQAYFESREALGFPMLPQQNKEAAQ" FT CDS 844007..846094 FT /transl_table=11 FT /gene="glyS" FT /locus_tag="azo0786" FT /product="Glycyl-tRNA synthetase, beta chain" FT /function="Glycyl-tRNA synthetase beta subunit" FT /EC_number="6.1.1.14" FT /note="Glycyl-tRNA synthetase beta chain (EC 6.1.1.14) FT (Glycine--tRNA ligase beta chain) (GlyRS)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3J8" FT /db_xref="InterPro:IPR006194" FT /db_xref="InterPro:IPR008909" FT /db_xref="InterPro:IPR015944" FT /db_xref="InterPro:IPR023279" FT /db_xref="UniProtKB/Swiss-Prot:A1K3J8" FT /protein_id="CAL93403.1" FT /translation="MTANTLLVELLTEELPPKALPRLGETFATKIAEGLKARGLAAADG FT AFRWFASPRRIAITMAGVAAEAAAKEVTEKLMPVAVALDADGKPTPALLKKMEAKGIPA FT SAVPAFERRMDGKAEALFHTAVVPGARLAEVLAAIVHDAVKALPIPKVMRWGDGDATFV FT RPVHKLVMLHGAEVVPGRVLDLDAGRSTRGHRFMSRGEIDIATADAYEPTLLAEGKVVP FT DFAERRADIERQLLAEAARLGAQLDDYTDLLDEVTALVEHPTVYVGEFEAEFLAVPQEC FT LILTMRANQKYFPLFDAAGKLQNRFLIVSNMRMEDPVNIVTGNARVVRPRLSDARFFFE FT TDKKHKLDSRLPRLANVVYHNKLGSVLERVERLEALAGKIAARLGSDEAAARRAARLAK FT ADLVSEMVGEFPELQGIMGRYYALHDGEGAVVADAVQAHYQPRFAGDALPAGNVAAAVA FT LADKLDALVGFFGIGMVPTGDKDPFALRRAALGVLRILMEAPLPLDLAALVADAAAGFK FT PGLLTADGFQAQLLDFMRERLKNLLRESGGEVAAIDAVLALAPTRIDLVPAKLAAVEAF FT RALPEAEALAAANKRIVNILKKAEGAPGEPDVALLQEDAEKALFHRVIEIAPLVKSHVA FT NEDYTDALCVLAGLRAEVDAFFDGVMVMAEEPLTRQNRLALLAQLAGLMNQVADISRLS FT A" FT CDS 846144..846677 FT /transl_table=11 FT /locus_tag="azo0787" FT /product="putative haloacid dehalogenase-like hydrolase" FT /EC_number="3.1.3.-" FT /note="Putative haloacid dehalogenase-like hydrolase, 60% FT Identity to TrEMBL;Q7W4K4,Q7WG29,Q7W0Q4. Has FT PF00702,haloacid dehalogenase-like hydrolase; IPR005834 FT Dehal_like_hydro; This family are structurally different FT from the alpha/ beta hydrolase family (Abhydrolase_1). This FT family includes L-2-haloacid dehalogenase, epoxide FT hydrolases and phosphatases. The structure of the family FT consists of two domains. One is an inserted four helix FT bundle, which is the least well conserved region of the FT alignment, between residues 16 and 96 of P24069. The rest FT of the fold is composed of the core alpha/beta domain." FT /db_xref="GOA:A1K3J9" FT /db_xref="InterPro:IPR004446" FT /db_xref="InterPro:IPR006543" FT /db_xref="InterPro:IPR006549" FT /db_xref="InterPro:IPR013954" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:A1K3J9" FT /protein_id="CAL93404.1" FT /translation="MKLIILDRDGVINYDSDQFIKSPEEWKPIPGSLEAIAKLNQWGWR FT VVVASNQSGVGRGLFGMDTLNAINEKMVKSLAQVGGRLDAIFFCPHAADSTCECRKPKP FT GLFLQIAARFNADLAGVPCVGDSLRDLQAGAAVGCQPYLVLTGKGLKTREDPALPDNAL FT IYPDLASVVADLTA" FT CDS 846695..847453 FT /transl_table=11 FT /locus_tag="azo0788" FT /product="probable acyltransferase" FT /function="1-acyl-sn-glycerol-3-phosphate acyltransferase" FT /EC_number="2.3.1.5" FT /note="Acyl-[acyl-carrier protein] can also acts as acyl FT donor.The animal enzyme is specific for the transfer of FT unsaturated fatty acyl groups. Catalytic Activity:- FT Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + FT 1,2-diacyl-sn-glycerol 3-phosphate. Entry name FT TREMBL:Q82VB2 Prim. accession # Q82VB2 InterPro:- FT IPR002123; Acyltransferase. Pfam:- PF01553; FT Acyltransferase; 1. Identity:- 56% Prediction: Signal FT peptide Signal peptide probability: 0.907 Number of FT predicted TMHs: 1" FT /note="Family membership" FT /db_xref="GOA:A1K3K0" FT /db_xref="InterPro:IPR002123" FT /db_xref="UniProtKB/TrEMBL:A1K3K0" FT /protein_id="CAL93405.1" FT /translation="MILLRSLLFAIVLAVVTPPYAILGMLMFPFSPHLRHRVITSWAPL FT VMWFVRHLLGIRYRVVGAENIPAGPAVILSKHQSAWETMALQVIFPPLCFVLKRELLKV FT PFFGWGLAAIPGIAIDRAAGKDALAQVVEQGRARLKEGFWVVVFPEGTRVAPGTARRYK FT VGGAWLAKRAGVPVVPVAHNAGEFWRRNAFLKHPGEITVSIGPAIEVKGVKAEEINRRA FT EEWVEGEMRRLFPHHYTGDAPTLLPEVDAG" FT CDS complement(847542..848102) FT /transl_table=11 FT /locus_tag="azo0789" FT /product="probable phasin" FT /note="Probable phasin. Homology to p8 of Sphingomonas sp. FT A1 of 69% (gi|51773776|dbj|BAD38885.1|(NBCI ENTREZ)). No FT domains predicted. No TMHs. No signal peptide." FT /note="Family membership" FT /db_xref="InterPro:IPR010127" FT /db_xref="InterPro:IPR018968" FT /db_xref="UniProtKB/TrEMBL:A1K3K1" FT /protein_id="CAL93406.1" FT /translation="MTATPEQITAAAKANIETLLTLANSAFSNVERLAALNLNTARSVL FT EDGVANTKALLAAKDVQEFVSLQTSLAQPLIEKAVAYNRSVYEIASQSQEELSKLFEGQ FT VAELNKSLAAALDKAAKSAPAGSDVAVAAVKSAIAAANSAYDSVSKAAKQVAEIAEANV FT AAATNATVKAVTTTSKAASKKVA" FT CDS complement(848399..849175) FT /transl_table=11 FT /gene="paaF1" FT /locus_tag="azo0790" FT /product="probable enoyl-CoA hydratase" FT /function="Enoyl-CoA hydratase/carnithine racemase" FT /EC_number="4.2.1.17" FT /note="COULD POSSIBLY OXIDIZES FATTY ACIDS USING SPECIFIC FT COMPONENTS (BY SIMILARITY). CATALYTIC ACTIVITY: FT (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. FT Entry name :- SWISSPROT:PAAF_ECOLI Prim. accession # P76082 FT InterPro :- IPR001753; EnCoA_hydrtse. Pfam :- PF00378; ECH; FT 1. Identities = 109/250 (43%) Prediction: Non-secretory FT protein Signal peptide probability: 0.000 Number of FT predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K3K2" FT /db_xref="InterPro:IPR001753" FT /db_xref="InterPro:IPR018376" FT /db_xref="UniProtKB/TrEMBL:A1K3K2" FT /protein_id="CAL93407.1" FT /translation="MSFENILTETRGRVGLITLNRPKALNALNDALVDEVGQALDAFEA FT DENIGAIVITGSEKAFAAGADIGAMATFSYMDAYKGDYITRNWERVKTCRKPVIAAVAG FT FALGGGCELAMMCDIIIAADTAKFGQPEVKLGILPGAGGTQRLPRAVGKAKAMDMCLTA FT RFMDATEAERAGLVSRVVPADTLVDEALSAAEAIASYSLPVVMMIKESVNRAFESSLNE FT GLLFERRVFHAAFALNDQKEGMAAFVAKRKANFSHD" FT CDS complement(849202..849774) FT /transl_table=11 FT /locus_tag="azo0791" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein. Homology to FT rsc0410 of R. solanacearum of 42% (trembl|Q8Y2C6(SRS)) FT Pfam: OstA-like protein This family of proteins are mostly FT uncharacterised. However the family does include E. coli FT OstA P31554 that has been characterised as an organic FT solvent tolerance protein. signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3K3" FT /db_xref="InterPro:IPR005653" FT /db_xref="InterPro:IPR014340" FT /db_xref="UniProtKB/TrEMBL:A1K3K3" FT /protein_id="CAL93408.1" FT /translation="MKLLNRALLAPAALTLALAAAPALAERADRDQPVNIEANKVTVDD FT RNKVHIFEGDVVLTQGTLVIKGDKLVVTQDAGGFQNGVATASNPRLATFRQKREGSNEY FT VYGEAERIEYSSRTEKAKLFVRAKVTSGGDEVRGHFIEYDSMSENYLVTNAPGAAPAAT FT SGGDGRVRAVIQPKSDNKAGGAESAKP" FT CDS complement(849771..850349) FT /transl_table=11 FT /locus_tag="azo0792" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein. Homology to FT ebA1318 of Azoarcus sp. EbN1 of 47% FT (gnl|keqq|eba:ebA1318(KEGG)). Has PF06835, Protein of FT unknown function (DUF1239);IPR010664;This family consists FT of several hypothetical bacterial proteins of around 190 FT residues in length. The function of this family is unknown. FT No TMHs. Signal peptide." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR010664" FT /db_xref="UniProtKB/TrEMBL:A1K3K4" FT /protein_id="CAL93409.1" FT /translation="MQAAYRLYPVIALALLAGASVWLERVSRNDTPAAAPAQQTGPDFI FT AEQTRLIGFGKDGNIRYELVSERSAHFPQGDITRIALPRLVMFSEGRATRVTAAQGEVS FT PGGERVDLSGAVRVRRGGDGNGSELALDSETLSVWPDDHRAESQSPVSLVHGRNTAQAQ FT GMHADNLFGTLELIGQARVRLPRRQENPS" FT CDS complement(850359..850880) FT /transl_table=11 FT /locus_tag="azo0793" FT /product="probable phosphatase (HAD superfamily)" FT /function="Low specificity phosphatase (HAD superfamily)" FT /note="Catalyzes the hydrolysis of KDO 8-P to KDO and FT inorganic phosphate TREMBL:Q9JSU3: 43% identity, 59% FT similarity InterPro: IPR006549; HAD-SF-IIIA. IPR005834; FT Hydrolase. IPR008230; Sugar_Ptase. IPR010023; FT YrbI_phosphatas. Pfam: PF00702; Hydrolase TIGR00099: FT conserved hypothetical prote Absence of transmembrane FT helices." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3K5" FT /db_xref="InterPro:IPR010023" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:A1K3K5" FT /protein_id="CAL93410.1" FT /translation="MAQPESAAKIRLMGFDVDGVLTDGSLYFTPNGEEIKVFSSLDGHG FT IKMLQQAGIEVAIISGRSSRALALRAANLGIGELHMGVEDKRACLDDLLARRGIARAEA FT GYMGDDVVDLPILRACGFSATPADGHPFVREHVDFVASRDGGRGAVREVCDFLLASRGV FT LDAMHAAYLD" FT CDS complement(850880..851875) FT /transl_table=11 FT /locus_tag="azo0794" FT /product="sugar-phosphate isomerase" FT /function="possibly involved in the biosynthesis of an FT unidentified cell surface carbohydrate" FT /note="Arabinose 5-phosphate isomerase (EC 5.3.1.13). FT Catalyzes the interconversion of D-arabinose 5-phosphate FT and D-ribulose 5-phosphate (By similarity). InterPro: FT KpsF/GutQ family protein kpsF: KpsF/GutQ family protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3K6" FT /db_xref="InterPro:IPR000644" FT /db_xref="InterPro:IPR001347" FT /db_xref="InterPro:IPR004800" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:A1K3K6" FT /protein_id="CAL93411.1" FT /translation="MDPIAPGTAPTHRAAELARHVLRVEAAAVAALAERVGDDFERAVE FT LILGRSGRVIVTGIGKSGHIARKLAATLASTGTPAYFVHAAEAAHGDLGMITPEDVVIA FT LSNSGASEELLMIVPLVKRQGARLIALTGRPDSPLAREADVHLDGAVSEEACPLNLAPT FT ASTTAALALGDALAVALLDARGFGPDDFARSHPGGSLGRRLLTHVSDVMRPAPEVPVVG FT REAALAEALLAMTRGGMGMTVVADPDGRPLGIFTDGDLRRALEKGIDVRAARIADLMTP FT QPRHISPDALAAEAAEVMERQRISQLLVLDAAGKLAGALTTHDLMLAKVI" FT CDS 852075..854042 FT /transl_table=11 FT /locus_tag="azo0795" FT /product="putative glutathione-regulated potassium-efflux FT system protein" FT /function="Kef-type K+ transport systems membrane FT components" FT /note="Probable glutathione-regulated potassium-efflux FT system protein (K(+)/H(+) antiporter). Transport system FT that facilitate potassium-efflux possibly by FT potassium-proton antiport. 50% Na_H_porter.IPR006037; FT TrkAC.IPR003148; TrkA_N. Pfam: PF00999; Na_H_Exchanger; FT 1.PF02080; TrkA_C; 1.PF02254; TrkA_N; 1. TMhelix: 11." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3K7" FT /db_xref="InterPro:IPR003148" FT /db_xref="InterPro:IPR004771" FT /db_xref="InterPro:IPR006037" FT /db_xref="InterPro:IPR006153" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K3K7" FT /protein_id="CAL93412.1" FT /translation="MLNTLDLVLLLLAAAVVLVAVLRSVNLPPVLGYLLVGAMVGPHAF FT NLVPDSAGARHLAEFGVVFLMFSIGLEFSLPRLLAMKNIVFGLGAAQVVGSIALTLVLG FT RLGGLGWAAAFALGGTIAMSSTAILSKLLADRLELDSRHGREIIGVLLFQDLAVVPLLI FT LLPALSRPAEELAVTLGLAGIKAVVLLALVLVFGPRLMRWWFTLVARRRSGELFMLNVL FT FITLGLAWLSELVGLSLALGAFLAGMLISETEYRYQVEEDIKPFRDVLLGLFFVTVGMF FT LDVETIVWHLPAVIGLVVALLAAKFLIVFAASRAFRSPPGTAMRSGLWLCAGGEFGFVL FT LSEIVGLRLMPAGLVQVTVAALVLSMLVAPLIVQVSDKLVMRFVASEWLLRSMELTRVA FT AQSLNTDKHIIVCGYGRSGQYMARFLEQENLSYVALDLDPERVREAGAAGDTVVYGDAA FT RRETLMAAGIMRASALVISFAEVEAALRVMHHAHALRPGLPIVVRAVDEADMEKLSLGG FT AAEVVPEAFEGSIMLASHALALIGVPLSRVVKRIRDIRNQRYALMRGFFHGATDIGEVA FT ENSQARLHSVTVPDAAPAVGRTIGELALEEFGVGVSAVRRRGIRGLSPGPETRIVAGDV FT LVLLGLPQGLEQAEERVLKG" FT CDS complement(854050..854697) FT /transl_table=11 FT /locus_tag="azo0796" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrabe protein. Homology to FT Mflag03002444 of Methylobacillus flagellatus of 48% FT (gi|46120631|ref|ZP_00201765.1|(NBCI ENTREZ)). no domains FT predicted. No signal peptide. 1 TMHs" FT /db_xref="InterPro:IPR001120" FT /db_xref="InterPro:IPR012902" FT /db_xref="UniProtKB/TrEMBL:A1K3K8" FT /protein_id="CAL93413.1" FT /translation="MHSRQHGFTLVEIAIVLVIIGLLLGGVLKGQEILNNAKVKNLTQD FT FRGIPMLLHGYRDKYRATPGDDANARRHICPAAAGECTTNGNGDGLIGGNWNDTAASES FT FLFWQHVRMANLAAGATDTADPGYAPRNAEGGRLGIQSSGDAAPLGVPGSYALCSAAVP FT GRFVRQIDLAVDDGEPATGTLRAGTQGAGGLTALAADTPVDDAATYVLCLGF" FT CDS complement(854732..855430) FT /transl_table=11 FT /locus_tag="azo0797" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT Daro03002886 of Dechloromonas aromatica of 31% FT (gi|53729825|ref|ZP_00150246.2|(NBCI ENTREZ)). No domains FT predicted. No TMHs. Signal peptide." FT /db_xref="InterPro:IPR012902" FT /db_xref="UniProtKB/TrEMBL:A1K3K9" FT /protein_id="CAL93414.1" FT /translation="MPAMNRAPPPRHRRARGFTLAELAIVLVVIGLLTGGMLGPLASRL FT EARQRQETSERLRDIEQALYGFAILHGRLPCPSTEHDPGSPGYGRENAPPCDDSVEGML FT PWRTLGLGPVDAWGTPRSSPTAPWPGHWRYRVDRAFAAAGGISAATAPLSNLQLYDHDN FT RPITVESESRAVAIVYSTGNNLRADGLNASYSATHPRYQAGEATASFDDLLIWIGHPLL FT IARLAQAGRL" FT CDS complement(855418..856656) FT /transl_table=11 FT /locus_tag="azo0798" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. No TMHs. Signal peptide FT present." FT /db_xref="UniProtKB/TrEMBL:A1K3L0" FT /protein_id="CAL93415.1" FT /translation="MAHRSGGVALLGLLLLAAVVGAALFVAGTDLEGKIRARHTAASLE FT TLASARAALAGYALSYPERHPDQGYGYLPCPDSGNDGAPAGACGSRGLAAFGRFPYRTL FT GLADVRDGDGECLWYAVAASGKNNPKAQVFDWDSPGDFELRSLGGHVLAGSDAPSARAL FT AVVFAPGRALQGQQRPPSAARCSGGARAADDIAHYLEGGYVPTATGPLSVHQGEAGNTS FT NNDLIAWLTTDDIFDALRRRPEFAAYLNGFLDTAAAALVTASLQPAFVDRHAVPVAGPL FT AQGPLPDAAALGLALTAAARHDNWREQARFVVCTDGSACLTASLAESAAAPAPVGLGQC FT RVAVLFAGERIRSGNGAQRRGTAAEREDYANWFEGPNPQLLSGGGGQLAGYRHFAVADP FT RRPAHEDVVRCLP" FT CDS complement(856671..857057) FT /transl_table=11 FT /locus_tag="azo0799" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. no homology with the FT data bank. no domains predicted. signal peptide. no TMHS" FT /db_xref="UniProtKB/TrEMBL:A1K3L1" FT /protein_id="CAL93416.1" FT /translation="MKRRSALLPLLLALWSGSAPAAPLGRLFFTPAERAAGALAVSPPP FT TTSPTVAAPRLDGVLRTGSGGTLVWLDGEPRTLEAGARLRFDPAHGEATFSPAAAPLHL FT GDTDAPEPAPRWRRAITGTREPLP" FT CDS complement(857054..857644) FT /transl_table=11 FT /locus_tag="azo0800" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. No TMHs. Signal peptide FT present." FT /db_xref="UniProtKB/TrEMBL:A1K3L2" FT /protein_id="CAL93417.1" FT /translation="MNRRRAWRTHASSYRALVLGAALLLIGGATLAAALTHQEVERAAS FT ARLQRELADTSAGIDATRQSLLQLRSDLASYRALLAHGTFGPERTARWADTLARQLATQ FT ELGHVSVQFTAARPLLANSPQGLHAATARIAVELSHEEALLDLLDGVAGTADALVIGRG FT CDVLRRSTNPAPTALHAECEFDWIALSGPGRAP" FT CDS complement(857641..859065) FT /transl_table=11 FT /locus_tag="azo0801" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. Signal peptide present. 1 FT TMH present." FT /db_xref="UniProtKB/TrEMBL:A1K3L3" FT /protein_id="CAL93418.1" FT /translation="MGRDCLLLISAAGARAWTQQRGGLAPGPHFAADAAGHAAFSEWLS FT TRPAASFTLLADLAGESLRLETLPRSGGRDRTSLISRRCRQHFPDTPYTAAQPFRAPSG FT APPRETVLLSALTPADALEPWLQRLAAQGSAVRSLHGMGFALALWVRRHGRRQPVLRGD FT FLLVSASPAGERHSYFQHGQLRFSRLIGDGEEAPLRRSEAHLYAHDLTDRRTPLTIVGV FT GAEDLVAAHNSGPHHEGGIPAPFQPVALHLPSPAGPDAAWLAPLHRLLSRALHPQAGHA FT PADLVRVFRTRRALATLGGVATAVGVIALAGAASVALSTRPLVQHNAALTERLAVDART FT LAALQADTPATPHPPAEMRAIAAELGRQRRLHAEPRQALATIAAVLDRHPQAVLHELRW FT ERPPQDSAGPAPLRVTLRLELDGSDDRASARGAERLAADLARQPGIQLRPLPAETAPGA FT TPAGHLRLELQFLEPA" FT CDS complement(859072..860277) FT /transl_table=11 FT /gene="gspF1" FT /locus_tag="azo0802" FT /product="general secretion pathway protein F" FT /function="Type II secretory pathway component PulF" FT /note="Type II secretory pathway component F," FT /note="Specificity unclear" FT /db_xref="GOA:A1K3L4" FT /db_xref="InterPro:IPR003004" FT /db_xref="InterPro:IPR018076" FT /db_xref="UniProtKB/TrEMBL:A1K3L4" FT /protein_id="CAL93419.1" FT /translation="MSRLQAHAYRAVNGDGRRVRGRAHALHLNDLEARLATRGLTLIHG FT EVARRSLRPQPRLPARELGAFCAQLAHLLEAGIPLVEALRDLGEGNATPAARPWDDIAT FT ALEGGDTLSDACAARADLFDEVFVSLLRAGEQAGRLPAVLHHLAATLERSAQVAAHLRR FT MSIYPAFVLAVLAVAAGTALVFVVPQLSSLFRSLGETLPWQTRALLSLSDLVLRHGAWA FT TVVAILCLAGLRLALLRSIAFRLQVHAALLRLPVVGGLWHTALLARVCQVLAVSYEAGV FT PIVAAVTAAAGTAGNLVVRTGLEQVADDIAAGADLSGALASTRVFPPRVTRMLRAGEHS FT GTLDRALRHAGAFYERELQEGVARLQAAVEPALTVLLGLLMLWIMSAILGPIYDVLGKL FT PL" FT CDS complement(860274..861974) FT /transl_table=11 FT /gene="gspE1" FT /locus_tag="azo0803" FT /product="general secretion pathway protein E" FT /function="type II secretion system protein E" FT /note="Bacterial type II secretion system protein E," FT /note="Specificity unclear" FT /db_xref="GOA:A1K3L5" FT /db_xref="InterPro:IPR001482" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR007831" FT /db_xref="UniProtKB/TrEMBL:A1K3L5" FT /protein_id="CAL93420.1" FT /translation="MAPLPDHDALATLLLAAGVIGQDQLRIARMEQQRAPRPLADLLLG FT LGFLSESALRGVISEASGRRPVDLARSLPDDAALALVPVEFARRNQLLPLSLDTDQAVL FT TIATAATDDRAVIDKLLALCPQLRRVECLLAAGPELGRAIERHYGQAQSLESILHELET FT GAPPPPQRPGGEGHPQALVRLVDALLLDAVKRDASDIHFEPEAHHLRIRCRIDGVLRQT FT RALHATYWPAMAVRIKVLAGLNIAETRVPQDGRFSFDVAGHAIDFRVSCMPTLHGENVV FT LRLLDRSKGVVPLSDLGLGAGDLAALEAMIARPEGLILVTGPTGSGKTTTLYSLLAHLN FT TEARSIMTLEDPVEYPMPRLRQTQVADSGRIGFAEGVRAMLRQDPDVLLIGEIRDADTA FT AMALRAAVTGHQVYSTLHAGSALGALPRLRELGVSPEMLAGNLIGIVAQRLVRRLCPDC FT AETVAIEPWARPYLATDDSAAATRMQARGCARCNFQGYRGRLALMEILPVDTGLDDLLA FT RGANRSDLLAHAQRQGHVGLAAAGLARVRAGDTTLEELLRVVDVRGARR" FT CDS complement(861980..862615) FT /transl_table=11 FT /locus_tag="azo0804" FT /product="hypothetical protein" FT /note="Hypothetical protein. No homology to a protein of FT similar size. No domains predicted. No signal peptide. No FT TMHs" FT /db_xref="GOA:A1K3L6" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="InterPro:IPR019734" FT /db_xref="UniProtKB/TrEMBL:A1K3L6" FT /protein_id="CAL93421.1" FT /translation="MLLAVLALCTARAEGGTPLQDDATPYTSLAAAHAALEAGQLDAAR FT AHYIHALRQAPTAVEARNGVAVVLLRQGDAAGAASWFRAALEVSPDDPVAHAALYSLGA FT ETAPASEDRLRRLLGRHPDAAALYLALGNLLARQDRWAEAQDAYFRAYTFNPDEPDVLF FT NLAVGLDHLRQRSAAGFYARALEAALLRPHSFDPEQARGRLHALTATR" FT CDS complement(862681..864423) FT /transl_table=11 FT /gene="gspD1" FT /locus_tag="azo0805" FT /product="general secretion pathway protein D" FT /function="Type II secretory pathway component PulD" FT /note="Type II secretory pathway component D, weak FT similarity to SWISSPROT:HOFQ_ECOLI (18%). A number of FT proteins are involved in the general secretion pathway FT (GSP); one of these is known as protein D (GSPD protein). FT Protein D is involved in the type II general secretion FT pathway within Gram-negative bacteria, a signal FT sequence-dependent process responsible for protein export. FT InterPro (PF00263): General (type II) secretion pathway FT (GSP) D protein" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3L7" FT /db_xref="InterPro:IPR001775" FT /db_xref="InterPro:IPR004845" FT /db_xref="InterPro:IPR004846" FT /db_xref="InterPro:IPR011514" FT /db_xref="UniProtKB/TrEMBL:A1K3L7" FT /protein_id="CAL93422.1" FT /translation="MLLTGNASPTRGIHDGLSARVPKRPEISFCHLRIHPLECRVYSFA FT ISANTPMRPQPITAVLAALLAAACAPLQAPPALGHLGTTPATAVLAPIPAPAPGALTLP FT PPRPAAAEETYSIVVNKVPVESLLFSLARESGLEIDLHPALQGTVTLNAVNQPLRQLLE FT RIARQVDMRFELEGRHLTVMPDAAFHRTYRLDYVNLTRGMTGTVATSTQIATSSSALGA FT ARTSGGNASITQIESTSANRFWESLEANLRAILELGKDADAVVSNRESGVLVVRATARQ FT HSRIAEFIDAVQRAARRQVMIEATIVEVALGDEYQQGIDWRRLGNPNWRVAARGSGDAN FT ALTPTLSYLSDRLDVRLDLLETFGSAKILSSPRLSVLNNQTAMLKVVEEVVYFLVDAST FT TQYDDADREKTTATTTPQSVSVGMVMALTAQVSAGGEIILNVRPTISSISGFKDDPNPS FT LGSIPNRVPQIRTREIESVLRLRSGETAVLGGLIEDKVDYDTGRIPLLGSLPLLGEVFS FT HRDNAVRRSELVIFLRPVVVEDPALGGDYAELRQHLPDAGFFDIGHPHGTPLRVRANPG FT LGQP" FT CDS 864497..865330 FT /transl_table=11 FT /locus_tag="azo0806" FT /product="conserved hypothetical ABC transporter FT ATP-binding protein" FT /note="Conserved hypothetical ABC transporter ATP-binding FT protein. Homology to rs01335 of R. solanacearum of 67% FT (trembl|Q8XV69). ATP-binding cassette (ABC) transporters FT are multidomain membrane proteins, responsible for the FT controlled efflux and influx of substances (allocrites) FT across cellular membranes. They are minimally composed of FT four domains, with two transmembrane domains (TMDs) FT responsible for allocrite binding and transport and two FT nucleotide-binding domains (NBDs) responsible for coupling FT the energy of ATP hydrolysis to conformational changes in FT the TMDs. Both NBDs are capable of ATP hydrolysis. Pfam: FT ABC transporter (PF00005). No signal peptide. No TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3L8" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K3L8" FT /protein_id="CAL93423.1" FT /translation="MPPVPVPSSQHADPLVRLHGVRFAYGEREVLRGIDLAVGKGQVVA FT IMGGSGCGKTTLLRLIGGQLKASSGVVEVGGENVAGLSAARLYELRRRMGMLFQFGALF FT TDMTVFDNVAFPLREHTDLDADLIRDLVLMKLNAVGLRGAHALKPAELSGGMARRVALA FT RAVALDPMLILYDEPFAGLDPISLGVIGQLIRKLNDALGASSVMVTHDIHESLEIVDYV FT YFVSEGRIVAQGTPDEIRASRDPFVHQFVHAEADGPVPFHYPAPPVASLIEETPR" FT CDS 865327..866118 FT /transl_table=11 FT /locus_tag="azo0807" FT /product="conserved hypothetical membrane protein" FT /function="ABC-type transport system involved in resistance FT to organic solvents permease component" FT /note="Conserved hypothetical membrane protein Similar to FT TREMBL:Q7P0W7 (65% identity); TREMBL:Q82SF6 (65% identity); FT TREMBL:Q7VSZ9 (57% identity). InterPro (IPR003453): Domain FT of unknown function DUF140. Pfam (PF02405): Domain of FT unknown function DUF140. TIGRFAM (TIGR00056): Conserved FT hypothetical protein. TMHMM reporting five transmembrane FT helices." FT /db_xref="InterPro:IPR003453" FT /db_xref="UniProtKB/TrEMBL:A1K3L9" FT /protein_id="CAL93424.1" FT /translation="MSGLVAALRRLGGMSIDAVWRLGFATRFLLMVLVYSGQSVRRIHL FT TLREIYFAGVLSLLIILVSGLFVGLVLGLQGYETLQRFGSSDALGVLVALSLTRELGPV FT VAALLFASRAGSAVTAEIGLMKATEQLKAMDMMAVNPLARVVAPRFWGGVISMPLLAAM FT FSAMGVFGGWLIGVVFIGVDDGAFWSQMQAAVDVRYDVLNGVIKSFVFGVAVSLIAVFE FT GYDCTPTAEGVSRAITRTVVSSALAILALDFVLTSFMFRGQ" FT CDS 866118..866591 FT /transl_table=11 FT /locus_tag="azo0808" FT /product="conserved hypothetical secreted protein" FT /function="ABC-type transport system involved in resistance FT to organic solvents periplasmic component" FT /note="Conserved hypothetical secreted protein. Similar to FT TREMBL:Q8XV71 (59% identity); TREMBL:Q82SF7 (55% identity); FT TREMBL:Q7VSZ8 (55% identity). Pfam (PF02470): mce related FT protein. This family of proteins contains the mce FT (mycobacterial cell entry) proteins from Mycobacterium FT tuberculosis. The archetype (Rv0169), was isolated as being FT necessary for colonisation of, and survival within,the FT macrophage. This family contains proteins of unknown FT function from other bacteria. SignalP reoprting signal FT peptide. TMH in signal peptide" FT /note="Family membership" FT /db_xref="InterPro:IPR003399" FT /db_xref="UniProtKB/TrEMBL:A1K3M0" FT /protein_id="CAL93425.1" FT /translation="MSRTTLDLWVGIFVALGLAALVFLAMKVGNFSGLNGAALYSIEAP FT FDNIGGLKVRAPVKSAGVLVGRVADIRFDPESYRAVVRLDIDTRYRFPRDTIATILTSG FT LLGEQYVGLEPGADVEMLAGGERVQLTQSAVVLEKLIGQFLFNKAAEPAAQPQ" FT CDS 866632..867492 FT /transl_table=11 FT /gene="vacJ" FT /locus_tag="azo0809" FT /product="putative surface lipoprotein" FT /function="Surface lipoprotein" FT /note="Putative surface lipoprotein. Homology to vacJ of S. FT flexneri of 26% (sprot|VACJ_SHIFL) Required for FT intercellular spreading. Pfam: VacJ like lipoprotein signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3M1" FT /db_xref="InterPro:IPR007428" FT /db_xref="UniProtKB/TrEMBL:A1K3M1" FT /protein_id="CAL93426.1" FT /translation="MSYRFRSVAGSRGLRVVLAALLAGGCATATTHPQDPLENYNRAMF FT AFNDRVDRAVIKPVAEAYETVVPSPVRSGVGNVFGNLGDPWIAINNLLQGKLLDALSDG FT ARFVMNTTVGVLGILDVATAAGLTKHDEDFGQTLGAWGVGEGAYLVLPFFGPRTVRDAA FT ALPLDVMADDVWAIQHVPTRNSMTALRLVHTRSTLLGTEKTLEEGTIDKYAYSRDFYLE FT QRRYKVFDGNPPRKYEDFDDEGAALPQPTQADFVARAAVESLEVLAVGGEFAQALPPNN FT EESNP" FT CDS 867498..868145 FT /transl_table=11 FT /locus_tag="azo0810" FT /product="conserved hypothetical secreted protein" FT /function="ABC-type transport system involved in resistance FT to organic solvents auxiliary component" FT /note="Conserved hypothetical secreted protein. Similar to FT TREMBL:Q82SF8 (54% identity); TREMBL:Q8XV73 (42% identity); FT TREMBL:Q7VSZ6 (40% identity). SignalP reporting signal FT peptide. no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR008869" FT /db_xref="InterPro:IPR023094" FT /db_xref="UniProtKB/TrEMBL:A1K3M2" FT /protein_id="CAL93427.1" FT /translation="MRSWLSLCLRLALLAAVLSAPTARAADPMGPDVLVRNVTEEVLAI FT VRQDKAIQSGDVGRVLGLVDEKVLPHFNFRRMTMLAVGRDWRQASPQQQDHLVNAFRTL FT LVRTYSNALTQYRDQTIDFKPARYGEADTTVQVRTEVRQAGAQPIAIDYTLEKTAAGWK FT VFDVIVAGVSLVTNYRGSFGEEIRKGGLDGLIRTLEEKNRSLERAAAPQSRA" FT CDS 868216..868497 FT /transl_table=11 FT /locus_tag="azo0811" FT /product="conserved hypothetical protein" FT /function="predicted NTP binding protein (contains STAS FT domain)" FT /note="Conserved hypothetical protein. Homology to rsc2957 FT of R. solanacearum of 42% (trembl|Q8XV74). Pfam: STAS FT domain The STAS (after Sulphate Transporter and AntiSigma FT factor antagonist) domain is found in the C terminal region FT of Sulphate transporters and bacterial antisigma factor FT antagonists. It has been suggested that this domain may FT have a general NTP binding function. no signal peptide no FT TMHs" FT /db_xref="InterPro:IPR002645" FT /db_xref="UniProtKB/TrEMBL:A1K3M3" FT /protein_id="CAL93428.1" FT /translation="MSAGDALRLEGEITLATASGWRERGRAALAAGARVVDFAAVTHVD FT SAALALLLEWRRCARAGAGGPLRVANLPPALVSLAEVYGIDSLLPVAA" FT CDS 868505..869401 FT /transl_table=11 FT /locus_tag="azo0812" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type multidrug transport system ATPase FT component" FT /note="ATP-binding cassette (ABC) transporters form a large FT family of proteins responsible for translocation of a FT variety of compounds across biological membranes. They are FT composed of two transmembrane domains responsible for FT binding and transport and two nucleotide-binding domains FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the TMDs, TREMBL:Q7P0X8 (62% FT identity); TREMBL:Q82SG0 (58% identity). InterPro FT (IPR003593): AAA ATPase. InterPro (IPR001687): FT ATP/GTP-binding site motif A (P-loop). InterPro FT (IPR003439): ABC transporter. Pfam (PF00005): ABC FT transporter. TC (3.A.1): The ATP-binding Cassette (ABC) FT Superfamily." FT /note="Family membership" FT /db_xref="GOA:A1K3M4" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K3M4" FT /protein_id="CAL93429.1" FT /translation="MTTPAIRISAVTKRYGALQALGGVDLEIGQGEFFGLLGPNGAGKT FT TLISALAGLVRPDSGTLQVMGHDVVSDYRNARRALGVVPQELVFDPFFSVRELLRIQSG FT YFGIRNNDAWIDEILASLDLLPKAEANMRALSGGMKRRVLVAQALVHRPPVIVLDEPTA FT GVDVELRQGLWQFVRKLNRDGHTIVLTTHYLEEAETLCGRIAMLKAGKVVALDTTDDLL FT RRFATHNLRVRVERPEVAVGLGGILGEGGWIEFGFETYADVEQLLARLREAQASILELQ FT LGEPDLERVFVEVMHHA" FT CDS 869394..870194 FT /transl_table=11 FT /locus_tag="azo0813" FT /product="ABC-2 type transporter permease protein" FT /function="ABC-type multidrug transport system permease FT component" FT /note="Similar to TREMBL:Q8XV76 (69% identity); FT TREMBL:Q7P0X7 (66% identity); TREMBL:Q82SG1 (64% identity). FT InterPro (IPR000412): ABC transporter, family 2. Pfam FT (PF01061): ABC-2 type transporter. TMHMM reporting seven FT transmembrane helices. TC (3.A.1): The ATP-binding Cassette FT (ABC) Superfamily." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3M5" FT /db_xref="InterPro:IPR000412" FT /db_xref="InterPro:IPR013525" FT /db_xref="InterPro:IPR013526" FT /db_xref="UniProtKB/TrEMBL:A1K3M5" FT /protein_id="CAL93430.1" FT /translation="MPEPHVEVQAGAVSPLTGFRTLLYKEVLRFWKVSFQTVMAPVLNA FT VLFLLIFSHVLDRHVTVYGEIGYTAFLVPGLVMMSLLQNAFANSSSSLIQSKITGNIIF FT VLLPPLSYREFYAAYVIAAVLRGLFVGTGVLLVSIPFVDLHVAHPLWVLAFALMGGAIL FT GSLGVIAGIWAEKFDQLAAFQNFLIMPLTMLSGVFYSIHSLPPLWQDVSHVNPFFFMID FT GFRYGFFGQSDVSPWLSFGVVGLCFVLLAALTLAMLARGYKLRG" FT CDS 870223..870480 FT /transl_table=11 FT /locus_tag="azo0814" FT /product="conserved hypothetical BolA-like protein" FT /function="predicted transcriptional regulator BolA FT superfamily" FT /note="Conserved hypothetical BolA-like protein. Homology FT to ne2377 of N. europaea of 47% (trembl|Q82SG2). InterPro: FT BolA-like protein This family consist of the morphoprotein FT BolA from E. coli and its various homologues. In E. coli FT over expression of this protein causes round morphology and FT may be involved in switching the cell between elongation FT and septation systems during cell division. The expression FT of BolA is growth rate regulated and is induced during the FT transition into the the stationary phase. BolA is also FT induced by stress during early stages of growth and may FT have a general role in stress response. It has also been FT suggested that BolA can induce the transcription of FT penicillin binding proteins 6 and 5. Pfam: BolA-like FT binding protein no signal peptide no TMHs" FT /note="Function unclear" FT /db_xref="InterPro:IPR002634" FT /db_xref="UniProtKB/TrEMBL:A1K3M6" FT /protein_id="CAL93431.1" FT /translation="MFDPNEVKRLIEQGLPCEFVAIEGDDGTHFTGIVVSAAFEGKLPV FT RQHQAVYATLGTLMGNEIHALQLQTYTPAKWETVRGELGL" FT CDS 870517..871767 FT /transl_table=11 FT /gene="murA" FT /locus_tag="azo0815" FT /product="UDP-N-acetylglucosamine FT 1-carboxyvinyltransferase" FT /function="Provides a precursor for murein biosynthesis" FT /EC_number="2.5.1.7" FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase FT (EC 2.5.1.7) (Enoylpyruvate transferase) FT (UDP-N-acetylglucosamine enolpyruvyl transferase) (EPT). FT Cell wall formation. Adds enolpyruvyl to FT UDP-N-acetylglucosamine (By similarity). tim: FT triosephosphate isomerase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3M7" FT /db_xref="InterPro:IPR001986" FT /db_xref="InterPro:IPR005750" FT /db_xref="InterPro:IPR013792" FT /db_xref="UniProtKB/TrEMBL:A1K3M7" FT /protein_id="CAL93432.1" FT /translation="MDKLLIEGGRRLSGEVAISGAKNAALPILCAALLTREPVTFTNVP FT RLNDIGTLLKLLGQMGVKVEREDDRVTLDASALDNPVAPYEMVKTMRASILVLGPLVAR FT CGDARVSLPGGCAIGARPVDQHIKGLQAMGAEVRVEHGYVQAQVPRLKGARLFTDMVTV FT TGTENLMMAACLAQGETVIENAAREPEVVDLANCLVAMGAQISGAGTDVIRIRGVDALH FT GATHRIMPDRIETGTYLCAAAVTGGEVRLTGTSSCYLDAVIDKLMDAGCEVVSERDAIR FT LAAPRRPQAVNLRTAPYPAFPTDMQAQFMALNCVADGAAMIRETIFENRFMHAVELQRL FT GADIRIDGNTAVVRGVERLQGATVMATDLRASASLVVAGLVAEGETVIERIYHLDRGYE FT RLEEKLAALGASVRRLS" FT CDS complement(871799..872206) FT /transl_table=11 FT /gene="rnk" FT /locus_tag="azo0816" FT /product="putative regulator of nucleoside diphosphate FT kinase" FT /function="Transcription elongation factor" FT /note="Regulator of nucleoside diphosphate kinase. RNK AND FT SSPA CAN FUNCTIONALLY REPLACE P.AERUGINOSA ALGINATE FT REGULATORY GENE ALGR2. 49% 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3M8" FT /db_xref="InterPro:IPR001437" FT /db_xref="InterPro:IPR023459" FT /db_xref="UniProtKB/TrEMBL:A1K3M8" FT /protein_id="CAL93433.1" FT /translation="MKPEIIVSSLDLERLEGLLAAPAARSRCDLDALRAELDRADVREP FT EEMPADVITMNSRARFREETSGREYELTLAYPKDADGAAGKVSVFSPAGSALLGLAAGQ FT AIDWRTPEGSAIRLQVLEVVWQPEAAGCLAL" FT CDS 872316..872990 FT /transl_table=11 FT /gene="hisG" FT /locus_tag="azo0817" FT /product="HisG protein" FT /function="ATP phosphoribosyltransferase" FT /EC_number="2.4.2.17" FT /note="ATP phosphoribosyltransferase," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3M9" FT /db_xref="InterPro:IPR001348" FT /db_xref="InterPro:IPR013820" FT /db_xref="InterPro:IPR018198" FT /db_xref="InterPro:IPR024893" FT /db_xref="UniProtKB/Swiss-Prot:A1K3M9" FT /protein_id="CAL93434.1" FT /translation="MTARSIKVRSVSSITLALSKGRIFEETLPLLAAAGITPTDNPESS FT RKLIIGTNRPEVRLVIVRATDTPTYVQYGAADLGIAGKDVLIEHGGAGLYQPLDLNIAR FT CRLCVAVRKGFDYAAATRPGGRIRVATKYINSAKAHFAGKGMHVDLIKLYGSMELAPLV FT GLADAIVDLVSTGSTLRANNLEEVEDIAPISSRLIVNQASLKLKRELIQPVLDAFAGAI FT KP" FT CDS 872987..874297 FT /transl_table=11 FT /gene="hisD" FT /locus_tag="azo0818" FT /product="HisD protein" FT /function="Histidinol dehydrogenase" FT /EC_number="1.1.1.23" FT /note="Histidinol dehydrogenase (HDH) catalyzes the FT terminal step in the biosynthesis of histidine in bacteria, FT fungi, and plants, the four-electron oxidation of FT L-histidinol to histidine. Similar to sprot|HISX_PSEAE FT (66%) and to sprot|HISX_ECOLI (41%). Pfam (PF00815): FT Histidinol dehydrogenase TIGRfam (TIGR00069): Histidinol FT dehydrogenase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3N0" FT /db_xref="InterPro:IPR001692" FT /db_xref="InterPro:IPR012131" FT /db_xref="InterPro:IPR016161" FT /db_xref="InterPro:IPR022695" FT /db_xref="UniProtKB/TrEMBL:A1K3N0" FT /protein_id="CAL93435.1" FT /translation="MSFATPIRRLDARQPDFLATLDALLAFESEADERIDSAVTEILRA FT VRSTGDAAVMEYTRRFDHVEAKSMVELELPKAELQAALDSLTVEQREALRIAADRVRIY FT HERQRAESWDYVEADGSRLGQKVTPLDRVGLYVPGGRASYPSSVLMNAIPAKVAGVEEL FT IMVVPTPRGEKNPLVLAAAAITGVDRVFTIGGAQAVAALAYGTQTIPQVDKIVGPGNAF FT VAEAKRRVFGTVGIDMVAGPSEVLIISDGSGHADWVAMDLFAQAEHDELAQSILLCTDA FT GFLDAVHAAIDRLLPTMPRRETIARSLANRGALIHVGSLEQACAIANRIAPEHLELSME FT DAERWIDAIRHAGAIFVGHWAVEALGDYCAGPNHVLPTMRSARFSSPLGVYDFQKRTSI FT VQISEAGAQHLGKIASVLAHGEGLQAHARSAEMRLKV" FT CDS complement(874352..875542) FT /transl_table=11 FT /gene="aspC" FT /locus_tag="azo0819" FT /product="probable aminotransferase" FT /function="Aspartate/tyrosine/aromatic aminotransferase" FT /EC_number="2.6.1.1" FT /note="Aminotransferases share certain mechanistic features FT with other pyridoxal-phosphate dependent enzymes,such as FT the covalent binding of the pyridoxal-phosphate group to a FT lysine residue. On the basis of sequence similarity, these FT various enzymes can be grouped into subfamilies; these FT sequences are defined by the aminotransferases class-I FT pyridoxal-phosphate attachment site signature, which FT contains the lysine residue involved in pyridoxal-phosphate FT binding. Similar to pir|D83057 (55%) and to trembl|Q8P544 FT (55%). Pfam (PF00155): Aminotransferases class-I FT pyridoxal-phosphate-binding site HTH reporting nucleic acid FT binding motif." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3N1" FT /db_xref="InterPro:IPR001176" FT /db_xref="InterPro:IPR004838" FT /db_xref="InterPro:IPR004839" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:A1K3N1" FT /protein_id="CAL93436.1" FT /translation="MRPVRLPRLSQRSADVQPFHVMELLRRARDLEAMGRDIIHMEVGE FT PDFPTPAPVVAAATRFLDGGDVHYTPALGLPALREAIARFYHDRFGADVAPDRIIVTAG FT ASGALMLALAATTNPGDEWLLPDPGYPSNRHLVRSFEGVAQALPVDAATRYQPTAAQVD FT AAWSARTLGLMVATPSNPTGTLLDAAELAALHRGTQARGGLLIVDEIYQGLTYGVEAST FT VLSQPALNAADDLFVVNSFSKYFGMTGWRLGWLVAPPAYVREIEKLAQHFFIAPSTPAQ FT HAALAAFAPDTTEILEARRHEFAARRDTLLPALRELGFVVATEPQGAFYIYADVSALAS FT DSEQLARRLIEEAGVAATPGLDFGHHHPRRHLRIAYTTRQDRLLEAAERIAAVLRP" FT CDS complement(875655..877499) FT /transl_table=11 FT /gene="pckG" FT /locus_tag="azo0820" FT /product="probable phosphoenolpyruvate carboxykinase" FT /function="Phosphoenolpyruvate carboxykinase (GTP)" FT /EC_number="4.1.1.32" FT /note="Probable phosphoenolpyruvate carboxykinase. Homology FT to pckG of M. smegmatis of 60% (sprot|PPCK_MYCSM). FT Phosphoenolpyruvate carboxykinase (GTP) (EC: 4.1.1.32) FT (PEPCK) [1] catalyzes the formation of phosphoenolpyruvate FT by decarboxylation of oxaloacetate while hydrolyzing GTP: FT GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.This FT is a rate limiting step in gluconeogenesis (the FT biosynthesis of glucose). InterPro: Phosphoenolpyruvate FT carboxykinase (GTP)(IPR008209) Pfam: Phosphoenolpyruvate FT carboxykinase no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3N2" FT /db_xref="InterPro:IPR008209" FT /db_xref="InterPro:IPR008210" FT /db_xref="InterPro:IPR013035" FT /db_xref="InterPro:IPR018091" FT /db_xref="UniProtKB/TrEMBL:A1K3N2" FT /protein_id="CAL93437.1" FT /translation="MNQRFSDAAIAAAPAYVRHEGLKKWVAEIAALTEPDRVVWCDGSQ FT EEYDRLCAEMVESGMLIKLNPEKRKNSYLAFSDPSDVARVEDRTFICSKDKNDAGPTNN FT WEDPETMRGTLNGLFKGAMHGRTMYVIPFSMGPLGSPIAHIGVEISDSPYVVTNMRTMT FT RMGKGAIDVLGTDGEFVPCVHTVGAPLAHGEKDSRWPCNPTTKYIVHFPETREIWSYGS FT GYGGNALLGKKCFALRIASTMARDEGWLAEHMLILGVESPEGEKTYVAAAFPSACGKTN FT FAMLIPPQSFGGWKITTVGDDIAWIKPGKDGKFYAINPEAGFFGVAPGTSEKTNFNAMA FT TLKENVIFTNVALTDDGDVWWEGMSKEAPAHLIDWQGKDWTPEIARETGRKAAHPNARF FT TAPASQCPSIDAAWESPEGVPISAFIFGGRRATTVPLVYQAFNWNFGVYMAATLGSETT FT AAAFGAQGVVRRDPFAMLPFCGYHMGDYFNHWLKMGHVVEQTPKIFCVNWFRMNEEGQF FT MWPGFGENMRVLKWIVDRVKGRVAAKETTLGWMPKFEDIDWSGSDVTREEFDALTQVDA FT DAWKSELALHKEWFDKLQDRLPKQLVLKRELFELALKV" FT CDS 877831..880107 FT /transl_table=11 FT /gene="maeB1" FT /locus_tag="azo0821" FT /product="probable malate dehydrogenase FT (oxaloacetate-decarboxylating) (NADP+)" FT /function="Malic enzyme" FT /EC_number="1.1.1.40" FT /note="Probable malate dehydrogenase FT (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40) FT (NADP-ME). Homology to dme of S. meliloti of 60% FT (sprot|MAO1_RHIME). Required for symbiotic nitrogen FT fixation. Plays a key role in the conversion of malate to FT acetyl-CoA for efficient tricarboxylic acid cycle function FT in nitrogen-fixating bacteria. Tigrfam: pta: FT phosphotransacetylase Pfam: Malic enzyme; Phosphate FT acetyl/butaryltransferase no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3N3" FT /db_xref="InterPro:IPR002505" FT /db_xref="InterPro:IPR012188" FT /db_xref="InterPro:IPR012301" FT /db_xref="InterPro:IPR012302" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K3N3" FT /protein_id="CAL93438.1" FT /translation="MDELIRAAALDYHRYPRPGKIAVAPTKVLSNQRDLSLAYSPGVAA FT ACDAIVEDPAEAANLTSRSNLIGVITNGTAVLGLGNIGALAAKPVMEGKGVLFKKFAGI FT DVFDLEIAEPDPDKLIDMIAALEPTFGGINLEDIKAPECFYIESKLRERMKIPVFHDDQ FT HGTAIVVGAAILNGLQMQGKDLKQVKLVTSGAGAAALACLGLLVKLGVPVENIWVTDLE FT GVVYEGRTALMDPIKARYAKKTEARKLAEVIEGADVFLGLSAGGVLKGEMVAKMAAKPL FT ILALANPTPEILPEEVKAVRDDAIIATGRSDYPNQVNNVLCFPFIFRGALDVGATTITD FT EMQLAAVRAIAELARAEQSDIVAAAYGEKVSGFGTEYIIPRPFDPRLIVKIAPAVAEAA FT MSSGVATRPITDWDAYRGHLNNFVWHSGLLMKPVFAAAKKAPKRIIFSEGESEKVLRAV FT QTVIDEGMARPILIGRPDVIANNITRFGLRMEAERDFELVNPESDPRFKELWTHYHALT FT ERKGVSVEYAKKEVRRRTTLIGSLLLKFGYGDGLICGTYGMHRLHLDFVETVLGRREGV FT NHCYTLNVLSLPERTLFLADTYVNYDPTPEQVVEMTRLAAEEMQRFGVEPRVALLSHSS FT FGSADSPTAEKMRTALRLLHERHSELQVEGEMHGDSALDAKLRTQIFPNARMREDANLL FT IFPTLDAANIAFNLLKSAAGEGMTVGPILLGAAKPVHILTPSATVRRIINMTALTVVEA FT GQQGA" FT CDS 880162..881298 FT /transl_table=11 FT /locus_tag="azo0822" FT /product="conserved hypothetical protein" FT /function="predicted esterase of the alpha-beta hydrolase FT superfamily" FT /note="Probable Hypothetical UPF0028 family protein FT YML059C. TREMBL:Q82SM1: 50% identity, 68% similariry FT InterPro:IPR002641; Patatin. Pfam:PF01734; Patatin bioF: FT 8-amino-7-oxononanoate synthase Signal peptide present FT (SinalP predicted) TMHMM predicted TMH's" FT /note="Function unclear" FT /db_xref="GOA:A1K3N4" FT /db_xref="InterPro:IPR002641" FT /db_xref="InterPro:IPR016035" FT /db_xref="UniProtKB/TrEMBL:A1K3N4" FT /protein_id="CAL93439.1" FT /translation="MATTGGLAGLVLTGGGARAAYQVGVLSAIREIRGPRPGNPFPVII FT GTSAGGINAAALAVYSADFNAAVRKMAHIWRHFHVEQVYRVDAAALLGSGLRWGSALFT FT GWAMRQTPRSLLDNAPLRQLLEQTLDFSAIERAVAAGYIHAVSVTASGYTSGESLSFFQ FT AAAGVTPWRRAQRLGVRAAIGVEHLLASSAIPFVFPAVKINREYFGDGSMRQLAPISPA FT IHLGADRILVVGSGRLAEEGRQRAESYPSPAQIAGHAMSSIFLDGLAVDLERMQRINAT FT LGAFTAEQRAAAGLALRPIETLVIAPSKRLDAIAGHHRESLPPLLRAILRGIGAMRREG FT STLLSYLLFEPGYTRALMDLGYADTMARRAEVEQFLRI" FT CDS 881699..882541 FT /transl_table=11 FT /gene="pbpG" FT /locus_tag="azo0823" FT /product="D-alanyl-D-alanine carboxypeptidase" FT /function="Involved in murein bisynthesis" FT /note="Penicillin-binding protein 5 precursor (PBP-5) FT (D-alanyl-D-alanine- endopeptidase) (DD-endopeptidase)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3N5" FT /db_xref="InterPro:IPR001967" FT /db_xref="InterPro:IPR012338" FT /db_xref="InterPro:IPR018044" FT /db_xref="UniProtKB/TrEMBL:A1K3N5" FT /protein_id="CAL93440.1" FT /translation="MSLRQNAVIDDDAGELTLDARGNPQLRSAAFYVANQATGEVLLEK FT NSSTVLPIASITKLMTAMVVLDAGLGLNDELAISDADIDTLKGTGSRLVLGTRLTREEM FT LRLALMSSENRAASALARHYPGGERAFVEAMNVKARLLGAWDTRYYDSTGLNPANVSSP FT RDLAKVVSAAATYPLIREFSTTSERFVDIGGRTLRFANTNSLVRSPDWEIAVSKTGYIS FT EAGRCLVMQAWMHHQPVVIVLMDSNGRYTRTADAQRVRKWIDTHAVPHVATAAARRDS" FT CDS complement(882604..883407) FT /transl_table=11 FT /gene="allR" FT /locus_tag="azo0824" FT /product="probable negative regulator of allantoin and FT glyoxylate utilization operons" FT /function="Transcriptional regulator" FT /note="Probable negative regulator of allantoin and FT glyoxylate utilization operons," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3N6" FT /db_xref="InterPro:IPR005471" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014757" FT /db_xref="UniProtKB/TrEMBL:A1K3N6" FT /protein_id="CAL93441.1" FT /translation="MVVKKPEPTPAAEAKNPIQVIERMMKLLDVLAHHADPVPLKQLAL FT ETGLHPSTAHRILGAMTQSGFVERSDAGVYRLGIRLLELGSLVKSRISLRETAMPAMLK FT LHATTGESVNLGIRAGDEIVYVERTSSGRSSVRVVHIVGARAPLHTTATGKLFLVEDGL FT ERVRDYARRTGLPASTSASITTLPLLEKELDKVRRHAVAFDLDEVEAGVRCIAAGIRDD FT SGELIAGLSLSTPSERFNPDWAPLVRDTADEISQALGWRQRRTAT" FT CDS 883506..883727 FT /transl_table=11 FT /locus_tag="azo0825" FT /product="hypothetical protein" FT /note="Hypothetical protein. No homology to the data bank. FT No domains predicted. No signal peptide. No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K3N7" FT /protein_id="CAL93442.1" FT /translation="MQRGFEDDRMKGRGPCKRDGAAQRRKSGGGNAKVTVTPGRAWSGA FT AMPMVIEARAKVAVPALAGRRWPEREAA" FT CDS 883724..884674 FT /transl_table=11 FT /locus_tag="azo0826" FT /product="glycerate dehydrogenase" FT /function="Lactate dehydrogenase and related FT dehydrogenases" FT /EC_number="1.1.1.29" FT /note="Glycerate dehydrogenase (EC 1.1.1.29) FT (NADH-dependent hydroxypyruvate reductase) (HPR) (GDH) FT (Hydroxypyruvate dehydrogenase) (Glyoxylate reductase) FT (HPR-A). PLAYS A CENTRAL ROLE IN ASSIMILATION OF CARBON. IT FT CONVERTS HYDROXYPYRUVATE TO GLYCERATE AS A KEY STEP IN THE FT SERINE CYCLE AND MAY ALSO PLAY AN IMPORTANT ROLE IN C2 FT REACTIONS BY INTERCONVERTING GLYOXYLATE AND GLYCOLATE." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3N8" FT /db_xref="InterPro:IPR006139" FT /db_xref="InterPro:IPR006140" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K3N8" FT /protein_id="CAL93443.1" FT /translation="MTLSIVCLERDAVGAAFGRPRAPHRWTEFPSSAQEQVVERLRDAE FT VAIINKLRLGASEIAALPRLQMVAVAATGSDNVDLEACRARGIVVSNVRGYAVHTVPEH FT ALMLMLALRRRLFDYVADVRAGRWARSDNFCFFDHPIGDLHGATLAIIGRGGLGDGVAR FT LGAAFGMRVIYAEHKGVAGVREGYTAFERVLAEADVLSLHCPLTPATRGLIGASELASM FT KREAVLVNTARGGVVDEPALAAALRAGVIAGAATDVLSSEPPREGNPLLAADIPNLIVT FT PHVAWASRQAMQTLADQVIDNIDAFAAGAPRNRLA" FT CDS 884876..886135 FT /transl_table=11 FT /locus_tag="azo0827" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT ORF428 of Roseateles depolymerans of 64% (tremble:BAB1967) FT Has PF07399:(IPR009978)Protein of unknown function FT (DUF1504); This family consists of several hypothetical FT bacterial proteins of around 440 residues in length. The FT function of this family is unknown." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR009978" FT /db_xref="UniProtKB/TrEMBL:A1K3N9" FT /protein_id="CAL93444.1" FT /translation="MNPSTFQLVGTALFAVAVAHTFLTKYFEHLAHLQPNHAGFWHLLG FT EVEVVFGFWAFVLLAFMAVAGGGAAAPAQYLEGLNYTEPAFVFVIMVVAASRPILELCK FT VGARLLARYIPLTDSLAFYFVCLSVLPLLGSFITEPAAMTLAALMLRDNFYSKNISHRL FT KYVTLGALFVNVSIGGTLTHFAAPPVLMVAAKWNWDMWYMLGHFGWKSALAVLTNAALA FT TLLFARELKALEVNAAGSERTVPWSLILLHVAFLVGIVYFAHHPIVFVGLFLLFLGVAE FT AYKHYHDRLMLREGLMVGFFLAGLVTLGAQQQWWLQDALTGMDSTALYFGATALTAITD FT NAALTYLGSLVEGTDTAFKHSLVAGAVTGGGLTVIANAPNPAGFAILRGYFDDEAINPL FT GLFVTALPPTIVAVLAFQVL" FT CDS 886288..887790 FT /transl_table=11 FT /locus_tag="azo0828" FT /product="pseudouridylate synthase" FT /function="16S rRNA uridine-516 pseudouridylate synthase FT and related pseudouridylate synthases" FT /EC_number="4.2.1.70" FT /note="Putative RNA pseudouridylate synthase. Homology with FT hits in the database only for the first half of protein. FT Has PF00849, RNA pseudouridylate synthase; IPR006145, FT PseudoU_synth; Members of this family are involved in FT modifying bases in RNA molecules. They carry out the FT conversion of uracil bases to pseudouridine. This family FT includes RluD P33643, a pseudouridylate synthase that FT converts specific uracils to pseudouridine in 23S rRNA. FT RluA from E. coli converts bases in both rRNA and tRNA. Has FT SMART;SM00363, S4 RNA-binding domain;IPR002942;The S4 FT domain is a small domain consisting of 60-65 amino acid FT residues that was detected in the bacterial ribosomal FT protein S4, eukaryotic ribosomal S9, two families of FT pseudouridine synthases, a novel family of predicted RNA FT methylases, a yeast protein containing a pseudouridine FT synthetase and a deaminase domain, bacterial tyrosyl-tRNA FT synthetases, and a number of uncharacterized, small FT proteins that may be involved in translation regulation. FT The S4 domain probably mediates binding to RNA." FT /note="Family membership" FT /db_xref="GOA:A1K3P0" FT /db_xref="InterPro:IPR000748" FT /db_xref="InterPro:IPR002942" FT /db_xref="InterPro:IPR006145" FT /db_xref="InterPro:IPR020103" FT /db_xref="UniProtKB/TrEMBL:A1K3P0" FT /protein_id="CAL93445.1" FT /translation="MSTIRKNPPQPAPSRIAGTLKLRKPAADDNGESAAGADPAQSVAA FT GSDKRARPSSAGEEGRAPRSGARGGQASRGERPRQDAEPRRQPRARPAQEGEAPRRSRR FT DPGDGGTERHPRRDAGASEERPRRREAADERQARPGYGRRDDGPARAGARPAREQGRER FT GEASGRRHGGEGGERASAPRAAYDERRRAGGDERAPRRAAGDAARTSPRPAGPRPAAAA FT PRPASAERAPRRREEAPARAPAAPRAPAVQSGDGEAPSGVRLSKVMADRGICSRREADE FT LIERGWVFVDGRRVSELGTRIDPDARVVLAPEAKKAQAQRVTILLHKPVGYVSGQPEPG FT YEPAVTLIGGDNQFDRDVAQRFHPSQLKGLAPAGRLDIDSTGLLVLTQDGRIARQLIGD FT DSKVEKEYLVRVEGELVDDGLALLNHGLSLDDKPLRPAKVEWINEDQLRFVLKEGRKRQ FT IRRMCELVGLRVVGLKRVRIGRVKLGDLPLGEWRYLRDDEVF" FT CDS complement(887858..888337) FT /transl_table=11 FT /gene="nuoB1" FT /locus_tag="azo0829" FT /product="conserved hypothetical NADH-quinone FT oxidoreductase chain B" FT /function="NADH:ubiquinone oxidoreductase 20 kD subunit and FT related Fe-S oxidoreductases" FT /EC_number="1.6.5.3" FT /note="Conderved hypothetical NADH-quinone oxidoreductase FT chain B. Homology to nuoB of C. violaceum of 77% FT (trembl|Q7NUE5). NDH-1 shuttles electrons from NADH via FMN FT and iron- sulfur (Fe-S) centers to quinones in the FT respiratory chain. Couples the redox reaction to proton FT translocation (for every two electrons transferred four FT hydrogen ions are translocated across the cytoplasmic FT membrane) and thus conserves the redox energy in a proton FT gradient (By similarity). Pfam: NADH ubiquinone FT oxidoreductase, 20 kd no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3P1" FT /db_xref="InterPro:IPR006137" FT /db_xref="InterPro:IPR006138" FT /db_xref="InterPro:IPR014406" FT /db_xref="UniProtKB/Swiss-Prot:A1K3P1" FT /protein_id="CAL93446.1" FT /translation="MQTPTLHGDGFLLTRLDTLCDMVRSNSMWYLTFGLACCAVEMMQA FT AASRYDMDRFGMIPRASPRQADLIIVAGTLTNKMAPAIRKIYDQMAEPRYVISMGSCAN FT GGGYYHYSYSVARGCDRILPVDIYIPGCPPTAEALLYGLIQLQNKLKRPPAVIAR" FT CDS complement(888370..889254) FT /transl_table=11 FT /locus_tag="azo0830" FT /product="putative AraC-family transcriptional regulator" FT /function="AraC-type DNA-binding domain-containing FT proteins" FT /note="Putative AraC-family transcriptional regulator," FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3P2" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR018060" FT /db_xref="UniProtKB/TrEMBL:A1K3P2" FT /protein_id="CAL93447.1" FT /translation="MSVSLVIPPHPALAPWVHHILVMGLDVCTSQLPSALSPCLTVFAR FT GGSRLEHADGSLQPVPRASLTGPYLHARRSRVAPGTVFLALMFRPGCMDEALGPAVAEV FT RERIVPLEDIAPAGAVGELLERIDASADPHAWATATQAVLLRMLRPTRDPARCAALLGE FT RANLFQPARLIADRLGIGERQLERRIARAYGANLRELRRIARFGFTLAAMTARPPARGE FT LTRIALDFGYYDQAHMDRDFRALAGLAPGALLRAIAGDDPGYWLYRFRHRQFRDLFLPD FT DVDSVQARLFAPA" FT CDS complement(889332..889562) FT /transl_table=11 FT /locus_tag="azo0831" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT Daro03000467 of Dechloromonas aromatica of 50% FT (gi|41725519|ref|ZP_00152277.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K3P3" FT /protein_id="CAL93448.1" FT /translation="MTFIDSPIARCEAVREMVLLDETQAECAREHDCPPGRICPLDGCF FT TAVSGIAEEHLAAVAKAHPHSAAGATQGGSA" FT CDS complement(890060..891259) FT /transl_table=11 FT /locus_tag="azo0832" FT /product="ABC transporter permease protein" FT /function="ABC-type antimicrobial peptide transport system FT permease component" FT /note="ATP-binding cassette (ABC) transporters form a large FT family of proteins responsible for translocation of a FT variety of compounds across biological membranes. They are FT composed of two transmembrane domains responsible for FT binding and transport and two nucleotide-binding domains FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the TMDs, TREMBL:Q8DJ46 (29% FT identity); TREMBL:Q8YZK5 (29% identity). InterPro FT (IPR003838): Protein of unknown function DUF214. Pfam FT (DUF214): Predicted permease. TMHMM reporting four FT transmembrane helices. TC (3.A.1.122.): The Macrolide FT Exporter (MacB) Family." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3P4" FT /db_xref="InterPro:IPR003838" FT /db_xref="UniProtKB/TrEMBL:A1K3P4" FT /protein_id="CAL93449.1" FT /translation="MLWRDFLQLALRSLTAHRLRSFLTLLGIGVGIAAVILLTSIGEGL FT HRFVLQEFTQFGTNIIKVTPGKTGARGGPPGLPSTTRELTLDDAAALARAPYVTGITPT FT VSGNSEVRANGRVRRTFIMGAGAQMQQVFSMRVKSGRFLPPDDAAHARAFVVLGATLKR FT ELFGNANALGERLQIGGERYRVIGVMESKGQFLGIDLDDAAYIPAARALALYNRDGLME FT INVTYNEGVSAARAAAEVRKVMRARHGREDFTLTTQEDMLATLSNILGILTAAVGALGG FT ISLLVGGVGIVTIMTIAVAERTAEIGLLVALGARRTTILGLFLGEAVALAAIGGAVGLA FT VGAGLAQLVGLAVPALPVSTPWRFVAIAEALAVLIGLTAGVLPARRAARLDPVEALRAQ FT " FT CDS complement(891269..892477) FT /transl_table=11 FT /locus_tag="azo0833" FT /product="ABC transporter permease protein" FT /function="ABC-type antimicrobial peptide transport system FT permease component" FT /note="ATP-binding cassette (ABC) transporters form a large FT family of proteins responsible for translocation of a FT variety of compounds across biological membranes. They are FT composed of two transmembrane domains responsible for FT binding and transport and two nucleotide-binding domains FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the TMDs, TREMBL:Q8YZK5 (28% FT identity); TREMBL:Q8DJ46 (29% identity). Pfam (DUF214): FT Predicted permease. TMHMM reporting five transmembrane FT helices. TC (3.A.1.122.): The Macrolide Exporter (MacB) FT Family." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3P5" FT /db_xref="InterPro:IPR003838" FT /db_xref="UniProtKB/TrEMBL:A1K3P5" FT /protein_id="CAL93450.1" FT /translation="MSPRDTLRFAAGAAFGYPLRTALMVLAMAIGVAAVVVLTALGDGA FT RRYVVGEFASLGANLIIVLPGRNETGGVNAGSFVTSTPRDLTVADASALLRAPLAARMA FT PLSVGNSEIAVGGKLREVMVLGTSADYLDIRHYSLSQGRFLPREDLNRAGAVAVIGDKL FT REELFGNEPAVGRMVRVGDTRLRIIGVMARGAQGLGLNTDELVIVPVATALAMFNTNTL FT FRIMVEARSREALGPAQKQMEDILRARHDGELDVTLITQDAVLGTFDRILGALTMAVAG FT IAAISLAVAGILVMNVMLVAVTQRTGEIGLLKALGASARTIRLAFLTEAALLSLAGALV FT GYGLGQLGAWAIRLTWPVLPAWPPDWAVVAGLGTALGTGLLFGVLPARRAARLDPVQAL FT AKR" FT CDS complement(892474..893181) FT /transl_table=11 FT /locus_tag="azo0834" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type antimicrobial peptide transport system FT ATPase component" FT /note="Putative efflux transporter for macrolide FT antibiotics (MacB-family). Acts in conjunction with MacA. FT Similar to TREMBL:Q82W68 (59% identity); TREMBL:Q8RAL4 (46% FT identity); SWISSPROT:P75831 (41% identity). InterPro FT (IPR003593): AAA ATPase. InterPro (IPR003439): ABC FT transporter. InterPro (IPR001687): ATP/GTP-binding site FT motif A (P-loop). Pfam (PF00005): ABC transporter. TC FT (3.A.1.122): The Macrolide Exporter (MacB) Family." FT /note="Family membership" FT /db_xref="GOA:A1K3P6" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K3P6" FT /protein_id="CAL93451.1" FT /translation="MAQIELSGIERVFTLGDSQVHALRDVSLEIEAGEYVAVMGPSGSG FT KSTLLNLLGLLDRPDAGHYRLEGRDVTTLSADEQAQVRRNRIGFVFQSFHLVPRLTAAE FT NIALPLMLAGLAPAERQARVGRALKDFGLETRADHRPDELSGGQRQRVAIARATIMQPA FT MLLADEPTGNLDRHTGQEVTELLEALNAAGTTLIVVTHDPAMGNRARRRLMMEDGMLRQ FT DLRDGTPAPTGTP" FT CDS complement(893195..894343) FT /transl_table=11 FT /locus_tag="azo0835" FT /product="membrane fusion protein" FT /function="Membrane-fusion protein" FT /note="The secretion of a number of proteins/molecules FT require the help of members belonging to the ABC FT transporter family and a membrane fusion protein belonging FT to the HlyD family," FT /note="Family membership" FT /db_xref="GOA:A1K3P7" FT /db_xref="InterPro:IPR006143" FT /db_xref="UniProtKB/TrEMBL:A1K3P7" FT /protein_id="CAL93452.1" FT /translation="MALSRRLIPVVIVIALLGAAGWWFTRPKPIVVVVHEVARGRVEAS FT VANTRAGEVEACQRTKLATITGGRIDYLGVKEGDRVQAGQVLMRLWQGDLRSRAAVAEA FT QLATARQRSTEACTVAANARSEAERQAALVKRGFVSASVEEKARTEAAARAAGCASAQA FT DVKTAERQLEAAGIDLNRVVIVAPFAGTVAKITGELGEISTPSPPGVPTPPAIDLIDDS FT CLYVKAPMDEVDAPKIHPGQPARISFEALPGKTFAGRVKRVAPYITAVEKQARTVEVDI FT DFANPEEARGLLVGYSVDVEIVLETRDDVLRVPSAAIREGNRVLVLGADGLIAERSIRP FT GLANWEQTEVLEGLAAGDRVVTSLERAGVVPGAHATAEAGAN" FT CDS complement(894555..896288) FT /transl_table=11 FT /gene="glnS" FT /locus_tag="azo0836" FT /product="glutaminyl-tRNA synthetase" FT /function="Glutamyl- and glutaminyl-tRNA synthetases" FT /EC_number="6.1.1.18" FT /note="Glutaminyl-tRNA synthetase (EC 6.1.1.18) FT (Glutamine--tRNA ligase) (GlnRS). glnS: glutaminyl-tRNA FT synthetase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3P8" FT /db_xref="InterPro:IPR000924" FT /db_xref="InterPro:IPR004514" FT /db_xref="InterPro:IPR011035" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR020056" FT /db_xref="InterPro:IPR020058" FT /db_xref="InterPro:IPR020059" FT /db_xref="InterPro:IPR020061" FT /db_xref="InterPro:IPR022861" FT /db_xref="UniProtKB/TrEMBL:A1K3P8" FT /protein_id="CAL93453.1" FT /translation="MNPNDNKDGAPAAPSNFIRNQIDEDNRSGKWSGRVETRFPPEPNG FT YLHYGHAKSICLNFGLAESYGGACHLRFDDTNPEKEEQEYVDSIIEAVQWLGFDWREHL FT YFASDYFDIMYACAESLIKAGKAYVDSLSAEEMRALRGTLTEPGKDSPFRTRSIDENLD FT LFRRMRAGEFAEGTHVLRARIDMASPNINLRDPAIYRIRRATHHRTGDNWCIYPMYTFA FT HPIEDAIENITHSICTLEFEDQRPFYDWLLDALASAGHFPRPLPQQIEFARLNLTYVVL FT SKRKLIQLVDEGHVDGWDDPRLPTLVGARRRGFTAEGFRLFAERIGVTKSDSWIDMSTL FT EECMREHLNEAAERRVAVLDPLKLVITNYAEGASEQCHAPNHPLKPELGKRDMPFGREL FT WIEREDFMEEPVKGFHRLYPGNTVRLRYGYVVKCTGCEKDADGNVTAVLAEYMADSKSG FT TPGADNYKVKGNLHWVSAAHGYAAEIRLYDRLFAHPHPGQRREGDPEGYERSFLEDINP FT DSKRVIRAWLEPALRAAKPEERFQFERHGYFVADRRDSVDGAPVFNRTVTLKDSWAKGG FT K" FT CDS 896453..896836 FT /transl_table=11 FT /locus_tag="azo0837" FT /product="conserved hypothetical CrcB family protein" FT /function="Integral membrane protein possibly involved in FT chromosome condensation" FT /note="Conserved hypothetical crcB family protein. Homology FT to ebA4067 of Azoarcus sp. EbN1 of 65% FT (gnl|keqq|eba:ebA4067(KEGG)). InterPro: CRCB protein. CRCB FT is a putative integral membrane protein possibly involved FT in chromosome condensation. Over expression in E. Coli also FT leads to camphor resistance. signal peptide. 2 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3P9" FT /db_xref="InterPro:IPR003691" FT /db_xref="UniProtKB/TrEMBL:A1K3P9" FT /protein_id="CAL93454.1" FT /translation="MQASAFLAVGGGAACGAWLRWGLGVWLNPLFAAMPLGTLAANLLG FT GFLMGLALAAIQAWPTLSPALKLMLTTGLLGGLTTFSTYSAESFHFLQRGAWGGFALHL FT LAHVAGSVMMTWAGYTVFNAVRG" FT CDS 896956..897630 FT /transl_table=11 FT /locus_tag="azo0838" FT /product="conserved hypothetical outer membrane protein" FT /function="Outer membrane protein and related FT peptidoglycan-associated (lipo)proteins" FT /note="Conserved hypothetical puter membrane protein FT Homology to cv1891 of c. violaceum of 64% (trembl|Q7NWT8) FT InterPro: Bacterial outer membrane protein (IPR006664) FT Pfam: OmpA family signal peptide 2 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3Q0" FT /db_xref="InterPro:IPR001035" FT /db_xref="InterPro:IPR006664" FT /db_xref="InterPro:IPR006665" FT /db_xref="InterPro:IPR008816" FT /db_xref="UniProtKB/TrEMBL:A1K3Q0" FT /protein_id="CAL93455.1" FT /translation="MKRIVISLSCLSLVAAGLGGCAGMSDTQRHTGTGAAIGAAAGAVL FT GAATSGKGNRGEATAIGAAAGAAIGAGGGYLWSQRMQAQKAEMERATAGTGVSVSQTAD FT NRLKLDIPSDVSFDTGRYDIKPEMRPVLDRFANTLNQHTVTTVSIIGHTDSTGSDAVNN FT PLSVNRAAATRDYLVARGVAGSRIAIDGRGAREPIADNGTVAGRAQNRRVEIFVAEPAA FT AR" FT CDS complement(897685..900981) FT /transl_table=11 FT /locus_tag="azo0839" FT /product="SWI/SNF family helicase" FT /function="Superfamily II DNA/RNA helicases SNF2 family" FT /note="SWI/SNF family helicase Pfam: Helicase conserved FT C-terminal domain" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3Q1" FT /db_xref="InterPro:IPR000330" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR007527" FT /db_xref="InterPro:IPR014001" FT /db_xref="UniProtKB/TrEMBL:A1K3Q1" FT /protein_id="CAL93456.1" FT /translation="MKSPDSYTEADVIAWLGQHEVDKGRAYLAAVTQLERKGDILHARV FT RGSRTTPYQVSAQVRSDPWRGTFLLSHCSCPLGDSCKHVAATLLSWLARRDGPERPRDQ FT VLAWIDAFRSAAGQAPTAAGEPRRAAPSVHALRYLIHDQADVQDYVVSCHKVRLDRQGQ FT IRSAEGWSNFERAFEAPPAFVDEVDLDILGLLWAQRPRTRYLPYALPLAGRNAAALMER FT LVASGRAHLDTLESPPLQVGEPRPGVPEWRTTREGLRAPGLRLTPPADRVLPLSPPWYV FT ERATGVAGPVTLELPAEQVVRLLALPPLTPTEAELVADTLHDVAPQLPAPLATGEPPLR FT LDGAPLPVLRIATLPVIGVDYRDYPGYSVNRFDYATLAFRYGPLTVEAADTALFHVLDD FT GRSARLTRDRAAEAAAARRLTQNGFGKVPAHAVHTGHGATPPHMLGLASEADWVHFTAE FT DIPALRREGWVVDMPEDFRHHALDIDELLLDVDEQGGWLDISPGIEVEGRRVSLAPLLA FT ELFAQDPRWLSGGLERIADSEPIILHHDILGRLRLPAGRLKPLVRALVDLFDNATGEHM FT RVSPLDAGRLAALQLPGRGADTLAAYARRLRDATGIEAVPQPKGFKAELRPYQLEGLAW FT LQHLVRNNLAGILADDMGLGKTAQTLAHLLALKHAGKLDRPALVVLPTSLVFNWQAEAE FT RFAPELRVLKLHGADRHGLFEQLEPGKRKPRVDVAITTYPLLWRDEEELQAREWSILIL FT DEAQTVKNVASKGAQVIRQLKARHRLGLTGTPLENHLGELWAQFDFLLPGFLGDAKHFT FT KTWRTPIEKHGDTVRRDLLAARLRPFILRRRKEDVATELPPKTIIVRSVALEGGQRDLY FT ETVRAAMDSKIRDEIAAKGYARSQIVILDALLKLRQVCCDPRLLKTTAAAAKVKERAKL FT DLLMSMLPELIDEGRRILVFSQFTQMLALIAAELDKAKIGWVALTGDTRDRRIPVEDFQ FT KGRAPVFLISLKAGGVGLNLTTADTVIHYDPWWNPAAENQATDRAHRIGQDKPVFVFKL FT ICAGSIEERILSLQDKKAALAASVLSEDANALAKFGEADIAALLAPLPPG" FT CDS complement(901163..903079) FT /transl_table=11 FT /gene="thiC" FT /locus_tag="azo0840" FT /product="thiamine biosynthesis protein" FT /function="Thiamine biosynthesis protein ThiC" FT /note="Thiamine biosynthesis protein thiC. Required for the FT synthesis of the hydromethylpyrimidine (HMP) moiety of FT thiamine (4-amino-2-methyl-5- hydroxymethylpyrimidine) (By FT similarity). TIGRFAM: thiC: thiamine biosynthesis protein FT ThiC" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Q2" FT /db_xref="InterPro:IPR002817" FT /db_xref="UniProtKB/Swiss-Prot:A1K3Q2" FT /protein_id="CAL93457.1" FT /translation="MNAKEHFIATEAKVDEAAIAPLPNSRKIYVEGSRPDIRVPMREIR FT QSDTPASFGAEPNPPIFVYDCSGPYTDPAAKIDIRSGLPALRAGWIAERGDTEQLADLS FT SEYGRQRAADPRLDELRFPGLHRKPLRARAGANVTQMHYARRGIVTPEMEYIAIRENLR FT RKDYLESLLAAGPTGQKMAALLTRQHPGQNFGAAIPNEITPEFVRDEVARGRAIIPANI FT NHPETEPMIIGRNFLVKINANIGNSALGSSIAEEVDKMTWSIRWGGDTVMDLSTGKNIH FT ETREWIIRNSPVPIGTVPIYQALEKVDGKAEDLTWEIFRDTLIEQAEQGVDYFTIHAGV FT LLRYIPLTANRMTGIVSRGGSIMAKWCLAHHKESFLYTHFEDICEIMKAYDVAFSLGDG FT LRPGSIYDANDEAQLGELKTLGELTDIAWKHDVQVMIEGPGHVPLHMIKENMDLQLEQC FT KEAPFYTLGPLTTDIAPGYDHITSGIGAATIGWYGTAMLCYVTPKEHLGLPNKQDVKEG FT IITYKLAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDKAKEFHDETLPK FT ESAKVAHFCSMCGPHFCSMKITQDVRDFAAQQGVDEAEALQKGMEVKAVEFVKSGAEVY FT RNV" FT CDS complement(903169..904023) FT /transl_table=11 FT /gene="thiD1" FT /locus_tag="azo0841" FT /product="phosphomethylpyrimidine kinase" FT /function="Hydroxymethylpyrimidine/phosphomethylpyrimidine FT kinase" FT /EC_number="2.7.4.7" FT /note="Phosphomethylpyrimidine kinase (EC 2.7.4.7) FT (HMP-phosphate kinase) (HMP-P kinase). CATALYZES THE FT PHOSPHORYLATION OF HMP-P TO HMP-PP. TIGRFAM: HMP-P_kinase: FT phosphomethylpyrimidine kinase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Q3" FT /db_xref="InterPro:IPR004399" FT /db_xref="InterPro:IPR013749" FT /db_xref="UniProtKB/TrEMBL:A1K3Q3" FT /protein_id="CAL93458.1" FT /translation="MSSSSTHPSSIPNVLSIAGVDPSGGAGIFADIKTFSALGAYGCGV FT IAALTAQNTQAVTGVHVPPTDFLRLQLDTLFADVAVHATKIGMLGSAEVTATVADRLAH FT WQAANVVLDPVMVAKSGDTLLAKNAIAMMREALFPQSFMITPNLPEAGVLLEQRAPESV FT KEMYRAAERLRELLPLSSERWVMLKGGHLPGSEVVDLLFDGDRMIELPAPRIDTRNTHG FT TGCTLSSAIAALLPQTAGGFRGVEAAVRQARQWLLGAIAHSGDLGVGSGHGPVHHFHAL FT WRR" FT CDS 904277..905893 FT /transl_table=11 FT /gene="ecaA" FT /locus_tag="azo0842" FT /product="putative carbonic anhydrase precursor" FT /function="Carbonic anhydrase" FT /EC_number="4.2.1.1" FT /note="Carbonic anhydrase precursor (EC 4.2.1.1) (Carbonate FT dehydratase).Involved in the reversible hydration of carbon FT dioxide. 40% Euk_COanhd.IPR000437; FT Prok_lipoprot_S.IPR006311;Tat. InterPro: belongs to the FT eukaryotic-type carbonic anhydrase family. Pfam:PF00194; FT carb_anhydrase; 1. TIGRFAMs:TIGR01409; TAT_signal_seq; 1. FT Signal peptide present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Q4" FT /db_xref="InterPro:IPR001148" FT /db_xref="InterPro:IPR023561" FT /db_xref="UniProtKB/TrEMBL:A1K3Q4" FT /protein_id="CAL93459.1" FT /translation="MKLRHLAALLILPLSPGWVPHAHADEWQLVLSDRERRVEIDRASI FT FDSDRGTKVSWGRVVLAPEEARKAGYGTVRALNRYDCMNRSFFTIKRVYLDTAGRVVRE FT EAVTDTSPVMVTRNSVDERMWREVCRPPTVSDLQKVAAAAGRSAAETRPAPTPAAKPAA FT AELKPAPSARTETKGAAPTPPVPPKTEPAATPAAGPAPAVVARAGAAETRDPPRSEGLR FT PADFQAPQAAAAAAARPATPAATPVSTAAAAPATPTTPATPVLPGTPGAPPVAAAPAAP FT AVPTPVQSAARVPAPRVAPAPVEAAPRPAAALEQRWSYDGETGPEHWARLRPDWRVCGD FT GKRQSPIDLREGVGVDLEPVRFDYRSTRFRIADTGTTLQVNVGEGMGMEVRGRRYELTH FT FTLHRPSEERVGGRAADMTVHFHHRDAEGRLAMVSVMLERGAEANPLLQALWNNLPLEK FT GTAYMPASSIDLGALLPASPGHFLYMGSLTTPPCTEGVLWVVMKTPVTISDEQLGIFAR FT LYPRNARPIQPANGRLILESR" FT CDS complement(905906..907309) FT /transl_table=11 FT /locus_tag="azo0843" FT /product="conserved hypothetical transcriptional regulator" FT /function="Transcriptional regulators containing a FT DNA-binding HTH domain and an aminotransferase domain (MocR FT family) and their eukaryotic orthologs" FT /note="Conserved hypothetical transcriptional regulator. FT Homology to rsc0989 of r. solanacearum of 47% (CAD14691). FT Pfam: Bacterial regulatory proteins, gntR family; FT Aminotransferase class I and II no signal peptide no TMHs FT bioF: 8-amino-7-oxononanoate synthase" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3Q5" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR004839" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:A1K3Q5" FT /protein_id="CAL93460.1" FT /translation="MLMVSLDSTHPTPLVEQIVGAVRSQIDDRILRPGMRLPPIRKFAE FT TQRVSRFTVVEAYDRLVALGYLRSRRGSGFFVAPRHEGGDGRPQAETDRAVDVAWLMRQ FT VLDDRPGLIKASAGWLPDDWLDQDGLRRHLRTLSRRADARLTGYGTPQGYLPLRQQLQV FT RLAEFGIGAAPGQIVLTEGATSALDIVARHLIKPGDTVLVDDPGYYNFFGNLRLQGAKL FT VGVPRLADGPDVEALEALLEHHQPRVFFTHSVLHNPTGSDLSPAVAFRILQLAEKHDFL FT IIEDDTYADFHPHNSARLATLDQLERVIFVGSFSKTLSGSLRVGFLAARPDLVAEMTDV FT KLLTTLCSSEFSEQLVYQMLTDGHYRKYLERMQSRLAQATETTLRLLERCGLETFVEPR FT GGVFVWARVPELDDSAALASRAALQNIMLAPGKAFRPQMQASPWLRFNVAFSAEKVLER FT FLGDTLAAL" FT CDS 907471..907926 FT /transl_table=11 FT /locus_tag="azo0844" FT /product="hypothetical secreted protein." FT /note="Hypothetical secreted protein. No homology to the FT data base. No domain predicted. No TMHs. Signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K3Q6" FT /protein_id="CAL93461.1" FT /translation="MRENGERHPPPEARRRTGVVVLALAVLMLAACQRPSAPVELEWRE FT RQQVFRLLAEPPRLEAYGLRGGVIPLGSVRLPAGACPRALALDAEAGRVQVWYADGGVE FT IDARALRIVGTLAGDGVASAGNRREGAAVLARMEPEGCIPGTTWAHR" FT CDS 908009..908686 FT /transl_table=11 FT /locus_tag="azo0845" FT /product="conserved hypothetical transcriptional regulator" FT /function="Transcriptional regulator" FT /note="Conserved hypothetical transcriptional regulator. FT Homology to RSc0698 of alstonia solanacearum of 48% FT (gnl|keqq|rso:RS01603(KEGG)). InterPro: IPR001647 HTH_TetR. FT Pfam: PF00440 Bacterial regulatory proteins,tetR family. FT HTH reporting nucleic acid binding motif. No signal FT peptide. No TMHs." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3Q7" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011075" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:A1K3Q7" FT /protein_id="CAL93462.1" FT /translation="MKVKDGQVGSGGAQRPRVRRKEARPQELLAAALALFVEKGYAATR FT LEEVAARAGVSKGTLYLYFDSKEALFKAVIREGVVPAIDAGEAMLGTFADDPVALLRAF FT LHAWWERIGSTELGGLPKLMMSEAGNFPDVAAYYNEAVIQRGLGLLRTAVRRGIDAGVF FT RAVDLDLVGTLLIAPLVHLSMWRHSFATCCATDIEPRAYVDAHIDLVLHGLRNDPVPAG FT VAR" FT CDS 908683..909771 FT /transl_table=11 FT /locus_tag="azo0846" FT /product="membrane fusion protein" FT /function="Membrane-fusion protein" FT /note="Similar to TREMBL:Q7NR61 (35% identity); FT TREMBL:Q8XYV3 (33% identity); TREMBL:Q88MQ4 (32% identity). FT InterPro (IPR006143): Secretion protein HlyD. SignalP FT predicting signal peptide. TC (2.A.6.1): The Heavy Metal FT Efflux (HME) Family." FT /note="Family membership" FT /db_xref="GOA:A1K3Q8" FT /db_xref="InterPro:IPR006143" FT /db_xref="UniProtKB/TrEMBL:A1K3Q8" FT /protein_id="CAL93463.1" FT /translation="MNPRSVLAPLAALLLVACSEAPPPPAAPRVVLVQRLAEPGAVESA FT ELYTGEIRARYESPLAFRIGGKLVERKVEVGSEVRRGQVLARLDPRDAELGAAAAAAQV FT AAARADAALAVAEYERAVGLRAQNFISGSALDARRSAREAAEAKLRQAEAQAAAARNQS FT GYTALVADSDGVVTALEAEVGQVLAEGQAVMTLARPGNRELLVHVPEGRMRELVPGREA FT EVRLWSAPLQTYRGRVREVAPMADAATRTYALRIALPDAGLPLGATASATFHTDAADSR FT VLPAAAVTRAGEGAVVWVVDNEERVRPVAVEVLAYDERGATLRGGPPAGTRVVIAGVHK FT LVEGEAVRAVESGAPVALDAQR" FT CDS 909768..912986 FT /transl_table=11 FT /locus_tag="azo0847" FT /product="RND efflux transporter, permease protein" FT /function="Cation/multidrug efflux pump" FT /note="AcrB/AcrD/AcrF family. Members of this family are FT integral membrane proteins. Some are involved in drug FT resistance. AcrB cooperates with a membrane fusion protein, FT AcrA, and an outer membrane channel TolC. The structure FT shows the AcrB forms a homotrimer, TREMBL:Q9A7D5 (35% FT identity); TREMBL:Q9HXW4 (55% identity). Pfam (PF00873): FT AcrB/AcrD/AcrF family. TIGRFAM (TIGR00914): Heavy metal FT efflux pump, CzcA family. TIGRFAM (TIGR00915): FT Hydrophobe/Amphiphile Efflux-1 (HAE1) Family protein. TMHMM FT predicting 12 transmembrane helices. TC (2.A.6.2): The FT (Largely Gram-negative Bacterial) Hydrophobe/Amphiphile FT Efflux-1 (HAE1) Family." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3Q9" FT /db_xref="InterPro:IPR001036" FT /db_xref="UniProtKB/TrEMBL:A1K3Q9" FT /protein_id="CAL93464.1" FT /translation="MSRRRGFNISAWGLAHPALVLYCLIALSLIGILAYSRLGQSEDPP FT FTFKIMVVRTEWPGASAREVEQQVTDKIEKKLQEIAQLDFVRSFSKPGESMVLVLAKDS FT TPAREVEGIWYQVRKKVGDIRDYLPAGVKGPYFNDEFGDTYGNIFALVGDGISHAELKR FT HAEAVRGELLRVPDVGKVSFFGEQAQRVYIELSNTKLATFGLGLADIAAALSAQNAKAG FT SGFFETADERIWLRPSGQFDDLQAIADTLIRAQGRVFRLGDVAEIRRGYVDPPSERMRF FT NGADAFGIGVAMRAGGDIVALGRHLDEAAARIEAQLPVGIRFERVADQPRAVRNSVGEF FT VQVLTEAVIIVMTVSLLSLGFRTGVVVLIIIPVVLAITFLFMHLFGIGLHKISLGALII FT ALGLLVDDAIIAVEMMATKMEQGWERAKAASFAYTSTAMPMLSGTLVTAAGFLPIATAA FT SSTGEYTRSIFQVTVTALLVSWVAAVLFVPYLGYHLLPDFRARNGRPSRLAGWIGRVSP FT GLAARLQARASHGHAQHDEYAIYHTPFYTRLRTLVGWCVAHRWLVIALTLASFVLSLVV FT FVRFVPQQFFPDSTRPELLVDLRLAEGASHEATERAVHRLEGWLQQQEGVENFVAWLGA FT GSPRFYLPLDQQLAQTNFAQLVVLTKGIAEREAVRSRLIRLFEDEAWPLRATINRLENG FT PPVGFPVQYRVSGQDIDTLRTIAHRVAEAMRTDRNLSNVHLDWEEPAKSIRLKVDQDKA FT RLLGVSSRDLASLLATSLQGTTVSEFREGTETIQMVLRGAGAERAHLGLLSDLAVPVSG FT GRSVPLAQLATLEYGFEEGVIWRRNRIPTVTVRASLYGGTQPAVVVQQLGPQIEAIRAA FT LPLGYRVEVGGAVEESSKGGGSVAAGVPLFIGVVLTVLMLQLQSFSRTLLVVLTAPLGM FT IGVTVFLLAFNKPFGFVAMLGTIALSGMIMRNSVILVDQIRQDVDAGRTPWDAVVEATV FT RRFRPIVLTAAAAILAMIPLSRSAFFGPMAVAIMGGLTVATVLTMLFLPALYAAWYRIR FT RTPAPLPPAPPSGANMEAVQGARM" FT CDS 913062..913715 FT /transl_table=11 FT /gene="pcm1" FT /locus_tag="azo0848" FT /product="putative protein-L-isoaspartate FT O-methyltransferase" FT /function="Protein-L-isoaspartate FT carboxylmethyltransferase" FT /EC_number="2.1.1.77" FT /note="Putative protein-L-isoaspartate O-methyltransferase FT (EC 2.1.1.77) Catalyzes the methyl esterification of FT L-isoaspartyl residues in peptides and proteins that result FT from spontaneous decomposition of normal L-aspartyl and FT L-asparaginyl residues. It plays a role in the repair FT and/or degradation of damaged proteins (By similarity). FT InterPro: Protein-L-isoaspartate(D-aspartate) FT O-methyltransferase (IPR000682), SAM binding motif FT (IPR000051) Tigrfam: pimt: protein-L-isoaspartate FT O-methyltransfase Pfam: Protein-L-isoaspartate FT (D-aspartate) O-methyltransferase no signal peptide no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3R0" FT /db_xref="InterPro:IPR000682" FT /db_xref="UniProtKB/TrEMBL:A1K3R0" FT /protein_id="CAL93465.1" FT /translation="MNFEKARFNMVEQQIRPWDVLDPAVLDLLMTVKREEYVPAAARAL FT AFADVEIPLGQGQVMLKPVIEGKILQSLQLHRSDSVLEVGAGSGYFAALLAARVEWVRT FT VDIEPELVRFAHANLARNGVENVIVEEGDAAQGWASRAPYDVIVVSGGLPVVPQALLEQ FT LKVGGRLFAFVGEAPVMKARLITCEAEGRFLTEDIFETLVPMLKNAPRQDSFRF" FT CDS 913724..914047 FT /transl_table=11 FT /locus_tag="azo0849" FT /product="conserved hypothetical sulfurtransferase protein" FT /function="Rhodanese-related sulfurtransferase" FT /EC_number="2.8.1.1" FT /note="Putative rhodanese-related sulfurtransferase. FT TIGR:NMB1884. InterPro:IPR001763; Rhodanese-like. InterPro: FT Rhodanese/cdc25 fold. Pfam:PF00581; Rhodanese; 1." FT /note="Function unclear" FT /db_xref="GOA:A1K3R1" FT /db_xref="InterPro:IPR001763" FT /db_xref="UniProtKB/TrEMBL:A1K3R1" FT /protein_id="CAL93466.1" FT /translation="MHEITPAQLAEWLADPAKIKPLLLDVREPWEYELCHIDGSVPMPM FT GTVAGRIGELDPEQVMVVVCHHGGRSAQVGMFLKRQGFKRVINLAGGVAEWAAKVDPSM FT PHY" FT CDS 914066..915382 FT /transl_table=11 FT /gene="tolC" FT /locus_tag="azo0850" FT /product="putative outer membrane efflux protein" FT /function="Outer membrane protein" FT /note="Putative outer membrane effluxe protein protein. FT Homology to tolC from E. coli of 33%. The OEP family (outer FT membreane effluxe protein) allow export of a variety of FT substrates in Gram negative bacteria. TolC is believed to FT be a membre af an ABC transporter system for protein FT secretion without cleavage of a signal sequence. Pfam: FT Outer membrane efflux protein Signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3R2" FT /db_xref="InterPro:IPR003423" FT /db_xref="InterPro:IPR010130" FT /db_xref="UniProtKB/TrEMBL:A1K3R2" FT /protein_id="CAL93467.1" FT /translation="MKRSLAAKLFAAGLAAAFGAPAAAADLLQTYRDALANDARYAAAR FT AERDAGMERVVQARAGLLPNLTASASTAYNDGEARTSAVSVDRRYNSNGYAVQLTQPLF FT RWQNWVQYKQGELQTALAETQFGQARQDLILRVAEAYFNVLNAQDALDAVVQLRTAAAE FT QLELARRSFEVGTVTITDVHEAQSRYDLASAQEIAARNDLDVQRQTLAQIIGREPDPLA FT PLRAGVELQRPQPDSIADWVGAAEQGSFGVQGQQLNREIAAREVERARAGHLPTLDLVA FT SRGLNQRPSITTERSEASSIGLQLNVPLYQGGAVSSRERETAALKLKADADLEDARRGA FT ALAARQSYLGVTSGLAQIRALEAARISSASALEANRLGYEVGVRINIDVLNAQTQLADT FT QQRLARARYDTLLAQLRLKAAAGTLGDEDVQAINALLAP" FT CDS complement(915379..916623) FT /transl_table=11 FT /gene="waaA" FT /locus_tag="azo0851" FT /product="3-deoxy-D-manno-octulosonic-acid transferase" FT /function="Involved in biosynthesis of the FT lipopolysaccharides (LPS) core component" FT /EC_number="2.-.-.-" FT /note="3-deoxy-D-manno-octulosonic-acid transferase (EC FT 2.-.-.-) (KDO transferase). TRANSFERS THREE 3-DEOXY-D-MONO FT OCTULONIC ACID (KDO) INDIVIDUALLY FROM CMP-KDO TO A FT TETRAACYLDISACCHARIDE 14- BISPHOSPHATE PRECURSOR OF LIPID A FT (LIPID IVA). InterPro: Glycosyl transferases group 1 FT 2A0115: benzoate transport" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3R3" FT /db_xref="InterPro:IPR001296" FT /db_xref="InterPro:IPR007507" FT /db_xref="UniProtKB/TrEMBL:A1K3R3" FT /protein_id="CAL93468.1" FT /translation="MLWALALPLVVARLAWRARKQPAYLHHLGERFGRYAAPPAAPLIW FT VHAVSVGETRAAEPLVRALLARWPQHDVLLTHMTPTGRATAQQLFDAEPRVRSVYLPYD FT LAWLAARFLRHFRPRFGVIMETELWPNLLATAARSGVPVVLANARLSARSAGRYARFPL FT LSRMTLGALAATGAQTAADAERLQALGATGVSVTGNIKFDMEAPAAALALGAAFRARCG FT ERPVVMAASTREGEEAALLDAFARMASPEALLLLVPRHPQRFDEVAALASERGLALQRR FT SDGQVVARTTRVWLGDSMGEMFAYYAAADVALIGGSWLPFGGQNPIEACAVGTPVVLGP FT HTFNFEWVADAAVTAGAALREPDAAAGMARALELLADRPRRTALAEAGRGFAAAHRGAT FT ARTLDLLQQADAARP" FT CDS 916809..917816 FT /transl_table=11 FT /gene="wbnF" FT /locus_tag="azo0852" FT /product="putative nucleotide sugar epimerase" FT /function="Nucleoside-diphosphate-sugar epimerases" FT /EC_number="5.1.3.-" FT /note="Probably involved in the biosynthesis of FT exopolysaccharides. 68% Epimerase_Dh.IPR008089; FT Nuc_sugar_epim. Pfam:PF01370; Epimerase; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3R4" FT /db_xref="InterPro:IPR001509" FT /db_xref="InterPro:IPR008089" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K3R4" FT /protein_id="CAL93469.1" FT /translation="MKILVTGAAGFIGMHTSERLLARGDEVVGLDNLNDYYDPRLKEDR FT LARLTPNDGFRFVRMDVADRAGMEALFAAEKFDRVIHLAAQAGVRYSLQNPHAYIDSNL FT VGFTNILEGCRHSKVQHLVYASSSSVYGGNTRMPFSEHDSVDHPVSLYAATKKANELMA FT HTYSHLYGLPTTGLRFFTVYGPWGRPDMALFLFTKAILEGRAIDVFNHGRMKRDFTYID FT DIVEGVLRTLDRVAEPDPAFDSDHPDPGRGKAPYRVFNIGNNNPVELMAFIEAIEGALG FT RTAEKNFLPLQDGDVPATYANTDELNAWTGFAPATSVSDGVGRFVAWYRAYYGL" FT CDS 917838..918635 FT /transl_table=11 FT /gene="apaH" FT /locus_tag="azo0853" FT /product="bis(5'-nucleosyl)-tetraphosphatase (symmetrical)" FT /function="Diadenosine tetraphosphatase and related FT serine/threonine protein phosphatases" FT /EC_number="3.6.1.41" FT /note="Bis(5-nucleosyl)-tetraphosphatase symmetrical (EC FT 3.6.1.41) (Diadenosine tetraphosphatase) (Ap4A hydrolase) FT (Diadenosine 55- P1P4-tetraphosphate pyrophosphohydrolase). FT Hydrolyzes diadenosine 55-P1P4-tetraphosphate to yield ADP FT (By similarity). Similar to TREMBL: trembl|Q7NQS0 FT InterPro:(IPR004617) ApaH.(IPR004843) M-ppestrase. Pfam FT (PF00149): Metallophos. TIGRFAM (TIGR00668): apaH. apaH: FT bis(5-nucleosyl)-tetraphosphata" FT /note="Family membership" FT /db_xref="GOA:A1K3R5" FT /db_xref="InterPro:IPR004617" FT /db_xref="InterPro:IPR004843" FT /db_xref="UniProtKB/TrEMBL:A1K3R5" FT /protein_id="CAL93470.1" FT /translation="MATYAIGDIQGCYEPLRRLLDLIRFDPAHDRLWVVGDLVNRGPES FT LMVLRYLHELGSAATVVLGNHDLYLLMVAAGVERRDKDDTLYQVLEAPDRDVLLDWLAR FT QPLLHVEGDHAMVHAGLLPVWTITRAQELAAEVSAALTGPDARHFLLHLAGNRPDRWAD FT NLKGWDRLRVIVNAMTRMRFCTPHGHLALRAKGPPDEAPAGTLPWFRAPDRFHRTHTIV FT CGHWSALGYYRGDGIIALDSGCVWGGKLTAFRLEDGEVFQVQG" FT CDS complement(918645..919436) FT /transl_table=11 FT /gene="plsC" FT /locus_tag="azo0854" FT /product="putative 1-acyl-sn-glycerol-3-phosphate FT acyltransferase" FT /function="1-acyl-sn-glycerol-3-phosphate acyltransferase" FT /EC_number="2.3.1.51" FT /note="Function:-Converts lysophosphatidic acid (LPA) into FT phosphatidic acid by incorporating acyl moiety at the 2 FT position (By similarity). CATALYTIC ACTIVITY: Acyl-CoA + FT 1-acyl-sn-glycerol 3-phosphate = CoA + FT 1,2-diacyl-sn-glycerol 3-phosphate. Entry name:- PLSC_NEIGO FT Primary accession number :- Q59601 InterPro IPR002123; FT Acyltransferase. IPR004552; AGP_acyltrn. Pfam PF01553; FT Acyltransferase; 1. Identities = 68/182 (37%) Prediction: FT Non-secretory protein Signal peptide probability: 0.096 FT Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K3R6" FT /db_xref="InterPro:IPR002123" FT /db_xref="UniProtKB/TrEMBL:A1K3R6" FT /protein_id="CAL93471.1" FT /translation="MRLALHILQGVLTIALLYPFCAPARQRNLRQRWSRRLLRTVGVEV FT RIEGAAVAPGALLVANHISWLDIYAINSLTPSAFVSKAEVRDWPVIGWLAARSETVFLR FT RGSRGHARIINGEIAALLDAGRNVAIFPEGTTSDGNRVLPFHAALLQAAVESAHPVQPV FT AVSYHDADGRRTTAAAYDGELSLGACLGNIVSHRRLQVRIRVGAAIDTAGADRKTVCRD FT ARAAIVALCGLTEAGTEMERKTGAAAMPATPAAAQEAVQVR" FT CDS complement(919508..920266) FT /transl_table=11 FT /locus_tag="azo0855" FT /product="conserved hypothetical protein" FT /function="Putative hemolysin" FT /note="Conserved hypothetical protein. Homology to cv0660 FT of C. violaceum of 59% (trembl|Q7P0A7) no domains predicted FT no singal peptide no TMHs" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:A1K3R7" FT /protein_id="CAL93472.1" FT /translation="MLQKSQLPATRPGRNLHVGLASCETEILEAQKLRYRVFAEEMGAR FT LATRTPGVDRDIYDPFCEHLIVRDEDAGRIVGTYRILSPAAARKVGGYYSENEFDITRL FT QHLRSRIVEIGRSCIDADYRSGAVIALLWAGLARYMQENGYDYLIGCASVSMADGGHAA FT ASLYNRLKETHLAPLEYHVFPRCPLPLELLRSDLPAEAPPLIKGYLRAGAWVCGEPAWD FT PDFNTADLPILMPMSKVDGKYAKHFLGRKD" FT CDS 920383..921654 FT /transl_table=11 FT /locus_tag="azo0856" FT /product="glycosyltransferase" FT /function="Involved in biosynthesis of an unidentified FT carbohydrate" FT /note="Similar to amylovoran biosynthesis glycosyl FT transferase amsK (EC 2.-.-.-). INVOLVED IN THE BIOSYNTHESIS FT OF AMYLOVORAN WHICH FUNCTIONS AS A VIRULENCE FACTOR. FT Similar to protein annotated as sulfolipid FT sulfoquinovosyldiacylglycerol biosynthesis proteins." FT /note="Family membership" FT /db_xref="GOA:A1K3R8" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:A1K3R8" FT /protein_id="CAL93473.1" FT /translation="MSRGGHVAVARRADDAAMDAPLSLQDLARASRQLRIALVTETFPP FT EINGVAMTTGRMVDGLLRLGHRVQLVRPRQGADDQPARGEGYEEVLARGLPIPRYNHLK FT MGLPARSTLTRMWSLRRPDVVQVVTEGPLGWSAVAAARKLRLPVITEFHTNFHSYSRYY FT GMGWLKQPVEAYLRRFHNKGDLCLAPTAELAAQLAARGVRKVDVVARGVDTALFAPARR FT SEALRSSWGARPETLVLTVVGRLAAEKNLGLALRAFDALRQRRADVRLVLVGDGPARAA FT LATASPETIFAGMRTGADLAAHYASADLFLFPSTTETFGNVTTEALASGLPVIGFDYAA FT AAERIRGGDNGCLAPLGDEQGFVEAVLRVGTDDALRLALAARARDSVADADWAAVAQRL FT AAVIERVVDRHEARLIGAAHVAAA" FT CDS 921718..922653 FT /transl_table=11 FT /locus_tag="azo0857" FT /product="putative carbohydrate kinase" FT /function="Sugar kinases ribokinase family" FT /EC_number="2.7.1.-" FT /note="38% PfkB.Family of carbohydrate kinases FT Pfam:PF00294; PfkB; 1." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3R9" FT /db_xref="InterPro:IPR002173" FT /db_xref="InterPro:IPR011611" FT /db_xref="UniProtKB/TrEMBL:A1K3R9" FT /protein_id="CAL93474.1" FT /translation="MSILVCGSMAYDSIMVFQDRFSNHILPEQIHILNVSFFVPELRRE FT FGGCAGNIAYNLKLLGSEPLIMATVGDDAGPYRERLQALGLRQDYVRGVPGTFTAQAFI FT TTDLDDNQITAFHPGAMMQSHLNDAGQAEGVRLAIVSPDGRDGMLRHAEGLAAAGVPFI FT FDPGQALPILSGDELLRCLQLATYCTVNDYEARLMSEKTGRSIEQLANEVDGLVVTLGA FT EGSRVHADGAAVIIPAVEADAVVDPTGCGDAYRAGLLHGLSQGWDWVRTGRLAAVMGAI FT KIAHRGGQNHAPTRADIAARYLAAFGEALW" FT CDS 922647..923120 FT /transl_table=11 FT /gene="slyB" FT /locus_tag="azo0858" FT /product="putative outer membrane protein SlyB" FT /function="Outer membrane lipoprotein" FT /note="Outer membrane lipoprotein SlyB. Homology to slyB of FT E. coli of 32% (sprot|SLYB_ECOLI) no domains predicted FT signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3S0" FT /db_xref="InterPro:IPR008816" FT /db_xref="UniProtKB/TrEMBL:A1K3S0" FT /protein_id="CAL93475.1" FT /translation="MVSVNPVGRRALALILVASLGLGGCAAGLGGGTYSRTEARRAMVV FT QFGVIESVRGVQLEGTKSPVGTVSGAAVGGIAGSSVGGNRGSAIGAVLGAVAGGLAGSA FT IEEGVTRKPGVEVTVQLENGQYLAVVQQDEGEQFMPGERVRILRDGGTTRVTR" FT CDS complement(923122..923514) FT /transl_table=11 FT /gene="dgkA" FT /locus_tag="azo0859" FT /product="probable diacylglycerol kinase" FT /function="Diacylglycerol kinase" FT /EC_number="2.7.1.107" FT /note="Probable Diacylglycerol kinase. Homology to dgkA of FT E. coli of 40% (sprot|KDGL_ECOLI) RECYCLING OF FT DIACYLGLYCEROL PRODUCED DURING THE TURNOVER OF MEMBRANE FT PHOSPHOLIPID (BY SIMILARITY). Pfam: prokaryotic FT diacylglycerol kinase no signal peptide 2 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3S1" FT /db_xref="InterPro:IPR000829" FT /db_xref="UniProtKB/TrEMBL:A1K3S1" FT /protein_id="CAL93476.1" FT /translation="MDPTNSKHAESPFKGKTGLPRIWNAFRYSLAGLRAALRHEDAFRQ FT ECLLAAVLIPLAIVAPTDGAGKALLVGSTLLVLIVELLNSAIEATVDRVSLDHHQLAKR FT AKDIGSAAVLVALLNLAMVWGLVLFG" FT CDS complement(923623..924912) FT /transl_table=11 FT /locus_tag="azo0860" FT /product="Hypothetical protein" FT /note="Hypothetical protein. No Domains,Features,Signal FT Pepetide or TMH reported Present. Most top hits suggest the FT possibillity of Transmembrane protein, but due to non FT existance of any TMH's domains it cant be considered as a FT choice." FT /note="Specificity unclear" FT /db_xref="InterPro:IPR011723" FT /db_xref="InterPro:IPR021834" FT /db_xref="UniProtKB/TrEMBL:A1K3S2" FT /protein_id="CAL93477.1" FT /translation="MLTRCPACQTIFRLRPEQLRARHGEVRCGHCFNPFNALDHLLEGQ FT QAQESAASEPGYAEPPSPPLTPPLTPPTQPAPLQPPPSAAPPATTSAFSDLEFDLPDGF FT DTAETPLQADADEKPFTVEPPAAPHVREPMFAPDADHAPQPAPTPEHHDDVHGGAPRVD FT FSAMVAAAGSRLAGNPIPDPVFPLEGNRRDAPEPSGPAAHRIEPLVEDMPSPEPVVAFE FT HEPRDEPAARDNAEPAAWIAPASDLPSSEDASGLDSDHLDAHYGPPPAAGPGSRLIPVT FT VLLLALVLFAQSAYLFRGQISRALPGLRPLYVSACAQLGCDMPLPRDAMLINIESPDLQ FT SEPGRPGRYILHATIQNRADYPQAWPHLELTLTDPADVPLVRRVLAPEEWYGSSTLPES FT FKARSDATVRLNFEAPDIAPTGYRVYVFYP" FT CDS complement(924919..925803) FT /transl_table=11 FT /gene="prmA" FT /locus_tag="azo0861" FT /product="ribosomal protein L11 methyltransferase" FT /function="Ribosomal protein L11 methylase" FT /EC_number="2.1.1.-" FT /note="Ribosomal protein L11 methyltransferase (EC 2.1.1.-) FT (L11 Mtase). Methylates ribosomal protein L11" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3S3" FT /db_xref="InterPro:IPR004498" FT /db_xref="InterPro:IPR010456" FT /db_xref="UniProtKB/TrEMBL:A1K3S3" FT /protein_id="CAL93478.1" FT /translation="MWISVILQAEAAKAEALSDALMDAGALSVSIEDADAGTEAEKPQF FT GEPGHLPTSLWDHSRVIALFDAATELAPALAQAAGAAGFDAVPPFTTEEVAEQNWVQLT FT QSQFDPIRITDRLWIVPSWHEAPDANAINIELDPGMAFGTGSHPTTRLCLEWLCDTVQP FT GTSVLDYGCGSGILGIAAARLGAGDVLGIDIDDKAIEAARDNASRNGVTLRLQHSAVPV FT GDTFAVVVANILTNPLCVLAPAIAARVAAGGRIALSGVLETQSQQVIDAWAPYLSLRVG FT AVLEGWVRLEGQR" FT CDS complement(925814..927175) FT /transl_table=11 FT /gene="accC1" FT /locus_tag="azo0862" FT /product="probable biotin carboxylase (a subunit of FT acetyl-coa carboxylase)" FT /function="Biotin carboxylase" FT /EC_number="6.3.4.14" FT /note="Function:-THIS PROTEIN IS A COMPONENT OF THE ACETYL FT COENZYME A CARBOXYLASE COMPLEX; FIRST BIOTIN CARBOXYLASE FT CATALYZES THE CARBOXYLATION OF THE CARRIER PROTEIN AND THEN FT THE TRANSCARBOXYLASE TRANSFERS THE CARBOXYL GROUP TO FORM FT MALONYL-COA (BY SIMILARITY). Identities = 312/444 (70%) FT InterPro IPR004549; AccC. IPR005482; Biotin_carb_C. FT IPR005479; CPase_L_D2. IPR005481; CPase_L_N. Pfam PF02785; FT Biotin_carb_C; 1. PF00289; CPSase_L_chain; 1. PF02786; FT CPSase_L_D2; 1. Prediction: Non-secretory protein Signal FT peptide probability: 0.000 Number of predicted TMHs: 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3S4" FT /db_xref="InterPro:IPR004549" FT /db_xref="InterPro:IPR005479" FT /db_xref="InterPro:IPR005481" FT /db_xref="InterPro:IPR005482" FT /db_xref="InterPro:IPR011054" FT /db_xref="InterPro:IPR011761" FT /db_xref="InterPro:IPR011764" FT /db_xref="InterPro:IPR013815" FT /db_xref="InterPro:IPR013816" FT /db_xref="InterPro:IPR013817" FT /db_xref="InterPro:IPR016185" FT /db_xref="UniProtKB/TrEMBL:A1K3S4" FT /protein_id="CAL93479.1" FT /translation="MFEKILIANRGEIALRVLRACRELGIKTVAVHSEADTEAKYVTLA FT DESVCIGPAPSGLSYLNVPAIISAAEVTDAEAIHPGYGFLSENADFAERVEQSGFVFIG FT PRPDTIRLMGDKVSAKDAMKAAGVPCVPGSDGALPEEPKEIVKIARAIGYPVIIKAAGG FT GGGRGMRVVHTEAALLNAVTTTRAEAGAAFGNPTVYMEKFLENPRHVEIQVLADQHGNA FT VYLGERDCSMQRRHQKVIEEAPAPGIDRKLIAKIGERCAEACRKIGYRGAGTFEFLYEN FT GEFYFIEMNTRVQVEHPVTEMITGIDIVQTQIRVAAGEKLPFQQRDIPFRGHAIECRIN FT AEDPFKFTPSPGRIDNWHTPGGPGIRVDSHVYNGYMVPPHYDSMIGKLIAYGDTREQAI FT RRMRIALSEMAVAGIKTNIPLHQELMMDARFVEGGTSIHYLEHKLAERSEVKKG" FT CDS complement(927168..927296) FT /transl_table=11 FT /locus_tag="azo0863" FT /product="hypothetical protein predicted by FT Glimmer/Critica" FT /note="Hypothetical protein predicted by Glimmer/Critica. FT no homology to the data bank. no domains predicted. no FT signal peptide. no TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K3S5" FT /protein_id="CAL93480.1" FT /translation="MSGNTLIASRGAPLPAGDAAAHPHRPATARGTGNFAAETTHV" FT CDS complement(927305..927757) FT /transl_table=11 FT /gene="accB" FT /locus_tag="azo0864" FT /product="probable biotin carboxyl carrier protein of FT acetyl-CoA carboxylase" FT /function="Biotin carboxyl carrier protein" FT /EC_number="6.4.1.2" FT /note="Function:-Biotin carboxyl carrier protein of FT acetyl-CoA carboxylase (BCCP). THIS PROTEIN IS A COMPONENT FT OF THE ACETYL COENZYME A CARBOXYLASE COMPLEX; FIRST BIOTIN FT CARBOXYLASE CATALYZES THE CARBOXYLATION OF THE CARRIER FT PROTEIN AND THEN THE TRANSCARBOXYLASE TRANSFERS THE FT CARBOXYL GROUP TO FORM MALONYL-COA. Entry FT name:-SWISSPROT:BCCP_ECOLI Prim. accession # P02905 FT InterPro :-IPR001249; AcCoA_biotinCC. IPR001882; Biotin_BS. FT IPR000089; Biotin_lipoyl. Pfam:- PF00364; Biotin_lipoyl; 1. FT Number of predicted TMHs: 0 Identity:- 94/157 (59%)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3S6" FT /db_xref="InterPro:IPR000089" FT /db_xref="InterPro:IPR001249" FT /db_xref="InterPro:IPR001882" FT /db_xref="InterPro:IPR011053" FT /db_xref="UniProtKB/TrEMBL:A1K3S6" FT /protein_id="CAL93481.1" FT /translation="MDLRKLKKLIDLVQESGISELEVTEGEEKVRIAKHLSAPVQATYY FT APPQAAAPQAAVAAPAVEAPAAADALPAGHIVKSPMVGTFYRSSAPGAKPFAELGQSVS FT EGDALCIIEAMKLMNEIEADASGTIKAVLVENGQPVEYGQPLFVIG" FT CDS complement(927813..928310) FT /transl_table=11 FT /gene="aroQ" FT /locus_tag="azo0865" FT /product="probable 3-dehydroquinate dehydratase" FT /function="3-dehydroquinate dehydratase II" FT /EC_number="4.2.1.10" FT /note="Probable 3-dehydroquinate dehydratase 1 (EC FT 4.2.1.10). Homology to aroQ of A. pleuropneumoniae of 58% FT (sprot|AROQ_ACTPL) Catalyzes a trans-dehydration via an FT enolate intermediate (By similarity). Pfam: Dihydroquinase FT II no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3S7" FT /db_xref="InterPro:IPR001874" FT /db_xref="InterPro:IPR018509" FT /db_xref="UniProtKB/TrEMBL:A1K3S7" FT /protein_id="CAL93482.1" FT /translation="MTRSKRSQKTETPPPPQGRILALHGPNLNLLGTREPDIYGRTTLA FT DVHAAMEARARADGVVVESFQSNHEGQLIDRVQAAAAEGVDFIIINPAGYTHTSVALRD FT ALAAVSIPYVEVHLSNIHAREPFRHHSYFSDRAAGVICGLGAYGYLAATEFVLGRLRER FT HL" FT CDS complement(928372..928908) FT /transl_table=11 FT /locus_tag="azo0866" FT /product="conserved hypothetical thioredoxin" FT /function="Thiol-disulfide isomerase and thioredoxins" FT /note="Hypothetical thioredoxin. Homology with BPP3919 of FT B. parapertussis of 38%. Participates in various redox FT reactions through the reversible oxidation of the active FT center dithiol to a disulfide. Tigrfam: dsbE: periplasmic FT protein thiol:disulfi signal peptide probable 1 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3S8" FT /db_xref="InterPro:IPR000866" FT /db_xref="InterPro:IPR005746" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR017937" FT /db_xref="UniProtKB/TrEMBL:A1K3S8" FT /protein_id="CAL93483.1" FT /translation="MSMRSHARTLVIALVAVLAAVAGYFASRPATPPTTRHSAAALYAL FT QLPDAAGQPQSLAAWKDKVLVVNFWATWCPPCRKEIPDFSAASRTFADQPVQFVGISID FT TPDKVQAFADEFEVPYPLLIAGPAQLELTAAFGNTSQALPFTLLIDRDGNVRASKLGTL FT NRAELEGKIRTLLAP" FT CDS complement(928905..929594) FT /transl_table=11 FT /locus_tag="azo0867" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein, 39% identity to FT TrEMBL;Q8XVP7; Signal Peptide present. Coils2 program FT reporting presence of coiled coil. No TMH present. FT TIGR00004: endoribonuclease L-PSP putat" FT /db_xref="UniProtKB/TrEMBL:A1K3S9" FT /protein_id="CAL93484.1" FT /translation="MAGILTDGAAASAATGPSRASDWFPGFPTMPSRTFPPRSGTLRRE FT IAALAARMMAEDGISDFGFAKRKAARQLGATDSEALPNNTEIEAELRAWQALYQDEEQA FT ERLLEMRRAAVEVMHLLEDFRPYLTGGALDGTAGRYSELEIELYPESAKEVEIFFLNRD FT FAYEHREPRRPAPGAPEAVLSFDWDDVPVRLSIFPAGAERNARRQDRARLAQVEAMLAA FT PRSPAAE" FT CDS 929650..930996 FT /transl_table=11 FT /gene="mpl" FT /locus_tag="azo0868" FT /product="UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate FT ligase" FT /function="involved in murein biosynthesis" FT /EC_number="6.3.2.-" FT /note="UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso- FT diaminopimelate ligase (EC 6.3.2.-) (Murein peptide FT ligase). REUTILIZES THE INTACT TRIPEPTIDE L-ALANYL-GAMMA-D- FT GLUTAMYL-MESO-DIAMINOPIMELATE BY LINKING IT TO FT UDP-N-ACETYLMURAMIC ACID. InterPro: Cytoplasmic FT peptidoglycan synthetases N-terminal ispD: FT 4-diphosphocytidyl-2C-methyl-D-er" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3T0" FT /db_xref="InterPro:IPR000713" FT /db_xref="InterPro:IPR004101" FT /db_xref="InterPro:IPR005757" FT /db_xref="InterPro:IPR013221" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K3T0" FT /protein_id="CAL93485.1" FT /translation="MHIHILGICGTFMGGVALLARAAGHTVTGCDSNVYPPMSTQLEEQ FT GIALSEGYDPAQLDLAPDVFVIGNAISRGNPLLEAILDRGLPYVSGPQWLAEHVLAGRW FT VLAVAGTHGKTTTTSLLAWMLEDAGLSPGFLVGGVPKNFGVSARLTDSPFFVIEADEYD FT TAFCDKRSKFVHYRPRTAILNNLEFDHADIFADLAAIETQFHHLVRTLPRQGRIVANAR FT EDALKRVLARGCWSELEWFNDAAQWSAAAGARDAEAVFRLGDEELGRVEMPLAGSHNRE FT NALAAIAAARHVGVPPQQAIASLARFEGIKRRLELRGRARGVAVYDDFAHHPTAIALTV FT EGLRRREPEGRILAVLEPRSNTMKLGVMKAQLPGSLAQADAVFCYAGGLGWDAAAALAP FT LGERAQVHEDLGALVQAVAATARPGDHVLVMSNGGFGGVHQKLLDALAR" FT CDS complement(931018..931668) FT /transl_table=11 FT /locus_tag="azo0869" FT /product="conserved hypothetical secreted protein" FT /function="predicted periplasmic or secreted lipoprotein" FT /note="Conserved hypothetical secreted protein. Homology to FT rsc3264 of R. solanacearum (trembl|Q8XUC7). Smart: FT Bacterial OsmY and nodulation domain (BON) The BON domain FT is typically ~60 residues long and has an alpha/beta FT predicted fold. There is a conserved glycine residue and FT several hydrophobic regions. This pattern of conservation FT is more suggestive of a binding or structural function FT rather than a catalytic function. Most proteobacteria seem FT to possess one or two BON-containing proteins, typically of FT the OsmY-type proteins; outside of this group the FT distribution is more disparate. signal peptide TMH in FT signal peptide" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007055" FT /db_xref="InterPro:IPR014004" FT /db_xref="UniProtKB/TrEMBL:A1K3T1" FT /protein_id="CAL93486.1" FT /translation="MKTTSRARAASGARRYLLAGLIAAALPALQGCFPVVATGVGAGAA FT MIADRRTSGAYVEDEGIEWKIANRLRERFGDAIHVNVTSYNRNVLLTGEVPTDTIRSEI FT ERSAAAADHVRGIVNETVVAGNSSLSARANDSLITSNVKARFVDSQRVSAHHVKVVTEA FT NVVFLMGLVTREEADAATEVARTSQGVKRVVRVFEYINQAEADRLDFKNRRSN" FT CDS complement(931665..932258) FT /transl_table=11 FT /gene="gmhA" FT /locus_tag="azo0870" FT /product="putative phosphoheptose isomerase" FT /function="Phosphoheptose isomerase" FT /EC_number="5.3.-.-" FT /note="Phosphoheptose isomerase is involved in FT lipopolysaccharide biosynthesis, and more specifically in FT the synthesis of glyceromannoheptose 7-phosphate. It may FT also have a role in virulence in Haemophilus ducreyi. 54% FT GmhA.IPR001347; SIS. Pfam:PF01380; SIS; 1. FT TIGRFAMs:TIGR00441; gmhA; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3T2" FT /db_xref="InterPro:IPR001347" FT /db_xref="InterPro:IPR020620" FT /db_xref="UniProtKB/Swiss-Prot:A1K3T2" FT /protein_id="CAL93487.1" FT /translation="MDLIDRISRQFEDSAQTKLAAVEWMAAPIAQAVEMMTASLMNNGK FT ILACGNGGSAADAQHFAAELLNRFEMERPPLAAVALTTDTSTLTSIANDYDFVQVFSKQ FT VRALGQPGDVLLAISTSGNSPNVIDAIQAAHEREMHVVALTGKGGGRIGEMLSPTDVHL FT CVPADRTARIQEVHLLTLHCLCDGIDCLLLGVEE" FT CDS complement(932374..932787) FT /transl_table=11 FT /locus_tag="azo0871" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to pa4424 FT of P. aeruginosa of 44% (pir|H83091). Pfam: Uncharacterised FT protein family UPF0102 (PF02021). Interpro: Protein of FT unkown function UPF0102 (IPR003509). no signal peptide. no FT TMHs." FT /db_xref="GOA:A1K3T3" FT /db_xref="InterPro:IPR003509" FT /db_xref="InterPro:IPR011335" FT /db_xref="InterPro:IPR011856" FT /db_xref="UniProtKB/Swiss-Prot:A1K3T3" FT /protein_id="CAL93488.1" FT /translation="MKTDRKAERSGIVGAAASPMQARGREGEERAAAHLAAQGVRILAR FT NRHCRGGELDLVGLHGDMLVFVEVRMRANPRFGGAAASITAEKRRRVILAAQWWLAGEG FT RRHAHRPCRFDVVLLEGPATTPPTWLQAAFDAD" FT CDS 932786..933673 FT /transl_table=11 FT /locus_tag="azo0872" FT /product="conserved hypothetical protein" FT /function="predicted methyltransferases" FT /note="Conserved hypothetical protein. Homology to pp1326 FT of P. putida of 56% ((AAN66950). InterPro: Uncharacterized FT protein family UPF0011 (IPR008189) TIGR00096: conserved FT hypothetical protein Pfam: Tetropyrrole (Crrin/Porphyrin) FT methyltransferase no signal peptide no TMHs" FT /db_xref="GOA:A1K3T4" FT /db_xref="InterPro:IPR000878" FT /db_xref="InterPro:IPR008189" FT /db_xref="InterPro:IPR014777" FT /db_xref="UniProtKB/TrEMBL:A1K3T4" FT /protein_id="CAL93489.1" FT /translation="MSEFPSTPTAVLSRTPSLYVVATPLGNLQDMSFRALGVLRAVDTI FT AAEDTRHSQRLLDAYGIRSKLLALHEHNEQAAAGQLIERLSQGENIALITDAGTPAVSD FT PGARAVARVRAAGFPVVPVPGPCAAVAALSVAGFGEDGFRFVGFLPPKQAARCARLAPL FT RDERAALVFYEAPHRVEECVADLAREFGPARRVLVARELTKLHEEIACFSLGEAAAWFA FT ADTNRVRGEFVLVVEGAPAREGLDAETERVLTLLLAELPVKRAARLAADITGAAKNALY FT ARALELKGEAEGEG" FT CDS 933728..934762 FT /transl_table=11 FT /gene="pyrC" FT /locus_tag="azo0873" FT /product="probable dihydroorotase" FT /function="Dihydroorotase" FT /EC_number="3.5.2.3" FT /note="Probable dihydroorotase (EC 3.5.2.3) (DHOase). FT Homology to pyrC of E. coli of 57% (sprot|PYRC_ECOLI(SRS)) FT Is involeved in the pyrimidine biosynthesis. CATALYTIC FT ACTIVITY: (S)-dihydroorotate + H(2)O = FT N-carbamoyl-L-aspartate. Needs 2 zinc ions per subunit. FT InterPro: Dihydroorotase homodimeric type (IPR004721); FT Dihydroorotase (IPR002195) Tigrfam: pyrC_dimer: FT dihydroorotase homodimeric type no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3T5" FT /db_xref="InterPro:IPR002195" FT /db_xref="InterPro:IPR004721" FT /db_xref="InterPro:IPR006680" FT /db_xref="UniProtKB/Swiss-Prot:A1K3T5" FT /protein_id="CAL93490.1" FT /translation="MQSITFTRPDDWHLHVRDGAALAAVVPHTAERFGRALIMPNLRPP FT VTTTAQALAYRDRIRAAVPAGLAFEPLMSLYLTDNTAPDEIERARASGAVIAAKLYPAG FT ATTNSDAGVTAIDKIYPVLERMEACGLVLCVHGEVTGGEVDVFDRERVFMEKILSPLVR FT RFPALKVVFEHITTAEAAQFVRAAGANVAATVTAHHLLLNRNAIFAGGIRPHHYCLPVL FT KRETHRVALVEAVTSGNPRFFLGTDSAPHARSTKEAACGCAGCYTAHAGIELYAEVFDA FT AGALERLEAFASLNGPAFYGLAPNADKITLVRESWSVPAGFPYLDDDPLVPLRAGESVG FT WRLA" FT CDS 934759..935190 FT /transl_table=11 FT /locus_tag="azo0874" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT Daro03003273 of Dechloromonas aromatica of 35% FT (gi|41723286|ref|ZP_00150229.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K3T6" FT /protein_id="CAL93491.1" FT /translation="MITRLRRVLLLAALPLLAACENSATAYSIEGSQHALILVREQSYF FT WDSEIKQAIVASRLPQCQKRVAIHPGSKVLTEVLVYEAGDRLWALQQGNRWYLASTERC FT LVQDWDKPADAPLGPLVGSFRLRDGAPAFVPAQEAAPVR" FT CDS 935993..936436 FT /transl_table=11 FT /gene="mraZ" FT /locus_tag="azo0875" FT /product="protein mraZ" FT /function="MraZ" FT /note="Protein mraZ." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR003444" FT /db_xref="InterPro:IPR020603" FT /db_xref="UniProtKB/Swiss-Prot:A1K3T7" FT /protein_id="CAL93492.1" FT /translation="MFQGAVALSLDAKGRLAIPARHRDALTPDGAPLVMTVHPHRCLLV FT YPLTAWEPIREKITSLPGMDQATLSFKRMLVGFAQEETLDAAGRVLVAQSLRQFAALDK FT QVWLVGQGTHFELWSDAGWQKQQEAMLALVDNPLPAGLENFVL" FT CDS 936433..937371 FT /transl_table=11 FT /gene="mraW" FT /locus_tag="azo0876" FT /product="SAM dependent methyltransferase" FT /function="predicted S-adenosylmethionine-dependent FT methyltransferase involved in cell envelope biogenesis" FT /EC_number="2.1.1.-" FT /note="S-adenosyl-methyltransferase mraW (EC 2.1.1.-). FT Exhibits a S-adenosyl-dependent methyltransferase activity FT (By similarity). TIGR00006: conserved hypothetical prote" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3T8" FT /db_xref="InterPro:IPR002903" FT /db_xref="InterPro:IPR023397" FT /db_xref="UniProtKB/Swiss-Prot:A1K3T8" FT /protein_id="CAL93493.1" FT /translation="MSAQLQHVSVLLTEAVDALAIKPEGIYVDGTFGRGGHSRAVLARL FT GAGGRLIAFDRDPAAIAAGQAIADPRLELVHAPFSEFAVVLDRLGVSAVDGVLLDLGVS FT SPQLDDASRGMSFRFDAPLDMRMDTSRGRTVAEWLAEASVAEITEVIRDYGEERFAYAI FT AKAIAAARTGGAIATTGQLAAIVEKAVRTREPGQHPATRSFQALRIFINQELEELTTVL FT PDCVARLSEGGRLVVISFHSLEDRIVKRFLRDEARPPQLPSRLPVRAADLPPPRLQLVG FT KAQRPGEAEVAANPRARSAVMRVAERCGVAA" FT CDS 937368..937631 FT /transl_table=11 FT /gene="FtsL" FT /locus_tag="azo0877" FT /product="putative cell division protein FtsL" FT /function="Cell division protein" FT /note="Putative cell division protein FtsL. Homology to FT ftsL of E. coli of 32% (sprot|FTSL_ECOLI). Protein involved FT in cell division and cell growth. May play some role in FT coupling cell division and peptidoglycan physiology. Pfam: FT Cell division protein FtsL signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3T9" FT /db_xref="InterPro:IPR007082" FT /db_xref="InterPro:IPR011922" FT /db_xref="UniProtKB/TrEMBL:A1K3T9" FT /protein_id="CAL93494.1" FT /translation="MIRFDAMLVALVVASALGVVAAQHQSRKLYIELEREMARAHSLDV FT EWGQLQLEQSTWAAHARVEKLARERLGMRPPVPGQIVVLEAQ" FT CDS 937628..939388 FT /transl_table=11 FT /gene="FtsI" FT /locus_tag="azo0878" FT /product="probable peptidoglycan glycosyltransferase" FT /function="Cell division protein FtsI/penicillin-binding FT protein 2" FT /EC_number="2.4.1.129" FT /note="Probable peptidoglycan glycosyltransferase. Homology FT to ftsI of E. coli of 43% (sprot|FTSI_ECOLI) Cell wall FT formation. Essential for the formation of a septum of the FT murein sacculus. Synthesis of cross-linked peptidoglycan FT from the lipid intermediates. InterPro: Penicillin binding FT protein transpeptidase domain (IPR001460) Pfam: FT Penicillin-binding protein dimerisation domain; Penicillin FT binding proetin transpeptidas domain signal peptide no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U0" FT /db_xref="InterPro:IPR001460" FT /db_xref="InterPro:IPR005311" FT /db_xref="InterPro:IPR012338" FT /db_xref="UniProtKB/TrEMBL:A1K3U0" FT /protein_id="CAL93495.1" FT /translation="MKKQRTVTFNHNPLLKRELPAWRARFVLVMLMGCSLALIGRALYL FT QGVNNSFLQAKGEMRYARVLEVPATRGRISDRNGDMLAVSTPVRSIWAIPADARLEPAA FT ARQLATLLEMDVRELNDKLAPGRDFVYLKRQLPPEVADRIAALKLPGVHQQQEYRRYYP FT GGDVTAHMLGFTGVEDRGQEGIELAYEKMLAGMPGSRRVIKDRRGRIVEDVESIRPPRD FT GDDISLAMDGKIQYIAYSALREAMQLNKAKAGAAVVLDARTGEVLALANAPTYNPNNRS FT NLTGAQLRNRVFTDSFEPGSVMKPFIAGLALETGKVKPTTVIDTSAGRMTIGTATISDS FT HRSGPLTVAEVIQKSSNIGTVKMALQFTPAEMWQLYHQLGFGSPLNLGFPGETGGRLRP FT AKTWRPIEQATMSYGHGISVTLIQMARAYLVFARDGELVPLSLTKLDGPPSGGTRIFSP FT QTVQTLRNMLETVTLPGGTATKAQVPGYRVGGKTGTALKLEGGHYTKRYIASFVGIAPI FT SNPRLVVAVMIDEPSAGNYYAGTVAAPVFARIMEGSLRTLGVAPDAPLTPLQLARKPNE FT PAPAAVRESM" FT CDS 939385..940890 FT /transl_table=11 FT /gene="murE" FT /locus_tag="azo0879" FT /product="probable FT UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate FT ligase" FT /function="UDP-N-acetylmuramyl tripeptide synthase" FT /EC_number="6.3.2.13" FT /note="Probable FT UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate FT ligase Homology to murE of E. coli of 40% FT (sprot|MURE_ECOLI) Cell wall formation. Diaminopimelic acid FT adding enzyme (By similarity). Pfam: Mur ligase family, FT catalytic domain; Mur ligase family, glutamate ligase no FT signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U1" FT /db_xref="InterPro:IPR000713" FT /db_xref="InterPro:IPR004101" FT /db_xref="InterPro:IPR005761" FT /db_xref="InterPro:IPR013221" FT /db_xref="UniProtKB/TrEMBL:A1K3U1" FT /protein_id="CAL93496.1" FT /translation="MSNPAFVLLDQLRASGVRPAGITADSRRVGPGAVFAAWPGHVTDG FT RRYIASAIERGAAAVLWEEGDGFHPGELPVPGFAVPRLRELAGALAHEIYDRPSARLWM FT AGVTGTNGKTTVTQWLARALGELGSRCGIVGTLGSGFPDQLSASLNTTPDALELHATLA FT RLLGEGAAAAAMEVSSIGLDQGRVNGVEFDVAVFTNLTRDHLDYHRTMDAYAEAKARLF FT ALPGISRAVINLDDAFGLTQARRLVAAGQVDVIGYTCVASNADAVPGARVLVADRLQAS FT PSGLQFSLHWAGRQSDLQVRMVAPFNVSNLLAVIGALVMRGVAVEEALAVVGRLNPPEG FT RMQLVGGIGEPLIVIDYAHTPDALAKVLEAVRGTVRSRGGRLVCVFGCGGDRDPGKRPL FT MGEVARQLADRVVVTSDNPRSEDPRKIIDAIAAGAGASADCIVDRAEAIRIAVGEAGPD FT DVVVLAGKGHEPYQEIHGQRLPFSDVEQAKAALAVWNDRRTTA" FT CDS 940863..942299 FT /transl_table=11 FT /gene="murF" FT /locus_tag="azo0880" FT /product="UDP-N-acetylmuramoylalanyl-D-glutamyl-2, FT 6-diaminopimelate-D-alanyl-D-alanine ligase" FT /function="involve in murein biosynthesis" FT /EC_number="6.3.2.10" FT /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine FT ligase (EC 6.3.2.10) (UDP-MurNAc-pentapeptide synthetase) FT (D-alanyl-D- alanine-adding enzyme). Involved in cell wall FT formation. Catalyzes the final step in the synthesis of FT UDP-N-acetylmuramoyl-pentapeptide the precursor of murein FT (By similarity). InterPro: Cytoplasmic peptidoglycan FT synthetases N-terminal mobB: molybdopterin-guanine FT dinucleot" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U2" FT /db_xref="InterPro:IPR000713" FT /db_xref="InterPro:IPR004101" FT /db_xref="InterPro:IPR005863" FT /db_xref="InterPro:IPR013221" FT /db_xref="UniProtKB/TrEMBL:A1K3U2" FT /protein_id="CAL93497.1" FT /translation="MERQENDGMMSLLDASRALSAHHAVAQGAVRFSSVGTDSRGIIPG FT QLFVALRGERFDGHEFVAAALKAGAAAAMVDARGFTEFGDASLPLLVVDDTRLALGTLA FT ATWRARFAIPVIGVTGSNGKTTVKEMCAEILRAQARRDGAGDEAVLATRGNLNNDIGLP FT LTLLELRDHHRAAVIEMGMNHPGEIAYLTGLARPTVAIVNNAQRAHLQGLGTLGEVAQE FT KGAIYQGLGAAGVAVVNADDPHAGYWRDLNAGRPIVSFGIDQPADVAGECTLHGLGSQL FT HIAAPQGRGEVELQVPGLHNASNALGAAAACLAAGVVFEAALEGLALYEGTRGRLQRRS FT GPQGAVILDDSYNANPDSVRAGIDVLASTPGHTFLVLGDMGEVGQTSAQVHDEIGGYAK FT SKGIDGLYALGEASAIAVRNFGEGAHHFDSVEALVAALAPRLDADAVVLVKGSRFMKME FT RVADALAALHNGAPQKDTNS" FT CDS 942301..943389 FT /transl_table=11 FT /gene="mraY" FT /locus_tag="azo0881" FT /product="phospho-N-acetylmuramoyl-pentapeptide FT transferase" FT /function="Involved in murein biosynthesis" FT /EC_number="2.7.8.13" FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase FT (EC 2.7.8.13) (UDP- MurNAc-pentapeptide FT phosphotransferase). First step of the lipid cycle FT reactions in the biosynthesis of the cell wall FT peptidoglycan (By similarity). mraY: FT phospho-N-acetylmuramoyl-pentape" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U3" FT /db_xref="InterPro:IPR000715" FT /db_xref="InterPro:IPR003524" FT /db_xref="InterPro:IPR018480" FT /db_xref="UniProtKB/Swiss-Prot:A1K3U3" FT /protein_id="CAL93498.1" FT /translation="MLLELALWLGQDIRGFNVFGYITLRTVLAALTALAISLTAGPGVI FT RWLAAKKIGQAVRDDGPKSHLTKAGTPTMGGALILIAIGITILLWGDLRNAYVWVTLLV FT TLGFGAVGWVDDWRKVVHRDPKGLASRWKYFWTSAIALGASIFLGLSATTPAETELIVP FT FFKAVAYPLGVYGFIALTYFVINGTSHAVNLTDGLDGLAIMPTVMVAGALAIFAYVAGH FT AGFSKYLGVPYIAGAGELAVFCGAICGAGLGFLWFNAYPAEVFMGDVGALALGAALGTI FT AVVVRQEIVLFIMGGLFVAETLSVMVQVLYFKASGGKRIFRMAPLHHHYELSGWKETQV FT VVRFWIITLMLVLFGLSTLKLR" FT CDS 943386..944804 FT /transl_table=11 FT /gene="murD" FT /locus_tag="azo0882" FT /product="probable UDP-N-acetylmuramoylalanine-D-glutamate FT ligase" FT /function="UDP-N-acetylmuramoylalanine-D-glutamate ligase" FT /EC_number="6.3.2.9" FT /note="Probable UDP-N-acetylmuramoylalanine-D-glutamate FT ligase. Homology to murD of P. aeruginosa of 45% FT (Sprot:MURD_PSEAE) Cell wall formation. Catalyzes the FT addition of glutamate to the nucleotide precursor FT UDP-N-acetylmuramoyl-L-alanine (UMA) (By similarity). FT InterPro: Cytoplasmic peptidoglycan synthetases N-terminal FT (IPR000713); Cytoplasmic peptidoglycan synthetases FT C-terminal (IPR004101) Pfam: Mur ligase family, catalytic FT domain; Mur ligase family, glutamate ligase domain no FT signal peptide no TMHs rpiB: ribose 5-phosphate isomerase FT B" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U4" FT /db_xref="InterPro:IPR004101" FT /db_xref="InterPro:IPR005762" FT /db_xref="InterPro:IPR013221" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K3U4" FT /protein_id="CAL93499.1" FT /translation="MTQPSFSSSLAGRHVLVLGLGESGLAIARWCARCGARLRVADSRT FT TPPGLEALRAAAPQAEVITGSFGDEVLEGIDVVAVSPGLDPRVGVIASARRRCLPITGE FT MALFAQALTDLGARDATRILAITGTNGKTTTTALTAALAQSAGLDAVAAGNISPAALDV FT LMARLDAGQALPQCWVLELSSFQIETAQALDADAATVLNVTDDHLDRYADLADYAATKA FT RIFQGRGAQVLNREDARVAAMVLSGRKVVRFGTDAPQNPADYGLVEDAGRCWLVRGGER FT LLALDELALAGRHNAANALAALALCETGLGLAPAQLLAGLRAFRGLPHRVELVAERADG FT VRYYDDSKGTNVGATVAALDGLGGRVVLIAGGDGKGQDFSPLAPVLTRHARAVVLIGRD FT AKLIEAAVAGCGVPLEHAADLDTAVLRANALARPGDAVMLSPACASLDMFRNYAHRAEV FT FIAAVRRLPEVSPR" FT CDS 944801..946033 FT /transl_table=11 FT /gene="FtsW" FT /locus_tag="azo0883" FT /product="cell division protein FtsW" FT /function="Bacterial cell division membrane protein" FT /note="This is a septum-peptidoglycan biosynthetic protein FT involved in cell wall formation. Plays a role in the FT stabilization of the ftsZ ring during cell division." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U5" FT /db_xref="InterPro:IPR001182" FT /db_xref="InterPro:IPR013437" FT /db_xref="UniProtKB/TrEMBL:A1K3U5" FT /protein_id="CAL93500.1" FT /translation="MKLGALFSAWFPSRPAPVGGGETARVVSRLARPGAPARELDLLLI FT WSAVGLLLLGLVMVYSASIAIAEGSRFTNNQSHYFLLRHAIFLAIGIGCGLAAFQLPMA FT KWQRLAPALFVGGVVLLIVVLIPGIGREVNGAQRWLSLGPVNLQPSELMKVFVALYAAD FT YTVRKLDAMGSFTRGFLPMMTVILFVGFLLLREPDFGAFVVITTIAFGVLFLGGVNVRV FT FALLAVVAVIGFIILIWTSPYRRERIFGFMDPWQDAFGKGYQLSHALIAFGRGEWFGVG FT LGGSVEKLFYLPEAHTDFLLAVIAEELGFAGVVMVVALFAILVQRTFAIGREAIKLERY FT FSGLVALGMGLWMGVQSFINMGVNMGLLPTKGLTLPMMSFGGSGIVANCVALAILLRID FT WEVRQLKRGGA" FT CDS 946030..947100 FT /transl_table=11 FT /gene="murG" FT /locus_tag="azo0884" FT /product="probable FT undecaprenyldiphospho-muramoylpentapeptide FT beta-N-acetylglucosaminyltransferase" FT /function="UDP-N-acetylglucosamine:LPS N-acetylglucosamine FT transferase" FT /EC_number="2.4.1.227" FT /note="Probable undecaprenyldiphospho-muramoylpentapeptide FT beta-N-acetylglucosaminyltransferase. Homology to murG of FT e. coli of 47% (Sprote:MURG_ECOLI) Cell wall formation. FT Catalyzes the transfer of a GlcNAc subunit on FT undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid FT intermediate I) to form FT undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc FT (lipid intermediate II) (By similarity). InterPro: FT Glycosyltransferase family 28 (IPR004276) Pfam: FT Glycosyltransferase family singal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U6" FT /db_xref="InterPro:IPR004276" FT /db_xref="InterPro:IPR006009" FT /db_xref="InterPro:IPR007235" FT /db_xref="UniProtKB/Swiss-Prot:A1K3U6" FT /protein_id="CAL93501.1" FT /translation="MKTLLVMAGGTGGHIFPGIAVAEALRAKGWRIVWMGNPDGMEARI FT VPSRGYDTAWVRFGALRGKGLVRKLLLPVNLLVGFWQALGQLRRIKPDVVLGMGGYITF FT PGGMMAALLGWPLVLHEQNSVAGLANRVLAGVADRVLSGFPSVLKKAGWVGNPVREDIA FT SVAAPAARFAGRSGPLNVLVVGGSLGAAVLNDTVPKALARIPLEFRPQVVHQAGEKQID FT ALRAAYAAAGVEGDLRPFIQDMAAAYAGADLVICRAGALTVAELAAVGVASLLVPFPHA FT VDDHQTGNARFLAEHGGAYLLPQNELDAERLAGILASLDRPQLLQMAEHARAQAKPRAT FT EAVARACEELAEGRKA" FT CDS 947097..948500 FT /transl_table=11 FT /gene="murC" FT /locus_tag="azo0885" FT /product="probable UDP-N-acetylmuramate-L-alanine ligase" FT /function="UDP-N-acetylmuramate-alanine ligase" FT /EC_number="6.3.2.8" FT /note="Probable UDP-N-acetylmuramate-L-alanine ligase. FT Homology to murC of P. aeruginosa of 58% (sprot:MURC_PSEAE) FT Cell wall formation. Pfam: Mur ligase family, catalytic FT domain; Mur ligase family, glutamate ligase domain no FT signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U7" FT /db_xref="InterPro:IPR000713" FT /db_xref="InterPro:IPR004101" FT /db_xref="InterPro:IPR005758" FT /db_xref="InterPro:IPR013221" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/Swiss-Prot:A1K3U7" FT /protein_id="CAL93502.1" FT /translation="MKHKVKRIHFVGIGGAGMSGIAEVLVNLGYSVSGSDLGDSAATRR FT LKAMGAKVVLGHDAANVEAADALVVSTAVKNDNPEVIAARARHIPIVPRAQMLAELMRL FT KSGIAIAGTHGKTTTTSLVASILAEGAMDPTFVIGGRLNAAGANARLGKGDFLVAEADE FT SDASFLMLSPVISVVTNIDADHMDTYGHDFARLKQAFVDFLQRLPFYGVAVLCEDDPHV FT RSIMPLVSKQVVRYGLSETANIRAENIRAEGGRMIFDVLRVNGSTTRLADVVLNLPGLH FT NVRNALAAIAVATEVQVPDEAIVKALAEFSGVGRRFQRYGEVAAPSGGTFTLIDDYGHH FT PVEMEATLAAARGAFPGRRLVLAFQPHRYTRTRDCFEDFVKVLSTVDALLLAEVYAAGE FT APIVAADGRALSRALRVAGKVEPVFVEDIGGMPQAVLEAVRDGDVVITMGAGSIGAVPG FT KLASNEEQA" FT CDS 948497..949411 FT /transl_table=11 FT /gene="ddlB" FT /locus_tag="azo0886" FT /product="probable D-alanine-D-alanine ligase" FT /function="D-alanine-D-alanine ligase and related ATP-grasp FT enzymes" FT /EC_number="6.3.2.4" FT /note="Probable D-alanine-D-alanine ligase. Homology to FT ddlB of E. coli of 54% (sprot|DDLB_ECOLI) Cell wall FT formation (By similarity). InterPro: D-alanine--D-alanine FT ligase (IPR005905) Pfam: D_ala D_ala liganse signal peptide FT no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3U8" FT /db_xref="InterPro:IPR000291" FT /db_xref="InterPro:IPR005905" FT /db_xref="InterPro:IPR011095" FT /db_xref="InterPro:IPR011127" FT /db_xref="InterPro:IPR011761" FT /db_xref="InterPro:IPR013815" FT /db_xref="InterPro:IPR013816" FT /db_xref="InterPro:IPR013817" FT /db_xref="InterPro:IPR016185" FT /db_xref="UniProtKB/Swiss-Prot:A1K3U8" FT /protein_id="CAL93503.1" FT /translation="MKQRFGKVAVLFGGSSAERDVSLMSGAAVLAALQGAGVDAHAFDP FT AERDLHILKEEGYDRVFIALHGRGGEDGTVQGALELMGIPYTGSGVMASALAMDKWRTK FT MVWLSCGLPTPRYAILDADSDFDAIARDLGLPIFVKPVHEGSSMGATKVTEAGQLRAAW FT ELAARYDSLVIAEEFISGQELTAPFLDDRALPLVRIVAPDGNYDYQHKYFTDDTRYDCP FT CGLPQAEEEALQALILKSARVLGCRGWGRADLILTPEGRPYLLEMNTSPGMTGHSLVPM FT SARVAGMSFEALCLAILAGARLG" FT CDS 949404..950234 FT /transl_table=11 FT /gene="FtsQ" FT /locus_tag="azo0887" FT /product="putative cell division protein FtsQ" FT /function="Cell division septal protein" FT /note="Putative cell division protein FtsQ. Homology to FT ftsQ of E. coli of 23% (Sprot:FTSQ_ECOLI) This protein may FT be involved in septum formation. Pfam: Cell division FT protein FtsQ no signal peptide 1 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K3U9" FT /db_xref="InterPro:IPR005548" FT /db_xref="InterPro:IPR013685" FT /db_xref="UniProtKB/TrEMBL:A1K3U9" FT /protein_id="CAL93504.1" FT /translation="MAEFRTRASAAAAPRGAARERARVERGLWHRPALLHLISDLLMLF FT AAVAFGWALVAWFVSRPLFPLREVILLSPAEEVTEAQLEYVARTAIRGNFFTVDLEAVR FT EAFESVPWVRRAEVRRRWPDGIELRLVEQRAVASWKPVEGGEPRLVNSDGELFAATTTD FT PMPALAGPQGTSQRLLARYQQLGAMLQPLNLHVVGVSLSAREAWQLTTDNGMVILLGRE FT SEQGVLDRRLKRFIAAWPQLQQHVGTTVAVADLRYPGGFALTPADGVIAGKGKQ" FT CDS 950231..951460 FT /transl_table=11 FT /gene="FtsA" FT /locus_tag="azo0888" FT /product="cell division protein FtsA" FT /function="Actin-like ATPase involved in cell division" FT /note="This protein may be involved in anomalous filament FT growth. May be a component of the septum. It may interact FT with ftsZ. InterPro: Cell division protein FtsA" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3V0" FT /db_xref="InterPro:IPR001023" FT /db_xref="InterPro:IPR003494" FT /db_xref="InterPro:IPR020823" FT /db_xref="UniProtKB/TrEMBL:A1K3V0" FT /protein_id="CAL93505.1" FT /translation="MSKEYKELIVGLDIGTAKITCMVAEVRPDGRLNVVGLGTQPTSGL FT KRGVVVNIEATVDAISRVIQEVELMADCKIRDVYTGIAGSHIKSFNSNGMVAIKDKEVT FT PLDVERVIEVARAMPIPAEQQILHILTQEFIIDGQGGVREPIGMSGVKLEVKVHIVTGA FT VSAAQNVIKCVRRCGLEVMDLILQPLASSYAVLTEDEKELGVCLVDIGGGTTDIAVFTQ FT GAIRHTAVLPIAGDQITNDIAMALRTPTAEAEDIKIHQGVAMHQMADAEEMIEVPGVGD FT RPPRKLSRQALADVIEPRVSELFELVQAELRRSGYEELLSSGIVLTGGSSVMRGMAELG FT EDVFHMPVRIGSPQYDGGLADVVCQPRYATAMGLVMEGAAQRRRGIQARDTRSVKQIFG FT RMKAWFEKNF" FT CDS 951602..952744 FT /transl_table=11 FT /gene="FtsZ" FT /locus_tag="azo0889" FT /product="cell division protein FtsZ" FT /function="Cell division GTPase" FT /note="This protein is essential to the cell-division FT process. It seems to assemble into a dynamic ring on the FT inner surface of the cytoplasmic membrane at the place FT where division will occur and the formation of the ring is FT the signal for septation to begin. Binds to and hydrolyzes FT GTP. ftsZ: cell division protein FtsZ" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3V1" FT /db_xref="InterPro:IPR000158" FT /db_xref="InterPro:IPR003008" FT /db_xref="InterPro:IPR008280" FT /db_xref="InterPro:IPR018316" FT /db_xref="InterPro:IPR024757" FT /db_xref="UniProtKB/TrEMBL:A1K3V1" FT /protein_id="CAL93506.1" FT /translation="MFEIVEKEPTGTIIKVIGIGGAGGNAVDHMIREGVQGVQFISANT FT DAQALSRCLASTKIQLGVTGLGAGSKPEAGRAAAQESREQIAAALEGAHMCFITGGMGG FT GTGTGAAPVVAEIAKEMGILCVAVVTKPFDFENRIRVAESGVEELTRHVDSLIVVLNDK FT LLDVFGDDAGFEECFRSADNVLRSAVGGIAEIINVPGLVNVDFQDVRTAMAEMGRAMMG FT SAEASGMDRARIAAEQAAVSPLLEGTELSGARCVLINITASKSLKMSEVRDAVKTVQAF FT AAPEAFVKYGTVFDESMGDNIRITVVATGLGTPRAARQPVMQVVQGTGTYGPMGGVDAN FT PAMPEVFRTGRGGARTTVDAMASNGMGNYDIPAFLRRQAD" FT CDS 952910..953833 FT /transl_table=11 FT /gene="lpxC" FT /locus_tag="azo0890" FT /product="probable UDP-3-O-acyl N-acetylglycosmaine FT deacetylase" FT /function="UDP-3-O-acyl-N-acetylglucosamine deacetylase" FT /EC_number="3.5.1.-" FT /note="Probable UDP-3-O-acyl N-acetylglucosamine FT deacetylase. Homology to lpxC of P. aeruginosa of 58% FT (Sprot:LPXC_PSEAE) Involved in the biosynthesis of lipid A FT a phosphorylated glycolipid that anchors the FT lipopolysaccharide to the outer membrane of the cell (By FT similarity). InterPro: UDP-3-0-acyl N-acetylglucosamine FT deacetylase (IPR004463) tigrfam: lpxC: UDP-3-0-acyl FT N-acetylglucosamine deacetylase Pfam: UDP-3-0-acyl FT N-acetylglucosamine deacetylase no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3V2" FT /db_xref="InterPro:IPR004463" FT /db_xref="InterPro:IPR011334" FT /db_xref="InterPro:IPR015870" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/Swiss-Prot:A1K3V2" FT /protein_id="CAL93507.1" FT /translation="MIRQRTLKSTVKATGVGLHGGRKVNLVLRPAAPDTGIVFHRVDLD FT PPLDLPADPYAVCDTRMCSGLEKGGQKVGTVEHLMSALAGLGIDNLHIDVDAPEIPILD FT GSSGPFVFLLQSAGIEEQKAPKRFLRVKKPVEYREGDKWVRLEPYDGFRLDFSIVFNHP FT AIDSTSTAVSIDFATHSYVRDVARARTFGFMQDVEFMRANGLALGGSLENAIVMDEYRV FT LNADGLRYADEFVKHKVLDAIGDLYLCGHPLLARYSAHKSGHALNNQILRVLLEDRSAW FT EIVSFEREAATPPAVAHQFAPVLAAA" FT CDS 953868..954056 FT /transl_table=11 FT /locus_tag="azo0891" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. signal peptide. 1 TMH" FT /db_xref="UniProtKB/TrEMBL:A1K3V3" FT /protein_id="CAL93508.1" FT /translation="MLIMRLAILLVVLGTGGSLLLWLATGKPRYKAWAWKSLRFGLVVV FT LVFFALLLVERVLAPTL" FT CDS complement(954061..954489) FT /transl_table=11 FT /locus_tag="azo0892" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to CV4285 FT of C.violaceum of 32% (tremble:Q7NQ55). No domains FT predicted. No TMHs No signal peptide." FT /db_xref="InterPro:IPR007922" FT /db_xref="UniProtKB/TrEMBL:A1K3V4" FT /protein_id="CAL93509.1" FT /translation="MTRLLQRYLGSGDALARLQDHAARLRRLQGVLERLLPPALADACR FT VANIKDDALVIAAQGGAAASRLKQMLPSLQAQFLQAGYPLQSIKVKVATPQQAEWRRPP FT PERHISQTARSSITDFAATLPADSPLRASLERLARRSS" FT CDS 954595..957324 FT /transl_table=11 FT /gene="secA" FT /locus_tag="azo0893" FT /product="preprotein translocase SecA subunit" FT /function="Preprotein translocase subunit SecA (ATPase RNA FT helicase)" FT /note="Preprotein translocase secA subunit. Involved in FT protein export. Interacts with the secY/secE subunits. SecA FT has a central role in coupling the hydrolysis of ATP to the FT transfer of pre-secretory periplasmic and outer membrane FT proteins across the membrane. InterPro: SecA protein no FT signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3V5" FT /db_xref="InterPro:IPR000185" FT /db_xref="InterPro:IPR004027" FT /db_xref="InterPro:IPR011115" FT /db_xref="InterPro:IPR011116" FT /db_xref="InterPro:IPR011130" FT /db_xref="InterPro:IPR014018" FT /db_xref="InterPro:IPR020937" FT /db_xref="UniProtKB/Swiss-Prot:A1K3V5" FT /protein_id="CAL93510.1" FT /translation="MISGLLKKLFGSRNDRLIRQYSQNVRKINALEPEIAALSDEALRG FT KTGEFRQRLADGATLNDLLPEAFAVVREAGKRVHGMRHFDVQLIGGMVLHDGKIAEMRT FT GEGKTLVATLAAYLNALPGKGVHVITVNDYLASRDAEMMGRIYGFLGLTTGCNLSRMGH FT AEKQLAYAADITYGTNNEFGFDYLRDNMVYATGERVQRGLNFAVVDEVDSILIDEARTP FT LIISGQAEDHTDLYLKMNQVAPLLKRQEGGLDDKDSVIEPGDYTVDLKAHQVLLTEQGH FT ENAEQILVRIGLLPEGAGLYEPGNILLVHHLYAALRAHALYHKDQHYVVQNGEVVIVDE FT FTGRLMAGRRWSDGLHQAVEAKEGVRIQAENQTLASITFQNYFRMYGKLAGMTGTADTE FT AFEFHHIYGLETVVIPTNRPMVRKDENDKVYRTAKEKWEAVIADIADCVKRGQPVLVGT FT TSIETNEYLSGLLNKAKIAHQLLNAKQHDSEAQIVAQAGRPGVVTIATNMAGRGTDIVL FT GGNIEKPVSQVRDDDSVPAAEKESRIAALREEWRKVHEQVIAAGGLHIIGTERHESRRI FT DNQLRGRSGRQGDPGSSRFYLSLEDPLMKIFAGERLNAIMVRLKMPEGEAIEHGMVTRS FT LESAQRKVEQRNFDIRKQLLEYDDVANDQRKVIYQQRNELLETEDISETIQAMRQGVLH FT DLFRTYVPVDSVEDQWDIAGLEQALASDYLLKLPLLEWVKAEPNLDDEAILKRIIDAGE FT EAYAAKIAQVDAAAWHQFERNVMLQSLDTHWREHLAALDHLRQGIHLRGYAQKNPKQEY FT KREAFELFETLLDTVRADVSKLLMTVQIRTEAQLDEAEAPPEMENVQYHHADYDEALAA FT AAASTAETPVQGGPKVGRNDPCPCGSGKKYKHCHGKLS" FT CDS 957401..958882 FT /transl_table=11 FT /locus_tag="azo0894" FT /product="GAF-domain containing protein" FT /function="predicted signal transduction protein" FT /note="GAF-domain containing protein," FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR003018" FT /db_xref="InterPro:IPR013976" FT /db_xref="UniProtKB/TrEMBL:A1K3V6" FT /protein_id="CAL93511.1" FT /translation="MANRPDDKSGAQRPQQAREPRGAQEWVVHIREQEMPGFGATVAAV FT HRVTGDEQASAGRLAQVILQDAALTTKVLKLANSAYYNPTRQPISTISRAIVVLGFNVV FT VEIAIGIMLVDALLTGGVRQRVVAEMAHSFHAAVQARALLQLRKERVGEEVFIAALLAR FT VGEMAFWCFGGATAQRLDGLLGAGNLGPEEAQQAVLGFGLRQLSLGLAREWRLGSLLVE FT VLEARPRPTVEELAVAHAHRLAAAAEKGWDSPAMEAMFESLAVFTGEPVEALRPLLAAS FT AAEAAQIASFYGASEAGRMIPLPAPAVLDTAAAEPLKEADPLLQLRILREISGRVAAGA FT SVGEVLELVLEGIYRAVGFERVLFALLAPNRQQLVGKAALGRGAEALSQRFVFTLDQAA FT DDLLNAFFRSPRLMRLGPGQHPAGLDAGRLELVAGAAHGCIAPIQVQGRLIGLFYADRP FT RARTPIDDDSLASMLLFSQQVSLAAARGLPGARQQ" FT CDS 958968..960209 FT /transl_table=11 FT /gene="argJ" FT /locus_tag="azo0895" FT /product="probable arginine biosynthesis bifunctional FT protein ArgJ" FT /function="N-acetylglutamate synthase (N-acetylornithine FT aminotransferase)" FT /EC_number="2.3.1.-" FT /note="Arginine biosynthesis bifunctional protein argJ. FT Homology to argJ of N. gonorrhoeae of 55% (AAA25447). FT Catalyzes two activities which are involved in the cyclic FT version of arginine biosynthesis: the synthesis of FT acetlyglutamate from glutamate (EC 2.3.1.35) and acetyl-CoA FT and of ornithine by transacetylation between FT acetylornithine and glutamate (EC 2.3.1.1) (By similarity). FT Tigrfam: ArgJ: glutamate N-acetyltransferase/amino acid FT biosynthesis Pfam: ArgJ family no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3V7" FT /db_xref="InterPro:IPR002813" FT /db_xref="InterPro:IPR016117" FT /db_xref="UniProtKB/TrEMBL:A1K3V7" FT /protein_id="CAL93512.1" FT /translation="MAVNLNTPNPADLLPVAGVRLGVAEAGIRKANRRDLTVIELAAGA FT RVAGVFTTNRFCAAPVQVCKANLAAGNPIRALVINTGVANAGTGEPGLAAANATCDALA FT RGLGIDAGQVLPFSTGVILEPLPVDRLVAGLPRAIADLRADAWFDAAHAIMTTDTLAKA FT VSSTVEIGGRRVTLTGISKGAGMIKPNMATMLGYLACDAAVSQALLDELVKEAADLSFN FT SITVDGDTSTNDSFILIATGQAGHAEITDPASADYRALRDAVVDVAIRLAQAIVRDGEG FT ATKFMTIAVEGGKDREECRKVAYAVGHSPLVKTAFFASDPNLGRILAAIGYAGIGDLDV FT AALRVWLGSPQESVLVAEHGGRAASYREEDGARIMKEAELTIRIDLARGGASATVWTCD FT FSYDYVKINADYRS" FT CDS 960324..961154 FT /transl_table=11 FT /locus_tag="azo0896" FT /product="putative phosphoprotein phosphatase" FT /function="Serine/threonine protein phosphatase" FT /note="Putative phosphoprotein phosphatase," FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K3V8" FT /db_xref="InterPro:IPR001932" FT /db_xref="InterPro:IPR015655" FT /db_xref="UniProtKB/TrEMBL:A1K3V8" FT /protein_id="CAL93513.1" FT /translation="MVRPSRRAAFACHIGGRAEQQDRAACFTSRDGRNHLLVVADGMGG FT HQGGELASHVVMEVAERAWSALDGLPHAPASFLERVCQQAHAEIRLAGQARGLRPCSTL FT AALLVSPHRAWWSYVGDSRIYVFRDGRPLWRTEDHTVVQQLVRSGRISEAEVVDHPDRN FT KLLRGLGGDEPLRATHGQLRIDAATGFVLCTDGFWATTSTEEMAPLLSASDLAAACTNA FT VAAAAQRGGPESDNVTIAVLQPERRTQAVNHRQLWPLYGALGLALLLLFSRFFN" FT CDS 961167..962186 FT /transl_table=11 FT /locus_tag="azo0897" FT /product="hypothetical secreted protein" FT /function="no function" FT /note="Hypothetical secreted protein. Homology to pp3428 of FT P. putida of 26% (tremble:Q88HD2). Domain structure: 111 aa FT - 157 aa LysM; 232 aa - 313 aa TRP. Pfam: LysM domain; TRP. FT signal peptide. no TMHs" FT /db_xref="GOA:A1K3V9" FT /db_xref="InterPro:IPR002482" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="InterPro:IPR013105" FT /db_xref="InterPro:IPR018392" FT /db_xref="InterPro:IPR019734" FT /db_xref="UniProtKB/TrEMBL:A1K3V9" FT /protein_id="CAL93514.1" FT /translation="MDRIPRLAPFVFLLALHGCAGLGSGGNGTDSQGAVQPAAPAAETP FT QAGARSVPVRDLRWIIDRLQDGQLAEGREALVGYLRREPGNPTARSLLQQIDTDPVALL FT GRNYTTYTLRPGETLGEIAGRHLGDPLRFVALARYNGIERARSVVAGQSLKIPAGRGGV FT AASAPPPATEADVVPAEERAEQFQKRIEAELAAGRIDSANAAIEQARAESPGGSGWNGW FT LDPLARRARALAFQQRGLAQLDRRQHEAAYDSLGQALALEPDLQPATRQRQAVRGKLVA FT EYHEAAVVRYRNQQLDEAIALWDKALKLDPGFEPARGYRTRALELKRRLQALGAAGNG" FT CDS complement(962191..963855) FT /transl_table=11 FT /locus_tag="azo0898" FT /product="putative serine/threonine protein kinase" FT /function="Serine/threonine protein kinase" FT /note="Putative serine/threonine protein kinase," FT /note="Family membership" FT /db_xref="GOA:A1K3W0" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:A1K3W0" FT /protein_id="CAL93515.1" FT /translation="MKTHLGRHTLHGELGRGAISVIYRGYDPDIGRMLAIKTLRREYAE FT REDYRERFLAEARVAGTLSHPGIVTIFDVGVSDGEPFIAMELLQGPTLAAFVEQRGRLP FT VRTVIRIAIQIADALDYAHRQAVVHQDIKPDNIAVTSLNGNVKVMDFGIARLRSGSAAS FT RGTAHVIAGTPDYMSPEQIRGKGIDGRSDLYSLGVVLYWLLAGHTPFHGDEVNELLRRI FT LNDAAPPCRPLDPDTPDALLDVVRTLLAKDPAERYQSGAELIDDLRRIDDTLAEREDAW FT AGRRIVPIRVRWTAVMGALVAITVALGLGVVYYKQNRAMERLALDYGLTLTQMLAVESA FT EDLLLDDGIAMQALVNEMARNREIVHLAISNRGGRVVASTDAERVGQPAAKPPTEQRLM FT ERGQQEVYSASDAEGNPYLLFESPIQYERHELGRLEVGLSTDALTAANRTTLAAMIAAM FT LVTLGTVFVGAYMLSRRLLVPIETLRVALGRIAQGRFDSRIRMHRSDEFERVFSAYNAM FT ADSLEARMLQARSGQAEGRPRRRGAGAAAPEPTEFVP" FT CDS complement(963863..964384) FT /transl_table=11 FT /locus_tag="azo0899" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No good homology to a FT protein of similar size of the data bank. Pfam: FHA domain FT (PF00498). The forkhead-associated (FHA) domain is a FT putative nuclear signalling domain found in a variety of FT otherwise unrelated proteins. The FHA domain comprise FT approximately 55 to 75 amino acids and contains three FT highly conserved blocks separated by divergent spacer FT regions.To date, genes encoding FHA-containing proteins FT have been identified in eubacterial and eukaryotic but not FT archaeal genomes. The domain is present in a diverse range FT of proteins, such as kinases, phosphatases, FT kinesins,transcription factors, RNA-binding proteins and FT metabolic enzymes which partake in many different cellular FT processes - DNA repair, signal transduction, vesicular FT transport and protein degradation are just a few examples. FT Interpro: Forkhead-associated (IPR000253). no signal FT peptide. 1 TMHs" FT /db_xref="InterPro:IPR000253" FT /db_xref="InterPro:IPR008984" FT /db_xref="UniProtKB/TrEMBL:A1K3W1" FT /protein_id="CAL93516.1" FT /translation="MGSLRSDPNSGRAGPQGTMLFSAGELDDVIASPSADQEGDLERAA FT LIGITPPFLDQRFVLKTGRTLIGRGEDNDIVLPDGSVSAQHAWILNENGRHRLMNMLST FT NGTFINDHKAHEAPLKDGDRIRLGRAEFVFRAGTAGPAPEAVRAPAVPLWVWGAAAMVV FT GLAVAAVLAL" FT CDS complement(964488..964871) FT /transl_table=11 FT /gene="apaG" FT /locus_tag="azo0900" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein affecting Mg2+/Co2+ FT transport" FT /note="ApaG protein. In S.typhimurium mutations in FT apaG/corD give a phenotype of low-level Co(2+) resistance. FT They also decrease Mg(2+) efflux but not influx via the FT corA Mg(2+) transport system. 57% DUF525. Pfam:PF04379; FT DUF525; 1." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR007474" FT /db_xref="InterPro:IPR023065" FT /db_xref="UniProtKB/Swiss-Prot:A1K3W2" FT /protein_id="CAL93517.1" FT /translation="MSKSETYRIEVEAVAEYVEAQSNPEDDHYVFAYNITIRNTGTVAA FT RLVSRHWVITDGTGHVQEVHGQGVVGEQPLLAPGESFRYTSGSVLETAVGTMHGSYQME FT ASDGHRFDAPIPAFMLAMPRVLH" FT CDS 965057..966433 FT /transl_table=11 FT /gene="purB" FT /locus_tag="azo0901" FT /product="adenylosuccinate lyase" FT /EC_number="4.3.2.2" FT /note="Adenylosuccinate lyase (Adenylosuccinase) (ASL)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3W3" FT /db_xref="InterPro:IPR000362" FT /db_xref="InterPro:IPR004769" FT /db_xref="InterPro:IPR008948" FT /db_xref="InterPro:IPR013539" FT /db_xref="InterPro:IPR020557" FT /db_xref="InterPro:IPR022761" FT /db_xref="InterPro:IPR024083" FT /db_xref="UniProtKB/TrEMBL:A1K3W3" FT /protein_id="CAL93518.1" FT /translation="MSLAAPSALTALSPLDGRYHGKVEGLRDHFSEHGLIRNRVKVEVE FT WLKALAADGALAEIAPFSAATIAELDSVVSAFAPADGEAVKAIEATTNHDVKAMEYWLK FT KRLGHNAEVMKVSEFIHFACTSEDINNTSHALMLKAGRDEVLLPAVDKVIARFRELAHQ FT LADLPMLSRTHGQPASPTTLGKEMANIAARLIRARAQIANVSLTAKFNGAVGNYNAHLS FT AWPEFDWEGFNKRFIESLGLEFNPYTIQIEPHDAMAELFDAIGRMNTILIDACRDIWMY FT ISFGYFKQKLKEGEVGSSTMPHKVNPIDFENAEGNLGIANAVLRHFSEKLPVSRMQRDL FT TDSTVLRNMGVGFGHTVLALDSALRGLGKLEAEPARLAADLAECWEVLAEPVQTVMRRF FT GIENPYEQLKAMTRGKGITREALQEFIGTLEIPQSERDRLLAMTPASYVGKAAELARRI FT " FT CDS 966512..966829 FT /transl_table=11 FT /locus_tag="azo0902" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to RS03757 FT of R.solanacearum of 44% (tremble:Q8XS71). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="InterPro:IPR016755" FT /db_xref="UniProtKB/TrEMBL:A1K3W4" FT /protein_id="CAL93519.1" FT /translation="MAFADTLKTLPGVSHLAAMNLVDAADAVVATIENKPGQAGSLAVY FT NHLAQLYGAITPEAAKKGLELYGEHSEDARLNPGKHPNIDRLIGLIERGESLRVKQVFA FT V" FT CDS complement(966923..967855) FT /transl_table=11 FT /gene="secF" FT /locus_tag="azo0903" FT /product="protein-export membrane protein SecF" FT /function="Preprotein translocase subunit SecF" FT /note="Protein-export membrane protein secF. Involved in FT protein export. Part of the prokaryotic protein FT translocation apparatus which comprise secA, secB, FT secD,secE, secF, secG and secY. InterPro: SecD/SecF/SecDF FT export membrane proteins 2A0604s01: protein-export membrane FT prot (Tigerfam) probable 6 TMHS no signal peptide Pfam: FT SecD-SecF" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3W5" FT /db_xref="InterPro:IPR005665" FT /db_xref="InterPro:IPR022645" FT /db_xref="InterPro:IPR022646" FT /db_xref="InterPro:IPR022813" FT /db_xref="UniProtKB/TrEMBL:A1K3W5" FT /protein_id="CAL93520.1" FT /translation="MEFFRIKKDIPFMRHALVFNVISLITFLLAVFFLATRGLHLSVEF FT TGGTLVEVSYSEAAELEPIRQSLAADGYTDVLVQHFGSTRDVLIRLPNREGADSKGVAE FT RVMATLEKSAGPKAELRRVEFVGPQVGKELASDGAMALLLVVVGIVIYLALRFEWRLGV FT ATIIANLHDVIIILGFFAFFQWEFSLAVLAATLAVLGYSVNESVVVFDRVRETFRKKRN FT LSTEQVVDHAITSTISRTMITHGSTQMMVLSMLIFGGETLFYFALALTIGICFGIYSSV FT LVASPLAIWLGVSREQFVKPKKEKEEAVV" FT CDS complement(967876..969750) FT /transl_table=11 FT /gene="secD" FT /locus_tag="azo0904" FT /product="protein-export membrane protein SecD" FT /function="Preprotein translocase subunit SecD" FT /note="Protein-export membrane protein secD. Involved in FT protein export. InterPro: SecD/SecF/SecDF export membrane FT proteins 2A0604s01: protein-export membrane pr (tigrfam) FT probable 4 TMHs, no signal peptide" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3W6" FT /db_xref="InterPro:IPR005791" FT /db_xref="InterPro:IPR022645" FT /db_xref="InterPro:IPR022646" FT /db_xref="InterPro:IPR022813" FT /db_xref="UniProtKB/TrEMBL:A1K3W6" FT /protein_id="CAL93521.1" FT /translation="MNRYPLWKNILIGLALLWGLIYTLPNFYGEVPAVQVSSAKATLKL FT EPASVTDRVAAILQGAGIEHDGIFADANSVRARFASTELQLRAKDAIERAFNTDPQDPS FT YVVALNLLSASPSWLTSIHALPMYLGLDLRGGVHFLLQLDMPGALLKRLDALSGDLRTL FT MRDKNVRHAGITREGTTVVIRFREAAQREAARSAIQGSTADLQLVDRDDGSEDLKLIAT FT LTPQAQQTMREYAIKQNISTLHNRINELGVAEPVIQQQGAERIVVQLPGVQDVAKAKDI FT LGRTATLEVRMVDDTPGALEQALTGNVPFGTELYRERGRGPLLVKKQVVLTGERLTDAQ FT PGFDGQTNEAAVHLTLDAAGARIFRDLTRENVGKRMAILLIEKGKGEVVTAPVIRTEIG FT GGRVQISGSMNTVEANDVALLLRAGSLAAPMEIIEERTVGPSLGAENIAKGFHSTLWGF FT VAIAVFMCVYYAVFGLVSTLALAANLLLLVALLSLLQATLTLPGIAAMALALGMAIDAN FT VLINERIREELRNGVSPQAAIAAGYDRAFSTILDSSVTSLIAGIALLVFGSGPVRGFAV FT VHCLGLLTSMFSAILVSRMLINLIYGRRRKIDKLAIGQVWKPGNVAGN" FT CDS complement(969851..970180) FT /transl_table=11 FT /gene="yajC" FT /locus_tag="azo0905" FT /product="probable preprotein translocase subunit YajC" FT /note="Probable preprotein translocase subunit YajC. FT Homology to yajC of E. coli of 41% (sprot|YAJC_ECOLI) FT Involved in the sec-dependent protein transport through the FT inner membrane of bacteria. Tigrfam: yajC: preprotein FT translocase, YajC subunit Pfam: Uncharcterized secreted FT protein, YajC family (PF02699) Interpro: YajC (IPR003849) FT no signal peptide. 1 TMH" FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR003849" FT /db_xref="UniProtKB/TrEMBL:A1K3W7" FT /protein_id="CAL93522.1" FT /translation="MVLISNAYAQAAASQDPTGGLMGMLPLILMFVVLYFLMIRPQMKR FT AKEHKSMVEALAKGDEVVTQGGIAGRVAEIGENFIHLEVADKTNIVVQKQAVATVLPKG FT TLKTL" FT CDS 970362..971201 FT /transl_table=11 FT /locus_tag="azo0906" FT /product="conserved hypothetical signal transduction FT protein" FT /function="predicted signal transduction protein" FT /note="Conserved hypothetical signal transduction protein. FT Homology to Daro03002984 of Dechloromonas aromatica of 39% FT (gi|53729872|ref|ZP_00150342.2|(NBCI ENTREZ)). No domains FT predicted. No signal peptide. No TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR013976" FT /db_xref="UniProtKB/TrEMBL:A1K3W8" FT /protein_id="CAL93523.1" FT /translation="MDEEKELQELVARGIRIPPQPRVLVELAERLRDGNYDARGLAALV FT ASDPGIAAMLFKVARSGLFHTGRSPDSLEQVLVRLGLKQTVNLVRVVALTTAFPAERAA FT PLERFWVRAREIARFAAVVAEDRVSVCNIFPDQAYMAGIFLDCGVPVLMQRFPSYCQKL FT MENEGLDLPSLREEDQRYNVDHASIGYLVARHWGLPDFVAQAILHYGEVPREELGAVRS FT LVAILHMAIHCYHLLHGVHDAQWPRIGAEVVRELGIHPDELADYLADVRDSFEIAGA" FT CDS complement(971214..972326) FT /transl_table=11 FT /gene="tgt" FT /locus_tag="azo0907" FT /product="queuine tRNA-ribosyltransferase" FT /function="Queuine/archaeosine tRNA-ribosyltransferase" FT /EC_number="2.4.2.29" FT /note="Queuine tRNA-ribosyltransferase (EC 2.4.2.29) FT (tRNA-guanine transglycosylase) (Guanine insertion enzyme). FT Exchanges the guanine residue with FT 7-aminomethyl-7-deazaguanine in tRNAS with GU(N) anticodons FT (tRNA-Asp -Asn -His and -Tyr). After this exchange a FT cyclopentendiol moiety is attached to the 7-aminomethyl FT group of 7-deazaguanine resulting in the hypermodified FT nucleoside queuosine (Q) (7-(((45-cis- FT dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7- FT deazaguanosine)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3W9" FT /db_xref="InterPro:IPR002616" FT /db_xref="InterPro:IPR004803" FT /db_xref="UniProtKB/Swiss-Prot:A1K3W9" FT /protein_id="CAL93524.1" FT /translation="MQFELLSTSAGARRGRLTLAHGAVETPVFMPVGTYGTVKAMTPAM FT LSDVGAQICLGNTFHLWLRPGLDIVGAHGGLHRFMGWDKPILTDSGGFQVFSLGALRKI FT SEEGVKFASPIDGARLFLTPEISMQIQTVLNSDVVMIFDECTPYPATRDEAAKSMRLSR FT RWARRSRDEFDRLENANALFGIVQGGMYEDLRDESLGALQDIGFHGFAIGGLSVGEPKD FT DMARILAHTAPRLPADKPRYLMGVGTPEDIVDGIANGIDMFDCVMPTRNARNGWLFTRY FT GDLKIKNAVHKADTRPLDPSCSCYTCRNFSRSYLHHLHRAGEILGSMLNTVHNLHYYQT FT LTAELRDAIAADRFADYVTRFRSERATGAH" FT CDS complement(972316..973353) FT /transl_table=11 FT /gene="queA" FT /locus_tag="azo0908" FT /product="S-adenosylmethionine:tRNA FT ribosyltransferase-isomerase" FT /function="S-adenosylmethionine:tRNA-ribosyltransferase- FT isomerase (queuine synthetase)" FT /EC_number="5.-.-.-" FT /note="S-adenosylmethionine:tRNA FT ribosyltransferase-isomerase (EC 5.-.-.-) (Queuosine FT biosynthesis protein queA). Synthesizes oQ from preQ1 in a FT single S-adenosylmethionine-requiring step. The ribosyl FT moiety of AdoMet is transferred and isomerized to the FT epoxycyclopentane residue of oQ." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3X0" FT /db_xref="InterPro:IPR003699" FT /db_xref="UniProtKB/Swiss-Prot:A1K3X0" FT /protein_id="CAL93525.1" FT /translation="MTLSLQDFDYDLPPDLIAQAPLAERSASRLLVVDGDVLADRRFVD FT LPDFIRPGDLLVFNDTRVLHARLFGVKATGGQVEVLVERPIGAHEALAQIRASKSPKPG FT STLRLADAVDVTVLGRSGEFFHLRFPDDENVVDVLERYGKLPLPPYIQRAAGDADEARY FT QTVFARAPGSVAAPTAGLHFDDAVLDRLRARGAGCAWVTLHVGAGTFQPVRVDDLAQHR FT MHSERYVIPQETVEAIARTRANGGRVVAVGTTSMRALEAAAQAGPLAAGSGETDIFILP FT GFRFRVADMLVTNFHLPKSTLLMLVSAFSGTDVIRRAYAHAVASRYRFFSYGDAMLLTR FT NDHAI" FT tRNA 973414..973498 FT /gene="tRNA-Leu" FT /locus_tag="azo_tRNA_0010" FT /product="transfer RNA-Leu" FT /anticodon=(pos:973448..973450,aa:Leu) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS complement(973554..974405) FT /transl_table=11 FT /gene="nhaR" FT /locus_tag="azo0909" FT /product="transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="Transcriptional activator protein nhaR (Na+/H+ FT antiporter regulatory protein). Plays a role in the FT positive regulation of nhaA. Similar to SWISSPROT: FT sprot|NHAR_ECOLI (34% Escherichia coli, and Shigella FT flexneri, transcriptional activator protein NhaR (na+/h+ FT antiporter regulatory protein)) InterPro: IPR000847 FT HTH_LysR. IPR009058 Winged helix DNA-binding. Pfam: PF00126 FT Bacterial regulatory helix-turn-helix protein,lysR family." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3X1" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K3X1" FT /protein_id="CAL93526.1" FT /translation="MRASERSGLAPQTLSGQIATLEASLGVTLFRRQGRGLALTETGRM FT VLDYAEEIFRLGAELEDALSSRAAGRAVPFRVGVADVVPKAIAYVLLAPSMHLPEPMRI FT VCRENKLDQLLGELATHKLDVVLADSPLPPNMDVRGYSHKLGESPLGFFATPALAATLQ FT GPFPACLDRAPLLVPGTEAAVRGPLLRWLETHKVRPRIVGEFDDAALMRAFGEAGAGVF FT PSAMLIHDEVCRQHGVSCLGTATEVTESFYAISVERRLTHPATRAISSASPLAGEGTTT FT EG" FT CDS 974584..974925 FT /transl_table=11 FT /locus_tag="azo0910" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ebD81 FT Azoarcus sp. EbN1 of 64% (gnl|keqq|eba:ebD81(KEGG)). No FT domains predicted. No signal peptid. No TMHs" FT /db_xref="GOA:A1K3X2" FT /db_xref="InterPro:IPR003489" FT /db_xref="UniProtKB/TrEMBL:A1K3X2" FT /protein_id="CAL93527.1" FT /translation="MRIDLRCDGVEAAPGLQEYVTRRMSFAIGRFRDHIQWARIKLADV FT NGPRGGADKRCVVQLRLRNLPDVVFAITQLDVRAAVDEAADRVGRVLAQRLRRQRNPRA FT ALAISQAPA" FT CDS 974987..975652 FT /transl_table=11 FT /gene="yccA" FT /locus_tag="azo0911" FT /product="probable carrier/transport protein" FT /function="Integral membrane protein interacts with FtsH" FT /note="Hypothetical protein PA2604. pir:D85624: 57% FT identity.73% similarity SIMILARITY:Belongs to the BI1 FT family. InterPro:Uncharacterized protein family UPF0005 FT IPR006213; Bax_inhbtr1. IPR006214; UPF0005. Pfam:ZIP: Zinc FT transporter Probable glutamatereceptor Signal peptide FT present (SignalP predicted) and transmembrane helices 7 FT (TMHMM predicted) Pfam:PF01027; UPF0005; InterPro: FT Uncharacterized protein family UPF0005 2_A_01_02: Multidrug FT resistance protein" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3X3" FT /db_xref="InterPro:IPR006214" FT /db_xref="UniProtKB/TrEMBL:A1K3X3" FT /protein_id="CAL93528.1" FT /translation="MENRVTALGRSEASTLSTNKVIRNTYMLLSMTLAFSALTAGVSLS FT LGLPHPGILITLVGYFGLLFLTTKFRNSGLGVLFVFALTGFMGYTLGPILSYYLALPNG FT SQVVMQAMGGTAAIFLGLSAYALTTRKDFSFMGGFLMVGILVAFLAGLGAVFFEMPGLS FT LAVSAMFVLLMSGLILFETSNIIHGGETNYVMATVSLYVSIYNLFTSLLHLLGFASND" FT CDS 975796..977517 FT /transl_table=11 FT /gene="rosB" FT /locus_tag="azo0912" FT /product="putative Potassium/proton antiporter" FT /function="Kef-type K+ transport system predicted FT NAD-binding component" FT /note="Probable potassium antiporter, rosB. 38% FT HPr_SerP_S.IPR004771; K_eff.IPR006153; Na_H_porter. FT IPR003148; TrkA_N. Pfam:PF00999; Na_H_Exchanger; 1.PF02254; FT TrkA_N; 1. TIGRFAMs:TIGR00932; 2a37; 1. TMhelix: 12." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3X4" FT /db_xref="InterPro:IPR003148" FT /db_xref="InterPro:IPR006153" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K3X4" FT /protein_id="CAL93529.1" FT /translation="MPHDVSLIATLAVGFGLALLLGFIADRLRLPALVGYLLAGILIGP FT ATPGFVADVGIAGQLAEIGVMLLMFGVGLHFSLEDLLAVRRIALPGAVVQMAVATLLGM FT GMAALWGWNLGAGLIFGLSLSVASTVVLLKALETRGILETVNGRIAVGWLVVEDLAMVV FT VLVLLPPLAGLLGGTAEVEPSQPLWRTVGLTLLQVGAFVALMLLVGRRVLPWLLWQVAG FT SGSRELFTLGVIAAAVSIAFGAAQLFGVSFALGAFFAGMVMRESEFSHRAAQESLPLRD FT AFAVLFFVSVGMLFDPSVLVEYPLHVLGVVAVIIVGKSIAAAALVIAFRYPLNTALTVA FT ASLAQIGEFSFILAGLGMALGLLPAAGQSLILAGALISIAANPFVFATVRPAGKWMLDN FT WSVARRLALRADPLTELPMSTERDFLEGQVVLVGYGRVGRRIAEALQARDIPYVVAEQN FT RERVDQLRKSGVAAVFGDAAHPAVLIQAHIAHAAMLVVATPKTIDVRKMAETARTLNPG FT IEIILRTHSEDDAELLARENIGRVFFGEEELAKGMAGHVVARFAPAPATHRPAQHA" FT CDS complement(977524..978858) FT /transl_table=11 FT /gene="ytfL2" FT /locus_tag="azo0913" FT /product="probable hemolysin" FT /function="Hemolysins and related proteins containing CBS FT domains" FT /note="Hypothetical protein sll0260. CBS domains are found FT in the intracellular regions of a number of different FT integral membrane proteins. Two CBS domains are found in FT intracellular loops of several voltage gated chloride FT channels. A family of magnesium transporters also contain FT CBS domains. TREMBL:Q8KEZ1: 61% identity, 74% similarity FT InterPro: Domain of unknown function DUF21 FT InterPro:IPR002550; CBS. IPR000644: CBS_domain. IPR005170: FT CorC_transpt-asc. Pfam: PF00571; CBS; 2. PF03471: FT CorC_HlyC; 1. PF01595: DUF21; gntP: gluconate transporter FT Signal peptide present Transmembrane helices 3" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3X5" FT /db_xref="InterPro:IPR000644" FT /db_xref="InterPro:IPR002550" FT /db_xref="InterPro:IPR005170" FT /db_xref="InterPro:IPR016169" FT /db_xref="UniProtKB/TrEMBL:A1K3X5" FT /protein_id="CAL93530.1" FT /translation="MEVFILIALIILNGAFAMSEIALVTARRARLAKLAEEGDASAAVA FT IKLGEEPTRFLSTIQIGITSIGILNGIVGEAALAAPLAAWLQDLGLAQRPSEIGATVLV FT VMVITYISIVVGELVPKRVGQLNPEAIARLVAKPMNTLSIVSRPFVRLLSGSTAVLLRI FT LGQRDESAPGVTEEEIHALLEEGSVAGIIEKNEHAMVRNVFRLDDRQIGSLMVPRSDIV FT WLDVTRPLESNLARMAESDHSRFPVCRGGLDDILGIISSKQLFNQTLKGGKADLTRHLE FT TPVYVPESLTGMELLDQFRASSSRMVFVIDEYGEVQGMVTLQDVMEAVTGEFQPHRLED FT AWAVQREDGSWLLDGLIPLPELKDRLELKSAPEEEKGRYHTLSGMIMWLLGRLPRTGDV FT TVWEQWRLEVVDLDGKRIDKILATRISNPEAGAPPQPATDTPEAP" FT CDS 979395..980357 FT /transl_table=11 FT /gene="terC" FT /locus_tag="azo0914" FT /product="putative tellurium resistance protein" FT /function="Membrane protein TerC possibly involved in FT tellurium resistance" FT /note="Tellurium resistance protein terC. Could conceivably FT alter the intracellular level of tellurium in a manner FT leading to resistance. Alternatively its presence in the FT membrane may provide a barrier to entry of the tellurium FT ions.32% TerC. Pfam: PF03741; TerC; 1. TMHelix:9." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3X6" FT /db_xref="InterPro:IPR005496" FT /db_xref="InterPro:IPR022369" FT /db_xref="UniProtKB/TrEMBL:A1K3X6" FT /protein_id="CAL93531.1" FT /translation="MESIGTWWMWAGFAFIVVAMLLVDLVVFKSGHQHRVSLREAAAWS FT LAWVTVALIFNAGLWWYLDATAGRAVANDKALSFLVGYLVEKSLAVDNVFVWMMIFSFF FT AVPLELQRRVLLYGIVGAVVMRTGMIFGGSWLITQFHWVLYIFGAFLVATGVKMAWVTE FT HQPDLARNPLVRWIRNHYPVTEQLEGERFFVVRQGVRHATPLLLALVLVEVSDVIFAVD FT SIPAIFAITTDPFIVLTSNLFAILGLRAMYFLLADLGNRFSLLRYGLALILVFIGTKML FT IVEWIKIPVAVSLGVVATILAVTVWLSVRRAAQAEGGAA" FT CDS 980435..981400 FT /transl_table=11 FT /gene="accA" FT /locus_tag="azo0915" FT /product="probable acetyl-coenzyme a carboxylase carboxyl FT transferase subunit alpha" FT /function="Acetyl-CoA carboxylase alpha subunit" FT /EC_number="6.4.1.2" FT /note="Function:-THIS PROTEIN IS A COMPONENT OF THE ACETYL FT COENZYME A CARBOXYLASE COMPLEX; FIRST BIOTIN CARBOXYLASE FT CATALYZES THE CARBOXYLATION OF THE CARRIER PROTEIN AND THEN FT THE TRANSCARBOXYLASE TRANSFERS THE CARBOXYL GROUP TO FORM FT MALONYL-COA (BY SIMILARITY). Identities = 207/313 (66%) FT Entry name:- SWISSPROT:ACCA_ECOLI Prim. accession # P30867 FT InterPro:- IPR001095; Ac-CoA_carboxylA. Pfam :-PF03255; FT ACCA; 1. Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K3X7" FT /db_xref="InterPro:IPR001095" FT /db_xref="InterPro:IPR011763" FT /db_xref="UniProtKB/Swiss-Prot:A1K3X7" FT /protein_id="CAL93532.1" FT /translation="MKTTFLDFEQPIAELEEKIEQLRFVQDDSAVDISEEIARLEVKSQ FT ALTKDLYAKLTPWQIAQVARHPQRPYTLDYVQHIFTDFEELHGDRAYADDKAIVGGLAR FT FNGQSCVIIGHQKGRDTKEKIARNFGMPRPEGYRKAMRLMKLAEKFGLPVFTFVDTPGA FT YPGIGAEERGQSEAIGHNLYVMAELKVPLICTVIGEGGSGGALAIAVGDQVMMMQYSTY FT SVISPEGCASILWKSAEKASEAAETMGITAARLKSLGLVDKVVNEPVGGAHRDHRAAAQ FT SLKRALAEALRQVDTLSPSELVEQRMEKLMGYGRFKEIAA" FT CDS 981412..982758 FT /transl_table=11 FT /gene="tilS" FT /locus_tag="azo0916" FT /product="putative tRNA(Ile)-lysidine synthetase" FT /function="predicted ATPase of the PP-loop superfamily FT implicated in cell cycle control" FT /note="Putative tRNA(Ile)-lysidine synthetase. Homology to FT tils of E.coli of 34% (gnl|keqq|eco:b0188(KEGG)). Pfam: FT PP-loop family. Tigrfam: tRNA(Ile)-lysidine synthetase. The FT only examples in which the wobble position of a tRNA must FT discriminate between G and A of mRNA are AUA (Ile) vs. AUG FT (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the FT wobble position of the tRNA(Ile) recognizing AUA is FT lysidine, a lysine derivative of cytidine. This family FT describes a protein domain found, apparently, in all FT bacteria in a single copy. Eukaryotic sequences appear to FT be organellar. The domain archictecture of this protein FT family is variable; some, including characterized proteins FT of E. coli and B. subtilis known to be tRNA(Ile)-lysidine FT synthetase, include a conserved 50-residue domain that many FT other members lack. This protein belongs to the ATP-binding FT PP-loop family ( PF01171). It appears in the literature and FT protein databases as TilS, YacA, and putative cell cycle FT protein MesJ (a misnomer). No signal peptide. No TMHs." FT /note="Family membership" FT /db_xref="GOA:A1K3X8" FT /db_xref="InterPro:IPR011063" FT /db_xref="InterPro:IPR012094" FT /db_xref="InterPro:IPR012795" FT /db_xref="InterPro:IPR012796" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR015262" FT /db_xref="InterPro:IPR020825" FT /db_xref="UniProtKB/Swiss-Prot:A1K3X8" FT /protein_id="CAL93533.1" FT /translation="MAVELAGPFAEVLRAAAIGPASRLCCALSGGVDSVVTLDLLTRLQ FT PRFGFTLTAVHVHHGLSPHADAWAQFCARLCAARGLTLAIRRVEVPTDTGQGLESAARA FT RRHAELVALPCDWLVFGHHQDDQAETVLFRLFRGSGLRGLGAMAAVEPGQHAMPGKLRP FT LLDIGRAGIVAYARAAGLEWIEDESNADCRFTRNALRHKVLPVVQAQFPAVAPTLARTA FT ALLREGADLLDDLARLDENACGGPVLAADVFASLPAARAANLLRWQTARMGARAPSRAR FT LGETLRQLREAPGPLRLPLGDLWCCAYQGRVWLERDDEAPLRAHLWCGESSLGWGAGQV FT RLSQGGGGAALRVAAGEAMLAPPAPGLRMRLGPGRPTRSFKNLCQEAGIPPWLRPRLPV FT LWVAGEPAWIGGIGIAAQFQCAEGEQGVVPAWVPASAAQQGQHLGQFDR" FT CDS complement(982714..983319) FT /transl_table=11 FT /locus_tag="azo0917" FT /product="two-component response regulator" FT /function="Response regulator" FT /note="C4-dicarboxylate transport transcriptional FT regulatory protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3X9" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:A1K3X9" FT /protein_id="CAL93534.1" FT /translation="MTQACAHIIDDDEAIRDALQWLFKTRSVNCRAWSSGEAFLGAWRP FT EWRGCIVLDIRMDGMSGLECFDALIERGCQLPVIFITGHGDVPMAVGALKKGAFDFIEK FT PFNDNQLVDLVEKAIQRDAERQRVAADRETVAARLATLTAREREVMDLILEGKFNKVIA FT DDLQISMRTVEAHRSRVFDKMEVRSAVELAQMLTLLRS" FT CDS complement(983320..985311) FT /transl_table=11 FT /gene="dctS" FT /locus_tag="azo0918" FT /product="two-component sensor kinase" FT /function="FOG: PAS/PAC domain" FT /EC_number="2.7.13.1" FT /note="C4-dicarboxylate transport sensor protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Y0" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="InterPro:IPR013767" FT /db_xref="UniProtKB/TrEMBL:A1K3Y0" FT /protein_id="CAL93535.1" FT /translation="MPTPPPPQLAAPPSEEGRRSRWVARLPYLALALFLGAIAALVWLT FT REYDEEEQRATLINDALWMEQNLRFQLDRNAAQLQQIAPDLLRTERLSGPTEAQLRQLL FT SPDRGLVQILWLDAEGRVRNSMPPQSEDKLIGETSGAVPSPDISRLARAVGRPVYGPAY FT PVLGDQTQFEAHVPVWGDEGFLGTVVGVYSLSDLVVRELPWWFSERYRVAVLDPDGREV FT ASKSKVAPLDPGRAYTIAFDPPGHGLTLQITPYKGETRWIPVLLSASMLLFAVIIVWSV FT WQLRRQLAARQAAEQAVRAESAYRRAMEDSLITGLRARDLSGRLTYVNSAFCRMTGYTA FT EELVGCKPPMPYWDPDHIAETQKLHEQIMAGGTSPEGVEVRLRRRNGERLDALVFEAPL FT IDAHGRHTGWMGSVLDITEQKRARELALQQEERLQATSRLVTMGEMASTLAHELNQPLA FT AIASYNTGCLNRLEADEFDRDELRDIHEKIGRQARRAGDIIRRVHDFVRRAEPRREALD FT LNEVIREALGLVEPDARKRRIHLVADLAADLPVVHADAVMIEQIIVNLVRNGMDAMQDT FT PEPNRSLRIGTRSAGAVVTVRVTDHGTGIDAETARHLFQPFFTTKQEGMGMGLNICRSI FT AELHHGRLGFEPAPDGGTIFTLTLPVDS" FT CDS 985540..986544 FT /transl_table=11 FT /gene="dctP2" FT /locus_tag="azo0919" FT /product="probable c4-dicarboxylate-binding periplasmic FT protein" FT /function="TRAP-type C4-dicarboxylate transport system FT periplasmic component" FT /note="TRAP-dicarboxylate transporter. Binds FT c4-dicarboxylates; part of the binding-protein-dependent FT transport system for uptake of C4-dicarboxylates. 70% FT TRAP_transptDctP. Pfam:PF03480; SBP_bac_7; 1. FT TIGRFAMs:TIGR00787; dctP; 1. Signal peptide: present. FT TMhelix:1" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Y1" FT /db_xref="InterPro:IPR004682" FT /db_xref="InterPro:IPR018389" FT /db_xref="UniProtKB/TrEMBL:A1K3Y1" FT /protein_id="CAL93536.1" FT /translation="MKVRALLLGLVAVGLSTTAAAADPIVIKFSHVVAQDTPKGKAADK FT FKELAEKYTAGAVKVEVYPNSTLYKDKEEMEALQLGAVQMLAPSLAKFGPLGVREFEVF FT DLPFIFDSYEDLHKVTYGQVGQQLFSKLEPKGIKGLAYWDNGFKSFSANSPIKKPEDLK FT GKKMRIQSSKVLEEQMRELKALPQVMAFSEVYQALQTGVVDGTENPISNLYTQKMHEVQ FT KHLAITDHGYLGYAVITNKKFWDGLPANVRTSLEKAMKESTEYANKIAKDENDQSLEMV FT KKSGKTEVTQLSKDERLAFKKALVPVHKKMESRIGAELIESIYKETGFDPAKL" FT CDS 986612..987310 FT /transl_table=11 FT /gene="dctQ2" FT /locus_tag="azo0920" FT /product="putative TRAP-type C4-dicarboxylate transport FT system, small permease" FT /function="TRAP-type C4-dicarboxylate transport system FT small permease component" FT /note="The dct locus encodes a high-affinity transport FT system for the C4-dicarboxylates malate,succinate, and FT fumarate. 45% DctQ. Pfam:PF04290; DctQ; 1. TMhelix:4." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR007387" FT /db_xref="UniProtKB/TrEMBL:A1K3Y2" FT /protein_id="CAL93537.1" FT /translation="MVKILDRLEEFIIGTLMAVATVVIFVSVVHRYASGFAIPGLQDWL FT LDMNFGWAQEFCIILFVWMAKFGAAYGVRTGIHVGVDILINKLSGAPRKLMVQVGLVCG FT VIFTGLIGIFGALFVWENGMAYETLSLLGRDTGSFFEGPITPDLEWPTWIVYSAVPLGS FT FLMCFRFLQVMVSFARTGELPTHDHGHVEGLDEDQDPNVLLEGEAITIGEDIAHGANGS FT SARNDSAGRR" FT CDS 987325..988611 FT /transl_table=11 FT /gene="dctM2" FT /locus_tag="azo0921" FT /product="putative TRAP-type C4-dicarboxylate transport FT system, large permease" FT /function="TRAP-type C4-dicarboxylate transport system FT large permease component" FT /note="The dct locus encodes a high-affinity transport FT system for the C4-dicarboxylates malate,succinate, and FT fumarate. 60% DctM.IPR000252; DedA.IPR004681; FT TRAP_transptDctM. Pfam:PF06808; DctM; 1.PF00597; DedA; 1. FT TIGRFAMs:TIGR00786; dctM; 1. TMhelix:13. Signal peptide: FT present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Y3" FT /db_xref="InterPro:IPR004681" FT /db_xref="InterPro:IPR010656" FT /db_xref="UniProtKB/TrEMBL:A1K3Y3" FT /protein_id="CAL93538.1" FT /translation="MTNTLAIFGLLIVLMAIGMPVGVALGLTVLSFMFIFTDVPLESVA FT LKMFTGIEKFEIMAIPFFILAGNFLTHGGVARRMINFATSMVGHLRGGLGMSAVLACAL FT FAAVSGSSPATVVAIGSILIPAMIKQGYPLRFGAGVVASAGGLGILIPPSIVMVMYSVT FT TNTSVGALFMAGVIPGLLLAFMLGLCTWYVAHKNNYPTLPRTSWAERIKHFRKAFWGLM FT LIVVVMGGIYSGMFTPTEAAAMSAVYAFIIAVFVYKDLTFKQIPRVLLDSANMSAMLLF FT IIASAVLFSFILTSEQIPQRMADAIVASGMGPIGFLIVVNLLLLVAGALMEPSSIILIL FT APILFPVAVALGIDPIHFGVMIVVNMEIGMITPPVGLNLFVASGITKAGLTEMSKAVMP FT WLVTMLVFLMLITYIPSISTFLPKALGVM" FT CDS 988762..989409 FT /transl_table=11 FT /gene="dedA" FT /locus_tag="azo0922" FT /product="DedA protein" FT /function="uncharacterized membrane-associated protein" FT /note="DedA family protein, 57% identity(75% similarity) to FT TrEMBL;Q88QF4. TrEMBl;Q889M5(57% identity). FT SwissProt;P09548(55% identity) Has PF00597, DedA FT family;IPR000252;This family combines the DedA related FT proteins and YIAN/YGIK family. Members of this family are FT not functionally characterised. These proteins contain FT multiple predicted transmembrane regions." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR015414" FT /db_xref="UniProtKB/TrEMBL:A1K3Y4" FT /protein_id="CAL93539.1" FT /translation="MDIIASFIDLFLHLDRHLAELLADYGSWIYAILFLIVFCETGLVV FT MPFLPGDSLLFMAGALAAGGGMDPAVLIGVLFVAAVLGDSLNYTIGRRFGQRISQWPDS FT RFFNRKALERTHAFYERHGGKTIVIARFMPIIRTFAPFVAGMGQMEYRRFIAFNVLGAA FT LWVGPLIMAGYWFGNLPVVKNNLSIVVLGIIVLSLMPLVIGWLRQQAGRASA" FT CDS 989496..989921 FT /transl_table=11 FT /gene="ndk" FT /locus_tag="azo0923" FT /product="Nucleoside-diphosphate kinase" FT /EC_number="2.7.4.6" FT /note="Nucleoside diphosphate kinase (NDP kinase) FT (Nucleoside-2-P kinase). InterPro: Nucleoside diphosphate FT kinase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Y5" FT /db_xref="InterPro:IPR001564" FT /db_xref="InterPro:IPR023005" FT /db_xref="UniProtKB/Swiss-Prot:A1K3Y5" FT /protein_id="CAL93540.1" FT /translation="MAIERTLSIIKPDAVAKNVIGKIYQRFEDAGLKIIAAKMVHLSEQ FT EAGQFYAVHKERPFYKDLVSFMTSGPVMIQCLEGENAIAKNRELMGATDPKKADAGTIR FT ADFADSIDANAVHGSDAPETAAVEVAFFFPGMNVYSR" FT CDS 990009..991136 FT /transl_table=11 FT /locus_tag="azo0924" FT /product="conserved hypothetical protein" FT /function="predicted Fe-S-cluster redox enzyme" FT /note="Hypothetical protein yfgB. putative fe-s-cluster FT redox enzyme TREMBL:Q7NS85: 70% identity; 80% similarity. FT InterPro:IPR004383; Cons_hypoth48. IPR007197: Radical_SAM. FT Pfam:PF04055; Radical_SAM; No signal peptide. No FT transmembrane helices. TIGR00048: conserved hypothetical FT prote" FT /note="Function unclear" FT /db_xref="GOA:A1K3Y6" FT /db_xref="InterPro:IPR004383" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="UniProtKB/Swiss-Prot:A1K3Y6" FT /protein_id="CAL93541.1" FT /translation="MNTPVNLLDFDVDGLVDWFAGLGEKPFRARQVMRWMHREGCDDFD FT QMTDVAKSLRAKLKEIAVIRPPVPVRDSVSSDGTRKWLLDVGNANAVETVFIPETNRGT FT LCVSSQAGCALDCAFCSTGKQGFNRNLTAAEIIGQLWLANKLLGAARDAAADLEAGEKD FT NGRIISNVVMMGMGEPLANFDNVVTALRLMLDDHAYGLSRRRVTVSTSGIVPAIDRLRD FT ECPVALAVSLHASNDALRDRLVPINQKYPLRELMAACQRYLERAPRDFITFEYVMLDGV FT NDQEAHARELIALVRDVPCKFNLIPFNPFPNSGFQRSNAERIRRFAGILLDAGIVTTTR FT KTRGDDVDAACGQLAGQVQDKTRRTVRLKQSMEVR" FT CDS 991136..991951 FT /transl_table=11 FT /gene="pilF" FT /locus_tag="azo0925" FT /product="putative type 4 pilus biogenesis protein" FT /function="type 4 fimbrial biogenesis protein" FT /note="Type 4 pilus biogenesis protein," FT /note="Function unclear" FT /db_xref="GOA:A1K3Y7" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="InterPro:IPR013360" FT /db_xref="InterPro:IPR019734" FT /db_xref="UniProtKB/TrEMBL:A1K3Y7" FT /protein_id="CAL93542.1" FT /translation="MARKAASLLLMMLALSGCVTSTTRPGPAVSSGSGTGASRPLSELP FT PSSEAESRAKVHVDLGIAYFDVGRNDVALDEAAIALHEKPGYAPAYHLRALVYMAIDDV FT AAARENFQAALSAAPGDPDFNNSYGWFLCQQGREQEGLEHLARAARNPYYRYPTRPYNN FT AGLCHLRLGQDAAAEAQFVRAVQADPQNGEALFQLATLAYRRGDLEAARGHLVRLHQMK FT GPTAASAWLGLRTERRLGNRDAEASYAAQLRSRFSKSPEFQLMSQGKYE" FT CDS 991948..992856 FT /transl_table=11 FT /locus_tag="azo0926" FT /product="transcriptional regulator" FT /function="uncharacterized protein conserved in bacteria" FT /note="Transcriptional regulator , 36% identity to FT TrEMBL;Q88PJ8. Weak homology with other proteins spanning FT entire length. Prosite,PS50943; HTH_CROC1; The cro/C1-type FT HTH domain is a DNA-binding, helix-turn-helix (HTH) domain FT of about 50-60 residues present in transcriptional FT regulators. The domain is named after the transcriptional FT repressors cro and C1 of temperate bacteriophages 434 and FT lambda, respectively." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3Y8" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:A1K3Y8" FT /protein_id="CAL93543.1" FT /translation="MSNADPINPAPEGVPAPGQQLRLARESRGESRAEVAQSLKLSLRQ FT VEALEQGDYTALPGPAFVRGFMRNYARHLGLDPAPLLATLDGAEAGAPVELALVSNAAG FT EMPQGGAERRASRLGATLAVILLFAVLAGWYFDWFRTDPPPGLNSDVGETVLPPAGDVA FT VEPVPTEPAPVPAGGAPAPVEQQPGTGSAPAPAPAPPAPAPASAAPASAPLSAADGGAQ FT PATPQLLFRFGGESWVEVRDGSGAVIYSGLGSTGSTRSVQGRPPFALVVGNAKDVRLEF FT NGREIDLQPHTRVAVARLTVQ" FT CDS 992856..994103 FT /transl_table=11 FT /gene="gcpE" FT /locus_tag="azo0927" FT /product="probable 4-hydroxy-3-methylbut-2-en-1-yl FT diphosphate synthase" FT /function="Enzyme involved in the deoxyxylulose pathway of FT isoprenoid biosynthesis" FT /EC_number="1.17.4.3" FT /note="Probable 4-hydroxy-3-methylbut-2-en-1-yl diphosphate FT synthase (EC 1.17.4.3). Homology to gcpE of T. thermophilus FT of 61% (trembl|Q84GJ3(SRS)). Converts FT 2C-methyl-D-erythritol 24-cyclodiphosphate (ME-24cPP) into FT 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (By FT similarity). Tigrfam: gcpE: gcpE protein no signal peptide FT no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Y9" FT /db_xref="InterPro:IPR004588" FT /db_xref="InterPro:IPR016425" FT /db_xref="UniProtKB/TrEMBL:A1K3Y9" FT /protein_id="CAL93544.1" FT /translation="MVEQAFPFGSLPRRPTRQVRIGGVSVGSAAPVVVQSMTNTDTADV FT LGTAMQVAELARAGSELVRITVNNEAAAKAVPHIRDRLLALNMDVPLVGDFHYNGHKLL FT MDNPACAEALAKLRINPGNVGAGAKRDPQFAAIVEMACKYDKPVRIGVNWGSLDQSVLA FT RIMDENATRAEPRDAGAVMREALVVSALESAAKAEEYGLAGDRIILSAKVSSVQDLIAV FT YRDMARRCDYPLHLGLTEAGMGSKGIVASTAALSVLLQEGIGDTIRISLTPEPNGSRTQ FT EVVVAQEILQTMGLRAFTPMVTACPGCGRTTSTFFQELASGIQGYVREQMPLWREQYDG FT VETMTLAVMGCVVNGPGESKHANIGISLPGTGESPAAPVFVDGEKTVTLRGDNIAAEFK FT AIVDNYVATRYQKKAG" FT CDS 994138..995439 FT /transl_table=11 FT /gene="hisS" FT /locus_tag="azo0928" FT /product="Histidine--tRNA ligase." FT /function="Histidyl-tRNA synthetase" FT /EC_number="6.1.1.21" FT /note="Histidyl-tRNA synthetase. hisS, 75% idemtity to FT TrEMBL;Q5P7B4. Has Pfam;PF00587, tRNA synthetase class II FT core domain (G, H, P, S and T).Other tRNA synthetase FT sub-families are too disIPR002314,tRNA-synt_2b. Has FT Pfam;PF03129,Anticodon binding domain. This domain is found FT in histidyl, glycyl, threonyl and prolyl tRNA synthetases FT it is probably the anticodon binding domain" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Z0" FT /db_xref="InterPro:IPR002314" FT /db_xref="InterPro:IPR004154" FT /db_xref="InterPro:IPR004516" FT /db_xref="InterPro:IPR006195" FT /db_xref="InterPro:IPR015807" FT /db_xref="UniProtKB/Swiss-Prot:A1K3Z0" FT /protein_id="CAL93545.1" FT /translation="MSQTLQAVRGMNDILPDEAETWEHFEDIVRDWLKSYGYRPIRMPL FT VEPTPLFKRAIGEVTDIVEKEMYSFEDALNGEHLTLRPEGTASCVRAAIQHNLVAGHGP FT QRLYYHGPMFRHERPQKGRYRQFHQIGVEALGFAGPDIDAEHIIMCARLWDDLGLEDVS FT LEINSLGAAEERAQHRAALIAYLEQHRDKLDEDGQRRLYTNPLRILDTKNPDLQPVVEA FT APRLADYLGDESRAHFDAVQLFLKDAGIPYRINHRLVRGLDYYNRTVFEWVTTRLGAQG FT TVCAGGRYDGLVAQLGGKPQPAAGFAMGVERLLALWQESGGEPERQAPDVYVVHLGEAA FT QRLAFQAAEALRGHGFSAVLHCGGGSFKSQMKKADGSGASIAVVIGEDEAAAGEVGVKP FT LRGPGGQQRVTLAALAEAVGGVLYSDQGDDDGGV" FT CDS 995426..996070 FT /transl_table=11 FT /locus_tag="azo0929" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Putative membrane protein, 32% identity to FT TrEMBL;Q7WHN2. Signal Peptide present." FT /note="Specificity unclear" FT /db_xref="GOA:A1K3Z1" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR018704" FT /db_xref="UniProtKB/TrEMBL:A1K3Z1" FT /protein_id="CAL93546.1" FT /translation="MAVYDLEEQEQISELKAWWARYGKLVTALAVAAAVASVAWQGWRW FT YQNRQAAEAGGLYFAVQQAVTQQDAQKARELTGRLIDQFGGTVYAQLGALVSAGLQFSK FT GDLDNARAPLEWAAGQGKDESLRDLARLRLAAVLLQQGAHDQALAQLQREPGKAYRARF FT ADLRGDALAAQGKAADARTAYQAAITALEAEGDEAAMLREVVRVKLESLEA" FT CDS 996074..997216 FT /transl_table=11 FT /locus_tag="azo0930" FT /product="conserved hypothetical protein" FT /note="PQQ enzyme repeat protein, 40% identical(60% FT similarity)to TrEMBL;Q82XU7. Signal Peptide present. Has 6 FT copies SMART;SM00564, PQQ, beta-propeller repeat;IPR002372; FT Beta-propeller repeat occurrs in enzymes with FT pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like FT Ser/Thr kinases, and in prokaryotic dehydrogenases." FT /note="Specificity unclear" FT /db_xref="InterPro:IPR011047" FT /db_xref="InterPro:IPR017687" FT /db_xref="InterPro:IPR018391" FT /db_xref="UniProtKB/TrEMBL:A1K3Z2" FT /protein_id="CAL93547.1" FT /translation="MKVRALRMLPVLAAVLLTTACSSLNPFASSTPKPAKLTDLKPSAD FT LRTAWSVGVGDSGPYVFQPAVANGSVFAASHKGRVVRIEGGKEVWRADADTRLSAGVGS FT NGKLAVVVSTAGVVIAYDGATGAERWRAPVGAEVLAAPAVSDDLVLVRASDQRLIALAA FT KDGARRWIYQRANPPLALRSFSGVIMEGGVALAGFPGGKLVAVNLTNGGALWELTVASP FT RGATELERVADVAGVPVVGRREVCAVTYQGRAACFDASNGNALWTREFSSSVGMDRDTR FT FAVITDDKDAVQALDVYSGASVWKQDALARRGVSRPLIVGDYVAVGDVEGYVHVLRRED FT GAFAARDRADSSPIVADLRGYGRGFVVQTRSGDVVAYEVR" FT CDS 997232..998560 FT /transl_table=11 FT /gene="engA" FT /locus_tag="azo0931" FT /product="probable GTP-binding protein" FT /function="predicted GTPases" FT /note="GTP-binding protein engA. SPROT:Q8Y026: 65% FT identity, 78% similarity. GTPase of unknown physiological FT role. InterPro: GTP-binding protein (HSR1-related) FT FUNCTION: GTPase of unknown physiological role. SIMILARITY: FT Belongs to the era/trmE family of GTP-binding proteins. FT EngA subfamily InterPro:IPR003593; AAA_ATPase. IPR005289; FT GTP-bindding_dom. IPR006073; GTP1_OBG. IPR002917; MMR_HSR1. FT IPR005225; Small_GTP. Pfam: PF01926; MMR_HSR1; 1. thdF: FT tRNA modification GTPase TrmE No signal peptide. Absence of FT transmembrane helices" FT /note="Specificity unclear" FT /db_xref="GOA:A1K3Z3" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005225" FT /db_xref="InterPro:IPR006073" FT /db_xref="InterPro:IPR015946" FT /db_xref="InterPro:IPR016484" FT /db_xref="UniProtKB/Swiss-Prot:A1K3Z3" FT /protein_id="CAL93548.1" FT /translation="MKPTIVLVGRPNVGKSTLFNRLTKTRDALVADQPGLTRDRHYGVG FT RVGDRDYLVVDTAGFDPVAKDGIMHEMARQAEQAIAEADVLLFLVDGRAGRTPHDDQIA FT AHLRRAGRPVVVVVNKAEGLDRATVAADFHALGLGAPLAVSAAHGDGVKALVELVLAPF FT PADDEVEAAEDAGPRVAIVGRPNVGKSTLVNTLLGEERVIAFDMPGTTRDAIAIPFERG FT GKQYTLIDTAGLRRRGKVFEAVEKFSVIKTLQAIQEANVVVLVLDAAQDISDQDAHIAG FT FVLDTGRALVVAINKWDAVDDYRRARLKEDMARKLAFLSFARFHQISALRAEGIAALLK FT SVDGAYAAAMSNLSTPRLTRTMQAAVAKQAPPRHGSARPKLRYAHQGGMNPPVIVIHGN FT ALDHIPNSYVRFLERTFMEAFKLQGTPLRIQFRTAHNPYATKA" FT CDS 998667..998909 FT /transl_table=11 FT /gene="hfq" FT /locus_tag="azo0932" FT /product="RNA-binding regulatory protein" FT /function="uncharacterized host factor I protein" FT /note="Hfq protein. RNA-binding protein that stimulates the FT elongation of poly(A) tails (By similarity). TREMBL:Q7NS93: FT 87% identity, 94% similarity InterPro:IPR005001; Hfq. FT IPR001163; snRNP_Sm. Pfam: PF01423; LSM No transmembrane FT helices" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Z4" FT /db_xref="InterPro:IPR001163" FT /db_xref="InterPro:IPR005001" FT /db_xref="InterPro:IPR010920" FT /db_xref="UniProtKB/Swiss-Prot:A1K3Z4" FT /protein_id="CAL93549.1" FT /translation="MSNKGQLLQDPFLNTLRREHVPVSIYLVNGIKLQGQIESFDQYVV FT LLKNTVTQMVYKHAISTVVPARPVTIQQQDGEGGN" FT CDS 998991..1000130 FT /transl_table=11 FT /gene="hflX1" FT /locus_tag="azo0933" FT /product="probable GTP-binding subunit of protease specific FT for phage lambda" FT /function="GTPases" FT /EC_number="3.1.5.1" FT /note="GTP-binding protein hflX. trembl:Q7NS94: 66% FT identity; 78% similarity. InterPro:IPR006073; GTP1_OBG. FT These proteins contain GTP-binding motifs and are GTP1OBG FT Pfam:MMR_HSR1:GTPase of unknown function thdF: tRNA FT modification GTPase TrmE No Signal peptide present (SignalP FT predicted) Absence of transmembrane helices (TMHMM FT predicted)" FT /note="Family membership" FT /db_xref="GOA:A1K3Z5" FT /db_xref="InterPro:IPR006073" FT /db_xref="InterPro:IPR016496" FT /db_xref="UniProtKB/TrEMBL:A1K3Z5" FT /protein_id="CAL93550.1" FT /translation="MFDRPATGERAVLVQMDLGQGAIEERLSELELLATSAGATVEAVV FT RGRRSAPDSALFAGSGKVQEIAEALQAHGGDLVIFNHALSPAQQRNLERSLSCRVIDRT FT ALILDIFALRARSHEGKLQVELAQLQHLSTRLVRGWTHLERQKGGIGLRGPGEKQLETD FT RRLLGGRVKLLKSRLAQIEKQRRVRRRARERNDALTVSLVGYTNAGKSTLFNALTKAGA FT YAADQLFATLDTTSRRLFVGGGNVVLSDTVGFIRDLPHALVAAFEATLEETAHADVLLH FT VVDAASEDRDAQIEAVNRVLEEIGAAEVPQILVWNKIDLTHAAPAVERGDCDRIRRVFL FT SARTGEGLELLREALAELACRDALPGSGAADPVGNQPIQ" FT CDS 1000148..1001389 FT /transl_table=11 FT /gene="hflK" FT /locus_tag="azo0934" FT /product="putative Hflk protein" FT /function="Membrane protease subunits stomatin/prohibitin FT homologs" FT /note="Putative HflK protein. Homology to hflK of E. coli FT of 40% (sprot|HFLK_ECOLI). hflc and hflk govern the FT stability of phage lambda cii protein and have been FT proposed to encode or regulate a cii- specific protease. FT Pfam: SPFH domain/band 7 family no signal peptide 1 TMH" FT /note="Family membership" FT /db_xref="GOA:A1K3Z6" FT /db_xref="InterPro:IPR001107" FT /db_xref="InterPro:IPR001972" FT /db_xref="InterPro:IPR010201" FT /db_xref="InterPro:IPR020980" FT /db_xref="UniProtKB/TrEMBL:A1K3Z6" FT /protein_id="CAL93551.1" FT /translation="MSLNDPRWGGQGGNNGDRGDGNRGGNQGPPDLEEVWRDFNQRLSG FT MFGGKRQGRGSGGGGGDGPQLPNFSFRQFGGGLGALVALVLIVWLASGLYTVDANQRGV FT VLRLGKFTETTEPGLRWRLPYPFETHEIVDLTGVRTVEVGYRGSERNKVLRESLMLTDD FT ENIINIQFAVQYVLNSPENYVFNNRFPDESVAQAAETAMREIVGKSRMDFVLYEGREEI FT AATAHELMQRILDRYQTGILISRVTMQNAQPPEQVQAAFDDAVKAGQDRERQKNEGEAY FT ANDVIPRARGTASRLIEEANAYQARVVANAEGEASRFSQILAEYKRAPDVTRERLYLET FT MQQVLSSTSKVMIDAKGNGNLLFLPLDKLVQQAAAGTTGAGEPTASVPPPSPSSGLPDT FT RTRELTRNRDRGER" FT CDS 1001389..1002270 FT /transl_table=11 FT /gene="hflC" FT /locus_tag="azo0935" FT /product="conserved hypothetical protein HflC" FT /function="Membrane protease subunits stomatin/prohibitin FT homologs" FT /note="Conserved hypothetical protein. Homology to hflC of FT E. coli of 37% (sprot|HFLC_ECOLI). hflc and hflk govern the FT stability of phage lambda cii protein and have been FT proposed to encode or regulate a cii- specific protease. FT Pfam: SPFH domain/ Band 7 family signal peptide" FT /note="Family membership" FT /db_xref="GOA:A1K3Z7" FT /db_xref="InterPro:IPR001107" FT /db_xref="InterPro:IPR001972" FT /db_xref="InterPro:IPR010200" FT /db_xref="UniProtKB/TrEMBL:A1K3Z7" FT /protein_id="CAL93552.1" FT /translation="MRDKLSVIAGVVLFAIVLASMSLFTVDQRQYAIVFQLGQVKEVID FT APGLNFKLPLIQNVRYFEKRILTMDTPEPERFITSEKKNVLVDHFVKWRIIDPRLYYES FT VAGDETRARTRLNQTVNSGLREEFGKRTVHDVVSGARDQIMEDMRAKADQDARKIGVQI FT LDVRLKRVDLPNEVSESVYRRMEAERKRVANELRSQGAAEAEKIRADADRQREVLIAGA FT YREAQQVKGAGDAKATQIYAEAFGQSPDFYSFYRSLEAYRASFDGKDDVMVVDPSSDFF FT KFMKNSGGARRN" FT CDS 1002278..1002463 FT /transl_table=11 FT /locus_tag="azo0936" FT /product="conserved hypothetical membrane protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical membrane protein. Homology to FT NE1283 of Nitrosomonas europaea of 60% (trembl|Q82V27). No FT domains predicted. Signal peptide. 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR019201" FT /db_xref="UniProtKB/TrEMBL:A1K3Z8" FT /protein_id="CAL93553.1" FT /translation="MGSSVMMAFALMLIIEGILPFVAPTAWRETFLRLASMADGQIRFI FT GLSSMLLGLVLLFVFN" FT CDS 1002471..1003625 FT /transl_table=11 FT /gene="hisZ" FT /locus_tag="azo0937" FT /product="conserved hypothetical ATP FT phosphoribosyltransferase regulatory subunit" FT /function="ATP phosphoribosyltransferase involved in FT histidine biosynthesis" FT /note="Conserved hypothetical ATP phosphoribosyltransferase FT regulatory subunit Homology to hisZ of R. solanacearum of FT 57% (sprot|HISZ_RALSO). May allow the regulation of ATP FT phosphoribosyltransferase activity by histidine (By FT similarity). Tigrfam: hisS_second: histidyl-tRNA synthetase FT 2, putative no TNHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K3Z9" FT /db_xref="InterPro:IPR004516" FT /db_xref="InterPro:IPR004517" FT /db_xref="UniProtKB/Swiss-Prot:A1K3Z9" FT /protein_id="CAL93554.1" FT /translation="MRWVLPDHIQDALPSEAASLEALRRRLLDAFRVRGYQLVMPPLLE FT YLDSLTTGAGQDLKLRTFKLVDQVSGRTMGVRADMTPQVTRIDAHLLNRAGVSRLCYCG FT SVLHTLPSTLTATREPLQLGAELYGHAGIDADIEIVRLLADVLRLAEVPASRIDIGHVG FT LFHALAALAGMVPEREEELFDLLQAKDVPGLKEITVGVAEPVRTALLRLPALYGGAEVI FT DEAAACMPESAEIRAALDDLRRLAAALEDLPISFDLADLRGYHYHSGVVFAAYGGGSPA FT ALALGGRYDRVGEAFGRARPATGFSLDLRELALRLPAAVVPGAILAPLEGTAGLAAAVE FT ALRAAGEAVMSRLPGHEGTWNDAGCDRQLVMRQGAWVVEPLQGE" FT CDS 1003629..1004939 FT /transl_table=11 FT /gene="purA" FT /locus_tag="azo0938" FT /product="adenylosuccinate synthase" FT /EC_number="6.3.4.4" FT /note="Adenylosuccinate synthetase (IMP--aspartate ligase) FT (AdSS) (AMPSase). InterPro: Adenylosuccinate synthetase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K400" FT /db_xref="InterPro:IPR001114" FT /db_xref="InterPro:IPR018220" FT /db_xref="UniProtKB/Swiss-Prot:A1K400" FT /protein_id="CAL93555.1" FT /translation="MAKNVVVVGTQWGDEGKGKIVDWLTDHARGVVRFQGGHNAGHTLV FT IGQKEYKLNLVPSGIVREGVACYIGNGVVLDAHHLLSEIRVLEAGGIKVRERLRISPGC FT PLILGYHAALDRAREAAKAACDKIGTTGKGIGPTYEDKVARRALRVYDLFDRERFAAKL FT KANLEYHNFVLTQHLGAEPVGFDEVFDEAMADAAEILPMVADVSAELYAVNKAGGSLLF FT EGAQGTLLDIDHGTYPFVTSSNCVAGQAAAGSGVGPGRLHYVLGITKAYCTRVGGGPFP FT TELDIETPGTPGQQMSTKGREFGTVTGRKRRCGWLDLAALKRSIIINGVTGLCITKLDV FT LDGLAELKLCTGYMLDGKRIDLLPMGSEEVTRCEPIYETLSGWSGTTFGAQSWDALPQE FT ARAYLHRIEEICEIPIDVISTGPERDETILRRHPFGA" FT tRNA complement(1005095..1005179) FT /gene="tRNA-Leu" FT /locus_tag="azo_tRNA_0011" FT /product="transfer RNA-Leu" FT /anticodon=(pos:1005143..1005145,aa:Leu) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA complement(1005353..1005437) FT /gene="tRNA-Leu" FT /locus_tag="azo_tRNA_0012" FT /product="transfer RNA-Leu" FT /anticodon=(pos:1005401..1005403,aa:Leu) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 1005674..1008655 FT /transl_table=11 FT /gene="vacB" FT /locus_tag="azo0939" FT /product="exoribonuclease II" FT /function="Exoribonuclease R" FT /EC_number="3.1.13.1" FT /note="Ribonuclease R (EC 3.1.-.-) (RNase R) (VacB protein FT homolog). 3-exoribonuclease that participates in an FT essential cell function. Acts nonspecifically on poly(A) FT poly(U) and ribosomal RNAs. Similar to SWISSPROT: FT sprot|RNR_ECOLI (38% Escherichia coli, ribonuclease R; FT RNase R / VacB protein) InterPro: IPR004476 3_prime_RNase. FT IPR003029 RNA binding S1. Pfam: PF00773 RNB-like protein. FT TIGRFAM: TIGR00358 VacB and RNase II family 3'-5' FT exoribonucleases." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K401" FT /db_xref="InterPro:IPR001900" FT /db_xref="InterPro:IPR003029" FT /db_xref="InterPro:IPR004476" FT /db_xref="InterPro:IPR011129" FT /db_xref="InterPro:IPR011805" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR013223" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR022966" FT /db_xref="InterPro:IPR022967" FT /db_xref="UniProtKB/TrEMBL:A1K401" FT /protein_id="CAL93556.1" FT /translation="MQYDYPLPSREYIEQTLAEQGVPMSFAALAGALDIQPHELEHFER FT RLRAMERDGQLMRNRRDAFLLPDKADLIRGRVEGHPDGFGFLVRDDGQPDIFLGPKEMR FT EVLHGDRAIVRIAGQDRRGRPEGKVVEILERANSRVVGRVLNEHGVMIVVPENRRLAQD FT ILVAPGGKKVQPGQVVTVELIEQPTKYAQPIGRVTEVLGNYADPGMEIEIALRKHDLPF FT EFSSEAKADTRKLPTAVRKKDWAGREDITALPLVTIDGETAKDFDDAVYCERQGRGFRL FT VVAIADVSHYVEAGSALDRDAYERGNSVYFPRRVIPMLPEKLSNGLCSLNPQVERLCMV FT ADMGISMTGEIKAYRFYPAVMFSHARLTYTKVAAALYDNDATALDEIGGLLPHLENLDK FT LFRVLLKARAKRGAIDFETTETRMIFDDNGKIERIVPETRNDAHRLIEECMLAANVCAS FT DFLHKNDHPALYRVHEGPTPEKLEKLRTFLSEFGLPLGGGDEPRAKDYAALLDKVKDRP FT DAQLLQTVMLRSLRQAVYSPDNVGHFGLAYEAYTHFTSPIRRYPDLLVHRAIKAVLAGE FT HYAAGDWDDIGLHCSTTERRADEATRDVVAWLKCYYMQDKVGEEFEGSVSAVVPFGLFV FT ALDGIFIEGLLHVSELGADYFHYDEARHAMLGERTGKQFRLSDRVRVQLVRVDMETNKI FT DFRLVEGPLLAKPARKAAAPATEALVEVPQDAVVPVAPAGGRKRKPAVEKAPQRATETV FT ESPPPQTAPAKTKRARKAPVVEVAVEVTPTAAAEPAKAPATRTRRRRAGAVAETAAEAA FT GTVASQAETPADAVVAESAPKAKTRKTVKRAGQEDGVASAGESVPAEPAVPAKTRRKAA FT APAPVPEAKAKPATRARAAKPAAPAEAPATEQAPSAGAAPRKRAAPKTTAAARPAAEDV FT PTPKAPITKKGAKAKAPAAVAAGAATGAKAAARSRARATTTTETGDKAEPAKPATAKKG FT KRIG" FT CDS 1008648..1009412 FT /transl_table=11 FT /locus_tag="azo0940" FT /product="tRNA/rRNA methyltransferase" FT /function="rRNA methylases" FT /EC_number="2.1.1.-" FT /note="Specificity unclear" FT /db_xref="GOA:A1K402" FT /db_xref="InterPro:IPR001537" FT /db_xref="InterPro:IPR004441" FT /db_xref="InterPro:IPR013123" FT /db_xref="InterPro:IPR024915" FT /db_xref="UniProtKB/TrEMBL:A1K402" FT /protein_id="CAL93557.1" FT /translation="MAKPAESSATRLIYGFHAVSAKLRHAPEAVLEVYLSGDRKDARVK FT KFLATAEAIGTRIVPSEHERLDALVGTRRHQGVVARIDATRREIKLADVLDNLDENALI FT LVLDGVQDPHNLGACLRVADAAGAHAVVAPKDRAVGLNATAAKVASGAADTVPYITVTN FT LARALREMQEAGVWVVGAAGEAEKSVYQVDQRGPLAWVLGAEGDGLRRLTRDTCDELAQ FT IPMHGSVESLNVSVASGICLFEARRQRADVSA" FT CDS 1009579..1010880 FT /transl_table=11 FT /locus_tag="azo0941" FT /product="probable nitrate regulatory protein" FT /function="Response regulator with putative antiterminator FT output domain" FT /note="Probable nitrate regulatory protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K403" FT /db_xref="InterPro:IPR005561" FT /db_xref="InterPro:IPR010910" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR013587" FT /db_xref="UniProtKB/TrEMBL:A1K403" FT /protein_id="CAL93558.1" FT /translation="MKSALGFLVAAKRCEIHGLEQLEVTCGLVKGVSELVHMLQKERGA FT SNVFLASRGSRFADKRSEQVAATEAVEIQVRDLFDRLATDSARMAGGMRLFSRIAYVLH FT ALNALPALREQIEGLHLGPEQATHSFSELIAGLLAVVFEAADTAVDPAISRALVSLFNF FT MQGKELAGQERAVGAAALAAGRFEAGEQQRMLHLIEAQERCFQLFIEFADPTLRTIWRN FT AQVAPEIAELERMRRIATTTPAGRPVDDTSQRWFDCATARIDVMRQVEDCATNALLQLC FT ENTLAAARTELAEHAALLDTLEAAGGPDVLPPAALSALVERAGVTAPAGAPAAPEALHA FT ADGLGPQLGRSVFELMQDQAQRLQTMSDELNTVRAALNERKVVERAKGLLMASRGLSEE FT EAYKLLRQTAMNQNRRLVEVAEATLALADVLRSE" FT CDS 1011215..1012474 FT /transl_table=11 FT /gene="nasF" FT /locus_tag="azo0942" FT /product="nitrate transport system, periplasmic-binding FT protein" FT /function="ABC-type nitrate/sulfonate/bicarbonate transport FT systems periplasmic components" FT /note="Part of the ABC transporter complex NasFED involved FT in nitrate import. 59% Similar to the putative FT periplasmic-binding protein NasF in Klebsiella oxytoca. FT TREMBL:Q48466 InterPro:IPR010067; SsuA_fam.IPR006311; Tat. FT TIGRFAMs:TIGR01728; SsuA_fam; 1.TIGR01409; TAT_signal_seq; FT 1. Signal peptide present." FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR019546" FT /db_xref="UniProtKB/TrEMBL:A1K404" FT /protein_id="CAL93559.1" FT /translation="MTKQTFTTPELSRRGFLKASAAAGTATLLSGLFPGGVWAAGSDAP FT EKKEIKVGFIPLTDCSSVVMAAAQKFDEKYGIKIVPSKEASWAAVRDKLVSGELDAAHV FT LYGLVYGVHLGIGGPKKDMAVLMTLNNNGQAITLSNQLKEKGVTDGASLKKVVAASPAG FT TYTFAQTFPTGTHAMWLNYWLAANGINPLQDVKSIVVPPPQMVANARVGNMHGYCVGEP FT WNQRAIVDGVGFTAVTTQDIWVDHPEKVLGTTGDWVTKNPNAARALTAAILDASRWIDA FT SIANRRTTAETVAARSYVNTDMDVILGRMLGRYENGLGKTWDDANAMKFFNDGAVNFPY FT LSDGMWFLTQHRRWGLIDKDPDYLGVAKAINRIDIYKQAATAANVALPKSDMRSSKLID FT GVVWDGKDPAKYAAGFKIKA" FT CDS 1012491..1013423 FT /transl_table=11 FT /gene="nasE" FT /locus_tag="azo0943" FT /product="putative nitrate transport system, permease FT protein" FT /function="ABC-type nitrate/sulfonate/bicarbonate transport FT system permease component" FT /note="Nitrate transport permease protein nasE. 41% Similar FT to the nitrate permease protein, nrtB in Synechococcus FT sp.Part of the ABC transporter complex nrtBCD involved in FT nitrate import.Probably responsible for the translocation FT of the substrate across the membrane. FT SWISSPROT:NRTB_SYNP7.P38044. InterPro:IPR000515; FT BPD_transp.IPR005889; NtrB. Pfam:PF00528; BPD_transp; 1. FT TIGRFAMs:TIGR01183; ntrB; 1. TMHelix: 4." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K405" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR005889" FT /db_xref="UniProtKB/TrEMBL:A1K405" FT /protein_id="CAL93560.1" FT /translation="MATATVTVEEAAAVAAPLESGPARSVAARNDKPAPAPVQAAPAAE FT PRASRAGEWLGAIVRAVLPPVIGLALLVGLWHLGTMNGGGLPSPAKTWNAAVVLFSDPF FT YQAGPNDQGIGWNVLSSLQRVGIGFGIAALVGIPAGFMLGRFAVLSQMMNPIISLLRPV FT SPLAWLPIGLLVFQRADPAATWTIFICSIWPMILNTAQGVTRVPQDYLNVARVLNLSEW FT KVFTKILFPAVLPYMLTGIRLSIGTAWLVIVAAEMLTGGVGIGFWVWDEWNNLKVEHII FT IAIFVIGTVGLILEQALMLIARRFNYESR" FT CDS 1013436..1014230 FT /transl_table=11 FT /gene="nasD" FT /locus_tag="azo0944" FT /product="putative nitrate transport system, ATP-binding FT protein" FT /function="ABC-type nitrate/sulfonate/bicarbonate transport FT system ATPase component" FT /EC_number="3.6.3.23" FT /note="Part of the ABC transporter complex nasFED involved FT in nitrate import. 64% Similar to the nitrate transport FT membrane protein, nasD in Klebsella oxytoca. Probably FT responsible for energy coupling to the transport system. FT SWISSPROT:NASD_KLEOX.P39459. InterPro:IPR003593; FT AAA_ATPase.IPR003439; ABC_transporter.IPR005890; NtrCD. FT Pfam:PF00005; ABC_tran; 1. TIGRFAMs:TIGR01184; ntrCD; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K406" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005890" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K406" FT /protein_id="CAL93561.1" FT /translation="MSKKIVQIEKVSQTFETKKGKFTALRDIHLDIHEGESISLIGHSG FT CGKSTLLNLIAGLTRPTSGVMLCDGREIAGPGPERAVVFQNHSLLPWLTCFDNVYLAVE FT RVFARKEGKAKLKQRTHEALALVGLTHAENKYPHEISGGMKQRVGIARALSMQPRILLM FT DEPFGALDALTRANLQDELMKILAATKATMVMVTHDVDEAVLLSDRVVMLTNGPAATIG FT EILEVKLERPRDRLALAHDPQFGECRAAIMEFLYQKQLRVAA" FT CDS 1014601..1015365 FT /transl_table=11 FT /gene="cobA1" FT /locus_tag="azo0945" FT /product="Uroporphyrin-III C-methyltransferase." FT /function="Uroporphyrinogen-III methylase" FT /EC_number="2.1.1.107" FT /note="Uroporphyrin-III C-methyltransferase (EC 2.1.1.107) FT (Urogen III methylase) (SUMT) (Uroporphyrinogen III FT methylase) (UROM). CATALYZES BOTH METHYLATIONS AT C-2 AND FT C-7 OF UROGEN III LEADING TO PRECORRIN-1 AND PRECORRIN-2; FT THEIR OXIDATIVE ESTERIFICATION GIVES RESPECTIVELY FACTOR I FT OCTAMETHYL ESTER AND SIROHYDROCHLORIN (BY SIMILARITY). FT dph5: diphthine synthase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K407" FT /db_xref="InterPro:IPR000878" FT /db_xref="InterPro:IPR003043" FT /db_xref="InterPro:IPR006366" FT /db_xref="InterPro:IPR014776" FT /db_xref="InterPro:IPR014777" FT /db_xref="UniProtKB/TrEMBL:A1K407" FT /protein_id="CAL93562.1" FT /translation="MAKVTLVGAGPGAADLLTVRAVRAIGQADVLLADALVTEEVLALA FT KPGARVLRVGKRGGMKSTAQDFIHRVMARYARRGCAVARVKGGDPFLFGRGGEEAEYLE FT ALGIEVEVVPGLTSGIAVPAAVGIPVTHRAHTHGVTLVTGTAGDGRDEPNWAALAKCGT FT TLVIYMGLGRLLNIVARLIAAGMPPDTPAAAIASGTLPGQRHVKGTLADLPLRVTAEGL FT SSPAIIVVGEVAALARVPGLAMDESDVRALAA" FT CDS 1015380..1016627 FT /transl_table=11 FT /gene="nasC" FT /locus_tag="azo0946" FT /product="putative nitrate reductase small subunit" FT /function="NAD(P)H-nitrite reductase" FT /note="Putative nitrate reducatse small subunit. Homology FT to nasC of K. oxytoca of 38% (trembl|Q48467). NasC probably FT mediates electron transfer from NADH to NasA, the nitrate FT reductase. InterPro: FAD-dependent pyridine FT nucleotide-disulphide oxidoreductase (IPR001327) Pfam: FT Pyridine nucleotide-disulfide oxidoreductase no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K408" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K408" FT /protein_id="CAL93563.1" FT /translation="MRKQKLVMVGNGMAGVKTLEELLKHAPDAFEITVFGAEPHGNYNR FT ILLSPVLAGEMSLPEIMLNDIGWYRAHGITLHAGRRVVEIDRARRIVRADDGTEAAYDR FT LLLATGSAPFILPVPGRELPGVIAYRDIADTEAMIDAARQHRHAVVIGAGLLGLEAANG FT LVLRGMDVTVVHLGGWIMDRQLDQPAAELLQASLEAKGMRFRLQAQTAALLPGTGGRVA FT AVQLQDGSTLPADLVVMAAGIRPNTALAEAAKLRCERGIVVHDTLQTVTDPRIYAVGEC FT VNHRGTAYGLVAPLFEQARVCANHLAGHGIGRYTGSVTSTKLKVTGVDVFSAGDFMGGE FT GCDEIVLHDRAGGIYKKLVLKENRLAGAVMVGDTADGAWYFQLVREGGDVSALRDHMMF FT GQRFTQSQLAGAACPG" FT CDS 1016664..1019438 FT /transl_table=11 FT /gene="nasA" FT /locus_tag="azo0947" FT /product="probable nitrate reductase" FT /function="Anaerobic dehydrogenases typically FT selenocysteine-containing" FT /EC_number="1.7.99.4" FT /note="Probable Nitrate reductase. Homology to nasA of K. FT oxytoca of 41% (sprot|NASA_KLEOX). Nitrate reductase is a FT key enzyme involved in the first step of nitrate FT assimilation in plants fungi and bacteria. InterPro: FT Prokaryotic molybdopterin oxidoreductases (IPR006655) Pfam: FT Molybdopterin oxidoreductase; Molydopterin dinucleotide FT binding domain no signal peptide no TMH Helixturnhelix FT motif" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K409" FT /db_xref="InterPro:IPR006656" FT /db_xref="InterPro:IPR006657" FT /db_xref="InterPro:IPR006963" FT /db_xref="InterPro:IPR007419" FT /db_xref="InterPro:IPR009010" FT /db_xref="UniProtKB/TrEMBL:A1K409" FT /protein_id="CAL93564.1" FT /translation="MEPHMNLADLGLKANETRSVCCYCGTGCGVIVERDGGRITGVRGD FT PAHPANFGRLCTKGSTLHLAAAPGGRALYPELRSTRADSRRRVGWDEALDTAADRFAVI FT IREHGPDAVAFYISGQLLTEDYYVFNKLARALVGTNNIDSNSRLCMSSAVAGYKGTLGT FT DSVPASYEDLALADHLLITGANPAWAHPIVFRRIEEAKRANPDLFITVIDPRRTETAEF FT ADLHLQIAPGTDVLLYNAMLHVLLWEDLIDRDFIRDHTSGFDALREQLADCSPAKIAGL FT CGVPADKIVEAARRFGKARGAVSLWCQGLNQSHHGVANNSALIHLHLATGQIGRPGAGP FT FSLTGQPNAMGGREVGAMATILPAHRDPANADDRADLARLWGVPALPEAPGLAAVQMFD FT AIGEGRIKAVWIACTNPAQSLPDQDKVRAALDKAEFVVVQEAFADTETVPYADLLLPAA FT SWGEKSGSVTNSERRVSRVRGVVPAPGEARPDWAIAADFARRLQARLAPAAAAGFDWAD FT EAAVFAEHVSLSAGRDCDMSGLSYGVLEALGPQQWPYPQGAGGGTPRLFTDGRFNTADG FT RARFNPVGFPVRHAPLPEPTDAAHPFVLTTGRLRDQWHGMSRTGKVAALWGHTPRAEVA FT VNPADLDRRGLAAGQLVKVASRRGALVLPVAADSGVAPGQAWIPMHWGGATLAQSGTNL FT VTSAATDPVSKQPALKQAAVSIAPVDFGWRAAWAAQARDGAEAVAWMAALQPRLAAFGY FT AALSLAGRERSVVVLQVADTAPAPAERLADIDQLFGCVAEDHAVLAFRDSRRGIDKRAR FT IADGTLVAIRLVGEVAAADWLIAAIVAGEPAEPLRPWLFAPLSRPPAGLARAERTVCNC FT FGIGEQQIREAIGGGADLDALQGALKCGTACGSCLPALRRMVAEGAVAEVAGA" FT CDS 1019477..1020664 FT /transl_table=11 FT /locus_tag="azo0948" FT /product="putative methyl-accepting chemotaxis protein" FT /function="Methyl-accepting chemotaxis protein" FT /note="Putative methyl-accepting chemotaxis protein," FT /note="Specificity unclear" FT /db_xref="GOA:A1K410" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004089" FT /db_xref="InterPro:IPR004090" FT /db_xref="UniProtKB/TrEMBL:A1K410" FT /protein_id="CAL93565.1" FT /translation="MTTMAMATAARARAVPWRPARGLLGLWGATVAATSVLFLAEGIAL FT QAVGALGMLAALVAALRAGGRFERRLAELDAFAAACAGGHFTARLTTPADDALTPLAEH FT LNAAARCIAQVLAELDGAGAELRNVSRETLADVAAGEAGVRSQRDITVSSAATLEQLIT FT SLAATRDAAADAAQAAEGAAREAARGEAEAGAVAAAMGAVAADVDAAADVATALAERSR FT RIEGIAATIGGIAARTNLLALNAAIEAARAGEAGRGFAVVADEVRQLADGSAAATAEIG FT SLIQEVLAEVDRLARVIGDTRRSAGDSCARAQAAASLLATIRDAAGQTQLRIREIAEAS FT AEQSIAGERIAGDVEQVARLADDNALRIGESGELARYQDELVGRLEERLGAYRYE" FT CDS 1020736..1021629 FT /transl_table=11 FT /locus_tag="azo0949" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT Daro03002329 of Dechloromonas aromatica of 40% FT (gi|53730441|ref|ZP_00348795.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR013587" FT /db_xref="UniProtKB/TrEMBL:A1K411" FT /protein_id="CAL93566.1" FT /translation="MMEWQMGMAAALGGAAALWALHRVFGAGAAAGGRRALAALGSVGR FT LTELIAQVQQHRGMSGAWLAGDASFANRLPARQAAVAALFDALVEDATREDFERLPCFG FT SAELEALQRDWQQLVEQLPRLSPEESFLRHCRLIAVVLGWLGALGEARIAQQGAANLAP FT AVRKAVADLPALAECLGQARALGSAVAARGRCAPVARVRLHFLVSRAGGLLARAAQGAG FT AGAARPVGAFLQALRERVLQGERVGMDAATCFRLGTEAVDAVYVWLAQERSGIEHALHG FT LPSARPRWGERAGVRG" FT CDS 1021632..1023464 FT /transl_table=11 FT /locus_tag="azo0950" FT /product="GGEF/EAL/PAS/PAC-domain containing protein" FT /function="predicted signal transduction protein containing FT a membrane domain an EAL and a GGDEF domain" FT /note="GGEF/EAL/PAS/PAC-domain containing protein," FT /db_xref="GOA:A1K412" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001633" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K412" FT /protein_id="CAL93567.1" FT /translation="MAALLLPALLAGACALALGLALRLRALHRQRDAAAAQAAEAELRF FT RSIFDNAVLGMYQTTEDGHYLAANQALADLYGYPTPAALMAGLSDIAGRLYVERGRRDD FT FKALIRARARVVDFESEVYRRDGERIWISENAHAVHGADGRFLYYEGSVEDISERRRHR FT TLLEHQATHDPVTGLPNRYLLQDRLDRAMGAARRRDERLMVAFIDLDNFKFVNDSMGHA FT VGDRLLVEMARRLQACVRETDTLARYGGDEFVLIISSAAAQAGPVQVLERVHDAVRQPL FT ALEGRDLSVGCSMGVAVYPRDGADLETLLRHADAAMYQAKAAGKGQFRFYEAGLNAAVQ FT ERLALESALRRTLENDSDEFQVAYQPKFDASGDVCGCEALARWHSTESGTVAPDRFIPL FT AEETGLIVLLTARVLHAACAEAVRWSGQGGAAPGVAVNISARHFRRDGQLAALVRAALE FT QSGLPPGRLQLELTESLFVGNVEETVAILGELKALGVTIAIDDFGTGYSSLAYLKRFPV FT DVLKIDRSFVGECDRADDARSITGAVLSLGRSLGLRVVAEGVERPAQAAYLLAHGCDEL FT QGYLYAQPMPAAALRDFLASYRGGRRAPALAAVG" FT CDS 1023516..1023875 FT /transl_table=11 FT /locus_tag="azo0951" FT /product="conserved hypothetical phosphomannose protein" FT /EC_number="5.3.1.8" FT /note="50%Cupin.IPR007113; Cupin_sup. Pfam:PF00190; Cupin; FT 1. 28%" FT /db_xref="GOA:A1K413" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR013096" FT /db_xref="InterPro:IPR014710" FT /db_xref="UniProtKB/TrEMBL:A1K413" FT /protein_id="CAL93568.1" FT /translation="MKTRLADCPAYVTKDGSEIRELLHPALHGARNQSLAEAVVAPGMR FT TVLHRHRRSEELYHVTAGSGIMTLGEDRFAVEVGDTVLIPPGTAHCIQAGEAAALHILC FT CCSPAYAHSDTELLE" FT CDS 1024028..1024933 FT /transl_table=11 FT /locus_tag="azo0952" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein, 38% identity (50% FT similarity) to TrEMBL;Q7WXG4 Signal Peptide Present.TMH not FT Present. Has PF04471:Restriction FT endonuclease;(IPR007560:Mrr_cat):Prokaryotic family found FT in type II restriction enzymes containing the hallmark FT (D/E)-(D/E)XK active site. Presence of catalytic residues FT implicates this region in the enzymatic cleavage of DNA. FT PF01396:Topoisomerase DNA binding C4 zinc finger;(IPR000380 FT DNA_tpisomrase):Prokaryotic topoisomerase I , otherwise FT known as relaxing enzyme,untwisting enzyme or swivelase, FT catalyses the ATP-independent breakage of single- stranded FT DNA, followed by passage and rejoining of another FT single-stranded DNA region [4]. This reaction brings about FT the conversion of one topological isomer of DNA into FT another: e.g.,relaxation of superhelical turns; FT interconversion of simple and knotted rings of FT single-stranded DNA; and intertwisting of single-stranded FT rings of complementary sequences." FT /note="Family membership" FT /db_xref="GOA:A1K414" FT /db_xref="InterPro:IPR007560" FT /db_xref="InterPro:IPR011335" FT /db_xref="InterPro:IPR011856" FT /db_xref="InterPro:IPR013498" FT /db_xref="UniProtKB/TrEMBL:A1K414" FT /protein_id="CAL93569.1" FT /translation="MAGRDREPHEAGRKGGAPGGAPVLFVLGGLVAAAVLAVLAISGAY FT LAVAVVTLTLLLFAAVLTGGPRETQDGGVEITTSRREPTASPGSRGPEPDELDRALASV FT YPSPPLSETRPPRPTVWSAEVLDRMEWKRFEDLCCAFYREKGIRAETTRLGADGGVDVR FT LFQDDADPARLTAIVQCKAHSRQVGVKPVRELRGVMAHEKVEKAFFMAPRGFTDEARAF FT AAENRITLLDGKLFLAMLQRLPAESAQRLLDFATAGDWTTPTCPSCGAPMTARKGQRGA FT FWGCSTYPRCRGLLPMRGAG" FT CDS complement(1024961..1025785) FT /transl_table=11 FT /gene="nfsA" FT /locus_tag="azo0953" FT /product="putative oxygen-insentive NADPH nitroreductase" FT /function="Nitroreductase" FT /EC_number="1.6.99.-" FT /note="Putative oxygen-insensitive NADPH nitroreductase. FT Homology to snrA of S. typhimurium of 37% FT (sprot|NFSA_SALTY) REDUCTION OF NITROAROMATIC COMPOUNDS FT USING NADH. REDUCES NITROFURAZONE BY A PING-PONG BI-BI FT MECHANISM POSSIBLY TO GENERATE A TWO-ELECTRON TRANSFER FT PRODUCT. MAJOR COMPONENT OF THE OXYGEN- INSENSITIVE FT NITROREDUCTASE ACTIVITY IN E.COLI. Pfam: Nitroreductase FT family no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K415" FT /db_xref="InterPro:IPR000415" FT /db_xref="InterPro:IPR016446" FT /db_xref="UniProtKB/TrEMBL:A1K415" FT /protein_id="CAL93570.1" FT /translation="MNQPDTLFQTRYGDAAARAPAAWSPVIEHLLGHRSVRAYLPDPVS FT EDELVAIVAAAQSAASSSNLQAWSVVAVRDPATRAALAECAGGQAHVRDAPLQLVWLAD FT LARLEHLALANERPSAALDYLEMFLVGVIDAALAAQNAAAAAESLGLATVYIGGMRNQP FT ERVAELLRLPSKVVAVFGMCVGRPDPAQPAEIKPRPPQSVVLHHETYTPLPAQDEGIAA FT YNGAMAQFYERQNMKVHGTWAVHSAKRVAGPESLSGRDRLVEALHNRGFTLK" FT CDS complement(1025891..1026424) FT /transl_table=11 FT /gene="isiB" FT /locus_tag="azo0954" FT /product="probable flavodoxin" FT /function="Flavodoxins" FT /note="Probable flavodoxin. Homology to isiB of FT Synechococcus sp. of 45% (pir|B47673) Flavodoxins are FT electron-transfer proteins that function in various FT electron transport systems. Flavodoxins bind one FMN FT molecule, which serves as a redox-active prosthetic group FT and are functionally interchangeable with ferredoxins. FT Pfam: Flavodoxin no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K416" FT /db_xref="InterPro:IPR001094" FT /db_xref="InterPro:IPR001226" FT /db_xref="InterPro:IPR008254" FT /db_xref="InterPro:IPR010086" FT /db_xref="UniProtKB/TrEMBL:A1K416" FT /protein_id="CAL93571.1" FT /translation="MSRIGIFYGSSSGVTKAAAEKLAGFLGEDRCDLYSMEEDFVDFDE FT MLDYDFLLFGCSTWGSGEVQNDWRDPLLDLDNDKPDFSGKTIAVFGAGDYVSHGEQFVS FT ALGILYDKFKARGATLVGSFPTEGYTYKYSFAERDGQFVGLPFDDINEADKTEARLQAW FT VEVLQAYLPEAEEA" FT CDS complement(1026770..1027678) FT /transl_table=11 FT /gene="gufA" FT /locus_tag="azo0955" FT /product="putative cation transporter protein" FT /function="predicted divalent heavy-metal cations FT transporter" FT /note="Putative GufA protein. 31% Zn_transpt_Zip.InterPro: FT ZIP Zinc transporter Pfam: PF02535; Zip; 1. TMHelix: 9. FT Signal peptide present." FT /note="Specificity unclear" FT /db_xref="GOA:A1K417" FT /db_xref="InterPro:IPR003689" FT /db_xref="UniProtKB/TrEMBL:A1K417" FT /protein_id="CAL93572.1" FT /translation="MVAKVARLHFMPASPASAARALAGWLIALTGLALLATRLAGEIGG FT GAIGGPVGDALAGGAMSAAATALGALPLLVMRRIGAGVQGLLLGFGAGVMLAASVFSLL FT LPAFDAAHALGTTGPAAVGVVAAGLALGAALLLVMDRALPHSHAPDGTRSATAVWLFVF FT AIAVHNIPEGLAIGVATGMNVTEAGSANAVATGISLQNVPEGLIVAIALAAAGYGRLFA FT FAVAAISGLIEPVAAVAGSMLVSTATALLPWGLAGAAGAMLFVVSHEIIPESHRRGHET FT LATAGLVAGFIAMLMMDRLLG" FT CDS complement(1027781..1029013) FT /transl_table=11 FT /gene="cfa1" FT /locus_tag="azo0956" FT /product="probable cyclopropane-fatty-acyl-phospholipid FT synthase" FT /function="Cyclopropane fatty acid synthase and related FT methyltransferases" FT /EC_number="2.1.1.79" FT /note="Probable cyclopropane-fatty-acyl-phospholipid FT synthase. Homology to cfa of E. coli of 54% FT (Sprot:CFA_ECOLI) TRANSFERS A METHYLENE GROUP FROM FT S-ADENOSYL-L-METHIONINE TO THE CIS DOUBLE BOND OF AN FT UNSATURATED FATTY ACID CHAIN RESULTING IN THE REPLACEMENT FT OF THE DOUBLE BOND WITH A METHYLENE BRIDGE. Pfam: FT Cyclopropane-fatty-acyl-phosphotlipid no signal peptide no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K418" FT /db_xref="InterPro:IPR003333" FT /db_xref="UniProtKB/TrEMBL:A1K418" FT /protein_id="CAL93573.1" FT /translation="MNSADTDRAASRPVAPPAYSRAHRGAAARRGGDDGARRAFAELLA FT LADVSVDGERPWDIQVHHPDTAARVLAQGSLGLGEAYMDGWWDCARLDEFFRRVLGAHL FT DEKVGTTSLMVQSLRARLFNLQNLRRAWHVGQTHYDLGNDFFEAMLDPHMAYTCGYWAS FT AGSLEEAQRAKLDLVCRKLELRPGMRLLDIGCGWGSLMKFAATHYGVQCVGLTISREQA FT EFGRARCAGLPVEFRLADYREFRPAEGEHFDRSASLGMFEHVGHKNHPAYFDAVRRCLP FT DDDPQALFLLHTIGKNLRRMPTDPWIDRYIFPNGDLPTLGQITDAAEDRFIIEDVHNFG FT ADYDRTLMAWHARFETAWPRFAERYGERFHRMWRYYLLACAGTFRARTTQLWQIVMSPT FT GTPGGYRRPLI" FT CDS 1029315..1031303 FT /transl_table=11 FT /gene="dnaX" FT /locus_tag="azo0957" FT /product="DNA polymerase III subunit Tau" FT /function="DNA polymerase III gamma/tau subunits" FT /EC_number="2.7.7.7" FT /note="DNA polymerase III subunit tau (EC 2.7.7.7) FT [Contains: DNA polymerase III subunit gamma]. The gamma FT chain seems to interact with the delta subunit to transfer FT the beta subunit on the DNA. InterPro: AAA-protein (ATPases FT associated with various cellular activities)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K419" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003959" FT /db_xref="InterPro:IPR008921" FT /db_xref="InterPro:IPR012763" FT /db_xref="InterPro:IPR022754" FT /db_xref="UniProtKB/TrEMBL:A1K419" FT /protein_id="CAL93574.1" FT /translation="MSYQVLARKWRPKSFGTLVGQEHVVRALSHALATGRLHHAYLFTG FT TRGVGKTTISRILAKALNCETGVTAEPCGQCEACRAIDADRFPDYVEMDAASNRGVEDM FT AALLDKAVYAPVQGRYKVYMIDEVHMLTGHAFNAMLKTLEEPPEHVKFILATTDPQKIP FT VTVLSRCLQFNLKQMPQGHIVEHLDRVLTAEAVPFEPPALRHIAKAANGSMRDALSLLD FT QAIAHGAGKVAEEQVTHMLGTVGDDHLHAVLEALAAADMAALLAVADGMEARSLSFDAA FT LQALASLLHRVALYQFAPAAITDPLERSRVEVHAAAFDAEFLQLAYQIAIHGREELPLA FT PDEYTGFTMTLLRLHAFRPEQPPALGSTPTGADGGAGGERRPLPARAPAPAAATPQMQS FT AGAGHPPNAVAATSRPVPPAATTAAPAPVSAAPVRQAPSSFAAPPAPAAPVAPPEGPAV FT SPPAGDVPPWEELPPEAQWDEGDRAAAGGAERFDEELNDAPPRPAPLAVVRPSTAPAVA FT PAADEAPGDAVLAAPQALAAGDWRSLVRALGLTGMLRELAQHCEWVGLDGEQLELRLSA FT THRHLLDINRSAPERLQEQLGAALGRTLRVRIVIGTIEGETPAQRDEIERRQRHAEAVA FT ALECDPFVRELIERFDATLLEDTVRPL" FT CDS 1031349..1031678 FT /transl_table=11 FT /locus_tag="azo0958" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="conserved hypothetical protein Pfam: Uncharacterized FT BCR, YbaB family" FT /db_xref="InterPro:IPR004401" FT /db_xref="UniProtKB/TrEMBL:A1K420" FT /protein_id="CAL93575.1" FT /translation="MIMMKGGIAGLMKQAQQMQDNMKKMQDQLASVEVEGQAGAGVVKV FT VMTCKYDVRRVSIDDAVMDDKEMLEDLVAAALNDAVRKVETTTQEKMAGFTAGLNLPPG FT FKLPF" FT CDS 1031759..1032358 FT /transl_table=11 FT /locus_tag="azo0959" FT /product="recombination protein RecR" FT /function="Recombinational DNA repair protein (RecF FT pathway)" FT /note="Region start changed from 1031918 to 1031759 (159 FT bases)" FT /db_xref="GOA:A1K421" FT /db_xref="InterPro:IPR000093" FT /db_xref="InterPro:IPR006171" FT /db_xref="InterPro:IPR023627" FT /db_xref="InterPro:IPR023628" FT /db_xref="UniProtKB/Swiss-Prot:A1K421" FT /protein_id="CAL93576.1" FT /translation="MSSPPSSLDELIAALRCLPGVGPKSAQRMAYHLLQRDQRGAARLA FT GALGHALEVLRHCQRCNNFSEEAVCQRCANPRRDPATLCVVEMPADLAMIEQTQSYNGL FT YYVLMGRLSPLDGVGPRELGLERLIARATDGEVKEVILATNFTNEGEATAHTVATLLGA FT RGVKVSRISRGVPVGGELEHTDTGTIAQALVERRAF" FT CDS 1032540..1033133 FT /transl_table=11 FT /gene="petA1" FT /locus_tag="azo0960" FT /product="probable ubiquinol-cytochrome c reductase FT iron-sulfur protein" FT /function="Rieske Fe-S protein" FT /EC_number="1.10.2.2" FT /note="Probable ubiquinol-cytochrome c reductase FT iron-sulfur protein (Rieske iron-sulfur protein) (RISP). FT Homology to petA of R. gelantinosus of 63% (trembl|Q93SY7). FT Component of the ubiquinol-cytochrome c reductase complex FT (complex III or cytochrome b-c1 complex) which is a FT respiratory chain that generates an electrochemical FT potential coupled to ATP synthesis. Pfam: Rieske [2Fe-2S] FT domain singal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K422" FT /db_xref="InterPro:IPR005805" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR006317" FT /db_xref="InterPro:IPR014349" FT /db_xref="InterPro:IPR017941" FT /db_xref="InterPro:IPR019470" FT /db_xref="UniProtKB/TrEMBL:A1K422" FT /protein_id="CAL93577.1" FT /translation="MSVEQKMDNGRRTLLLATSAAGGVAAVATAVPFVASLTPSERAKA FT AGAPVEVDVGKLAPGEMMTVEWRGKPVWILRRTPEMLASLDKTDDKVSDPQSDKLQQPE FT YAKNKHRSIKPEYLIAVGICTHLGCSPSDKFKVGAESGVGADWPGGFLCPCHGSQFDLA FT GRVYKSMPAPDNLEIPPHKYVADTTILVGEDGKA" FT CDS 1033137..1034405 FT /transl_table=11 FT /gene="petB" FT /locus_tag="azo0961" FT /product="ubiquinol-cytochrome c reductase cytochrome b FT protein" FT /function="Cytochrome b subunit of the bc complex" FT /note="Ubiquinol-cytochrome c reductase cytochrome b FT protein. Homology to petB of R. gelatinosus of 72% FT (trembl|Q93SY6). Component of the ubiquinol-cytochrome c FT reductase complex (complex III or cytochrome b-c1 complex) FT which is a respiratory chain that generates an FT electrochemical potential coupled to ATP synthesis (By FT similarity). Pfam: Cytochrome b (N-terminal)/b6/petB; FT cytochrome b (C-terminal)/b6/petD no signal peptide 10 FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K423" FT /db_xref="InterPro:IPR005797" FT /db_xref="InterPro:IPR005798" FT /db_xref="InterPro:IPR016174" FT /db_xref="InterPro:IPR016175" FT /db_xref="UniProtKB/TrEMBL:A1K423" FT /protein_id="CAL93578.1" FT /translation="MTTKSQALLNWVDERFPLTSSIKGHLTEYYAPKNFNFWYFFGSLA FT LLVLVIQIVTGIFLVMHYKPDASLNAAGVPVAFASVEYIMRDVPGGWLIRYLHSTGASA FT FFIVVYLHMFRGLLYGSYRKPRELIWIFGTLIFLALMAEAFMGYLLPWGQMSFWGAQVI FT VNLFSAIPLIGPDLSLVIRGDFVVSDATLNRFFSFHVIAVPLVLIGLVAAHIVALHEVG FT SNNPDGVEIKKKKDANGIPLDGIPFHPYYTVKDIVGVVAFLFFFSAVVFFAPEGGGYFL FT EFNNFIPADPLKTPPHIAPVWYFTPFYSILRAVTYPLFGLDAKFWGVVAMGASVVIIAF FT LPWLDRSPVKSVRYKGPIFKAALVVFVICFFILGYLGVLPPTPGRTLVSQICSVLYFAF FT FLAMPWYSKLDKCKSEPERVTFK" FT CDS 1034402..1035157 FT /transl_table=11 FT /gene="petC" FT /locus_tag="azo0962" FT /product="conserved hypothetical ubiquinol-cytochrome c FT reductase cytochrome c1 protein" FT /function="Cytochrome c1" FT /note="Conserved hypothetical ubiquinol-cytochrome c FT reductase cytochrome c1 protein. Homology to petC of R. FT solanacearum of 52% (trembl|Q8XVA4). Component of the FT ubiquinol-cytochrome c reductase complex (complex III or FT cytochrome b-c1 complex) which is a respiratory chain that FT generates an electrochemical potential coupled to ATP FT synthesis. c1 functions as an electron donor to cytochrome FT c. InterPro: Cytochrome c1 (IPR002326) Pfam: Cytochrome_c1 FT signal peptide 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K424" FT /db_xref="InterPro:IPR002326" FT /db_xref="InterPro:IPR009056" FT /db_xref="InterPro:IPR021157" FT /db_xref="UniProtKB/TrEMBL:A1K424" FT /protein_id="CAL93579.1" FT /translation="MKSRVMSFIKRVAAVAAFAPALAMAAGDVLHLDKAPVSKDPAALQ FT HGAKIFVNYCLNCHGASYLRYNRLQEIGLSEQLIRDNLLFTGEKTGDLMKIAMQRDEAK FT AWFGAAPPDLTVIARSRASEFGSGADWLYTYLRQFYRDPARPTGWNNVIFANVGMPHAL FT WQLQGEQVAKVTTDEHGAKHVELQLAKPGLLSVEDYDKTVADLVSFLVWMGEPVAEKRR FT SIGTVVLIFLAGLFVLSYALKKSFWKDIH" FT CDS 1035265..1035861 FT /transl_table=11 FT /gene="sspA2" FT /locus_tag="azo0963" FT /product="probable stringent starvation protein A" FT /function="Glutathione S-transferase" FT /note="Probable Stringent starvation protein A. Homology to FT sspA of E. coli of 43% (sprot|SSPA_ECOLI). FORMS AN FT EQUIMOLAR COMPLEX WITH THE RNA POLYMERASE HOLOENZYME (RNAP) FT BUT NOT WITH THE CORE ENZYME. IT IS SYNTHESIZED FT PREDOMINANTLY WHEN CELLS ARE EXPOSED TO AMINO ACID FT STARVATION AT WHICH TIME IT ACCOUNTS FOR OVER 50% OF THE FT TOTAL PROTEIN SYNTHESIZED. Pfam: Glutatione FT S-transferase,N-terminale domaine no TMHs" FT /note="Family membership" FT /db_xref="InterPro:IPR004045" FT /db_xref="InterPro:IPR004046" FT /db_xref="InterPro:IPR010987" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR017933" FT /db_xref="UniProtKB/TrEMBL:A1K425" FT /protein_id="CAL93580.1" FT /translation="MMNLYSGTTDPFSHRCRIVLFEKGMDFEVIDVDLYNKPEDIAVIN FT PYNRVPVLVDRDLVLYESNIINEYIDERFPHPQLMPPDPIMRARARQLLHTFEHELFSH FT IEALEANQKGVDKTRAHVRDHLVQLAPIFTKQKFMLGEEFSMLDVAIAPLLWRLEHYGI FT ELPKTAAPLMKYAERIFSRQGFIDALTPSEKVMRR" FT CDS 1035915..1036355 FT /transl_table=11 FT /gene="sspB" FT /locus_tag="azo0964" FT /product="putative stringent starvation protein B" FT /function="Stringent starvation protein B" FT /note="Putative stringent starvation protein B. Homology to FT sspB of E. coli of 38% (sprot|SSPB_ECOLI) Seems to act in FT concert with sspA in the regulation of several proteins FT during exponential and stationary-phase growth. The exact FT function of sspB is not yet known. Pfam: Stringent FT starvation protein B no signal peptide no TMHs" FT /db_xref="InterPro:IPR007481" FT /db_xref="UniProtKB/TrEMBL:A1K426" FT /protein_id="CAL93581.1" FT /translation="MSNISTKPYLIRAIYEWCTDQGYTPYIAAVVDEETRVPPGYARDG FT QIVLNVGQDATHQLHMDNDLITFQARFNGVVHSLVIPVGNVVAIYARENGHGMAFEVEG FT AAEADVAGDAPAASTPAPVPVESSTDGGSRPPPRGNHLKIVK" FT CDS complement(1036339..1037562) FT /transl_table=11 FT /locus_tag="azo0965" FT /product="glycosyltransferase" FT /function="Involved in the biosynthesis of an unidentified FT carbohydrate" FT /EC_number="2.4.-.-" FT /note="InterPro: Glycosyl transferases group 1" FT /note="Family membership" FT /db_xref="GOA:A1K427" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:A1K427" FT /protein_id="CAL93582.1" FT /translation="MNILMVSDVYFPRVNGVSTSIETFRRSLHQQGVRSTLIAPAYPGG FT GADDDGVLRIPSRFVPLDPEDRMMRSGHIAARADELAGEGFDLIHIHTPFVAHYAGLAL FT ARKLRLPCVATYHTFFEEYLFHYVPTLPRSWLRALARRFSRTQCNALHAVIVPSRAMAA FT ALLDYGVERPLEILPTGIPPDQFQGGDGRFFRSRYEIPADARLLLFVGRVAHEKNIGFL FT IEMIDHLRHTEPRALLLITGEGPALATLRNAVAQRGLERHVRFLGYLDRHSELHDCYRA FT ADLFVFASRTETQGLVLLEAMALGTPVVALAQMGTCDILEGETGCRIGPDDPAAFAALV FT ASLLSRPELLERLAEEARQRARHWHADDIAARLVRLYARWIDASGSPRRVPELTAGSAG FT RRRLTSRS" FT CDS 1037729..1038217 FT /transl_table=11 FT /locus_tag="azo0966" FT /product="Hemerythrin-like protein" FT /note="Hemerythrin-like protein, 49% Identity to FT SProt;Q8Y1B3. Has PF01814, Hemerythrin HHE cation binding FT domain; IPR002063, Hemerythrin; Iteration of the HHE family FT found it to be related to Hemerythrin. It also demonstrated FT that what has been described as a single domain in fact FT consists of two cation binding domains. Members of this FT family occur all across nature and are involved in a FT variety of processes. For instance, in Nereis diversicolor FT P80255 binds Cadmium so as to protect the organism from FT toxicity . However Hemerythrin is classically described as FT Oxygen-binding through two attached Fe2+ ions. And the FT bacterial Q7WX96 is a regulator of response to NO, which FT suggests yet another set-up for its metal ligands. In FT Staphylococcus aureus P72360 has been noted to be important FT when the organism switches to living in environments with FT low oxygen concentrations; perhaps this protein acts as an FT oxygen store or scavenger." FT /db_xref="GOA:A1K428" FT /db_xref="InterPro:IPR012312" FT /db_xref="InterPro:IPR012827" FT /db_xref="UniProtKB/TrEMBL:A1K428" FT /protein_id="CAL93583.1" FT /translation="MQQMEWGEQLALGLGRMDTTHREFVELYNLLAASEAEDFINRLDA FT FIVHTEAHFDQENRWMEQVNFPGCHRAEHDRVLTVMRDVRERAARGDAFLGRRLVEELP FT PWFENHVNGMDAALAFHLQTIGFDVEREAFIEGRQEGCGDAASGPCACSSAPAPSAAA" FT CDS complement(1038235..1039485) FT /transl_table=11 FT /gene="dadA1" FT /locus_tag="azo0967" FT /product="probable D-amino acid dehydrogenase small FT subunit" FT /function="Glycine/D-amino acid oxidases (deaminating)" FT /EC_number="1.4.99.1" FT /note="The L-alanine catabolic pathway proceeds in two FT steps: racemization of the L-isomer to D-alanine by alanine FT racemase and oxidative deamination of D-alanine to pyruvate FT and ammonia by D- amino acid dehydrogenase. Similar to FT trembl|Q7NRT8 (52%) and to sprot|DADA_ECOLI (40%). Pfam FT (PF01266): D-amino acid oxidase" FT /note="Specificity unclear" FT /db_xref="GOA:A1K429" FT /db_xref="InterPro:IPR006076" FT /db_xref="UniProtKB/TrEMBL:A1K429" FT /protein_id="CAL93584.1" FT /translation="MHVMVLGAGVTGVTTAWYLRQAGFEVSIVDRQPAPGMETSFANGG FT QISVSHPEPWANPSAPLTVLRWLGREDAPLRFRPHAQAAQWRWALSFLHECLPWRSRRN FT TAAIAALAMDSARRLRELRETAALHYDQRQRGILHLFYNRSSFASVAARVRELQHFGMD FT VRACSAAECVAIEPALGHVASTLRGGLYAPDDESGDAHLFTQALAERLREDGVRFHLNT FT RIERLSQTGGRIDGVEVRDEAGRTGILLADHYVLCLGSYGTALMARLGVRLPIYPVKGY FT SLTAAVIAPERAPEVSLTDESRRIVCSRLGDRLRVAGTAELDGFNTALRPERGRMLADW FT LNSRFPGAIDPAAATLWAGLRPATPGNVPLIGKSPFERLWYNTGHGTLGWTLACGSGAA FT TADLIAGRRPTPRFPFR" FT CDS 1039663..1040664 FT /transl_table=11 FT /gene="cbbF" FT /locus_tag="azo0968" FT /product="putative fructose-1,6-bisphosphatase" FT /function="Fructose-16-bisphosphatase" FT /EC_number="3.1.3.11" FT /note="Fructose-16-bisphosphatase FT cytosolic(D-fructose-16-bisphosphate 1-phosphohydrolase) FT (FBPase).Involved in the reaction: D-fructose FT 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + FT phosphate., 62% In_FB_phphtase. Pfam:PF00316; FBPase; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K430" FT /db_xref="InterPro:IPR000146" FT /db_xref="UniProtKB/Swiss-Prot:A1K430" FT /protein_id="CAL93585.1" FT /translation="MRRVTLTQFLIEQQRAGRVSADLRLLIEVVARAVKAISVNVSKGA FT LAGVLGEAGTDNVQGEAQKKLDVIANEILLQANEWGGHLAAMASEEVETVHQIPFDYPK FT GGYLLLFDPLDGSSNIDVNISVGTIFSVLRFPEGEAEPTEQSFMQPGREQVAAGYAVYG FT PSTQLVLTVGHGVHAFTLDREMGSFIYTHPFMTIPDDTHEFAINASNARFWEEPVQRYV FT GELQAGKTGPRGKDFNMRWVASMVADVHRILTRGGIFMYPLDEKCRAQGGKLRLMYEAN FT PMAMLVEQAGGAATTGRERILDLMPTKLHQRVPVILGSRNEVERVTAYHRES" FT CDS 1040676..1042403 FT /transl_table=11 FT /locus_tag="azo0969" FT /product="conserved hypothetical outer membrane protein" FT /function="predicted outer membrane protein" FT /note="conserved hypothetical outer membrane protein. FT Homology to ne0930 of N. europaea of 44% (trembl|Q82VX0) FT Pfam: Bacterial surface protein signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K431" FT /db_xref="InterPro:IPR000184" FT /db_xref="InterPro:IPR010827" FT /db_xref="UniProtKB/TrEMBL:A1K431" FT /protein_id="CAL93586.1" FT /translation="MRCSLRLATAVVLLCAAGVAGAQSPLEIELDVPDRLRPLLEQHVR FT ALRDDALRPEDPADRRALVRRTRKEVADLLATEGYFSPEITLDRGERWRLSVDPGPRTT FT VAAVELGFEGELGDDPAMAGRVEELRRAWSLQVGEPFRQADWDDAKRSLIDEVSRRRYA FT AARITASRAEVDPENAAVGLAVTVDSGPAFRLGELDVRGLEHLPADLVARYSTLQAGDF FT YDRDLLLAFQTSLQNAPYFASVVVDVEADPARAAAVPVRVQVSEALPRRVGFGVGFSSN FT TGYRVEGSFRDANLFGRAWELVSGLRLEQRRQSAYADVFLPPRDVRHRDSVGALMERSD FT LEGLRLSTQAVGVARSTVRGDIETRIALRYQQEELRPDGAKATEHDTLTANWTWTRRAV FT DNLLDPRRGFVLEFQVGGGSSIALAEQDFVRLYSRFVRYQPVGDTDNLILRLEGGVTLA FT PSRQGIPQDFLFRTGGAQTVRGYAYQSLGVREGDAVVGGRYLGVASAEYVHWFRPQWGS FT AFFVDAGDAADDRRGFDPKVGYGVGARWRSPAGPLAADLAWSQEERRLRLHFGVAIAF" FT CDS 1042491..1043462 FT /transl_table=11 FT /locus_tag="azo0970" FT /product="conserved hypothetical secreted protein" FT /function="ABC-type uncharacterized transport system FT periplasmic component" FT /note="Conserved hypothetical secreted protein. Homology to FT bb3356 of B. bronchiseptica of 83% (trembl|Q7WH54). Pfam: FT DUF534 This is a family of putative secreted proteins of FT unknown function. signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007487" FT /db_xref="UniProtKB/TrEMBL:A1K432" FT /protein_id="CAL93587.1" FT /translation="MSLIKPAARMLAALALCLPFATPVAAQQKSVAVTAIVEHPALDAV FT RDGVKDALAKAGYEDGKNLRWQYQSAQGNTGTAAQIARKFVGDQPDVIVAIATPSAQAV FT VAATKQVPVVYSGVTDPVAAQLVPGMGPSGSNVTGVSDMLALDKQVELIRRVVPAAKRV FT GMVYNPGEANSVVVVKALRELLPKHGMSLVEAAAPRSVDVGSAARSLTGKVDVIYTNTD FT NNVVSAYESLVKVGNDAKIPLVAADTDSVKRGAIAAVGINYRDLGEQTGRMVVRILKGE FT QPGAMASETSSKLELFVNPAAAKKQGVQLSDELLKSAARIIE" FT CDS 1043538..1044428 FT /transl_table=11 FT /locus_tag="azo0971" FT /product="conserved hypothetical ABC transporter, permease FT protein" FT /function="ABC-type uncharacterized transport system FT permease component" FT /note="Conserved hypothetical ABC transporter, permease FT protein. PART OF THE BINDING-PROTEIN-DEPENDENT TRANSPORT FT SYSTEM. PROBABLY RESPONSIBLE FOR THE TRANSLOCATION OF THE FT SUBSTRATE ACROSS THE MEMBRANE. InterPro: Binding-system FT dependent bacterial transporters (araH livH/limM families) FT (IPR001851) Pfam: Branched-chain amino acid transport FT system/permease component no signal peptide 8 TMHs 2A78: FT Carboxylate/Amino Acid/Amine Tran" FT /note="Specificity unclear" FT /db_xref="GOA:A1K433" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:A1K433" FT /protein_id="CAL93588.1" FT /translation="MSLYTLLGAFEIGLIFSLVALGVFISFRLLRFPDLTVDGSFPLGG FT AVAATLIASGHDPFVATAAAALAGALAGLLTGWLNVRLKIMDLLASILVMIALYSINLR FT VMGRPNVPLITEPTVFALLQPESLADYVFRPLLLVGVVVVAKLGLDWFFTTELGLAMRA FT TGSNPRMARAQGANTGRMLLGGMALSNALVGLAGALFAQTQGGADISMGVGTIVIGLAA FT VIVGESILPSRKLVLATLAVIAGAIVYRFFIALALNSDFIGLQAQDLNLVTAALVTVAL FT VLPMAKRRLPGRKGN" FT CDS 1044430..1045224 FT /transl_table=11 FT /locus_tag="azo0972" FT /product="probable ABC transporter, ATP-binding protein" FT /function="ABC-type uncharacterized transport system ATPase FT component" FT /note="Thiamine transport ATP-binding protein thiQ. PART OF FT THE BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM TBPA-THIPQ FT FOR THIAMINE AND TPP. PROBABLY RESPONSIBLE FOR ENERGY FT COUPLING TO THE TRANSPORT SYSTEM. TREMBL:Q7WH56: 84% FT identity, 92% similarity Description:putative FT abc-transporter atp-binding component InterPro: IPR003593; FT AAA_ATPase. IPR003439; ABC_transporter. Pfam:PF00005; FT ABC_tran; ProDom PD000006; ABC_transporter; 1. SMART FT SM00382; AAA recf: DNA replication and repair protein NO FT transmembrane helices" FT /note="Function unclear" FT /db_xref="GOA:A1K434" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K434" FT /protein_id="CAL93589.1" FT /translation="MLRAQDLHMTFNAGTPIETRALRGLSLEIPSGQFVTVIGSNGAGK FT STFLNAVSGDMAVDRGVIEIDGKDVTRRPVWARASRVARVFQDPMAGTCEDLSIEENMA FT LADLRGSGRGFGRAVKGARREAYRAHLATLGLGLENRLSDRIGLLSGGQRQAVSLLMAA FT LRPSRILLLDEHTAALDPRTADFVLQLTARIVAEHKLTTMMVTHSMRQALDVGERTVML FT HQGRVVLDVSGKEREGLDVTDLLAMFERVRGEKLDDDALLLG" FT CDS 1045436..1045726 FT /transl_table=11 FT /gene="groES1" FT /locus_tag="azo0973" FT /product="chaperonin GroES" FT /function="Co-chaperonin GroES (HSP10)" FT /note="Chaperonin GroES. Homolgy to groES of B. japonicum FT of 61% (sprot|CH11_BRAJA) Binds to Cpn60 in the presence of FT Mg-ATP and suppresses the ATPase activity of the latter. FT InterPro: Chaperonins cpn10 (10 Kd subunit)(IPR001476) FT Pfam: Chaperonin 10 kd subunit no signal peptide no TMH" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K435" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR018369" FT /db_xref="InterPro:IPR020818" FT /db_xref="UniProtKB/TrEMBL:A1K435" FT /protein_id="CAL93590.1" FT /translation="MKIRPLHDRVIVKRLEAERKTASGIVIPDSAGEKPDQGEVLAVGN FT GKILDDGKVRPMAVQVGDKVLFGKYAGQSVKVEGEELLVMREEDIMGVVEA" FT CDS 1045775..1047424 FT /transl_table=11 FT /gene="groEL1" FT /locus_tag="azo0974" FT /product="chaperonin GroEL" FT /function="Chaperonin GroEL (HSP60 family)" FT /EC_number="3.6.4.10" FT /note="Chaperonin GroEL. Homology to groEL of B. japonicum FT of 62% (SWISSPROT:CH61_BRAJA). Prevents misfolding and FT promotes the refolding and proper assembly of unfolded FT polypeptides generated under stress conditions (By FT similarity). no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K436" FT /db_xref="InterPro:IPR001844" FT /db_xref="InterPro:IPR002423" FT /db_xref="InterPro:IPR018370" FT /db_xref="UniProtKB/Swiss-Prot:A1K436" FT /protein_id="CAL93591.1" FT /translation="MAAKEVKFGDSARERMVAGVNVLANAVKVTLGPKGRNVVLERSFG FT APTVTKDGVSVAKEIELKDKFENMGAQMVKEVASKTSDIAGDGTTTATVLAQSIVREGM FT KFVAAGMNPMDLKRGIDKAVVATIEELKKLSKPCSTNKEIAQVGSISANSDADIGGIIA FT QAMEKVGKEGVITVEDGKSLNNELDVVEGMQFDRGYLSPYFINNPDKQVAILENPFVLL FT FDKKISNIRDLLPVLEQVAKAGRPLLIIAEDVDGEALATLVVNNIRGILKTCAVKAPGF FT GDRRKAMLEDIAILTGGQVIAEEVGLTLEKATLQDLGQAKRIEIGKENTIIIDGAGEAS FT RIEARVKQIRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDA FT LHATRAAVEEGIVPGGGVALLRARASLAGLKGDNHDQDAGIKIVLRAMEQPLREIVANA FT GDEASVVVNKVVEGSGNFGYNAATGEYGDMVEMGVLDPTKVTRTALQNAASVASLMLTT FT DCMVGELAEDKPAGGMPGMGGMGGMGGMDMGM" FT CDS 1047710..1048396 FT /transl_table=11 FT /gene="basR" FT /locus_tag="azo0975" FT /product="probable two-component response regulatory FT protein" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="Probable two-component response regulatory FT protein,Response_reg. IPR001867; Trans_reg_C. Pfam: FT PF00072; response_reg. PF00486; trans_reg_C. SMART: FT SM00448; REC." FT /note="Specificity unclear" FT /db_xref="GOA:A1K437" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:A1K437" FT /protein_id="CAL93592.1" FT /translation="MRILLAEDDPVIADGIVRALKRGGYAVDHVGNGAEADTAVASQPF FT DLLILDLGLPRLPGIEVLKRLRARKSALPVLILTAQDGVEDRVRGLDAGADDYLTKPFA FT LPELEARVRALTRRGTGQPRCIEVGNLSYDQADRVVKICGQVVELSAREIGLLEVFILR FT VGRLVSKDQLVDHLCGWGEEVSSNAIEVYVHRLRKKLEASGVRIVTVRGLGYCLENPDA FT APTQKV" FT CDS 1048371..1049858 FT /transl_table=11 FT /gene="basS" FT /locus_tag="azo0976" FT /product="putative two-component system histidine kinase" FT /function="Signal transduction histidine kinase" FT /EC_number="2.7.13.1" FT /note="Putative two-component system histidine kinase," FT /note="Specificity unclear" FT /db_xref="GOA:A1K438" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR003661" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR009082" FT /db_xref="InterPro:IPR013727" FT /db_xref="UniProtKB/TrEMBL:A1K438" FT /protein_id="CAL93593.1" FT /translation="MRPRRKKSDRNSAGRRVPGQPNSLFGEILDWMLAPLLFLWPISII FT VTHNVADNIANQPYDRALADSVRSLARLVVVEGGEISVQFPGPPRAFFRADQDDAVYYQ FT VANQSGETLTGDREIPWVPPPPRLLAEEVLFRDEVIHGEEARVAYQFLKAWPEPASPLV FT LVQVAETRNKRSDLASRVVTGVLLPQFAIIPLAVVLVWVGLTRGIAPLNRLQSLIRRRR FT PTDLSPIVPASVPEEVRPLIVAFNDMMARLEENLQAQQRFIADAAHQMRTPLTGLKMQT FT DLALLENDPEQLRASLTHIADSADRASHLINQLLSLARAEASFEKLYTVEPVDLEAVVR FT EVAQELFPRALAKGIDLGVESSGQVLQVEGNSVLLRELVKNLVDNAIKYTPAGGSVTAR FT TRVAGAPILEVEDTGVGIPEADRERVFERFYRVLGSGADGSGLGLPIVREIAELHRAAV FT TLSPNPAGQGTLAQVVFPRTHHPSPPPPVHGDFFPLG" FT CDS 1050037..1050345 FT /transl_table=11 FT /locus_tag="azo0977" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT XCC4058 of Xanthomonas campestris of 55% (trembl|Q8P3L3) FT Has PF04341, Protein of unknown function,DUF485; FT IPR007436;This family includes several putative integral FT membrane proteins. no signal peptide 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007436" FT /db_xref="UniProtKB/TrEMBL:A1K439" FT /protein_id="CAL93594.1" FT /translation="MQDDLVAKIVANPKYQRLTSARSSFGWLLTAIMMIVYYGYTAIIA FT FDKELFHQRIGDGVMTLGIPVGFGVIVFTIVITGIYVRRANAEFDALTQDIVKESGK" FT CDS 1050342..1052060 FT /transl_table=11 FT /locus_tag="azo0978" FT /product="conserved hypothetical sodium:solute symporter" FT /function="predicted symporter" FT /note="Conserved hypothetical sodium:solute symporter. FT Homology to an orf of R. capsulata of 81% (trembl|O68042). FT Sodium/substrate symport (or co-transport) is a widespread FT mechanism of solute transport across cytoplasmic membranes FT of pro- and eukaryotic cells. Thereby the energy stored in FT an inwardly directed electrochemical sodium gradient FT (sodium motive force, SMF) is used to drive solute FT accumulation against a concentration gradient. The solutes FT transported may be sugars, amino acids, FT nucleosides,inositols, vitamins, urea or anions, depending FT on the system. Tigrfam: sss: SSS sodium solute transporter FT superfamily Pfam: Sodium:solute transporter family signal FT peptide 13 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K440" FT /db_xref="InterPro:IPR001734" FT /db_xref="InterPro:IPR018212" FT /db_xref="InterPro:IPR019900" FT /db_xref="UniProtKB/TrEMBL:A1K440" FT /protein_id="CAL93595.1" FT /translation="MIGRFARISGGLALATLSAAALAAGADLGQAEKQATNWTAIIMFA FT VFVVATLFITKWAAAKTKSAADFYTAGGGITGFQNGLAIAGDYMSAASFLGISAAVMMN FT GYDGLIYSIGFLVGWPVITFLMAERLRNLGKFTFADVAAYRFKQTPIRAFAASGTLVVV FT AFYLIAQMVGAGQLIKLLFGLEYWMAVVIVGALMMVYVLFGGMTATTWVQIIKACLLLG FT GASFMAFMVLLNYGFSPEKLFAAAVEVKAGVATAAGKTPEEAATLGQAIMGPGSFIKDP FT ISAISFGMALMFGTAGLPHILMRFFTVPDAKEARKSVFWATTWIGYFYILTFIIGFGAI FT VLVSTNPQFLDAKGGLLGGGNMAAIHLANAVGGNIFLGFISAVAFATILAVVAGLTLSG FT ASAVSHDLYATVFKNGNADSAAELRVSRITTICLGVIAVVLGIAFEKQNIAFMVSLAFA FT IAASANFPVLFMSVLWKDCTTRGACWGGFLGLITAVGLTVVSPSVWEATLGNPKGSALF FT PYTSPALFSMAAGFLGIWLFSILDNSARAKEDRAGYLAQSVRSETGIGAAAASAH" FT CDS complement(1052174..1052845) FT /transl_table=11 FT /gene="tctD" FT /locus_tag="azo0979" FT /product="probable transcriptional regulatory protein" FT /function="Response regulators consisting of a CheY-like FT receiver domain and a winged-helix DNA-binding domain" FT /note="Probable transcriptional regulatory FT protein,Response_reg. IPR001867; Trans_reg_C. Pfam: FT PF00072; response_reg. PF00486; trans_reg_C. SMART: FT SM00448; REC. Transcriptional regulatory protein tctD. FT TRANSCRIPTIONAL ACTIVATOR OF THE TCTI TRICARBOXYLATE FT TRANSPORT SYSTEM OPERON." FT /note="Specificity unclear" FT /db_xref="GOA:A1K441" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K441" FT /protein_id="CAL93596.1" FT /translation="MHILVADDDDRFTRPLAAFLRTRGDQVTVAVDGTAADGLLQHSPF FT DFALVEVNLAGVNGYELVRRLRSRRQTTPVIFISARQALEDRIHGLDLGADDYVVKPAE FT ISEITARMRAVLRRGPYRIGDEMRFGPIMLDADGRLASLNGQALPLTGREWEILEALVA FT ADGRTVAKDRLQADSGGNAAEVYISRLRPRLEPAGVLIRTVRGFGYRLELQAVAGEDAP FT G" FT tRNA 1052967..1053042 FT /gene="tRNA-Phe" FT /locus_tag="azo_tRNA_0013" FT /product="transfer RNA-Phe" FT /anticodon=(pos:1053000..1053002,aa:Phe) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 1053183..1054436 FT /transl_table=11 FT /locus_tag="azo0980" FT /product="HemA protein" FT /function="Glutamyl-tRNA reductase" FT /EC_number="1.2.1.-" FT /note="Glutamyl-tRNA reductase (EC 1.2.1.-) (GluTR). FT catalytic activity: glutamyl-trna(glu) + nadph = FT glutamate-1- semialdehyde + nadp(+) + trna(glu). pathway: FT porphyrin biosynthesis by the c5 pathway; first step. FT similarity: belongs to the glutamyl-trna reductase family." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K442" FT /db_xref="InterPro:IPR000343" FT /db_xref="InterPro:IPR006151" FT /db_xref="InterPro:IPR015895" FT /db_xref="InterPro:IPR015896" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR018214" FT /db_xref="UniProtKB/Swiss-Prot:A1K442" FT /protein_id="CAL93597.1" FT /translation="MQLYALGLNHHTAPLAIRERVAFQPDRLDQALQALTDSRTVSEAA FT ILSTCNRTELYFAAEQPQRAADWLAGFHQLPLAQVSPYLYSYPQRDAVRHVFRVASGLD FT SMVLGEPQILGQVKEAARRAEEAGTLGTLLHKLFQNTFAVAKEVRSTTAIGANIVSMAA FT AAVHLTGRIFERVSDQHVLFIGAGEMIELCAAHFAGAGPRSMTVANRTEARAEALAARL FT GAQTMRLDAIADALPRFDVVVSCTASPLPIVGLGMVERAVKVRRHRPIVMVDLAVPRDV FT EPEVGQLDDVFLYTVDDLAQVVDAGIESRQQAVVEAEGIIDQRVDGFLHWLHARDAVPT FT IRALREHAETLRRGEIERALRQLAKGEDPQAVLDALSHGLTNKLMHGPTRFLTQAEGEG FT QAEASRVVQQLFNLSRHD" FT CDS 1054469..1055554 FT /transl_table=11 FT /gene="prfA" FT /locus_tag="azo0981" FT /product="peptide chain release factor" FT /function="Protein chain release factor A" FT /note="Peptide chain release factor 1 (RF-1). Peptide chain FT release factor 1 directs the termination of translation in FT response to the peptide chain termination codons UAG and FT UAA." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K443" FT /db_xref="InterPro:IPR000352" FT /db_xref="InterPro:IPR004373" FT /db_xref="InterPro:IPR005139" FT /db_xref="UniProtKB/Swiss-Prot:A1K443" FT /protein_id="CAL93598.1" FT /translation="MKQSIRDKLEHLAGRLAELDRELSSEDATRDMNAFRDLSRERAEL FT EPVVALYGAYRQAEQDCATARELLDDPEMQELGRSELEAGEARIAALDGDLQRALLPRD FT PNDERNLFLEIRAGTGGDEAALFAGDLLRMYSRYAERQRWRVEIVSSNPSDLGGYKEVI FT ARIVGAGAYSRLKFESGGHRVQRIPVTETQGRIHTSACTVAVMPEADELAAVEINPADL FT RIDTFRASGAGGQHINKTDSAVRITHLPTGLVVECQDDRSQHRNKAQAMAVLAARLNDA FT QLRARQSAEAATRRSLIGSGDRSERIRTYNFPQGRVTDHRINLTLYKLDAVMQGELDEL FT LAALVLEHQAEQLAALAEEGL" FT CDS 1055551..1056387 FT /transl_table=11 FT /gene="hemK" FT /locus_tag="azo0982" FT /product="HemK protein" FT /function="Methylase of polypeptide chain release factors" FT /EC_number="2.1.1.-" FT /note="Protein methyltransferase hemK (EC 2.1.1.-) FT (Protein-glutamine N- methyltransferase hemK) FT (Protein-(glutamine-N5) MTase hemK) (M.StyLTHemKP). FT Methylates the translation termination release factor RF1 FT on Gln-235 and RF2 on Gln-252." FT /note="Family membership" FT /db_xref="GOA:A1K444" FT /db_xref="InterPro:IPR002052" FT /db_xref="InterPro:IPR004556" FT /db_xref="InterPro:IPR007848" FT /db_xref="InterPro:IPR019874" FT /db_xref="UniProtKB/TrEMBL:A1K444" FT /protein_id="CAL93599.1" FT /translation="MSLPPDIAGALSWARERIEQVDARVLLRYALACPASRLVAWPEQR FT LSAEEWENFSRLVERRVEGEPVAYLIGEREFYGRSFAVTPAVLIPRPDTELLVELAVAH FT FSAQQRVRVLDLGTGSGALAITLALELDAADVTALDRSREALWVAMANAARLGASVSFV FT QSDWFDALGEERFQLIVANPPYIAADDAHLEEGDLRFEPRSALAAGTAGLDDLSEIAAA FT APAHLEAGGWLFLEHGYDQAMSVRGLLADAGFAAISSWKDLAGIERVTGGRWLGRD" FT CDS 1056474..1056797 FT /transl_table=11 FT /locus_tag="azo0983" FT /product="conserved hypothetical protein" FT /function="Glutaredoxin-related protein" FT /note="Conserved hypothetical protein. Homology to ne1911 FT of N. europaea of 67%. InterPro: Glutaredoxin-related FT protein (IPR004480) TIGR00365: glutaredoxin-related protein FT no signal peptide no TMHs" FT /db_xref="GOA:A1K445" FT /db_xref="InterPro:IPR002109" FT /db_xref="InterPro:IPR004480" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR014434" FT /db_xref="UniProtKB/TrEMBL:A1K445" FT /protein_id="CAL93600.1" FT /translation="MDIKDVIREQVTTHPVALYMKGVPQAPACGFSATAVQILKASGVK FT DFFSVNVLADDAVRQGIKEFSNWPTIPQLYVKGEFVGGADIMREMYQSGEIQQLLKDAG FT VTA" FT CDS complement(1056828..1057925) FT /transl_table=11 FT /locus_tag="azo0984" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT NE1634 of Nitrosomonas europaea of 34% (trembl|Q82U71(SRS)) FT No domains predicted. No TMHs Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K446" FT /protein_id="CAL93601.1" FT /translation="MPLIATAAGSCGLLLDVLAQPSHATSLTPPQWTALLAAARAANLL FT GTLAARLTDAGIDLPPAPARHLSGALHLSLRQADSVRWETHCIARALAPLGTPVVLLKG FT AAYVLTAQPPARGRLFGDIDILVPRDAVGRAELRLMVHGWTTGKSDPYDQRYYREWMHE FT IPPLMHVRRGTMLDVHHTILPLTSRHRPDPAKLIARAVDTQVPGIKALSPLDLVLHSIT FT HLVHEGELHNGLRDLVDIDALLRAQCGSADDWRVLAERAAELDLEESVGLGLHLAARHL FT STPVPSEWIERLLRNRRSRRMLDWAYDRALAPAVESEEAGWAGLARSLIYIRAHWLRMP FT PLLLARHLGRKAWMGWRARTAPATP" FT CDS complement(1057916..1058776) FT /transl_table=11 FT /locus_tag="azo0985" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein, 35% identity (56% FT similarity) to TrEMBL;Q82U70. Signal peptide Present. No FT TMH reported Present." FT /db_xref="UniProtKB/TrEMBL:A1K447" FT /protein_id="CAL93602.1" FT /translation="MIDLAFRLPPFNVRVRSDFSSVADHVADLYPALQRLDSDSFVDFD FT IRILRGKGHRRWLGQQARFLLDAQEPFLPLPGSQAPALLEWGLNWSIAARPLGYLVLHA FT AVLARGTDAVVMPGFPGAGKSTLCASLAFLGGWRLLSDELAILDPGTLALHPNPRPISV FT KNESIDIVGRFPGAAVGPVYHDTRKGRLSHLAPPRESALAAEETARCRWIVFPSFQRDD FT EHGWHEEISRAEAFALISEQSFNKERMGEQGFHALCGMLDGARCFQIGYGSTAAGLELI FT DRLCR" FT CDS complement(1058789..1059091) FT /transl_table=11 FT /locus_tag="azo0986" FT /product="Hypothetical protein" FT /note="Hypothetical Protein. No Good functional or similar FT proteins matching in the database. No domains, FT repeats,motifs or features present." FT /db_xref="UniProtKB/TrEMBL:A1K448" FT /protein_id="CAL93603.1" FT /translation="MESGITTAAPATLSWLDGRRLTFSPVWDEDELSVVFDAASGDFWV FT VACEARRLIEHLGVSPLMDADAIEMLRSGDLPAPDSARAILDNLVEVGILQRNAT" FT CDS complement(1059121..1059837) FT /transl_table=11 FT /locus_tag="azo0987" FT /product="hypothetical protein predicted by FT Glimmer/Critica" FT /note="Hypothetical protein predicted by Glimmer/Critica. FT No homology to data bank. no domains predicted. no signal FT peptide. no TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K449" FT /protein_id="CAL93604.1" FT /translation="MTPNELDSQPNIDPRAAEGLSIRQGNPTRRRLISGAAGGLGVLLA FT VQAKTALGQQVCQSPSAMMSGNTSPRPETPPCSGGRSPGFWKQPQHFSSWAVAGATPPT FT FKPGVVVQTCVSGMQGLSLKDLKTPGTLASTALGGSVPGDPGIWAVLAFPNSFVDGMLV FT RHLCAAWLNAGYFPDYAISRTQIQAMWAQLSTNGNYCPGNVTCTDPMTKDDVKAYIEGL FT YDFNADLTEPDLCKKK" FT CDS complement(1060017..1061303) FT /transl_table=11 FT /locus_tag="azo0988" FT /product="putative serine/threonine protein kinase" FT /function="Serine/threonine protein kinase" FT /note="Putative serine/threonine protein kinase," FT /note="Family membership" FT /db_xref="GOA:A1K450" FT /db_xref="InterPro:IPR000595" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR008271" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR014710" FT /db_xref="InterPro:IPR017441" FT /db_xref="InterPro:IPR017442" FT /db_xref="InterPro:IPR018488" FT /db_xref="InterPro:IPR018490" FT /db_xref="UniProtKB/TrEMBL:A1K450" FT /protein_id="CAL93605.1" FT /translation="MSGGRIGKYEIRRLLGEGATSAVHLAWDPFNQREVALKQLYPEVL FT RDREHGRLYRHLLMNEAALAGKLTHPHIVQIFDAVIGDDEAYVVMEYVPGGTLEALARV FT ETRPGFERLIEIVFKCTRALDYAFHRGITHRDIKPANILLADPAGQDIRISDFGAALRT FT ATDTTQISGIGSPAYMSPQQVREMPLDHRTDIYSLGVVMYQLLTSRLPFESENNYSLLY FT RIAHETPPAPSELRPDVPPALDAIVRRAMEKDLERRYQTWAEFSHDLALAFRNRSVAVA FT DNVIPDAAKFQTLRAMPFFREFSDPELWEVIALAQWSHAQPGTVLLKDGEAGDFFCFLA FT QGEARVKKRGRLLNVLTAGDCFGEVAIFSAGGGVRSASVEAASVVEVITVRAAALKRAS FT DTCRMHFYKAFLGVLATRLSLASARIANL" FT CDS complement(1061310..1062752) FT /transl_table=11 FT /gene="argH" FT /locus_tag="azo0989" FT /product="ArgH protein" FT /function="Argininosuccinate lyase" FT /EC_number="4.3.2.1" FT /note="Argininosuccinate lyase (EC 4.3.2.1) FT (Arginosuccinase) (ASAL)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K451" FT /db_xref="InterPro:IPR000362" FT /db_xref="InterPro:IPR003031" FT /db_xref="InterPro:IPR008948" FT /db_xref="InterPro:IPR009049" FT /db_xref="InterPro:IPR020557" FT /db_xref="InterPro:IPR022761" FT /db_xref="UniProtKB/Swiss-Prot:A1K451" FT /protein_id="CAL93606.1" FT /translation="MTDTTPSADLGASSQQPAKAWSGRFSEPVSDLVKRYTASVFFDNR FT MAEQDIRGSLAHAKMLARQGIIGAQDLADIERGMAQIKGEIERGEFNWNLDDEDVHLNI FT EKRLTALVGDAGKRLHTGRSRNDQVATDIRLWLRDAIDQILALIGDFQKNLLDVAEANA FT ATPMPGFTHLQVAQPVTFGHHLMAYFEMTRRDAERFADCRKRVNRLPLGSAALAGTSYP FT IDREFVARELGFDEVCYNSLDAVSDRDFAIEFCAASSLLMTHLSRFSEELILWMSPRFG FT FIDLADRFCTGSSIMPQKKNPDVPELVRGKTGRVNGSLIALLTLMKGQPLAYNKDNQED FT KEPLFDTADTVIDTLRIYADMITGIRVKADNMRGALTQGYATATDLADYLVKKGLPFRD FT AHEAVALAVRAAEVRGCDLPQFSLDELRAAMAHVPGAADKLADDIFGVLTVEGSLDSRN FT HIGGTAPAQVLAAVAHARTRLG" FT CDS 1062841..1063866 FT /transl_table=11 FT /gene="algZ" FT /locus_tag="azo0990" FT /product="putative alginate biosynthesis protein AlgZ/FimS" FT /function="predicted signal transduction protein with a FT C-terminal ATPase domain" FT /note="Putative alginate biosynthesis protein AlgZ/FimS," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K452" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR010559" FT /db_xref="UniProtKB/TrEMBL:A1K452" FT /protein_id="CAL93607.1" FT /translation="MKSIKQKPNPLAVPALPDFRNLGVVLRVLLVVNLLALLTALVRVD FT SVDAFVAETMLTAARVELPLFVIVLVLYAVHARLAALPSSHALGLVFGLVLAVVAAAFP FT LLAGPGDNLLRWLFWGVAAGAGVVFYFDYRNRRYSPALTEARLLALTARIRPHFLFNSL FT NGVLGVMRADPRRAERALEELADLFRALMQDNRELVPLGDELDLCERYADLESLRLGDR FT LQVRWEIDPEVARERLMQVRVPPLLLQPLLENAVYHGIEPAEGAGEVVVRVLRRGDELH FT LEVENPVIEVERHTAGNRMALANIRERLMLFFDLEAGLDIDSDDVRYRVRIRLPYRHGA FT T" FT CDS 1063863..1064624 FT /transl_table=11 FT /gene="algR" FT /locus_tag="azo0991" FT /product="probable alginate biosynthesis regulatory protein FT AlgR" FT /function="Response regulator of the LytR/AlgR family" FT /note="Probable alginate biosynthesis regulatory protein FT AlgR," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K453" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR007492" FT /db_xref="InterPro:IPR011006" FT /db_xref="UniProtKB/TrEMBL:A1K453" FT /protein_id="CAL93608.1" FT /translation="MNDTLRVLIVDDETPARTRLRDLLGDIGATCPNVVVGMAANGVEA FT LRLIEQAGGADVVLCDIRMPVMDGVELARHLGRMTEPPAVIFTTAYDQYAVQAFELAAV FT DYLLKPVRAERLAAALAKVRQRRVPTDQALAALAPGERRHFSVNERGRILLLPVVDVRY FT LKAELKYVTARTIEREFVLDEALTQIEHEFGERFLRIHRNCLVARAAVAGVERAGEQDG FT EAHWEILLTGVPERLPVSRRQWPAVKQALGL" FT CDS complement(1064654..1067407) FT /transl_table=11 FT /gene="ppc" FT /locus_tag="azo0992" FT /product="probable phosphoenolpyruvate carboxylase" FT /function="Phosphoenolpyruvate carboxylase" FT /EC_number="4.1.1.31" FT /note="Probable phosphoenolpyruvate carboxylase. Homology FT to ppc of R. palustris of 61% (sprot|CAPP_RHOPA). Through FT the carboxylation of phosphoenolpyruvate (PEP) it forms FT oxaloacetate a four-carbon dicarboxylic acid source for the FT tricarboxylic acid cycle. Pfam: Phosphonenolpyruvate FT carboxylase no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K454" FT /db_xref="InterPro:IPR015813" FT /db_xref="InterPro:IPR018129" FT /db_xref="InterPro:IPR021135" FT /db_xref="InterPro:IPR022805" FT /db_xref="UniProtKB/Swiss-Prot:A1K454" FT /protein_id="CAL93609.1" FT /translation="MTPDKDAPLREDIRLLGRLLGDTVRDQQGAASFDLIERIRQTSVR FT FRRDEDLAARRELEDTLDALSREQTIQVVRAFSYFSHLANIAEDQHHIRRSRAHLLAGS FT APREGSLAHAVGHALDEQRLDPTDLAAFFDTALISPVLTAHPTEVQRKSILNCQTVIAR FT LLDERDRMQLTPDEAEANLDALRRAVLTLWQTRMLRPAKLSVIDEVNNGLSYFETTFLR FT ELPRLYAALEDRLAGAQPALANHELPAFLQVGSWIGGDRDGNPYVTADVLEEALAMQAR FT VALDYYLDELHTLGSQLSLSQGLVGASDALLALADRSPDQSPHRSDEPYRRAIAGIYAR FT LSATYRNLLGHPPARHAVAEAEPYADVAALADDLDTLHRSLVANGTAALARGRLRHLRR FT AVRVFGFHLAPIDLRQNSDVHERVVAELLEVARPGAAYLAQDEAGRCALLLDELATARP FT LASPHVRYSDDSEGELAIFRAARRAHLRYGRGAIHNCIISKTDDLSDLLELAVLLKEAG FT LLRPLEKALDVNIVPLFETIGDLENAAGVMDRLFSIPVYRELLAARDQTQEVMLGYSDS FT NKDGGFLTSGWALYKAEGELVEVFGRHGVRLRLFHGRGGSVGRGGGPSYQAILAQPDGA FT VQGQIRLTEQGEVIAAKYGNPEVGRRNLEVLVAATLETSLRRDGGDATPRTFLDTMQAL FT SDAAFTCYRGLVYETPGFEQYFWESTVISEIAGLNIGSRPASRKKGTRIDDLRAIPWVF FT SWSQCRLMLPGWFGFGSAVKQWLAAHPKDGLGLLQRMYREWSFFATLLSNMDMVLSKTD FT LAIASRYAELVKDPVLRDSIFERIRSEWKDTVDALLAITEQVELLDANPLLKRSIRNRF FT PYLDPLNHVQVELLRRHREGNGEDARIRNGIHISINGIAAGLRNSG" FT CDS 1067713..1068663 FT /transl_table=11 FT /gene="hemC" FT /locus_tag="azo0993" FT /product="hydroxymethylbilane synthase" FT /function="Porphobilinogen deaminase" FT /EC_number="2.5.1.61" FT /note="Porphobilinogen deaminase (HMBS). FT Tetrapolymerization of the monopyrrole PBG into the FT hydroxymethylbilane preuroporphyrinogen in several discrete FT steps. InterPro: Porphobilinogen deaminase hemC: FT porphobilinogen deaminase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K455" FT /db_xref="InterPro:IPR000860" FT /db_xref="InterPro:IPR022417" FT /db_xref="InterPro:IPR022418" FT /db_xref="InterPro:IPR022419" FT /db_xref="UniProtKB/TrEMBL:A1K455" FT /protein_id="CAL93610.1" FT /translation="MTSTTSSSPAAPERIVIATRESRLALWQAEHVKARLEALYPACTV FT ELLGMTTRGDQILDRPLAKVGGKGLFVKELETALLDGRADIAVHSMKDVPMEMGKAFAL FT PCISAREVPLDAFVSNRYASLADMPPGTVVGTSSLRRESQLHAQYPFLAVTSLRGNLDT FT RLRKLDEGQYDAIILAAAGLTRLGLADRIRATLPAEVSLPAAGQGALGIECLSSRPEVA FT AWLAPLNDPATSACVRAERAVARALAGSCEVPLGAYAELRGARLWLRGFVARPDGSEIV FT RAEREGDPAAAEALGGALADDLRAQGAERILAELG" FT CDS 1068679..1069476 FT /transl_table=11 FT /gene="hemD" FT /locus_tag="azo0994" FT /product="HemD protein" FT /function="Uroporphyrinogen-III synthase" FT /EC_number="4.2.1.75" FT /note="Uroporphyrinogen-III synthase (Uroporphyrinogen-III FT cosynthetase) (Hydroxymethylbilane hydrolyase [cyclizing]). FT catalytic activity: hydroxymethylbilane = FT uroporphyrinogen-iii + h(2)o. pathway:porphyrin FT biosynthesis; fourth step. ribH: riboflavin synthase beta FT subunit" FT /note="Specificity unclear" FT /db_xref="GOA:A1K456" FT /db_xref="InterPro:IPR003754" FT /db_xref="UniProtKB/TrEMBL:A1K456" FT /protein_id="CAL93611.1" FT /translation="MTRPHGQTDPKLPLAGRLVAVTRPEAQALSLCEAIRRAGGQVLLF FT PVLAIGAVEDPAALDEAIARLDHFDLAFFVSPNAVEHALAAVKARRHWPERLEVSTVGK FT GSERALREAGFSAVIAPSEGFDSEAVLALPAFSATAINGRRVVIFRGDGGRELLADALR FT ARGAVVEQVSCYRRYRPAADAAPLIQAAGTGRLDALVLTSSEGVRNLVEMVGEKGFGVL FT RRVTVFAPHPRIVAHARAAGFDRVEETPPGDDGLLETLVRHFG" FT CDS 1069486..1070682 FT /transl_table=11 FT /gene="hemX" FT /locus_tag="azo0995" FT /product="Uroporphyrin-III C-methyltransferase" FT /function="uncharacterized enzyme of heme biosynthesis" FT /EC_number="2.1.1.107" FT /note="Putative uroporphyrin-III C-methyltransferase. FT catalytic activity: 2 s-adenosyl-l-methionine + FT uroporphyrin iii = 2 s-adenosyl-l-homocysteine + FT sirohydrochlorin. pathway: siroheme and cobalamin FT biosynthesis." FT /note="Specificity unclear" FT /db_xref="GOA:A1K457" FT /db_xref="InterPro:IPR007470" FT /db_xref="UniProtKB/TrEMBL:A1K457" FT /protein_id="CAL93612.1" FT /translation="MNEETPALTSSPAAAQPAASVEPPPSDPRPAAPSRSSGASGWAVL FT LAVLALGGAGLAGWQAWETRARVGELRQELASRLNAGDTVAAEARALARQQQEAMAALQ FT GRVGALAAQIEATEGQAAALEALYQEFSRSREDRVVAEVEQAVNVAAQQLQLAGNIEAA FT LIALQGAEARLALQDKGQLAVLRRALAKDIEQLKLQPEVDVGGIALRLERLLERGDALP FT LAFESQPPANAEHGGEQAAAVEPGRLNVALAFITELGRDVWRELRSLVRVERLDQSEPV FT LLAPAQSTFLRENLKIRLLTARLALLARDGRTYAADLAQARSWMERFFDTRDERVREAI FT GELKALEAMSVGDERPALTESFAALRVLQTRAGEPRTPAVAAEPARPANGGRAPAPQR" FT CDS 1070695..1071894 FT /transl_table=11 FT /gene="hemY" FT /locus_tag="azo0996" FT /product="HemY protein" FT /function="uncharacterized enzyme of heme biosynthesis" FT /note="HemY protein. involved in a late step of protoheme FT ix synthesis." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K458" FT /db_xref="InterPro:IPR000048" FT /db_xref="InterPro:IPR010817" FT /db_xref="InterPro:IPR011990" FT /db_xref="UniProtKB/TrEMBL:A1K458" FT /protein_id="CAL93613.1" FT /translation="MRALFWLIGIFATAVGLAMLARLNDGYVLVVLPPWRVQLSLNLLV FT VLLLLGFAAGYLVLRLVGRTLELPARVSSWRERRRREKAGRALREALRALFEGRFAQAV FT KHASGAFASGESPAMAALVAARAAHAMRDDTRYRIWIGHAADQGEDARAARLMTEAELA FT VEGRRFEEAAERLEMLRLSGHRHIAALRLSLRVASALQQWDEVLRLTRQLYKHKALSDE FT QAAPLLRRAHAERLKELGGDAAALADYWNGIPADELRDRRFVERAVPMLSAAGRGALAR FT RTLERLLDEEWDSGLARLYAHCGDGEGDAVACLARGEAWLKKHPRDAGLLFALGRLCLA FT AQLWGKAQSYLEASLNLAPTVETHLALARLLDRLERSDEAQTHYRAAALRVDGTAVALA FT " FT CDS 1072050..1072769 FT /transl_table=11 FT /gene="glcC" FT /locus_tag="azo0997" FT /product="glc operon transcriptional activator" FT /function="Transcriptional regulators" FT /note="Glc operon transcriptional activator," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K459" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K459" FT /protein_id="CAL93614.1" FT /translation="MSALLPRPQRLSDTVARQLESLIRDEGMAPGARLPTEKVLCERLG FT VSRAVVREAVSRLKAEGSVETRQGLGAFVAASPGQGSFRLVRGGKASLAEVEEIFEIRC FT VVEAGAAELAARRRSAADLSRLAAALSRMDRALDGAPDGAQADDAFHVAIAAATGNTQL FT ERFLAFVGRQFSETRAPTWDAGGLRSGRAAEAQAEHRRIFSAIEAGDAEAARAAARAHL FT VAAARRLGLTGLAAAFP" FT CDS 1072863..1074362 FT /transl_table=11 FT /gene="glcD1" FT /locus_tag="azo0998" FT /product="probable glycolate oxidase subunit GlcD" FT /function="FAD/FMN-containing dehydrogenases" FT /note="Probable glycolate oxidase subunit glcD. Homology to FT glcD of E. coli of 64% (sprot|GLCD_ECOLI) InterPro: FAD FT linked oxidase C-terminal (IPR004113); FAD linked oxidase FT N-terminal (IPR006093) Pfam: FAD binding domain; FAD linked FT oxidase, C-terminal domain Tigrfam: glcD: glycolate oxidase FT subunit GlcD no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K460" FT /db_xref="InterPro:IPR004113" FT /db_xref="InterPro:IPR006094" FT /db_xref="InterPro:IPR016164" FT /db_xref="InterPro:IPR016166" FT /db_xref="InterPro:IPR016167" FT /db_xref="InterPro:IPR016168" FT /db_xref="InterPro:IPR016171" FT /db_xref="UniProtKB/TrEMBL:A1K460" FT /protein_id="CAL93615.1" FT /translation="MAPEEAGIAERDFSALDKARVVEALARVLPAGALMFEAEDLRPYE FT CDGLSAYRALPLAVVLPATEDEVVAVLTVCAELGVPVVARGAGTGLSGGALPHRHGVLL FT SLARFTRILHLDPHARTAVVQPGVRNLAISEAAAPYGLYYAPDPSSQIACTIGGNVAEN FT SGGVHCLKYGLTVHNLLRVRGVTIEGEVVEFGSHALDTPGYDLLALVTGSEGMLAVVTE FT VTVRLTPKPQLAQCVLAAFDDVVKAGEAVAAIIAAGIIPAGLEMMDQPATAAVEQFVHA FT GYPLDARAILLCESDGTPEEVAEEIVAVRAVLEASGATEIRVSQDEAERLRFWAGRKAA FT FPAAGRLSPDYYCMDGTIPRKRLGEMLEAIQGMEQKYGLACINVFHAGDGNLHPLILFD FT ANQPGELERAEAFGTDILELSVALGGTVTGEHGVGVEKINQMCSQFGEGERLQFFRVKA FT AFDPLGLLNPGKAIPTLHRCAEYGRMRVSGGALPHPELPRF" FT CDS 1074367..1074513 FT /transl_table=11 FT /locus_tag="azo0999" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. No signal pepitde. 1 TMH" FT /db_xref="UniProtKB/TrEMBL:A1K461" FT /protein_id="CAL93616.1" FT /translation="MGDKAWVQFLFVAVPVLSLVGAWLALRAVGGRNGRRPQGKQQREA FT KEQ" FT CDS 1074510..1075571 FT /transl_table=11 FT /gene="glcE" FT /locus_tag="azo1000" FT /product="probable glycolate oxidase subunit GlcE" FT /function="FAD/FMN-containing dehydrogenases" FT /note="Probable glycolate oxidase subunit GlcE. Homology to FT glcE of E. coli of 47% (sprot|GLCE_ECOLI) InterPro: FAD FT linked oxidase N-terminal (IPR006093) Pfam: FAD binding FT domain Tigrfam: glcD: glycolate oxidase subunit GlcD no FT singla peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K462" FT /db_xref="InterPro:IPR004113" FT /db_xref="InterPro:IPR006094" FT /db_xref="InterPro:IPR016164" FT /db_xref="InterPro:IPR016166" FT /db_xref="InterPro:IPR016168" FT /db_xref="InterPro:IPR016171" FT /db_xref="UniProtKB/TrEMBL:A1K462" FT /protein_id="CAL93617.1" FT /translation="MTDIVSAWADRIRAAAAADTPLQLRGGGTKAFYGRSGEGEVLDLT FT DNRGVVSYEPTELVVTVRGGTPLAELEALLARHDQFLAFEPPAFGPAATVGGCVAAGLS FT GPRRASAGAVRDFVLGARLLDGRGEALSFGGQVMKNVAGYDVSRLLAGSLGTLGVLLEV FT SLKVLPRPAAEATLRFECDEASAIQRLNDWGGQPLPLSASTWHDGVLTVRLSGASAAVA FT AAQARLGGERLDEALATAFWTSIREHTAPWFAARPLWRLSLPSSAAPLRLAGGQLIEWG FT GALRWLHTDLPATAVRERVAQLGGTAALFAGGNRSGEVFHPLPEPLLRIHRRLKAAFDP FT AGIFNRGRLYQGL" FT CDS 1075575..1076819 FT /transl_table=11 FT /gene="glcF" FT /locus_tag="azo1001" FT /product="probable glycolate oxidase iron-sulfur subunit" FT /function="Fe-S oxidoreductases" FT /note="Probable glycolate oxidase iron-sulfur subunit. FT Homology to glcF of E. coli of 56% (sprot|GLCF_ECOLI) Pfam: FT Domain of unknown function (DUF224) (192-256 aa; 329-391 FT aa) no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K463" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR004017" FT /db_xref="InterPro:IPR012257" FT /db_xref="InterPro:IPR012285" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K463" FT /protein_id="CAL93618.1" FT /translation="MQTQLADFIRDTPEGREADEILRKCVHCGFCTATCPTYQLLGDEL FT DGPRGRIYLIKQLLEGQPVTEKTRLHLDRCLTCRACETTCPSGVHYSRLADIGRHLVEQ FT RVPRRGADRAARWVLRELVPRAAVFGAALKAGRSVRGMLPATLRDKVPMVRAPGPWPRP FT RHARRMYALAGCAQPAMAPSINAATARVLDSLGISLLEAPSAGCCGAVRFHLHDHDGAR FT AEARRNIDAWWPAIEGGEVEGLVMTASGCGVQVKDYGHLLQHDPAYSAKAARIAALTRD FT VAEVVSAQEASLKALLRSKTGGETAVAWHAPCTLQHGLKIRGAVEQLLGAAGFRLTPVR FT DAHLCCGSAGTYSLLQPEIAQQLRENKLAALGEGGAPLILSANIGCITHLQAGTATPVR FT HWIEAIDARLNGFPI" FT CDS 1076945..1077721 FT /transl_table=11 FT /locus_tag="azo1002" FT /product="putative phosphoprotein phosphatase" FT /function="Serine/threonine protein phosphatase" FT /note="Putative phosphoprotein phosphatase," FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K464" FT /db_xref="InterPro:IPR001932" FT /db_xref="InterPro:IPR015655" FT /db_xref="UniProtKB/TrEMBL:A1K464" FT /protein_id="CAL93619.1" FT /translation="MPLIAETCVARHTGDRKEQQDRVALFAHPTETGTLLAVLADGMGG FT HSGGAMAAEQVTIKAKQNFEAFQPAHETGRHLLQSIVDEAHVVIKLTRFTSEQDPHSTA FT VVFLMQPGKAAWAHCGDSRLYHFRGREPCFRTQDHSLVGEMLRKGRLDEAGALNHPQRN FT VLLSCLGSEREPRVEYGETDTLMAGDSFLLCSDGLWSYFSDDELGLVVDNHRPREAAQL FT LIDLARSRAGGYGDNISLALIKLSDPKSSPRPAFIG" FT CDS 1077900..1079021 FT /transl_table=11 FT /gene="pntAA" FT /locus_tag="azo1003" FT /product="probable NAD(P) transhydrogenase, subunit alpha FT part 1" FT /function="NAD/NADP transhydrogenase alpha subunit" FT /EC_number="1.6.1.2" FT /note="Probable NAD(P) transhydrogenase, subunit alpha part FT 1. Homology to pntAA of R. rubrum of 44% FT (sprot|PNAA_RHORU). The transhydrogenation between NADH and FT NADP is coupled to respiration and ATP hydrolysis and FT functions as a proton pump across the membrane. Tirfam: FT pntA: NAD(P) transhydrogenase alpha subunit Pfam: Alanine FT dehydrogenase/pyridine nucleotide dehydrogenase no signal FT peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K465" FT /db_xref="InterPro:IPR007698" FT /db_xref="InterPro:IPR007886" FT /db_xref="InterPro:IPR008143" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K465" FT /protein_id="CAL93620.1" FT /translation="MPLTIGVPAERIPGERRLPVVPDVVKKYLGLGARVVIESGAGVPA FT HYRDETFGDVTLGAAAEVFAQSDIVLCVQPPSAEHLATMKPGALLIGLLQPWSDPERIK FT LLQDKQITAFAMELLPRISRAQSMDVLSSQAAVAGYECALIAADHSPKFFPMLTYAAGT FT IRPAKVLVIGAGVAGLQAIATARRIGAMVEAYDVRPETREQIESLGAKFVDTGVSAAGS FT GGYARELTDEEKAKQAERLAKAVAQCDALITTAAIPGKKAPKIITADMIARMKPGAVVV FT DMAAETGGNVEGTVAGEKTWINDVLVIGPTHIASRMPVHAAEMLAKNLFNFIGPFIKDG FT ALTLDWDDEVLAGTCLTHAGELRHAGVKAALGL" FT CDS 1079035..1079343 FT /transl_table=11 FT /gene="pntAB" FT /locus_tag="azo1004" FT /product="conserved hypothetical NAD(P) FT transhydrogenase,subunit alpha part 2" FT /function="NAD/NADP transhydrogenase alpha subunit" FT /note="Conserved hypothetical NAD(P) FT transhydrogenase,subunit alpha part 2. Homology to pntA of FT X. axonopodis of 74% (trembl|Q8PNW6). The FT transhydrogenation between NADH and NADP is coupled to FT respiration and ATP hydrolysis and functions as a proton FT pump across the membrane. 3 TMHs no signal peptide" FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR024605" FT /db_xref="UniProtKB/TrEMBL:A1K466" FT /protein_id="CAL93621.1" FT /translation="MDGFTAIYIFMLAAFTGYEVISRVPVILHTPLMSGSNFVHGVVLV FT GAMVVLGHADPESPLQLAIGFVAVFLGAANAAGGYVVTERMLAMFNKSGSSKKEGAQ" FT CDS 1079340..1080719 FT /transl_table=11 FT /gene="pntB" FT /locus_tag="azo1005" FT /product="probable NAD(P) transhydrogenase, subunit beta" FT /function="NAD/NADP transhydrogenase beta subunit" FT /note="Probable NAD(P) transhydrogenase, subunit beta. FT Homology to pntB of R. rubrum of 46% (sprot|PNTB_RHORU) The FT transhydrogenation between NADH and NADP is coupled to FT respiration and ATP hydrolysis and functions as a proton FT pump across the membrane. Pfam: NAD(P) transhydrogenase FT beta subunit signal peptide 7 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K467" FT /db_xref="InterPro:IPR012136" FT /db_xref="UniProtKB/TrEMBL:A1K467" FT /protein_id="CAL93622.1" FT /translation="MTAKWFIDASYFAVAVVFILALKAMSSPVTARRGIVWGGIAMVFA FT TLVTFATPGLHNFGWMIVAIVSGAAVAWWSGKTVKMTDMPQMVAIYNGMGGGAAAAIAA FT LEFARGEVHGPVVTTLAVLGALIGSVAFSGSCIAFAKLQGIMKKAWRLPAQNAVNVVLA FT LVTVGLGIAIIAAPSIDPVLVIVFFVLALILGAILTSPIGGADMPVVISLLNAFTGLAV FT GFEGYVLGNPALIVAGIVVGASGTLLTQLMAKAMNRPISNVLFTPISGAASGGGEGIEG FT TMKEFSSLDAASVMRYASKVIIVPGYGMAVAGAQHKVWEMAQLLEEGGVEVVFAIHPVA FT GRMPGHMNVLLAEAGVPYDKIFDLEEINADFAQAEVALVIGANDVVNPVARTDKSSPIY FT GMPILNADMAQNVIVVKRGKGAGYSGIENALFYKDNCRMLYGSAQQAIAEVITHVKALE FT A" FT CDS 1080834..1081184 FT /transl_table=11 FT /locus_tag="azo1006" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. No TMHs. Signal peptide FT present." FT /db_xref="UniProtKB/TrEMBL:A1K468" FT /protein_id="CAL93623.1" FT /translation="MSPLRSILILMLPASLAWAQAVAPQAPTTPAGAAAPAGPAPAANA FT PKPADDWRDTSNYIFPAIAKTVTDMQNVAYAMTLRDYCADRRVPDDFVRDRLKRFSAMT FT GREETCRSLMDY" FT CDS complement(1081178..1083613) FT /transl_table=11 FT /locus_tag="azo1007" FT /product="hypothetical signaling protein" FT /function="predicted signal transduction protein containing FT a membrane domain an EAL and a GGDEF domain" FT /note="Hypothetical signaling protein," FT /db_xref="GOA:A1K469" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001633" FT /db_xref="InterPro:IPR013767" FT /db_xref="UniProtKB/TrEMBL:A1K469" FT /protein_id="CAL93624.1" FT /translation="MLPPMNPSGRPRGDDHSDEAPKEPFRPDLSEGAETGVYLALLELL FT DEGLIITGDETVLDANSAACALLQRDYRELAGQPLANLFPSERAFIEARARLFIQGQMR FT GTLTVALPAGGTAALRFIAAPRLRPGIHALILSPLPSATAAAQPAPTPADTVWPRLAAA FT LSQGVLVLDDGDRITAANAAALHLLGRTRDDVLSRPLADHLDVSWPAPGQPALAHVTLP FT HASAPLPARVLAGPRAGWRLLVLPPRTEDTATEGLHLPVDVFDAASQAILVTDDQNRIV FT AVNRAFTEITGYSRDEVLGQNPRLLSSGRQEPAFYAEMWQTLEASGQWQGEIWNRRQNG FT EIFPEWLTITAVRDAQGAARHYLAMFTDLTARRQAEARAEYIAHHDILTGLPNRRLFEA FT RFKEAAEQARRRRCSVGVLRIDIDQFKAVNREHGDNTGDAFLQQIARRLQASLPRGAVA FT ARERSDTFLALLPELDLASAASRAADDILAALGPAFRTESCEVAISASIGIALFPGDGA FT DLDTLLRHAGIALRQARQLGGNSHQRYQAGQGGGIEQAEFGAELHGALTRRQLEVYFQP FT LVDARSGRVRAGEALLRWRHPELGLIPYRHFVATARHNGLVAAFGDWALVTACNAAARW FT PQGAQGVPAVTVNVALEQVLRGDFATTVDKALAASGLAATRLELDLDEAILASDDEVTL FT ATLRTLAKRGIRFAIDDFGRGLSSIPRLRRFPVQALKLDPALVGGVGKDEDAEAVVEAI FT ARLAASLGIEVLARGVADPAQQAFLSALDCHFQQGPLFGAPLPAPAFAALLETATGVQ" FT CDS complement(1083711..1085195) FT /transl_table=11 FT /gene="rhlE2" FT /locus_tag="azo1008" FT /product="putative ATP-dependent RNA helicase" FT /function="Superfamily II DNA and RNA helicases" FT /note="Putative ATP-dependent RNA helicase rhlE." FT /note="Family membership" FT /db_xref="GOA:A1K470" FT /db_xref="InterPro:IPR000629" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR014001" FT /db_xref="InterPro:IPR014014" FT /db_xref="UniProtKB/TrEMBL:A1K470" FT /protein_id="CAL93625.1" FT /translation="MSFADLGLIPELQRAVADAGYTEPTPIQRQAIPIVIAGNDVMGGA FT QTGTGKTAGFTLPLLHRLARHANTSTSPARHQTRALILAPTRELAMQVYESVKTYSKHL FT PLRATCIYGGVDMNPQIQELRRGIEIVIATPGRLLDHVQQKTINLTQVEMLVLDEADRM FT LDMGFIPDIKRILALLPASRQSLLFSATFSDEIKKLADQMLKNPQLIEVARRNMVSETI FT THRVHPVSSGMKRNLLAHLLRHQPDTQALVFVDTKLVCGRLAHFLERHSISADSIHGDK FT SQQQRTETLEAFKAGKLRVLVATDVAARGIDIDELPYVINYELPHTAEDYVHRIGRTGR FT AGHQGNAVSLVCTEEKHLLADIQKLIKLEIPQEVVPGFEPDPDFFEAGSRAHRGRRPVE FT DFDERPRREPRGGREERPPREERAPREDRGARNVVAKRPPRSTIAPDGFDFSKPYVAKP FT VVLAEGAAPDASPAEAGTPRRGQRPIAFLLGGLGRK" FT CDS complement(1085393..1086487) FT /transl_table=11 FT /locus_tag="azo1009" FT /product="conserved hypothetical protein" FT /function="predicted SAM-dependent methyltransferase" FT /note="Conserved hypothetical protein. Homology to xcc0816 FT of X. campestris of 49% (trembl|Q8PCB8) Pfam: FtsJ-like FT methyltransferase no signal peptide no TMHs" FT /db_xref="GOA:A1K471" FT /db_xref="InterPro:IPR002877" FT /db_xref="InterPro:IPR011224" FT /db_xref="UniProtKB/Swiss-Prot:A1K471" FT /protein_id="CAL93626.1" FT /translation="MSSHAPASSFSVSGLLAYCRAGFEKELAAEIDDLAADAGLIGYVR FT TEPGSGYAAFETFEPVPVIKLGEFADWRKPVFARQLLPWFDRIDDLPERDRARPLVDMV FT KGSGQRFSGVVLETPDTDEAKQRSGFCRRFTEPLTRELEKVGALRLGKPGFPVLHVMFP FT TATSAWLAAGLKDRCAPWPMGIPRLRMPSNAPSRSTLKLAEAIMTLLSDEERDSLLRAG FT MRAVDLGAAPGGWTWQLAQRGIRVTAIDNGPLRDTVMATEMVEHLKADGFTWRPQRPVD FT WMVCDMVEQPSRIASLMAEWIATGRCRHTIFNLKLPMKRRLEAVEQCRELIRKRLASIG FT PFDLRIKQLYHDREEVTAYLTLKK" FT CDS 1086606..1087658 FT /transl_table=11 FT /gene="tas" FT /locus_tag="azo1010" FT /product="probable oxidoreductase Tas" FT /function="predicted oxidoreductases (related to FT aryl-alcohol dehydrogenases)" FT /note="Probable oxidoreductase Tas. Homology to tas of E. FT coli of 51% (sprot|TAS_ECOLI). InterPro: Aldo/keto FT reductase family (IPR001395) Pfam: Aldo/keto reductase FT family no signal peptide no TMHs" FT /note="Function unclear" FT /db_xref="InterPro:IPR001395" FT /db_xref="InterPro:IPR023210" FT /db_xref="UniProtKB/TrEMBL:A1K472" FT /protein_id="CAL93627.1" FT /translation="MLQRSMEYRVLGRNGPRVSAICLGTMTFGQQNSEAEAHEQLDFAL FT AQGINFIDTAEMYPVPARAETSGATERFVGSWLARQARERIVLATKVAGPARSLGWIRG FT GPLALDRANIREAVEGSLRRLRTDYIDLYQLHWPERNQPMFGQWQYEPDKERECTSIRA FT QLEALAELVDEGKVRYVGLSNEHPWGVMEFVRLAALHGLPRVVSTQNAYSLLNRVFEYG FT LAEVCHRESVGLLAYSPLAFGHLTGKYLADPQAPGRLSLFEQFGQRYGKPNVVPAARAY FT AELAAERGLTPAQLALVFTYRRPCVASTIIGATTMAQLKENLSAWDVPLDAELVSAIDA FT IHLRYTNPAP" FT CDS complement(1087666..1088040) FT /transl_table=11 FT /locus_tag="azo1011" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT Rgel02001790 of Rubrivivax gelatinosus of 45% FT (gi|47573892|ref|ZP_00243929.1|(NBCI ENTREZ)) . No domains FT predicted. No TMHs. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K473" FT /protein_id="CAL93628.1" FT /translation="MRAIRRFPLLPAILFALPLLTACEQVGELLELPNPKKEAAQADAE FT GRAIGSACRHAGRSLEDCYVLNPGAQKAAVFAGWRDMNDYMMEHKLDVVPSQLPQVPPQ FT PKAAPAQAAEAPAAARAAQH" FT CDS 1088233..1089531 FT /transl_table=11 FT /gene="ugpB" FT /locus_tag="azo1012" FT /product="putative glycerol-3-phosphate-binding periplasmic FT protein" FT /function="ABC-type sugar transport system periplasmic FT component" FT /note="Glycerol-3-phosphate-binding periplasmic protein FT precursor. SN-glycerol-3-phosphate and glycerophosphoryl FT diester-binding protein interacts with the binding FT protein-dependent transport system ugpACE. 30% FT SBP_bac_1.IPR006061; SBP_dom1. Pfam:PF01547; SBP_bac_1; 1. FT Signal peptide:present." FT /note="High confidence in function and specificity" FT /db_xref="UniProtKB/TrEMBL:A1K474" FT /protein_id="CAL93629.1" FT /translation="MNLRTLKIGLLTLPLALAAALPAMAASSKPAPAKAAKAPAAPAGP FT VAIELFHHLPADRAEALKGLVARFNAQNNDAQVVLVERDWRSGDAPDLLILEGDDEESF FT LAGKPRYKPVHALMKEAGVPLQTLRPPAMMTRTPVDAKGQVLALPIGLTTPVLFVNREA FT FRRAGLNPDSATMSTWFDLQQTLGRLAGSGHQCPYTVAEPARVMVENLSAWHNEPVAAE FT RGKAQAPSFNGMFQVKHVAMMASWYRARYLQIFDRADAERRFAAGECAVIAAPSASWTD FT FRKAGADVGVMRLPYYDDFPGAPQNTIADGPALWAAAGKKPAEYKVAARFVSFWLQPEN FT QVAWQRETGYLPLNRAGLLAAQSDLLGPDLENVRVAVAQLTNKPATAASSAQPVMQREK FT VRRILDEELAAVWADRKPAKEALDTAVARASGI" FT CDS 1089536..1090285 FT /transl_table=11 FT /gene="ugpQ" FT /locus_tag="azo1013" FT /product="probable glycerophosphodiester phosphodiesterase" FT /function="Glycerophosphoryl diester phosphodiesterase" FT /EC_number="3.1.4.46" FT /note="Probable glycerophosphodiester phosphodiesterase. FT Homology to ugpQ of E. coli of 45% (sprot|UGPQ_ECOLI). FT GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE HYDROLYZES FT DEACYLATED PHOSPHOLIPIDS TO G3P AND THE CORRESPONDING FT ALCOHOLS. Pfam: Glycerophosporyl diester phosphodiesterase FT no signal peptide" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K475" FT /db_xref="InterPro:IPR000909" FT /db_xref="InterPro:IPR004129" FT /db_xref="InterPro:IPR017946" FT /db_xref="UniProtKB/TrEMBL:A1K475" FT /protein_id="CAL93630.1" FT /translation="MTIGWPLPRVLAHRCGGRLAPENTLAGLNAAAALGCRGVEFDVML FT SADGIPVLIHDETLERTTDGSGPVAETTYGALACLDAGSRFCARFAGEPVPRLDAALAR FT CAALGLAVNLELKPSTGCEAETGTVVGRALTANWATFAPHLVLSSFSERALVAAADAAP FT GFLRALLVERVPADWRDRCAALGAVALHVSCEGLDPGDVTAIRAAGLHIAIYTENSPAR FT AAPWLALGVDTVVTDHPERFLAPPFVQ" FT CDS 1090402..1091427 FT /transl_table=11 FT /gene="ispB" FT /locus_tag="azo1014" FT /product="octaprenyl-diphosphate synthase" FT /function="Geranylgeranyl pyrophosphate synthase" FT /EC_number="2.5.1.-" FT /note="Polyprenyl synthetase,82% identity to TrEMBL;Q5P1Y1. FT Has Pfam;PF00348, Polyprenyl FT synthetase.(IPR000092,Polyprenyl_synt)A variety of FT isoprenoid compounds are synthesized by various organisms. FT For example in eukaryotes the isoprenoid biosynthetic FT pathway is responsible for the synthesis of a variety of FT end products including cholesterol, dolichol, ubiquinone or FT coenzyme Q. In bacteria this pathway leads to the synthesis FT of isopentenyl tRNA, isoprenoid quinones, and sugar carrier FT lipids. Among the enzymes that participate in that pathway, FT are a number of polyprenyl synthetase enzymes which FT catalyze a 1'4-condensation between 5 carbon isoprene FT units. It has been shown that all the above enzymes share FT some regions of sequence similarity. Two of these regions FT are rich in aspartic-acid residues and could be involved in FT the catalytic mechanism and/or the binding of the FT substrates." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K476" FT /db_xref="InterPro:IPR000092" FT /db_xref="InterPro:IPR008949" FT /db_xref="InterPro:IPR017446" FT /db_xref="UniProtKB/TrEMBL:A1K476" FT /protein_id="CAL93631.1" FT /translation="MTRVVGHPYHPGFSTSTAVLSVQQLFAPIAADMQAVDALIRKALY FT SDVVLIRQVAEYIINSGGKRLRPALVLFSAGAVGYRGTQHHRLAAVVEFIHTSTLLHDD FT VVDESELRRGNKTANALFGNAASVLVGDFLYTRAFQMMVEVDSMRVMQILADATNIIAE FT GEVLQLLNCHNADVEVEDYLRVIRYKTAKLFEAASRLGAVLGGADPALEESMAAFGMHL FT GTAFQLIDDVLDYSADEADTGKHLGDDLAEGKPTLPLIHVMQHGSAEQAALVRGAIENG FT GRDDFAAVLAAIQQTGALEVTRRHAREEADRAIAALQGLPPSNFKESLLQLSDFAVERN FT H" FT tRNA 1091451..1091527 FT /gene="tRNA-Pro" FT /locus_tag="azo_tRNA_0014" FT /product="transfer RNA-Pro" FT /anticodon=(pos:1091485..1091487,aa:Pro) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 1091631..1092566 FT /transl_table=11 FT /locus_tag="azo1015" FT /product="probable transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="Probable transcriptional regulator, LysR family," FT /note="Family membership" FT /db_xref="GOA:A1K477" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K477" FT /protein_id="CAL93632.1" FT /translation="MPVRPDVRFPSIEGLRAFEAAARLGTFERAADELSVTASAVSKRV FT AAVEELVGALLFSRSGKTLVPTPAGREYLEQVRAALGLLAAMPLHRRAVQRMTRLRVCA FT PPTFARQILVPALDGFVAEHPDVELEIVLSVPYLDAASADVDVEIRHGGPQHHGGDVLI FT RDVLLPMAAPALLAQTGPLTRPADLQRLRLLRTPLEPWTQWFAAAGLDWPEPARGARLV FT DLGLLLEAAVCGQGVALGRPSLARQWLRSGALVALFDVAPPSRTHYFLAPQPASLSETA FT RDVRAAFENWLRAVCAGVEREAAELVSGAP" FT CDS 1092645..1093793 FT /transl_table=11 FT /gene="lldA" FT /locus_tag="azo1016" FT /product="L-lactate dehydrogenase" FT /function="L-lactate dehydrogenase (FMN-dependent) and FT related alpha-hydroxy acid dehydrogenases" FT /EC_number="1.1.2.3" FT /note="L-lactate dehydrogenase. Homology to lldA of N. FT meningitidis of 72% (trembl|Q51135). InterPro: FT FMN-dependent alpha-hydroxy acid dehydrogenases FT (IPR000262); Proteins binding FMN and related compounds FT core region (IPR003009 Pfam: FMN-dependent dehydrogenase no FT signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K478" FT /db_xref="InterPro:IPR000262" FT /db_xref="InterPro:IPR008259" FT /db_xref="InterPro:IPR012133" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:A1K478" FT /protein_id="CAL93633.1" FT /translation="MPAAPITCIDDLRRLALKRVPRMFYDYADSGSWTESTYRANEADF FT QSIKLRQRVAVNMDGRTLRTTMAGQEVAMPVAIAPTGLTGMQHADGEILAARAAEKFGV FT PFTLSTMSICSIEDVAAHTTAPFWFQVYVMRDRDFVERLIDRAKAARCSALMLTLDLQI FT LGQRHKDLKNGLSAPPKPTLANLINLATKPRWCLGMLRTPRRSFGNIVGHARGVGDMSS FT LASWTAEQFDPGLSWADVEWIKKRWGGKLILKGIMDAEDARLAADSGADALVVSNHGGR FT QLDGAPSSIHALPGIVDAVGKSIEVWMDGGIRSGQDVFKAVAMGARGTLIGRAFLYGLG FT AMGEAGVAKSLELIRKELDLTMAFCGHTDIRKVDRRVLLERA" FT CDS complement(1093840..1094649) FT /transl_table=11 FT /gene="comL" FT /locus_tag="azo1017" FT /product="probable competence lipoprotein precursor" FT /function="DNA uptake lipoprotein" FT /note="probable competence lipoprotein comL precursor. FT Homology to comL of N. gonorrhoeae of 47% FT (sprot|COML_NEIGO(SRS)) REQUIRED FOR EFFICIENT FT TRANSFORMATION OF NEISSERIA MENINGITIDIS BY SPECIES-RELATED FT DNA (By similarity). InterPro: TPR repeat (IPR001440) no FT signal peptide no TMH ccoS: cytochrome oxidase maturation FT pro" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K479" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="InterPro:IPR017689" FT /db_xref="UniProtKB/TrEMBL:A1K479" FT /protein_id="CAL93634.1" FT /translation="MARFTLGSVAGKFALIGALLLGACSSLPDEIDETSGWNAQKLYAE FT AKASMTEGGYDRAIKLFEKLEARYPYGRFAQQAQIEVAYAHYKSGEPGLALAAADRFIK FT LHPNHPNVDYVYYLKGLVNFNEDLGLLAGISNQDLSERDPKGAREAFDTFRELVTRFPE FT SKYAEDSRQRMQYLVNSLAAHDVHVARYYYRRGAFIAAANRAQTAVATYPGTPATEEAL FT YLMVKSYEALGLKDLQGDAERVLQKNFPNSVYYSGGPPDRRPWWQLW" FT CDS 1094663..1095637 FT /transl_table=11 FT /gene="rluD" FT /locus_tag="azo1018" FT /product="pseudouridylate synthase" FT /function="Pseudouridylate synthases 23S RNA-specific" FT /EC_number="4.2.1.70" FT /note="Ribosomal large subunit pseudouridine synthase D (EC FT 4.2.1.70) (Uracil hydrolyase). Responsible for synthesis of FT pseudouridine from uracil at positions 1911 1915 and 1917 FT in 23S ribosomal RNA." FT /note="Family membership" FT /db_xref="GOA:A1K480" FT /db_xref="InterPro:IPR002942" FT /db_xref="InterPro:IPR006145" FT /db_xref="InterPro:IPR006224" FT /db_xref="InterPro:IPR006225" FT /db_xref="InterPro:IPR020103" FT /db_xref="UniProtKB/TrEMBL:A1K480" FT /protein_id="CAL93635.1" FT /translation="MNEPEDYSPGDPDARASLPAPRRVPVELAGARLDQVLARLFPEHS FT RSRLQAWLKDGLIRLDGMERQAKHKVHGGEELVVAGLPPLPEQLAFEPEAIPLDVVYED FT ASILVIDKPAGLVVHPGSGNWSGTLLNALLHHAPALAGLPRAGIVHRLDKDTTGLMVVA FT KTLEAQTDLVRQLQQRTVARHYYALVYGDIASDGEIDADIDRHPVQRTRMAVVPGGRPA FT LTRYAVRQRLHGLTLVECRLQTGRTHQIRVHMAHLGHPLVGDPVYGPRRVTDSRVDGFS FT RQALHAFRLGLLHPASGEDMVWSAPLPADFAALLEKVGGRADA" FT CDS 1095700..1096395 FT /transl_table=11 FT /locus_tag="azo1019" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical protein. Homology to CV2191 FT of C.violaceum of 64% (tremble:Q7NVZ9). Has FT PF02578,Uncharacterised ACR, YfiH family COG1496. FT InterPro;IPR003730. No signal peptide. No TMHs. TIGR00726: FT conserved hypothetical protein" FT /db_xref="InterPro:IPR003730" FT /db_xref="InterPro:IPR011324" FT /db_xref="UniProtKB/TrEMBL:A1K481" FT /protein_id="CAL93636.1" FT /translation="MRALLTTRRGGHSAAPYDGFNLGTHVGDRPADVAANRALLQTALP FT AAPCWLDQVHGVDVADADCAHGVPVADAAVARRPGVVCAVMTADCLPVLFSDDAGTVVA FT AAHAGWRGLAAGVLEATVARMAVPPAHILAWLGPAIGPAAFEVGDEVRAAFVSADAGAA FT SAFRPAGTSGKWLADLFQLARRRLAAMGVMHVHGGDTCTYSDAARFYSYRRDGATGRFA FT SLIWREDHA" FT CDS complement(1096434..1096655) FT /transl_table=11 FT /locus_tag="azo1020" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT RS03993 of R.solanacearum of 48% (trembl|Q8XYX6(SRS)). No FT domains. No signal peptide. 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K482" FT /protein_id="CAL93637.1" FT /translation="MYLIAIAWLYVALLAAVSDDSVVGGVLTFIFFGLAPLALFLWLFG FT TPARRRHKAARSATDDSLNDRADSGRDQ" FT CDS 1096743..1098485 FT /transl_table=11 FT /gene="phaC" FT /locus_tag="azo1021" FT /product="probable polyhydroxyalkanoate synthase" FT /function="Poly(3-hydroxyalkanoate) synthetase" FT /EC_number="2.3.1.-" FT /note="Entry name :- TREMBL:Q9ZB54 Prim. accession # Q9ZB54 FT Identities = 290/560 (51%) InterPro:- IPR000073; FT A/b_hydrolase. IPR010941; PhaC_N. Pfam:- PF00561; FT Abhydrolase_1; 1. PF07167; PhaC_N; 1. Prediction: Signal FT peptide Signal peptide probability: 0.999 Number of FT predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K483" FT /db_xref="InterPro:IPR000073" FT /db_xref="InterPro:IPR010941" FT /db_xref="InterPro:IPR010963" FT /db_xref="UniProtKB/TrEMBL:A1K483" FT /protein_id="CAL93638.1" FT /translation="MSNSNEGQAAAAMQAMLLAGQAMAQTFFDNIAKQHSAVEDSGGGG FT VPPLPLPETETFSRLQHDFAEKHLALWSSMLGRKPQQPVAPVVKAVEADKRFNAPEWAD FT SPVFDYVRQAYMLNAGFLKEVADALPIADGRAKSRIQFLTRQYIDALAPTNFAATNPEF FT IRTALETRGESITTGVRNLIADLEKGRISMTDDEAFEVGRNLAVSPGAVIYQNELIQLI FT QYAPLTDKVAQVPLLIVPPCINKFYILDLQPENSLVRFLVEQGHTVFLVSWKNVRPDEG FT NFTWDDYLDKGVFAALDVVRAVTRVKKPNVLGFCVGGTILTSALAVARARGEDPVQSLT FT LMTTLLDFADAGELGCLVDEASVAAREAAIGKGGILRGQELANVFSSLRANDLVWQYVV FT GNYLKGQKPQAFDLLYWNSDSTNLPGPFLTWYLRNMYLENNLRVPGKLKMLGHKVDLGK FT VDAPAYVMAAREDHIVPWASSYLGRHLLGGETTFVLGASGHIAGAINPASKNRRSYWSS FT DAKSADPEEWLEQAVENKGSWWLHWAQWLTAHRGKTVAARGRLGNAKYAPIEPAPGRYV FT KDKA" FT CDS 1098596..1099336 FT /transl_table=11 FT /gene="phbB1" FT /locus_tag="azo1022" FT /product="Acetoacetyl-CoA reductase" FT /function="Dehydrogenases with different specificities FT (related to short-chain alcohol dehydrogenases)" FT /EC_number="1.1.1.36" FT /note="The short-chain dehydrogenases/reductases family FT (SDR) is a very large family of enzymes, most of which are FT known to be NAD- or NADP-dependent FT oxidoreductases,SWISSPROT:P14697 (60% identity); FT TREMBL:Q8XYX3 (59% identity). Pfam (PF00106): Short chain FT dehydrogenase." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K484" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR011283" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K484" FT /protein_id="CAL93639.1" FT /translation="MSRVALVTGGMGGLGEAICIKLAALGYRVVTTYSPGNSKAAEWLQ FT AMNNMGYGFRGYPCDVSDFDSCKACIAQVTEEVGPIDVLVNNAGITRDMTFKKMTKADW FT DAVISTNLDSVFNMTKQVMDGMVERKWGRVINVSSVNGQKGAFGQTNYSAAKAGMHGFT FT KALALEVARSGVTVNTISPGYIGTKMVMAIPQEILESKILPQIPVSRLGKPEEIAGLVA FT YLSSDEAAFVTGANISINGGQHMF" FT CDS 1099528..1100268 FT /transl_table=11 FT /gene="phbB2" FT /locus_tag="azo1023" FT /product="Acetoacetyl-CoA reductase" FT /function="Dehydrogenases with different specificities FT (related to short-chain alcohol dehydrogenases)" FT /EC_number="1.1.1.36" FT /note="The short-chain dehydrogenases/reductases family FT (SDR) is a very large family of enzymes, most of which are FT known to be NAD- or NADP-dependent FT oxidoreductases,SWISSPROT:P14697 (62% identity); FT TREMBL:Q8XYX3 (62% identiy). InterPro (IPR002198): FT Short-chain dehydrogenase/reductase (SDR). InterPro FT (IPR002347): Glucose/ribitol dehydrogenase. Pfam (PF00106): FT Short chain dehydrogenase. SignalP reporting signal FT peptide." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K485" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR011283" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K485" FT /protein_id="CAL93640.1" FT /translation="MSQKVALVTGAMGGLGTAICQSLAKDGIKVVANCLPGFPQKDEWL FT AKQKELGFDFVAAEGDVSDYESCKAMVEKIEAEVGPVDVLVNNAGITRDKFFPKMEKGQ FT WDAVINTNLNSLFNVTHHISPKMAERGWGRIINISSVNGVKGQAGQANYSTAKAGVLGF FT TKALAQELATKGVTVNAIAPGYIGTDMVMAIRDDIRQAITDSVPMKRLGKPEEIGGLCS FT YLASELAGYITGSTININGGLHMC" FT CDS 1100389..1101018 FT /transl_table=11 FT /gene="phbF" FT /locus_tag="azo1024" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="phbF protein, 57% identity to TrEMBL;Q7NYA7. Has 2 FT copies of PF05233, PHB accumulation regulatory FT domain;IPR007897, PHB_accumulat: The proteins this domain FT is found in are typically involved in regulating polymer FT accumulation in bacteria, particularly FT poly-beta-hydroxybutyrate (PHB)" FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR007897" FT /db_xref="InterPro:IPR010134" FT /db_xref="InterPro:IPR012909" FT /db_xref="UniProtKB/TrEMBL:A1K486" FT /protein_id="CAL93641.1" FT /translation="MAEQPRLIKKYPNRRLYDTRTSSYITLADVKELVLGHEEFQVVDA FT KTNEDLTRSILLQIILEEEAGGAPMFTSDLLAHMIRFYGNAMQGMMGKYLENNIKAFTD FT MQGKLQEQARSIYGDNSPVGQDLWAQFLNFQGPALQSMMGTYVEQSKRMFQQMQEQVES FT QTRNMFTGFQFPTYAKGTAKDDAGDKTERTGKAEDATAAGKGSTDK" FT CDS 1101080..1102411 FT /transl_table=11 FT /locus_tag="azo1025" FT /product="hypothetical protein" FT /function="2-methylthioadenine synthetase" FT /note="conserved hypothetical protein" FT /note="Family membership" FT /note="ORF2" FT /db_xref="GOA:A1K487" FT /db_xref="InterPro:IPR002792" FT /db_xref="InterPro:IPR005839" FT /db_xref="InterPro:IPR005840" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR013848" FT /db_xref="InterPro:IPR020612" FT /db_xref="InterPro:IPR023404" FT /db_xref="InterPro:IPR023970" FT /db_xref="UniProtKB/Swiss-Prot:A1K487" FT /protein_id="CAL93642.1" FT /translation="MSNIKTQDVPRVGFVSLGCPKATSDSEHILTRLRAEGYEISGSYD FT AADLVVVNTCGFIDAAVEESLDAIGEALAENGRVIVTGCLGAKDDVILAAHPQVLAVTG FT PHATEEVMQAVHRHLPKPHDPFSDLVPPQGIRLTPQHYAYLKISEGCNHRCTFCIIPSM FT RGDLVSRPIHDVMREAEALADAGVKELLVISQDTSAYGVDVKYRTGFWGGKPVKTRLYD FT LANALGELGIWIRMHYVYPYPSVDDLIPLMAEGKILPYLDVPFQHASPRILKAMKRPAN FT AENVLERVRKWREICPDLTIRSTFITGFPGETEEDFEQLLQFLEAAQLDRVGAFAYSPV FT EGAAANDLPDAVPDEVREERRARLMDFQEDISTQRLEAKIGREMTVLVDDVDEEGALAR FT SPGDAPEIDGLVVIPDGEGLAPGDFVRVRITDCDIHDLYAERVV" FT CDS 1102525..1103373 FT /transl_table=11 FT /gene="ychK" FT /locus_tag="azo1026" FT /product="probable esterase" FT /function="predicted esterase of the alpha-beta hydrolase FT superfamily" FT /note="Hypothetical protein ychK. TREMBL:Q89IT4: 42% FT identity, 58% similarity InterPro: Uncharacterized protein FT family UPF0028 InterPro:IPR002641; Patatin. Pfam:PF01734; FT Patatin hypA: hydrogenase expression/formation FT Non-secretory protein with signalpeptide probability:0.141 FT (SignalP predicted) Absence of TMH's" FT /note="Family membership" FT /db_xref="GOA:A1K488" FT /db_xref="InterPro:IPR002641" FT /db_xref="InterPro:IPR016035" FT /db_xref="UniProtKB/TrEMBL:A1K488" FT /protein_id="CAL93643.1" FT /translation="MLRALAADGIVPDVVCGCSIGAFVGAAAASGDLGKITDWAQSLKW FT QDVVSLLDVSLRGGLIKGERLIQFFQRNFVDRDFSELPTRFACVATELGSGREIWLHEG FT SVSAAVRASIALPGLMTPVLYRGKVLVDGGLVNPVPVSLCRAMGADLVIAVDLGSDMVG FT RAWKHAAVEPAPIEETESGWSDRLLARFRFGAAAGPNSAVEANLPSLITVLSSSINVMQ FT VRIARSRLAGEPADVLVSPRVGQLGLLDYHRAAEAIAEGEAAVARVRPLLDYALGRAGS FT A" FT CDS 1103397..1104803 FT /transl_table=11 FT /gene="glcD2" FT /locus_tag="azo1027" FT /product="putative glycolate oxidase subunit GlcD" FT /function="FAD/FMN-containing dehydrogenases" FT /note="Putative glycolate oxidase subunit GlcD. Homology to FT glcD of E. coli of 32% (sprot|GLCD_ECOLI). InterPro: FAD FT linked oxidase C-terminal (IPR004113);m FAD linked oxidas, FT N-terminal (IPR006093) Pfam: FAD binding domain; FAD linked FT oxidase, C-terminal domain Tigrfam: glcD: glycolate oxidase FT subunit GlcD no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K489" FT /db_xref="InterPro:IPR004113" FT /db_xref="InterPro:IPR006094" FT /db_xref="InterPro:IPR016164" FT /db_xref="InterPro:IPR016166" FT /db_xref="InterPro:IPR016167" FT /db_xref="InterPro:IPR016168" FT /db_xref="InterPro:IPR016171" FT /db_xref="UniProtKB/TrEMBL:A1K489" FT /protein_id="CAL93644.1" FT /translation="MDRIVEELIGIVGEANVLTTADDMAPYLTDWRGRYRGHARAVVRP FT AATAEVSAVLAACHAAAVPVVPQGGNTGLCGGATPSEAGVAVVLSLTRMNRIRSLDPDN FT NTVGVEAGCTLAALQEAAAAAERLFPLSLASEGSCTIGGNLSTNAGGVQVLRYGNTREL FT TLGLEVVLPDGRIWDGMRGLRKDNTGYDLKHLFIGAEGTLGVITAAVLKLFPAPRGFAT FT AWAAVSDPAAAVRLLGRLRHHCGDRISAFELVGRPALDLVLKHIPGARDPFSAPTQWAV FT LIELSDSLEGEGLAETLAGALGAEMEAGLVLDAVVASSLGQAQALWALRENISEAQRIE FT GVSIKHDVSVPVSRIAEFLERADVSLKSQWPGVRIVAFGHIGDGNLHYNLSRSETDDNA FT SFIARTEDVNRIVHDLVDALGGSISAEHGLGQLKRAEIRRYKSTVEMDMMEAIKNAFDP FT SRLMNPGKVL" FT tRNA 1104890..1104965 FT /gene="tRNA-Ala" FT /locus_tag="azo_tRNA_0015" FT /product="transfer RNA-Ala" FT /anticodon=(pos:1104923..1104925,aa:Ala) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA 1104986..1105061 FT /gene="tRNA-Glu" FT /locus_tag="azo_tRNA_0016" FT /product="transfer RNA-Glu" FT /anticodon=(pos:1105020..1105022,aa:Glu) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA 1105124..1105200 FT /gene="tRNA-Asp" FT /locus_tag="azo_tRNA_0017" FT /product="transfer RNA-Asp" FT /anticodon=(pos:1105158..1105160,aa:Asp) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA 1105287..1105362 FT /gene="tRNA-Ala" FT /locus_tag="azo_tRNA_0018" FT /product="transfer RNA-Ala" FT /anticodon=(pos:1105320..1105322,aa:Ala) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA 1105372..1105447 FT /gene="tRNA-Glu" FT /locus_tag="azo_tRNA_0019" FT /product="transfer RNA-Glu" FT /anticodon=(pos:1105406..1105408,aa:Glu) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA 1105508..1105584 FT /gene="tRNA-Asp" FT /locus_tag="azo_tRNA_0020" FT /product="transfer RNA-Asp" FT /anticodon=(pos:1105542..1105544,aa:Asp) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 1105799..1106650 FT /transl_table=11 FT /gene="hbdA" FT /locus_tag="azo1028" FT /product="probable 3-hydroxybutyryl-CoA dehydrogenase" FT /function="3-hydroxyacyl-CoA dehydrogenase" FT /EC_number="1.1.1.157" FT /note="Activity:- (S)-3-hydroxybutanoyl-CoA + NADP+ = FT 3-acetoacetyl-CoA + NADPH + H+ Entry name :- TREMBL:Q89GX2 FT Prim. accession # Q89GX2 Identities = 177/280 (63%) FT InterPro:- IPR006108; 3HCDH_C. IPR006176; 3HCDH_N. FT IPR008927; 6DGDH_C_like. IPR000205; NAD_BS. Pfam :-PF00725; FT 3HCDH; 1. PF02737; 3HCDH_N; 1. Prediction: Signal peptide FT Signal peptide probability: 0.873 Number of predicted TMHs: FT 0" FT /note="Family membership" FT /db_xref="GOA:A1K490" FT /db_xref="InterPro:IPR006108" FT /db_xref="InterPro:IPR006176" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR022694" FT /db_xref="UniProtKB/TrEMBL:A1K490" FT /protein_id="CAL93645.1" FT /translation="MSIKKVGVVGAGTMGNGIVQAFAVAGFDVVMTDIADAALQRGVQT FT ISGSFDRLIKKEKMTCDEKAAALGRVKTSTDLDAMADVDLVIEAATENLDLKLKIFAQL FT DSVVKADAIVASNTSSISITKLAAAMKRPEQFVGMHFFNPVPMMALVELIRGLQTSDAT FT YAAVEAAAKAVGKTPVQVRNSPGFVVNRLLCPMINEAIFALGEGLATAAEIDEAMKLGC FT NHPIGPLALCDLIGLDVELAVMQVLFEGFKDPKYRPAPLLVEMVEAGRLGRKVGKGFFD FT YA" FT CDS complement(1106727..1108178) FT /transl_table=11 FT /gene="rho" FT /locus_tag="azo1029" FT /product="transcription termination factor Rho" FT /function="Transcription termination factor" FT /note="Transcription termination factor rho. Facilitates FT transcription termination by a mechanism that involves Rho FT binding to the nascent RNA activation of Rhos RNA-dependent FT ATPase activity and release of the mRNA from the DNA FT template. Similar to SWISSPROT: sprot|RHO_ECOLI (60% FT Escherichia coli, transcription termination factor Rho) FT InterPro: IPR000194 ATPase_a/bcentre. IPR003593 AAA_ATPase. FT IPR004665 Term_rho. IPR002059 Cold_shock. Pfam: PF00006 FT ATP-synt_ab. TIGRFAM: TIGR00767 transcription termination FT factor Rho." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K491" FT /db_xref="InterPro:IPR000194" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR004665" FT /db_xref="InterPro:IPR011112" FT /db_xref="InterPro:IPR011113" FT /db_xref="InterPro:IPR011129" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="UniProtKB/TrEMBL:A1K491" FT /protein_id="CAL93646.1" FT /translation="MTATSKPEATPARSRGASRTRRRGARNRDGNSPQGNTSELDLLDA FT ELAMEEGSASSAESTAAAALHLSELKALHVSQLLEMAVANEIEGANRLRKQELVFALLK FT NRARKGEPIYGDGALEVLPDGFGFLRSPDTSYLAGTDDIYVSPSQIRRFNLHTGDTIEG FT EIRTPKDGERYFALVKLDKINGRPPEECKHKILFENLTPLHPQECLKLEREIRGEENVT FT SRIIDMIAPIGKGQRGLLVAPPKSGKTVMLQHIAHAITANHPDVELIVLLIDERPEEVT FT EMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLTEHKKDVVILLDSLTRLARAYNT FT VVPASGKVLTGGVDANALQKPKRFFGAARNIEEGGSLTIIATALIDTGSRMDDVIYEEF FT KGTGNMELHLDRRMAEKRVYPAINVNRSGTRREELLMKPDVLQKIWILRKLLYGMDDID FT AMEFLLDKVKATKGNAEFFDAMRRG" FT CDS complement(1108162..1108488) FT /transl_table=11 FT /gene="trxA1" FT /locus_tag="azo1030" FT /product="thioredoxin-disulfide reductase" FT /function="Thiol-disulfide isomerase and thioredoxins" FT /EC_number="1.8.1.9" FT /note="Thioredoxin-disulfide reductase. Homology to trxA of FT T. ferrooxidans of 69% (THIO_THIFE). Participates in FT various redox reactions through the reversible oxidation of FT its active center dithiol to a disulfide. InterPro: FT Thioredoxin (IPR006662) Pfam: Thioredoxin no signal peptide FT no TMHs" FT /note="Specificity unclear" FT /db_xref="GOA:A1K492" FT /db_xref="InterPro:IPR005746" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR013766" FT /db_xref="InterPro:IPR017937" FT /db_xref="UniProtKB/TrEMBL:A1K492" FT /protein_id="CAL93647.1" FT /translation="MSEHIHYVTDGSFEAEVLQSQTPVLVDYWAEWCGPCKMIAPILDE FT VAKDYAGKLKVAKLNIDENQETPAKYGIRGIPTLMIFKGGNIEATKVGALSKSQLTAFI FT DSNI" FT CDS 1108784..1109107 FT /transl_table=11 FT /gene="fdxA" FT /locus_tag="azo1031" FT /product="probable ferredoxin" FT /function="Ferredoxin" FT /note="Probable ferredoxin. Homology to fdxA of A. FT vineladii of 66% (sprot|FER1_AZOVI(SRS)). FERREDOXINS ARE FT IRON-SULFUR PROTEINS THAT TRANSFER ELECTRONS IN A WIDE FT VARIETY OF METABOLIC REACTIONS. THIS FERREDOXIN COULD PLAY FT A ROLE IN REGULATING GENE EXPRESSION BY INTERACTING FT DIRECTLY WITH DNA. InterPro: 4Fe-4S ferredoxin iron-sulfur FT binding domain IPR001450); 7Fe ferredoxin (IPR000813) Pfam: FT 4Fe-4S binding domain no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K493" FT /db_xref="InterPro:IPR000813" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="InterPro:IPR022569" FT /db_xref="UniProtKB/TrEMBL:A1K493" FT /protein_id="CAL93648.1" FT /translation="MAYVVTESCIRCKYTDCVDVCPVDCFREGENFLVIDPEECIDCTL FT CVAECPVEAIYAEDDVPADQQQFIALNAELARTWKPIVERKEPLPDAEQWAKVKGKTGE FT LKR" FT CDS 1109179..1109628 FT /transl_table=11 FT /locus_tag="azo1032" FT /product="conserved hypothetical protein" FT /function="FOG: CBS domain" FT /note="TREMBL:Q8XZ43; 52% identity, 70% similarity. FT TREMBL:Q8F5Y8; 30% identity, 56% similarity. Protein FT At5g10860 mitochondrial precursor. IPR000644: CBS domain FT Pfam:PF00571 - GARS_N TIGRFAM: rrf2 family, KpsF/GutQ FT family (by similarity) kpsF: KpsF/GutQ family protein" FT /note="Specificity unclear" FT /db_xref="InterPro:IPR000644" FT /db_xref="UniProtKB/TrEMBL:A1K494" FT /protein_id="CAL93649.1" FT /translation="MLVSEILAIKGKVLYTIAPNRSLAEAVTIMTEQDVGSLVVFAQGQ FT MAGLLTFREVLQAVHKGGGGWESLPVETAMLKGPLTAAPTMEMDELRRLMVDRHQRYLP FT VMDGNTLLGVVSFHDVAKAVLEEQSFENRMLKNYIRNWPAEEGEA" FT CDS 1109767..1111458 FT /transl_table=11 FT /gene="fadD1" FT /locus_tag="azo1033" FT /product="Long-chain-fatty-acid-CoA ligase" FT /function="Acyl-CoA synthetases (AMP-forming)/AMP-acid FT ligases II" FT /EC_number="6.2.1.3" FT /note="Esterification concomitant with transport of FT exogenous long-chain fatty acids into metabolically active FT CoA thioesters for subsequent degradation or incorporation FT into phospholipids, TREMBL:Q7NY16 (61% identity); FT TREMBL:Q7WLG0 (63% identity). InterPro (IPR000873): FT AMP-dependent synthetase and ligase Pfam (PF00501): FT AMP-binding enzyme." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K495" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR020845" FT /db_xref="UniProtKB/TrEMBL:A1K495" FT /protein_id="CAL93650.1" FT /translation="MSVDKIWLKSYPAGVPAEVDVGEFASIGDLFEQGVRRYGSRPAYI FT CMGRSLAYDELDVLVSRFAAYLQGELKLAHGARVALMMPNVLQYPVAMFAALRAGYTVV FT NVNPLYTARELEHQLRDAAAEAVILLENFAHTLEMVVQHLPIRHVVVTSVGDLLGFPKG FT AVVDFVLRRVRKLVPPWKLPGAVRFREALAAGAKHTFRPADVGHDDIAYLQYTGGTTGT FT AKGAILTHGNIIANLQQAHAWIRPQVREGAEVIITALPLYHIFSLTANCLTFFKIGATN FT VLITNPRDIRGFVKELGKHRFTAITGVNTLFNALLNNPDFARLDFSALHITLGGGMAVQ FT QAVAEKWRAVTGVPLIEAYGLTETSPAVAINPLDLKAFNHSIGLPVPSTEVSIRDDDGV FT EQPPGQRGELCVRGPQVTRGYWNRPEDSARAFTPDGFLRTGDIAVMDEAGYLRIVDRKK FT DMILVSGFNVYPNEVEDVVASHPGVLEVAAVGVPDARSGEAVKVFVVRKDASLTEADLI FT AYCRENLTAYKVPHRVVFRESLPKTNVGKILRRALRDEDEAAARQP" FT CDS 1111730..1113397 FT /transl_table=11 FT /gene="ilvB" FT /locus_tag="azo1034" FT /product="acetolactate synthase" FT /function="Thiamine pyrophosphate-requiring enzymes FT [acetolactate synthase pyruvate dehydrogenase (cytochrome) FT glyoxylate carboligase phosphonopyruvate decarboxylase]" FT /EC_number="2.2.1.6" FT /note="Acetolactate synthase isozyme I large subunit FT (AHAS-I) (Acetohydroxy-acid synthase I large subunit) FT (ALS-I). InterPro: Acetolactate synthase large subunit FT biosynthetic type acolac_lg: acetolactate synthase large FT subunit,biosynthetic type" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K496" FT /db_xref="InterPro:IPR000399" FT /db_xref="InterPro:IPR011766" FT /db_xref="InterPro:IPR012000" FT /db_xref="InterPro:IPR012001" FT /db_xref="InterPro:IPR012846" FT /db_xref="UniProtKB/TrEMBL:A1K496" FT /protein_id="CAL93651.1" FT /translation="MNQMTGAELIVRLLERQGVRTIAGIPGGAILPLYDALSQSDLIEH FT VLARHEQGAGFMAQGMARVSGVPGVCFASSGPGATNLVTAIADAQLDSIPMVAITGQVP FT LPMIGTDAFQEVDIYGMTVPITKHNFLVRSAEELLKVIPEAFRIAMSGRPGPVLVDVPK FT DVQNQRIEFAEFPPPAGRDAVPALDAAAIDRAAAMINEAERPVLYLGGGVIHSGASAQA FT VTLAEQAGLPTTMTLMALGAMAVDHPLSIGMLGMHGARYTNYVLEEADLLVCVGARFDD FT RAIGRAAQFCPGARIVHIDVDPSELHKIKTAHVAIHGDVAAVLDALLPKVKVQLRKRWL FT SHVESLKSRFPMQMPDLDDPRSHYGLIHAVAAALDDEAVIATDVGQHQMWVAQAYPFRR FT ARQWLTSGGLGTMGFGMPTAIGAALAAPERTVVCFSGDGSLQMNIQELATLAELGLNVK FT IVLMNNNSLGLVYQQQNLFYGKRTFASKYRGGPDFCRIAEGYGIAAVDLDASDNPRATL FT AEALQAPGPCLIHASIDREQFVYPMVPPGAANTEMIGG" FT CDS 1113400..1113714 FT /transl_table=11 FT /gene="ilvN" FT /locus_tag="azo1035" FT /product="acetolactate synthase" FT /function="Acetolactate synthase small (regulatory) FT subunit" FT /EC_number="2.2.1.6" FT /note="Acetolactate synthase isozyme I small subunit (EC FT 2.2.1.6) (AHAS-I) (Acetohydroxy-acid synthase I small FT subunit) (ALS-I). InterPro: Acetolactate synthase small FT subunit acolac_sm: acetolactate synthase small subunit" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K497" FT /db_xref="InterPro:IPR002912" FT /db_xref="UniProtKB/TrEMBL:A1K497" FT /protein_id="CAL93652.1" FT /translation="MIEQVADPLPQAGFAKVVLELEVRNHPGVMSHICNLFARRAFNVE FT GILCMPVSDGKKSRIWLLVFEDQRLEQMLRQLEKLEDVLAVRRHGAEHEVFERLEDFFH FT " FT CDS 1113825..1114961 FT /transl_table=11 FT /gene="aroC" FT /locus_tag="azo1036" FT /product="AroC protein" FT /function="Chorismate synthase" FT /EC_number="4.2.3.5" FT /note="Chorismate synthase, AroC. It catalyzes the FT 1,4-trans elimination of the phosphate group from FT 5-enolpyruvylshikimate-3-phosphate (EPSP) to form FT chorismate which can then be used in phenylalanine, FT tyrosine or tryptophan biosynthesis. Similar to FT sprot|AROC_VIBAN (60%) and to sprot|AROC_ECOLI (61%). FT TIGRFAM: chorismate synthase, aroC Pfam : Chorismate FT synthase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K498" FT /db_xref="InterPro:IPR000453" FT /db_xref="InterPro:IPR020541" FT /db_xref="UniProtKB/Swiss-Prot:A1K498" FT /protein_id="CAL93653.1" FT /translation="MSGNTLGTLFCVTSFGESHGPAIGCVIDGCPPGLSLTAADIQGEL FT DRRKPGTSRHVTQRREPDEVEILSGVFEGVTTGTPIALLIRNQDQRSKDYGNIAETFRP FT GHADYPYWQKYGIRDYRGGGRSSARETAVRVAAGAVARKWLSERYGIVIRGYMAQLGPL FT PIPFVSWDAVGDNPFFAPNAEIVPQLESYMDELRKSGDSVGARINVVASGVPVGWGEPV FT YDRLDADIAYAMMSINAVKGVEIGAGFASVAQLGTEHGDELTPEGFLSNNAGGVLGGIS FT SGQDVLVSMAIKPTSSIRLDRRSIDREGNPVIVNTHGRHDPCVGIRATPVAEAMLALVL FT MDHALRHRAQCGDVRTATPQIAALAPEGVQAVPSPRAE" FT CDS 1114958..1116148 FT /transl_table=11 FT /locus_tag="azo1037" FT /product="putative MFS metabolite transporter" FT /function="Permeases of the major facilitator superfamily" FT /note="Putative transport protein. Similarity to sugar FT transporters (lacY): lactose permease 2A0105.Similar to POT FT family of proteins with DUF domains and 12 transmembrane FT helices. 31% identity and 47% similarity to putative MFS FT metabolite transporter from Pseudomonas aeruginosa PA01" FT /note="Family membership" FT /db_xref="InterPro:IPR016196" FT /db_xref="UniProtKB/TrEMBL:A1K499" FT /protein_id="CAL93654.1" FT /translation="MTTAGGSGAGLPYWRLSAYYFSYFAFVGAFSPYFTLYLKALDFSA FT TEIAVLMSLMQVMRVLAPNLWGWLAEHLGVRLPIVRLSALMSVAGFAVFFFTESFSGIF FT AGMALMSFFWAAALPLVESLTFAHLATAAHRYGSIRAWGSVGFIAAVVGLGALLDLLPI FT RAVLWGTTAVLGAILVCSLLLPEAARAATRGAGASLREVLGRSEVKALLGACFLMSAAH FT GAFYVFFSILLVDHGYGKAAVGALWALGVVSEIIVFMFMPRLMRRVPLRAILLFAFCCA FT VVRFVLTGWGAASVAVVAAAQVLHGVTFGAYHAAAIAAINRWFSGRLQARGQALYGSLS FT FGAGGMLGGLVSGLGWETIGPAWTFTLGSVFALAGLLWLKLGWRPGLGDEVAGARA" FT CDS 1116163..1116984 FT /transl_table=11 FT /locus_tag="azo1038" FT /product="conserved hypothetical secreted protein" FT /function="Zn-dependent protease with chaperone function" FT /note="Conserved hypothetical secreted protein. Homology to FT bb2112 of B. bronchiseptica of 55% (trembl|Q7WKJ4). Pfam: FT Peptidase family M48 signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4A0" FT /db_xref="InterPro:IPR001915" FT /db_xref="UniProtKB/TrEMBL:A1K4A0" FT /protein_id="CAL93655.1" FT /translation="MKFLTQRVLPAALAVTMAVACQTVQTTGGGAVGVDRSQSMLISAQ FT EIEQASNQQYQEVLAEARRKNALNRNPEQVQRVRRIAARLTPATAAFRSDAPAWRWEVN FT VLSSDELNAWCMAGGKIAFYSGLIERLNLSDDEIAAVMGHEIAHALREHARERVSKAMA FT TGLGISVAGALLGVGQTGQDLMGTVAKVTFELPNSRLHETEADRIGVELAARGGYDPRA FT AVTLWNKMAAQSNGAPPQWLSTHPSHDSRQQDLANYAQRVMPLYERSRAGR" FT CDS 1117079..1118488 FT /transl_table=11 FT /gene="leuC" FT /locus_tag="azo1039" FT /product="LeuC protein" FT /function="3-isopropylmalate dehydratase large subunit" FT /EC_number="4.2.1.33" FT /note="3-isopropylmalate dehydratase large subunit," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4A1" FT /db_xref="InterPro:IPR001030" FT /db_xref="InterPro:IPR004430" FT /db_xref="InterPro:IPR015931" FT /db_xref="InterPro:IPR015932" FT /db_xref="InterPro:IPR015936" FT /db_xref="InterPro:IPR015937" FT /db_xref="InterPro:IPR018136" FT /db_xref="UniProtKB/Swiss-Prot:A1K4A1" FT /protein_id="CAL93656.1" FT /translation="MEAQTLYEKLWSSHVVHQEADGTALIYIDRHLVHEVTSPQAFEGL FT KLAGRKPWRISSIVATADHNIPTDHWEMGIQDPVSRQQVETLDANIREVGSLAYFPFKD FT QRQGIIHVIGPENGTTLPGMTVVCGDSHTSTHGAFACLAHGIGTSEVEHVMATQCLLQK FT KSKTMLIKVEGTLGRGVTAKDVVLAIIGRIGTAGGTGYAIEFGGSAIRSLSMEGRMTVC FT NMAIEAGARAGLVAVDETTIDYLKDKPFAPKGPQWDAAVAYWRTLKSDDGATFDTVVEL FT DATSILPQVTWGTSPEMVTTVDGRVPDPAAIADPVKREGVERALKYMGLAPNTPISEIA FT VDQVFIGSCTNSRIEDLREAAAVVKGRSKAASVRRVLVVPGSGLVKHQAEAEGLDKVFI FT EAGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAV FT TGHFTDVRTLN" FT CDS 1118505..1119143 FT /transl_table=11 FT /gene="leuD" FT /locus_tag="azo1040" FT /product="LeuD protein" FT /function="3-isopropylmalate dehydratase small subunit" FT /note="3-isopropylmalate dehydratase small subunit, leuD. FT Similar to sprot|LEUD_AZOVI (78%). 3-isopropylmalate FT dehydratase bind a Fe-4S iron-sulphur cluster and is split FT into large (leuC) and small chains in eubacteria. TIGRFAM: FT 3-isopropylmalate dehydratase, small, leuD Pfam: Aconitase FT C-terminal domain" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4A2" FT /db_xref="InterPro:IPR000573" FT /db_xref="InterPro:IPR004431" FT /db_xref="InterPro:IPR015928" FT /db_xref="InterPro:IPR015936" FT /db_xref="InterPro:IPR015937" FT /db_xref="UniProtKB/Swiss-Prot:A1K4A2" FT /protein_id="CAL93657.1" FT /translation="MKPFTVLDAIVAPLDRANVDTDAIIPKQFLKSIKRSGFGPNLFDE FT WRYLDVGQPGQDCSNRPKNPDFVLNQARYQGAQVLLARDNFGCGSSREHAPWALEDYGF FT RVIIAPSFADIFFNNSFKNGLLPIKLDAAELDVLFQQCEATEGYRLKVDLAAQTITRPD FT GKAIAFDVDPFRKECLLNGWDDIGLTLRHADKIRDFEAKRRAEHPYYFA" FT CDS 1119180..1120244 FT /transl_table=11 FT /gene="leuB" FT /locus_tag="azo1041" FT /product="3-isopropylmalate dehydrogenase" FT /function="Isocitrate/isopropylmalate dehydrogenase" FT /EC_number="1.1.1.85" FT /note="3-isopropylmalate dehydrogenase, leuB. Similar to FT sprot|LEU3_PSEAE (70%). 3-isopropylmalate dehydrogenase FT (IMDH) catalyzes the third step in the biosynthesis of FT leucine in bacteria and fungi, the oxidative FT decarboxylation of 3-isopropylmalate into FT 2-oxo-4-methylvalerate. InterPro (PF00180): Isocitrate and FT isopropylmalate dehydrogenases TIGRFAM : 3-isopropylmalate FT dehydrogenase, leuB" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4A3" FT /db_xref="InterPro:IPR001804" FT /db_xref="InterPro:IPR004429" FT /db_xref="InterPro:IPR019818" FT /db_xref="InterPro:IPR024084" FT /db_xref="UniProtKB/TrEMBL:A1K4A3" FT /protein_id="CAL93658.1" FT /translation="MKICVLPGDGIGPEITAEAVRVLRALDLKIELEEALLGGSAVDAT FT GTPYPEATQKLARAADAVLLGAVGGPKWDTLPREQRPERGLLGIRKDLSLFANLRPAIL FT YPELANASTLKPEVVSGLDILIVRELTGDIYFGQPRGIETREVNGAQQRVGWNTMIYAE FT YEIRRILKVAFEAAQKRGKKLCSVDKMNVLETTQLWRDIADEMAKDFPDVELSHMLVDN FT AAMQLVRNPKQFDVMVTGNMFGDILSDEASMLTGSIGMLPSASLDANNKGLYEPSHGSA FT PDIAGKGVANPLATILSAAMMLRYTFNQEEAAVRIERAVKKVLAQGFRTGDIYEAGTKK FT VGTREMGDAVLAAL" FT CDS 1120327..1121427 FT /transl_table=11 FT /gene="asd" FT /locus_tag="azo1042" FT /product="Asd protein" FT /function="Aspartate-semialdehyde dehydrogenase" FT /EC_number="1.2.1.11" FT /note="Aspartate-semialdehyde dehydrogenase, an enzyme FT involved in the biosynthesis of various amino acids from FT aspartate. Similar to sprot|DHAS_ECOLI (67%) and to FT trembl|Q845W2 (75%). Pfam: Semialdehyde FT dehydrogenase,dimerisation Pfam: Semialdehyde FT dehydrogenase, NAD binding" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4A4" FT /db_xref="InterPro:IPR000319" FT /db_xref="InterPro:IPR000534" FT /db_xref="InterPro:IPR011534" FT /db_xref="InterPro:IPR012080" FT /db_xref="InterPro:IPR012280" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K4A4" FT /protein_id="CAL93659.1" FT /translation="MVGSVLMQRMVDEGDFAHIEPVYFSTSAAGGKAPVFGGKEAALPL FT QDATSIDALKACDIIITCQGGDYTKEVFPKLRASGWDGHWIDAASALRMADDAVIILDP FT VNMHVIKDALAKGGKNWIGGNCTVSLMLMGLGGLFKHDLVEWVSAMTYQAASGAGAQNM FT RELIAQMGTIHASVADLLADPASAILDIDRKVAETIRSDSFPKKNFRNTPLAGSLIPWI FT DVPVDGGQSKEEWKGGAECNKILGKPAFRSQGSIPIDGLCVRIGAMRCHSQGLTIKLKK FT DVPLDEVTEIIATANDWVKVVPNEREISERELTPAAVTGTLTVPVGRLHKLAMGPDYLG FT AFTVGDQLLWGAAEPLRRMLRILLDA" FT CDS 1121643..1124558 FT /transl_table=11 FT /gene="fimV1" FT /locus_tag="azo1043" FT /product="putative type 4 pilus biogenesis" FT /function="Tfp pilus assembly protein FimV" FT /note="In Pseudomonas aeruginosa, FimV ist probable FT involved in remodelling of the peptidoglycan layer to FT enable assembly of the type IV fimbrial structure and FT machinery. And it is also required for twitching motility. FT Similar to trembl|O87015 (28%). Pfam (PF01476): LysM domain FT Pfam (PF04102): SlyX, may be a coiled-coil structure FT SignalP reporting Signal peptide" FT /note="Function unclear" FT /db_xref="GOA:A1K4A5" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR020011" FT /db_xref="InterPro:IPR020012" FT /db_xref="UniProtKB/TrEMBL:A1K4A5" FT /protein_id="CAL93660.1" FT /translation="MKKSLKASLIAVAIASFPFGSQAAGLGQINVLSGLGQPLRAEIQI FT NASPQELQSLRARIGSPESFRQANVPYSPVIPTLRVAVESRGSRSVVKLSTDRPVSDPF FT VDLLLELDWEGGRLSREYTFLLDPVDLGAPRALGARVDTPAAAPVPRSPRAEVAPRAPA FT VPAAAGSASADAGSYRVQRGDTLRRIADNTRPADASLDQMLVALFRANPAAFEGNNINR FT LKAGAILTVPPASTVQGLDPQEARREVLAQSADFDAYRRRLASSAVERPAEGQVEQAAG FT GRIVPRVDAPASTPSGDKLKVSRTQSGETAAGTEVANRLQSLEEELVSREKALDEANAR FT LAQLEQNIRELQKLLQLKSESLAQAQAAAGGAPAPATTPAPAPAAPAPADTPPAASAPA FT PGAEAPAAAVTPATPPAESKPAEAPKPKPKKVVPPPEPEPEPGFLESMLGNPTILAAGG FT GILALLLAYAGLRMRGRSAKKNATDSAALISEFPPESSGVFGATGGQSVDTSNSSVIHT FT DFSQSGLSAIDADEGVDPVAEADVYMAYGRDAQAEEILLDALKADPERLAIPLKLLEIY FT SKRKSAKQFESIASELYARTGGKGLDWEKTALMGRKLDPDNPLYSSKTVEPERTEAPST FT EMPAAPLAAAGVAGAAAAAVALEAAEQDAPEAPALANLDFTTSMSGVSNPQELTATWTE FT GVGQIGADAPEAPAEEPAADEQPVSMDVNLDALDFDLELDAPTPAAAPAAAAAPDLAAT FT SDLMLNLDLGGDTAPLGQGEEVDSAAPGNAAETGTVTVIGQDLDFAAADDAGLTFDLPE FT LSAPAPQADSPDLNATVVQADALEFGGDAAATTDLEATSFDSNLLDFDFDLDTPAATAA FT PAAPAAGLDLTSIDLNLEPPADADLGFDASPSVDELPALDGTAATVDSGIDQEVETKLE FT LARAYEEMGDKDGARELLDEVVREGTPTQQAAARELIARLA" FT CDS 1124621..1125232 FT /transl_table=11 FT /locus_tag="azo1044" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT ebA4769 of Azoarcus sp. EbN1 of 53% FT (gnl|keqq|eba:ebA4769(KEGG)). Pfam: Cobalt transport FT protein. signal peptide. 3 TMHs" FT /note="Family membership" FT /db_xref="InterPro:IPR003339" FT /db_xref="UniProtKB/TrEMBL:A1K4A6" FT /protein_id="CAL93661.1" FT /translation="MHAALVLLLWLVAVVVIQALPGPALLVAVAASIGVAAVIARPRAL FT RLMRRVRFLLLAIVVLFAGFTPGEALVADWPLLSPTREGVALALIHAGRLLAVVAAVAV FT LLEVLPAARLVGGLHVLCGPLRWIGVPPERVAVRLLLVLRYVETTPRGSGKSWHAWLVE FT EDSAAEEGMLLQREQWRARDVAVLLTVVLGLGLWVSGVVW" FT CDS 1125226..1126023 FT /transl_table=11 FT /locus_tag="azo1045" FT /product="pseudouridine synthase A" FT /function="Pseudouridylate synthase (tRNA psi55)" FT /EC_number="4.2.1.70" FT /note="Formation of pseudouridine at positions 38 39 and 40 FT in the anticodon stem and loop of transfer RNAs. InterPro: FT tRNA pseudouridine synthase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4A7" FT /db_xref="InterPro:IPR001406" FT /db_xref="InterPro:IPR020094" FT /db_xref="InterPro:IPR020095" FT /db_xref="InterPro:IPR020097" FT /db_xref="InterPro:IPR020103" FT /db_xref="UniProtKB/TrEMBL:A1K4A7" FT /protein_id="CAL93662.1" FT /translation="MVRLALGVEYAGDRFEGWQSQRHGRTVQDALEAALSRIAGEAVKL FT HCAGRTDTGVHATAQVAHFDTAAVRPLSAWIRGVNTHLPAGVAVRWAVEVDDAFHARFL FT AYERRYRYVLFNAPTRPALLAGRVGWFHLPLDEGAMAEAARCLVGMQDFSAFRAAECQA FT KTPVRDMREVRVQRSGDYLIFDFRADGFLHHMIRNLVGALVYVGKGRYPPGWLAEVLAG FT RDRSRAAPTFAPDGLYLCGVSYPGNWSLPDDGRIIALPRIPLV" FT CDS 1126024..1126647 FT /transl_table=11 FT /gene="trpF" FT /locus_tag="azo1046" FT /product="N-(5'-phosphoribosyl)anthranilate isomerase" FT /function="Phosphoribosylanthranilate isomerase" FT /EC_number="5.3.1.24" FT /note="N-(5-phosphoribosyl)anthranilate isomerase (PRAI) FT catalyzes the third step of tryptophan biosynthesis. FT Similar to sprot|TRPF_RALSO (56%) and to sprot|TRPF_PSEAE FT (58%). Pfam (PF00697): N-(5'phosphoribosyl)anthranilate FT isomerase (PRAI)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4A8" FT /db_xref="InterPro:IPR001240" FT /db_xref="InterPro:IPR011060" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:A1K4A8" FT /protein_id="CAL93663.1" FT /translation="MSRTRIKICGLTRPDDVRAAVDAGADAIGFVFYPPSPRAVDFGRA FT AELAALLPPFVTAVGLFVNPTREFVAAACAEVPLQLLQFHGDETEAECASHGRPWIKAA FT RVRAGTDLVEFCASHARARGILLDAFVDGYGGGGKTFDWSLIPPRLGRPLILSGGLNPS FT NVEEAVRRVRPWAVDVSSGVEVAKGIKDAARIAAFVAGVRHADG" FT CDS 1126595..1127848 FT /transl_table=11 FT /gene="trpB" FT /locus_tag="azo1047" FT /product="TrpB protein" FT /function="Tryptophan synthase beta chain" FT /EC_number="4.2.1.20" FT /note="Tryptophan synthase beta chain is for the synthesis FT of tryptophan from indole and serine. Similar to FT sprot|TRPB_RALSO (83%) and to sprot|TRPB_PSEAE (68%). FT TIGRFAM: trpB, tryptophan synthase, beta subunit" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4A9" FT /db_xref="InterPro:IPR001926" FT /db_xref="InterPro:IPR006653" FT /db_xref="InterPro:IPR006654" FT /db_xref="InterPro:IPR023026" FT /db_xref="UniProtKB/TrEMBL:A1K4A9" FT /protein_id="CAL93664.1" FT /translation="MRPGSPHSLPEFDMQMADTPYHYPDARGHFGRHGGVFVAETLMPA FT LDELREAYARYSQDPEFIAEFQYELKHYVGRPSPIYHAKRWSGILGGAQVYLKREDLNH FT TGAHKVNNCIGQALLARRMGKPRVIAETGAGQHGVATATVAARYGMECVVYMGAEDVKR FT QAANVYRMKLLGATVVPVESGSKTLKDALNEAMRDWVTNVADTFYIIGTVAGPHPYPMM FT VRDFQAVIGDECKVQMPELVGRQPDQVIACVGGGSNAMGIFYPYLDVPGVKLVGVEAAG FT EGLQTGRHAAPLTANAPVGVLHGNRTYLMQDEDGQIIETHSISAGLDYPGVGPEHAWLK FT DDGRAEYVAVTDSEALQAFHDLCRFEGIIPALESSHALAYAAKIAPTLPKDHVLLVNLS FT GRGDKDMHTVAERSGIQF" FT CDS 1127891..1128706 FT /transl_table=11 FT /gene="trpA" FT /locus_tag="azo1048" FT /product="TrpA protein" FT /function="Tryptophan synthase alpha chain" FT /note="Tryptophan synthase catalyzes the last step in the FT biosynthesis of tryptophan: L-serine + FT 1-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + FT glyceraldehyde 3-phosphate + H2O. Alpha chain is for the FT aldol cleavage of indoleglycerol phosphate to indole and FT glyceraldehyde 3-phosphate. Similar to trembl|Q8XXY2 (68%) FT and to sprot|TRPA_PSEPU (42%). Pfam (PF00290): Tryptophan FT synthase alpha chain TIGRfam (TIGR00262): Tryptophan FT synthase alpha chain InterPro (PS50264): Proteins binding FT FMN and related compounds core region" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4B0" FT /db_xref="InterPro:IPR002028" FT /db_xref="InterPro:IPR011060" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR018204" FT /db_xref="UniProtKB/Swiss-Prot:A1K4B0" FT /protein_id="CAL93665.1" FT /translation="MSKIQTTFQRLQAQGRKALIPFITAGDPDPTLTVPLMHALVAGGA FT DIIELGVPFSDPMADGPTIQRASERALAQGMTLRKVLQAVREFRSGDADTPVVLMGYAN FT PIEAMGQQAFVAAAREAGVDGALVVDYPPEECVEFAAASKAAGLDPIFLLAPTSSEQRF FT ADVARAGSGYIYYVSLKGVTGAGTLDLDEVARRIPQIRAAVGMPVGVGFGIRDAESARR FT IGAVADAVVIGSRIIEEIERSPREQACSNVTHFVKGIREALDTLPGVKQ" FT CDS 1128703..1129575 FT /transl_table=11 FT /gene="accD" FT /locus_tag="azo1049" FT /product="probable acetyl-coenzyme A carboxylase carboxyl FT transferase subunit b" FT /function="Acetyl-CoA carboxylase beta subunit" FT /EC_number="6.4.1.2" FT /note="Function:-THIS PROTEIN IS A COMPONENT OF THE ACETYL FT COENZYME A CARBOXYLASE COMPLEX; FIRST BIOTIN CARBOXYLASE FT CATALYZES THE CARBOXYLATION OF THE CARRIER PROTEIN AND THEN FT THE TRANSCARBOXYLASE TRANSFERS THE CARBOXYL GROUP TO FORM FT MALONYL-COA (BY SIMILARITY). Entry name FT :-SWISSPROT:ACCD_ECOLI Prim. accession # P08193 Identities FT = 178/287 (62%) InterPro:- IPR000438; ACoACC_transB. FT IPR000022; Carboxyl_trans. Pfam:- PF01039; Carboxyl_trans; FT 1. Signal peptide probability: 0.000 Number of predicted FT TMHs: 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4B1" FT /db_xref="InterPro:IPR000022" FT /db_xref="InterPro:IPR000438" FT /db_xref="InterPro:IPR011762" FT /db_xref="UniProtKB/TrEMBL:A1K4B1" FT /protein_id="CAL93666.1" FT /translation="MSWLQKLLPPKIKRSDAAARSKSIPEGLWSKCPSCEAVLYRSDLE FT SNQSVCPKCGHHQRLRARARLDLLLDPEGRFELGSEVVPVDPLKFKDSRRYPERLSTAV FT ADTGEADAMVVMQGAILTVPVVVACFEFEFLGGSMGSVVGERFVRGARAALEQRLPFIC FT ITATGGARMQEGLFSLMQMAKTTAAITQLAQRKLPFITLLTDPTMGGVSASFAFMGDVV FT IAEPGALIGFAGPRVIEQTVREKLPEGFQRSEFLLEKGAIDMIVDRRELRERLAALLTL FT MTRQPAVGN" FT CDS 1129592..1130890 FT /transl_table=11 FT /gene="folC" FT /locus_tag="azo1050" FT /product="dihydrofolate synthase / FT Tetrahydrofolylpolyglutamate synthase" FT /function="Folylpolyglutamate synthase" FT /EC_number="6.3.2.12" FT /note="FolC bifunctional protein [Includes: FT Folylpolyglutamate synthase (EC 6.3.2.17) FT (Folylpoly-gamma-glutamate synthetase) (FPGS); FT Dihydrofolate synthase (EC 6.3.2.12)]. Conversion of FT folates to polyglutamate derivatives." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4B2" FT /db_xref="InterPro:IPR001645" FT /db_xref="InterPro:IPR004101" FT /db_xref="InterPro:IPR013221" FT /db_xref="UniProtKB/TrEMBL:A1K4B2" FT /protein_id="CAL93667.1" FT /translation="MSLPHTLDGWLELLERRHAQAIQLGLERVRTVRDALGPGPETVVI FT TVGGTNGKGSTCAMLEAILRAEGYRVGCYTSPHLLRYNERVRVDGQDVDDARLVAGFEA FT VERARGDVPLTYFEHGTLAAWEVFRAAAPDVVILEVGLGGRLDAVNVFEPDCAIVTSVA FT MDHMDYLGDTREAIGYEKAGIFRSGRPAVCGDPQPPASLREHAEAIAAQLWISGRDFGF FT GGDQQQWGYWRYPAPATRGALVKRGGLAYPALRGANQLLNAAAVFTALDTLRDRIPVSM FT QAIRQGLMLVEVPGRFQVLPGKPAVVLDVAHNPQAAGVLAENLGGMGFYPETWAVLGML FT ADKDVEGVVERMRHRVDHWLLASLPGARGLDAETLAARLHAAGVAGDVRCFPDPQVAFS FT AARKSAAEGDRIVAFGSFLTVASVLAAIRAERH" FT CDS 1130902..1131543 FT /transl_table=11 FT /locus_tag="azo1051" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane proteine. Homology FT to BB2598 of Bordetella bronchiseptica of 37% FT (trembl|Q7WJA1(SRS)). Has 2 copies of PF05036, Sporulation FT related repeat;IPR007730, SPOR; This 35 residue repeat is FT found in proteins involved in sporulation and cell division FT such as FtsN, DedD, and CwlM. This repeat might be involved FT in binding peptidoglycan (Bateman A pers obs). FtsN is an FT essential cell division protein with a simple bitopic FT topology, a short N-terminal cytoplasmic segment fused to a FT large carboxy periplasmic domain through a single FT transmembrane domain. These repeats lay at the periplasmic FT C-terminus. FtsN localises to the septum ring complex. The FT CwlM gene is a cell wall hydrolase so this repeat may help FT localise the protein to the cell wall. no signal peptide. 1 FT TMH" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007730" FT /db_xref="UniProtKB/TrEMBL:A1K4B3" FT /protein_id="CAL93668.1" FT /translation="MSDADNLEIKKRARRRLVGAAALALTAAIVLPMMMEQEPAPSSPD FT IQVTIPDRDSPSASGRPDSEARTPDAALPPAPVEEPPQPGVAEAPSRPAPGAAEAPRAA FT SPASPRNAGDEEARVRALLDGKPPASAAAPATPAPAAKEGYVLQIGAFGDPAKAGSISS FT ELKQAGFSAYTEKAGAMTRVRVGPFASRDEAEKVAARLKAQGRNVVLTPR" FT CDS 1131554..1132045 FT /transl_table=11 FT /gene="cvpA" FT /locus_tag="azo1052" FT /product="putative colicin V production protein" FT /function="uncharacterized membrane protein required for FT colicin V production" FT /note="Colicin V production protein (dedE protein) (Pur FT regulon 18 kDa protein). REQUIRED FOR COLICIN V PRODUCTION FT FROM PLASMID INCFI COLV3-K30. TREMBL:Q82WH7: 29% FT identity,38% similarity InterPro:IPR003825; Colicin_V. FT Pfam:PF02674; Colicin_V TIGR00304: conserved hypothetical FT protei Signal peptide present (Signal P predicted) TMH's 4 FT (TMHMM predicted)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4B4" FT /db_xref="InterPro:IPR003825" FT /db_xref="UniProtKB/TrEMBL:A1K4B4" FT /protein_id="CAL93669.1" FT /translation="MTVFDYAFLAILAVSALVGLWRGLVSEILALVTWGIALLAAWRYA FT SVAAELFQGLLDEPLWRQAAGFVLIFVAILLIAALVRFLLRELLRAAGLRATDRFFGAL FT FGLARGVLIALAVVLLGGLVGIAREPWWANATFSPPLETAVIAAKPWLPEAVAARIRFR FT " FT CDS 1132057..1133586 FT /transl_table=11 FT /gene="purF" FT /locus_tag="azo1053" FT /product="amidophosphoribosyltransferase" FT /EC_number="2.4.2.14" FT /note="amidophosphoribosyltransferase (glutamine FT phosphoribosylpyrophosphate amidotransferase) (ATASE) FT (GPATase) (Q51342)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4B5" FT /db_xref="InterPro:IPR000583" FT /db_xref="InterPro:IPR000836" FT /db_xref="InterPro:IPR005854" FT /db_xref="InterPro:IPR017932" FT /db_xref="UniProtKB/TrEMBL:A1K4B5" FT /protein_id="CAL93670.1" FT /translation="MCGILGVVATSPVNQLLYDGLQVLQHRGQDAAGIATAEGGRFHMH FT KGSGLVRDVFRTRNMRNLEGNWGIAHVRYPTAGSAYNAAEAQPFYVNSPFGLLLAHNGN FT LTNSEELKREMFLADLRHINTNSDSEVLLNVLAHELQAACNGLKLDEDAVFRAVAGVHR FT RCRGAYAAVVMIAGYGLLAFRDPYGIRPLVIGRNDVAEGTEWLVASESVALDVLGFTLL FT RDVAPGEAVLIDTQGNFRSRQCAEKTVEAPCMFEFVYLARPDSIIDGISVYESRVKMGE FT FLAEKMKRTMPHAQIDVVIPIPDSSRPSAMEMAHRLGLPYREGFVKNRYIGRTFIMPGQ FT AKRRKSVRQKLNTIHQEFKGKSVLLVDDSIVRGTTSREIINMAREAGATKVYMASAAPP FT VRHANVYGIDMPTRSELIASDRSEDEICREIGADGLIYQDLDDLKASVRALNPAITFFE FT TSCFDGCYITGDITPEYLNGVENQRGEEKPAGRDDGEEGQLDLNLITHPDH" FT CDS 1133594..1134763 FT /transl_table=11 FT /gene="metZ" FT /locus_tag="azo1054" FT /product="Cys/Met metabolism pyridoxal-phosphate-dependent FT enzyme" FT /function="Cystathionine beta-lyases/cystathionine FT gamma-synthases" FT /EC_number="4.4.1.8" FT /note="A number of pyridoxal-dependent enzymes involved in FT the metabolism of cysteine, homocysteine and methionine FT have been shown to be evolutionary related. These enzymes FT are proteins of about 400 amino-acid residues. The FT pyridoxal-P group is attached to a lysine residue located FT in the central section of these enzymes. Similar to FT trembl|Q82WH6 (72%) and to sprot|CGL_MOUSE (36%). Pfam FT (PF01053): Cys/Met metabolism pyridoxal-phosphate-dependent FT enzymes" FT /note="Family membership" FT /db_xref="GOA:A1K4B6" FT /db_xref="InterPro:IPR000277" FT /db_xref="InterPro:IPR006234" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:A1K4B6" FT /protein_id="CAL93671.1" FT /translation="MDEFDFDTLAVRAGIERSQFNEHSEALYLTSSFVFKSAAQAAARF FT SGEEEGNVYARFSNPTVTAMQTRLAALEGAEACVATASGMSAILSLVMATLQAGDHIVA FT SNGLFGATQQLLGGIMSKFGIETTFVPATDIAAYRAAVRPRTRLFFIETPSNPLTEVVD FT IAAVAAVAHEAGALLAVDNCFCTPALQRPLALGADVVVHSATKYLDGQGRVLGGAVAGA FT RAVTDEVFKFLRTAGPTLSPFNAWVILKGLETLRVRMEAQSATALELARWLEQQPGVAR FT VYYPGLPSHPQHELAMRQQKTGGAILAFDVEGGRDAAWRVVDATRMISITANLGDTKTT FT ITHPATTTHGRVSAEARKAAGIGDGLLRVAVGLESIEDLKADLARGLAT" FT CDS complement(1134854..1135654) FT /transl_table=11 FT /gene="lpxH" FT /locus_tag="azo1055" FT /product="putative UDP-2,3-diacylglucosamine hydrolase" FT /EC_number="3.6.1.-" FT /note="UDP-2,3-diacylglucosamine hydrolase [lpxH], 54% FT identity to TrEMBL;Q5P1I2 Has Pfam;PF00149,Calcineurin-like FT phosphoesterase; This family includes a diverse range of FT phosphoesterases, including protein phosphoserine FT phosphatases, nucleotidases, sphingomyelin FT phosphodiesterases and 2'-3' cAMP phosphodiesterases as FT well as nucleases such as bacterial SbcD P13457 or yeast FT MRE11 P32829. The most conserved regions in this FT superfamily centre around the metal chelating residues. FT InterPro;IPR004843, M-pesterase." FT /db_xref="GOA:A1K4B7" FT /db_xref="InterPro:IPR010138" FT /db_xref="InterPro:IPR024654" FT /db_xref="UniProtKB/TrEMBL:A1K4B7" FT /protein_id="CAL93672.1" FT /translation="MSDPRTQAAATGGRAGDEPEAASVALPAFFISDLHLSEDQPDTVA FT AFVDFLAGPARDAGSLFILGDLFEYWAGDDDLEAPFNQRIASALRALAASGTAVYFMVG FT NRDLLAGHGLAAATGMQLLADPALVRLGQHETAPRVLLSHGDALCTDDTAYQAYRRQVR FT DPAWQAGFLSQPLAARKAFIASLRQQSERAKQDKAMTIMDVNPDAVAALLREYGYPELI FT HGHTHRPGQHTHLVDGRQCGRHVLADWHGRARWLAYDGTRFTSL" FT CDS complement(1135647..1136141) FT /transl_table=11 FT /gene="ppiB" FT /locus_tag="azo1056" FT /product="peptidyl-prolyl cis-trans isomerase B" FT /function="Peptidyl-prolyl cis-trans isomerase (rotamase) - FT cyclophilin family" FT /EC_number="5.2.1.8" FT /note="Peptidyl-prolyl cis-trans isomerase B. Homology to FT ppiB of E.coli of 71% (sprot|PPIB_ECOLI). PPIases FT accelerate the folding of proteins. It catalyzes the FT cis-trans isomerization of proline imidic peptide bonds in FT oligopeptides. InterPro: Cyclophilin-type peptidyl-prolyl FT cis-trans isomerase(IPR002130) Pfam: Cyclophilin-type FT peptidyl-prolyl cis-trans isomerase no signal peptide no FT TMH" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4B8" FT /db_xref="InterPro:IPR002130" FT /db_xref="InterPro:IPR020892" FT /db_xref="UniProtKB/TrEMBL:A1K4B8" FT /protein_id="CAL93673.1" FT /translation="MAVNLHTNYGVITLELDAEKAPVTVENFLTYVKDGHYDNTVFHRV FT IDGFMIQGGGFEPGMKQKPTREPIKNEADNGLKNERGTIAMARTQAPHSASAQFFINVA FT DNDFLNFRSQDLQGWGYCVFGRVTAGLDVVDAIRKVKTGSSGFHQDVPKEDVIIERAEV FT V" FT CDS complement(1136158..1136739) FT /transl_table=11 FT /gene="ppiA" FT /locus_tag="azo1057" FT /product="probable peptidyl-prolyl cis-trans isomerase A" FT /function="Peptidyl-prolyl cis-trans isomerase (rotamase) - FT cyclophilin family" FT /EC_number="5.2.1.8" FT /note="Probable peptidyl-prolyl cis-trans isomerase. FT Homology to ppiA of E. coli of 56% (SWISSPROT:PPIA_ECOLI) FT PPIases accelerate the folding of proteins. It catalyzes FT the cis-trans isomerization of proline imidic peptide bonds FT in oligopeptides. InterPro: Cyclophilin-type FT peptidyl-prolyl cis-trans isomerase (IPR002130) Pfam: FT Cyclophilin-type peptidyl-prolyl cis-trans isomerase Signal FT peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4B9" FT /db_xref="InterPro:IPR002130" FT /db_xref="InterPro:IPR020892" FT /db_xref="UniProtKB/TrEMBL:A1K4B9" FT /protein_id="CAL93674.1" FT /translation="MKRLIAFLALSTWLGLAAAANPQVLFTTNQGELVVELYPEKAPKT FT VANFLQYVKDKHYDGTIFHRVINGFMIQGGGMDAAMKEKSTRAPIENEAKNGLRNEPGT FT LAMARTGDPHSATAQFFINVAPNSFLDYPSRDGWGYAVFGKVVRGLDVVDTIARVPTRN FT VGFHQNVPAEPVVIQSARVIEAQPAGPAAR" FT CDS complement(1136784..1137980) FT /transl_table=11 FT /locus_tag="azo1058" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted proteins. Homology FT to of Dechloromonas aromatica of 56% FT (gi|41723709|ref|ZP_00150619.1|(NBCI ENTREZ)). Signal FT Peptide Present. No TMH present. Has FT PF03734:(IPR005490)ErfK/YbiS/YcfS/YnhG;This family of FT proteins are found in a range of bacteria. The conserved FT region contains a conserved histidine and FT cysteine,suggesting that these proteins have an enzymatic FT activity. Several members of this family contain FT peptidoglycan binding domains. So these proteins may use FT peptidoglycan or a precursor as a substrate." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4C0" FT /db_xref="InterPro:IPR005490" FT /db_xref="UniProtKB/TrEMBL:A1K4C0" FT /protein_id="CAL93675.1" FT /translation="MSPLHRLCAALLALGLLVPGGAATSAGLERKISDSGPDAALQDVF FT REIEANRLDAALDRTEALLAVYPNFRLAHLVKGDLLLARARPLKTFGNIEAAGSEVEGL FT REEAILRLRAYRERPPTEVVPRYLMQMGPDQRYAVVVDTRRARLYVYRNDNGKPRFVAD FT YYASHGKAGAEKMREGDNRTPLGVYHVTSFIEPKRLPDFYGSGAFPLNYPNDWDKRLGR FT TGHGIWLHGTPSDTYSRPPKASEGCVVLTNQDFTSLSSYVEPGSTPVIISNEVEWLSLD FT DWQSSRRSLNDAIERWRRDWESLDVDRLLSNYSREFRSDRYDRDGWARQKRRAAQGREW FT IKVGVDKVSMFRNPGKEELVVVTFEQTYRSNGLNDVHRKRQYWVREGGEWKIVYEGAA" FT CDS complement(1137983..1139239) FT /transl_table=11 FT /locus_tag="azo1059" FT /product="conserved hypothetical secreted protein" FT /function="FOG: TPR repeat" FT /note="Conserved hypothetical secreted protein. Homology to FT Daro03002816 of Dechloromonas aromatica of 42% FT (gi|53730051|ref|ZP_00348646.1|(NBCI ENTREZ)). domain FT structure: 59 aa - 92 aa TRP; 93 aa- 126 aa TRP; 127 aa FT -155 aa TRP. InterPro: TPR repeat (IPR001440); Type I FT antifreeze protein (IPR000104). Pfam: TRP Domain. signal FT peptide. no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4C1" FT /db_xref="InterPro:IPR001440" FT /db_xref="InterPro:IPR005158" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="InterPro:IPR019734" FT /db_xref="UniProtKB/TrEMBL:A1K4C1" FT /protein_id="CAL93676.1" FT /translation="MKIRLSAALGALALLQFLGASPVCAAEGPRDVHALLQQGKAAEAL FT VLATRLVEAQPRDAEARFARGVALAELGRQDEAISVFLKLTQDFPSQPEPYNNLAVLYA FT QQKQYDKARATLESALRTHPSYAVAHQNLGDLYARLASQAYEKALQADSTRSTETPTRL FT ALITELKSDAARTAAGPRASTAAAVPPAAPKGPALAAASGSPTIAAAPPTTAVAPPPAP FT PAAAPAKPVAPSAPGSAAPAVAATPNSPAIPQTTAGAPPQPAAAPRAASVPVPPAAEAP FT AGTTSQPGADTAVAERKPAAAPEKAAQDAVLRSVQGWAQAWSRKDVKSYLAAYDKDFEV FT PDGRARAVWERERQQRVGKAGAITVEVDNPRISVNGDRATVRFQQHYRSSGFNGSTNKT FT LELVRRGDQWKIRRETVGG" FT CDS 1139410..1140792 FT /transl_table=11 FT /gene="cysS" FT /locus_tag="azo1060" FT /product="CysS protein" FT /function="Cysteinyl-tRNA synthetase" FT /EC_number="6.1.1.16" FT /note="Cysteinyl-tRNA synthetase (EC 6.1.1.16) FT (Cysteine--tRNA ligase) (CysRS). InterPro: Cysteinyl-tRNA FT synthetase cysS: cysteinyl-tRNA synthetase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4C2" FT /db_xref="InterPro:IPR009080" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR015273" FT /db_xref="InterPro:IPR015803" FT /db_xref="InterPro:IPR024909" FT /db_xref="UniProtKB/TrEMBL:A1K4C2" FT /protein_id="CAL93677.1" FT /translation="MLSIHNTLSRSKEVFRPIEPGKVRMYVCGMTVYDYCHLGHARVMV FT VFDMVARWLRASGFDVTYVRNITDIDDKIIRRAQENGESIRALTDRFIAAMHEDADALG FT VLRPDHEPRATDYVASMQSLIERLHAKGLAYVAANHDVCYAVRKFEGYGKLSGKSLDEL FT RAGERVEVAGEKKDPLDFVLWKHAKAEEPDEAKWASPWGSGRPGWHIECSAMSSDLLGE FT HFDIHGGGQDLQFPHHENEIAQSEGAHGHAFVNYWMHNGFVRVDDEKMSKSLGNFFTIR FT DVLETYDAEVVRFFILRAHYRSPLNYSDAHLDDARQALTRLYTALRSVEAAPAAVDWTE FT SHALRFRAAMDDDFNTAEALAVLFELANEVNRGRDPLLAAQLKALGAVLGLLERDPVAF FT LQGSTPAASGLGPEDIEARIAARAAAKKAKDFAEADRIRAELLAAGIVLEDGAGGTTWR FT RA" FT CDS complement(1140857..1142011) FT /transl_table=11 FT /locus_tag="azo1061" FT /product="extracellular ligand binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems periplasmic component" FT /note="This family includes extracellular ligand binding FT domains of a wide range of receptors and it also includes FT the bacterial amino acid binding proteins of known FT structure. Similar to trembl|Q8XQ39 (40%) and to FT trembl|Q89G00 (32%). Pfam (PF01094): Receptor family ligand FT binding region SignalP reporting Signal peptide." FT /note="Family membership" FT /db_xref="GOA:A1K4C3" FT /db_xref="InterPro:IPR000709" FT /db_xref="InterPro:IPR001828" FT /db_xref="UniProtKB/TrEMBL:A1K4C3" FT /protein_id="CAL93678.1" FT /translation="MTSLRLPALFRRGLASLLAVAATCGAPAAFAQQGVDADAITLGHT FT GALSGPLAELNKEYLAGANLYFNQTNERGGINGRRIRLLTLDDAYDPNKAAENAQRLIE FT QHQVFALFACFGTGPSLKVVPLAAAAKVPFFAPYTGAEALREPLNPYVFHVRASYRQEV FT EKAVDHLTKLGVKSIGVVHHADPFGQAGLDAAVASLAKRNLTPAVVAPIASSGADAADT FT VKKVAAANPAAVIMITAGNSSAALLRALQQSGSQPMLYGLSVISSTQLIRELGEKAHGL FT VIAQVMPSPFRVDYPFVRDYRQAAEKAGIAYSYASLEGYLAARSFGEAVRRAGRDLTRE FT KLISALENMGDWDAGGMRMAFSPRRHVGMDYVDLTVISRGNFTR" FT CDS complement(1142201..1143328) FT /transl_table=11 FT /gene="dnaJ1" FT /locus_tag="azo1062" FT /product="chaperone protein DnaJ" FT /function="DnaJ-class molecular chaperone with C-terminal FT Zn finger domain" FT /note="Chaperone protein dnaJ (Heat shock protein J) FT (HSP40). Homology to dnaJ of E. coli of 61% FT (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates FT jointly with grpE the ATPase activity of dnaK (By FT similarity). Pfam: DnaJ domain; DnaJ central domain (4 FT repeats); DnaJ terminal region no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4C4" FT /db_xref="InterPro:IPR001305" FT /db_xref="InterPro:IPR001623" FT /db_xref="InterPro:IPR002939" FT /db_xref="InterPro:IPR003095" FT /db_xref="InterPro:IPR008971" FT /db_xref="InterPro:IPR012724" FT /db_xref="InterPro:IPR018253" FT /db_xref="UniProtKB/Swiss-Prot:A1K4C4" FT /protein_id="CAL93679.1" FT /translation="MSKRDYYEVLGVNRDAGDDEIKKAYRKLAMKYHPDRNPDSKEAEE FT KFKEAKEAYEVLSDAQKKGAYDRYGHAGVDPSMGGGGGGQGFEGFADAFGDIFGDLFGG FT RGGGGGRSNVYRGADLRYNLEISLEEAARGAEKTIRIPTVEECGTCHGSGAKPGTQPKT FT CPTCGGAGQVRIQQGFFSIQQTCPKCHGTGRIIPDPCGDCGGAGRVKKQKTLEVKIPAG FT IDEGMRLRHSGHGEPGVNGGPPGDLYVEIHIRQHPVFERDHDDLHCEMPISFATAALGG FT EIEIPTLEGMARIKIPAETQSGKVFRLRGKGIKNVRSHTHGDLMCHVVVETPVNLTERQ FT KELLREFEEVSKGDAERHNPKAKSWMDKVRDFFAT" FT CDS complement(1143424..1145349) FT /transl_table=11 FT /gene="dnaK" FT /locus_tag="azo1063" FT /product="chaperone protein DnaK" FT /function="Molecular chaperone" FT /note="Chaperone protein dnaK. Homology to dnaK of E. coli FT of 74% (sprot|DNAK_ECOLI). Acts as a chaperone (By FT similarity). InterPro: Heat shock protein hsp70 (IPR001023) FT Hsp70 protein no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4C5" FT /db_xref="InterPro:IPR001023" FT /db_xref="InterPro:IPR012725" FT /db_xref="InterPro:IPR013126" FT /db_xref="InterPro:IPR018181" FT /db_xref="UniProtKB/Swiss-Prot:A1K4C5" FT /protein_id="CAL93680.1" FT /translation="MGKIIGIDLGTTNSCVSVMEGGKPKVIENSEGARTTPSVVAYAED FT GEILVGAPAKRQAVTNARNTLFAVKRLIGRRFEEKEVQKDIDLMPYTIAKADNGDAWVE FT VRGKKIAPPQVSAEVLRKMKKTAEDYLGEEVTEAVITVPAYFNDSQRQATKDAGRIAGL FT EVKRIINEPTAAALAFGMDKKPGDSKIAVYDLGGGTFDISIIEIADIDGEHQFEVLATN FT GDTFLGGEDFDQRIIDYIVTEFKKEQGVDLKNDVLALQRLKEAAEKAKIELSSGSQTEV FT NLPYITADATGPKHLAIKITRAKFESLVEDLIERSIEPCRIALKDAGVKVSDIDDVILV FT GGQTRMPKVIEKVKEFFGKEPRRDVNPDEAVAVGASIQGGVLQGEVKDVLLLDVTPLSL FT GIETLGGVMTKLIQKNTTIPTKASQVFSTADDNQSAVTIHVLQGEREMASGNKSLGQFN FT LSDIPPAPRGMPQIEVTFDIDANGILHVSAKDKATGKENKIKIQANSGLSDEEVERMVR FT DAAAHAEEDKKAHELVDARNQCDALIHSTKKALAEHGDKIGADDKAKIEAAMKDAEEAI FT KSGDKDSIEAKSQALAMASQKLGEAMYGQQQAEGGAQAAGAAGGSSKADDADVVDAEFT FT EVKDKK" FT CDS complement(1145464..1146030) FT /transl_table=11 FT /gene="grpE" FT /locus_tag="azo1064" FT /product="probable heat shock protein GrpE" FT /function="Molecular chaperone GrpE (heat shock protein)" FT /note="Probable heat shock protein GrpE. Homology to grpE FT of L. pneumophila of 42% (sprot|GRPE_LEGPN) Stimulates FT jointly with dnaJ the ATPAse activity of dnaK. Helps to FT release ADP from dnaK thus allowing dnaK to recycle more FT efficiently (By similarity). Pfam: GrpE no signal peptide FT no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4C6" FT /db_xref="InterPro:IPR000740" FT /db_xref="InterPro:IPR009012" FT /db_xref="InterPro:IPR013805" FT /db_xref="UniProtKB/Swiss-Prot:A1K4C6" FT /protein_id="CAL93681.1" FT /translation="MPDPTQNPNVTPELEQHAAPEAAAEAAPESSADVMPSLEETLRQA FT ELKAAEHYDAWLRAKAEGENIRRRAQEDIAKATKFAAEKFASAMVPVKDSLEAALAVEN FT QTVEKLREGVELTLKQLVSAFEGAGLAEENPLGQKFDPNKHQAISAIEAEGEPNTVINV FT LQKGYLLHERVVRPALVVVSKAKAQ" FT CDS 1146167..1146412 FT /transl_table=11 FT /locus_tag="azo1065" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to an orf FT of Polaromonas sp. JS666 of 43% ( ZP_00361754). No domains FT predicted. No singal peptide. No TMHs" FT /db_xref="InterPro:IPR019180" FT /db_xref="UniProtKB/TrEMBL:A1K4C7" FT /protein_id="CAL93682.1" FT /translation="MLPSVKPSDPLTAPVRTLVDAEAAVAAIRGRLECAGLSLRPPPAP FT PTACCGRGCNGCVWEGYYSALGYWREDARRLLAGEG" FT CDS 1146520..1149153 FT /transl_table=11 FT /gene="gyrA" FT /locus_tag="azo1066" FT /product="DNA topoisomerase (ATP-hydrolysing)" FT /function="DNA gyrase (topoisomerase II) A subunit" FT /EC_number="5.99.1.3" FT /note="DNA gyrase subunit A (EC 5.99.1.3). DNA gyrase FT negatively supercoils closed circular double- stranded DNA FT in an ATP-dependent manner and also catalyzes the FT interconversion of other topological isomers of FT double-stranded DNA rings including catenanes and knotted FT rings. recN: DNA repair protein RecN" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4C8" FT /db_xref="InterPro:IPR002205" FT /db_xref="InterPro:IPR005743" FT /db_xref="InterPro:IPR006691" FT /db_xref="InterPro:IPR013757" FT /db_xref="InterPro:IPR013758" FT /db_xref="InterPro:IPR013760" FT /db_xref="UniProtKB/TrEMBL:A1K4C8" FT /protein_id="CAL93683.1" FT /translation="MTQFAKETLPISLEEEMRHSYLDYAMSVIVGRALPDARDGLKPVH FT RRVLYAMHELSNDWNRAYKKSARIVGDVIGKYHPHGDSAVYDTIVRMAQDFSLRYMLVD FT GQGNFGSVDGDNAAAMRYTEIRMARIGHELLADIDKETVDFGPNYDGSEKEPLILPARI FT PNLLINGSSGIAVGMATNIPPHNLGEVVDACLKLLEDPETDLEALIEIVKAPDFPTAGL FT IYGLHGVHEGYRTGRGRVVMRARTHIEPIGKNSDREAIIVDELPYQVNKRTLLERIAEL FT VNEKKVEGISEIRDESDKSGMRVVIELKRNEMPEVVLNNLYKHTQLQDTFGMNMVALVD FT GKPRLLNLKQMLVCFLEHRREVVTRRTIFELKKARDRGHILEGLAVALSNVDEIIALIK FT AAPTPADAKRGLMERTWRSPLVEEMLSRALADSYRPEGLDPEFGFSAQGYKLSDAQAQA FT ILELRLQRLTGLEQDKIVGEYREVMDLITDLLDILARPERITAIIVEELTAIRNQFGDP FT RRSEIVLSTAEINIEDLITPEDMVVTLSHTGYFKRQPLADYRAQRRGGRGKQATSMKDE FT DFIDHLFVANTHDTVLCFSSRGRAYWLKVYEVPEGTRNSRGKPIVNLFPLIEGEKITAV FT LPVQTFDEEHFVFMATSEGTVKKTALTAFANPRKAGIIAVNLDDGDHLIGVAITDGECD FT VMLFSDAGKAVRFAESDVRPMGREARGVRGMTLEDGQRVIAMLVAKGETQSVLTATENG FT YGKRTPVAEYTRHGRGTKGMIAIQTSDRNGKLVGAVLVDPTDEVMLISTGAVLIRTKVQ FT DIRELGRATQGVTLINLDEGTYLAGIEKVAESGAEADELVEGGEEGAADGEDAGAPGAA FT GEGEQE" FT CDS 1149150..1150247 FT /transl_table=11 FT /gene="serC" FT /locus_tag="azo1067" FT /product="phosphoserine transaminase." FT /function="Phosphoserine aminotransferase" FT /EC_number="2.6.1.52" FT /note="Phosphoserine transaminase. catalytic activity: FT o-phospho-l-serine + 2-oxoglutarate = FT 3-phosphonooxypyruvate + l-glutamate (by similarity). FT cofactor: pyridoxal phosphate (by similarity). pathway: FT required both in major phosphorylated pathway of serine FT biosynthesis and in the biosynthesis of pyridoxine (by FT similarity). similarity: belongs to the class-v FT pyridoxal-phosphate-dependent aminotransferase family. FT InterPro: Aminotransferase class-V" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4C9" FT /db_xref="InterPro:IPR000192" FT /db_xref="InterPro:IPR003248" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="InterPro:IPR020578" FT /db_xref="InterPro:IPR022278" FT /db_xref="UniProtKB/TrEMBL:A1K4C9" FT /protein_id="CAL93684.1" FT /translation="MTRVWNFAAGPAALPAEVLQQAAEEMLDWRGAGVGVMEMSHRSKE FT FVSIAEQAEADLRELMAIPANYRVLFMQGGAIAENAIIPMNLMGEEKRADYVVTGSWSV FT KSQKEARKYGEVNIAATSEASGYTTVPPMSEWKLSARPSYLFTCTNETIGGVEYPFEPD FT LARIGRAEVPVVADVSSHILSRPFDVTKYGLLFGGAQKNIGPAGLTIVIVRDDLLGRAA FT PFCPTAFDYRTVADNGSMYNTPPTYAIYIAGLVFQWLKRKGGVAGIEAQNIAKAELLYG FT FLDDCPFYENRIDPACRSRMNVPFFLKDESLNDRFLAGAKDAGLVQLKGHKSVGGMRAS FT IYNAMPLEGVQALVDYMRDFALRHG" FT CDS 1150262..1151326 FT /transl_table=11 FT /gene="pheA" FT /locus_tag="azo1068" FT /product="chorismate mutase/prephenate dehydratase" FT /function="Prephenate dehydratase" FT /EC_number="5.4.99.5" FT /note="Bifunctional chorismate mutase/prephenate FT dehydratase P-protein, pheA," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4D0" FT /db_xref="InterPro:IPR001086" FT /db_xref="InterPro:IPR002701" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR008242" FT /db_xref="InterPro:IPR010957" FT /db_xref="InterPro:IPR018528" FT /db_xref="InterPro:IPR020822" FT /db_xref="UniProtKB/TrEMBL:A1K4D0" FT /protein_id="CAL93685.1" FT /translation="MSDELLNLRNQIDRLDEEILARLAERARCAQRVGEIKHGNIYRPE FT REAQVLRRLADLNGGPLPDVAVQKIFREIMSACLGLEQPLKVAYLGPAGTFSESASRKH FT FGAAPNVLPTPSIDEVFRAVESGNADYGVVPVENSTEGAVGGTLDLLLANPLKVCGEVK FT LRIHQNLLSRAEGIGGAKRLYSHAQSLAQCHEWLNRNLAHLPRIPVASNAEAARLAAED FT PESCAIAGEAAAELYGLNKLATNIEDDPNNTTRFLVIASHDAGPSGNDKTSLVCSAQNR FT PGAMHALLEPLARHGVDMSKLESRPARSGLWEYVFYVDIQGHQTDAAVAAALRELNERA FT AFVKVLGSYPVAAI" FT CDS 1151344..1152441 FT /transl_table=11 FT /gene="hisC1" FT /locus_tag="azo1069" FT /product="histidinol-phosphate aminotransferase" FT /function="Histidinol-phosphate/aromatic aminotransferase FT and cobyric acid decarboxylase" FT /EC_number="2.6.1.9" FT /note="Histidinol-phosphate aminotransferase 2," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4D1" FT /db_xref="InterPro:IPR004839" FT /db_xref="InterPro:IPR005861" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:A1K4D1" FT /protein_id="CAL93686.1" FT /translation="MSVASRAPAYIRSIQPYQPGKPISELAREMGLPEADIVKLASNEN FT PLGMGAKARAAAEAAIREAFRYPDGGAFALKAALARKFGVDAAQLVIGNGSNDVLEIAA FT QTFLAPGTSAVFSQYSFAVYPLATNARGARCIQVPAQAYGHDLDAMAAAIAPDTRIVFI FT ANPNNPTGTFVGGAALEAFLAKVPEDVLVVLDEAYTEFLEPEQRYDSLAWLARFPNLLV FT SRTLCKAYGLAGLRVGYAIAHPDVADLMNRVRQPFNVSAVALAAAEAALGDDDFVARTA FT DINRRGKQQLTDAFASLGLEWIPSAGNFVTVRVGDAAAVNLALLRQGVIVRPIAGYGMP FT EWLRVSIGLPEENARFITALRNALG" FT CDS 1152457..1153347 FT /transl_table=11 FT /gene="tyrA" FT /locus_tag="azo1070" FT /product="probable prephenate dehydrogenase" FT /function="Prephenate dehydrogenase" FT /EC_number="1.3.1.12" FT /note="Prephenate dehydrogenases are involved in tyrosine FT biosynthesis. Similar to trembl|Q7NSL5 (54%) and to FT trembl|Q82XD9 (47%). Pfam: PDH, Prephenate dehydrogenase. FT TMHMM reporting one Tmhelix. SignalP reporting Signal FT peptide." FT /note="Specificity unclear" FT /db_xref="GOA:A1K4D2" FT /db_xref="InterPro:IPR003099" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A1K4D2" FT /protein_id="CAL93687.1" FT /translation="MALIGKLVVCGVGLIGGSFALALKQAGAVERVVGVGRNPATLARA FT VELGVIDEIAAGWRDALDGADFVLLATPVGQLDAIMEAMAPHLQPGTIVTDAGSTKRDV FT IEAVYRRLDPHLATVVPAHPIAGAEKSGVEAGFPTLYRGKKVVVTPLPENRPDAVERVR FT AAWTACGATVVEMSPQDHDRVFAAVSHLPHLLAFGLVHDLAGRANAELLFSHAASGFRD FT FTRIAGSHPEMWRDICLANRQALLAELDQYLAELAYLRALLLAGDGTRLEQLFGEARRA FT RDAWAAQFPPPSTAE" FT CDS 1153344..1155305 FT /transl_table=11 FT /gene="aroA" FT /locus_tag="azo1071" FT /product="3-phosphoshikimate 1-carboxyvinyltransferase" FT /function="5-enolpyruvylshikimate-3-phosphate synthase" FT /EC_number="2.5.1.19" FT /note="EPSP synthase catalyzes the sixth step in the FT biosynthesis from chorismate of the aromatic amino acids FT (the shikimate pathway) in bacteria. Similar to FT sprot|AROA_RALSO (46%) and to trembl|Q7NTK6 (47%). TIGRfam: FT (TIGR00017): Cytidylate kinase Pfam (PF02224): Cytidylate FT kinase Pfam (PF00275): EPSP synthase (3-phosphoshikimate FT 1-carboxyvinyltransferase)" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4D3" FT /db_xref="InterPro:IPR001986" FT /db_xref="InterPro:IPR003136" FT /db_xref="InterPro:IPR006264" FT /db_xref="InterPro:IPR011994" FT /db_xref="InterPro:IPR013792" FT /db_xref="InterPro:IPR023193" FT /db_xref="UniProtKB/TrEMBL:A1K4D3" FT /protein_id="CAL93688.1" FT /translation="MTMEFLDLPPMLAARGQVRLPGSKSISNRSLLLAALAEGETDIRD FT LLASDDVERMLEALQALGVRWSREEGTDNYRVHGVGGPFPVKKGDLFLGNAGTAFRPLT FT AALALSGGDYRLSGVARMHERPIGDLVDALRQAGADIEYVGNEGFPPLHIRPATIRPGG FT VLKVRGDVSSQFLTALLMALPLTGVETTIEVVGELISKPYIAITLDLMARFGVDVVRED FT WQRFTVPGGARYRSPGVLYVEGDASSASYFLAAGAIGGGPVRVEGVGRDSIQGDVRFAD FT ALAQLGAVITVGDNWIEAAAPAGGRLRAFDLDLNHIPDAAMTLAVAALFADGPCTLRNI FT ASWRVKETDRIAAMATELRKVGAEVEEGADYLRIMPPAVLRPAAIDTYDDHRMAMCFSL FT VSLGGCRVRINDPRCVNKTFPSYFEAFATVAAPVPVVAIDGPSASGKGTVGARVAAALG FT WHHLDSGSLYRLVALSAERGGIDLDDEVALAAIAGDLPARFEGERVWLGTDDVTDAIRS FT EQCSAGASKVAVLPAVRAALLGRQRDYRQGPGLVAEGRDIGSVIFPDASVKIFLTASVE FT ARAERRYKQLIGKGLAANMESLMQDLRERDARDAARTVAPLQKLPDAALLDTTDRDVEQ FT AVTFVLDLVRDHGLRGAN" FT CDS 1155409..1157115 FT /transl_table=11 FT /gene="rpsA" FT /locus_tag="azo1072" FT /product="30S ribosomal protein S1" FT /function="Ribosomal protein S1" FT /note="30S ribosomal protein S1. BINDS MRNA; THUS FT FACILITATING RECOGNITION OF THE INITIATION POINT. IT IS FT NEEDED TO TRANSLATE MRNA WITH A SHORT SHINE-DALGARNO (SD) FT PURINE-RICH SEQUENCE." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4D4" FT /db_xref="InterPro:IPR000110" FT /db_xref="InterPro:IPR003029" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR022967" FT /db_xref="UniProtKB/TrEMBL:A1K4D4" FT /protein_id="CAL93689.1" FT /translation="MSTATPVSTQESFAALFEESLALQEMRAGEVITAEVVRIDQNFVV FT VNAGLKSESYVPIDEFRNDRGELEVNPGDFIHVAIEALEDGYGETRLSRDKAKRIAAWN FT DLEKALNEGTLVKGVISGRVKGGLTVMTNSIRAFLPGSLVDMRPVKDTSPYEGKEYEFK FT VIKLDRKRNNVVVSRRAVLEESMGEERQKLLENLKEGTVVKGVVKNITDYGAFVDLGGI FT DGLLHITDLAWRRVRHPSEVLNVGDEIEAKVLKFDQEKNRVSLGLKQLGEDPWVGISRR FT YPQGTRLFGKVTNITDYGAFVEVEQGIEGLVHVSEMDWTNKNIHPTKVVQLGDEVEVMI FT LEIDEDRRRISLGMKQCASNPWDDFAINHKKGDKVRGQIKSITDFGVFIGLDGGIDGLV FT HLSDLSWSESGEDAVRKFKKGDEVEAVVLAIDVERERISLGIKQLEGDPFTNFIATHEK FT NSLVRGTVKSVDARGAVIGLGDEVEGYLRASEAAPHRVDDLTTMLKEGDELELMIINVD FT RKTRSINLSIRAKDQAEQTEAMQKLASESSAASGTTNLGALLKAKLNEQKQ" FT CDS 1157126..1157410 FT /transl_table=11 FT /gene="ihfB" FT /locus_tag="azo1073" FT /product="probable integration host factor, beta-subunit" FT /function="Bacterial nucleoid DNA-binding protein" FT /note="Probable integration host factor, beta-subunit FT (IHF-beta). Homology to ihfB of P. aeruginosa of 64% FT (sprot|IHFB_PSEAE(SRS)) Bacteria synthesize a set of small, FT usually basic proteins of about 90 residues that bind DNA FT and are known as histone-like proteins. The exact function FT os these proteins is not yet clear but they are capable of FT wrapping DNA and stabilizing it from denaturation under FT extreme environmental conditions. Theprotein exists as a FT dimer and two beta-arms function as the non-specific FT binding site for bacterial DNA. InterPro: Bacterial FT histone-like DNA-binding protein (IPR000119) Pfam: FT Pacterial DNA-binding protein no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4D5" FT /db_xref="InterPro:IPR000119" FT /db_xref="InterPro:IPR005685" FT /db_xref="InterPro:IPR010992" FT /db_xref="InterPro:IPR023630" FT /db_xref="UniProtKB/Swiss-Prot:A1K4D5" FT /protein_id="CAL93690.1" FT /translation="MTKSELIAQLAARFPQLVAKDADYAVKMILDAMSDALARGDRIEI FT RGFGSFALNYRPPRVGRNPKSGEKVHVPEKYVPHFKAGKELRERVDIVE" FT CDS 1157501..1157806 FT /transl_table=11 FT /locus_tag="azo1074" FT /product="conserved hypothetical membrane protein" FT /note="38% identity with Hypothetical protein from FT Chromobacterium violaceum TrEMBL:Q7NTL0,Genename CV3044 FT Signal Peptide present TMHMM reporting for transmembrane FT helices:2 present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR010445" FT /db_xref="UniProtKB/TrEMBL:A1K4D6" FT /protein_id="CAL93691.1" FT /translation="MRIVMWLLRFLLFFLLFGFAVKNDHLASLRFFFGGEWQLPVVFVI FT LVSFSAGALLGITATFASLLRQRREISRLRRQLVRAERSQGSASPPATDAQAPETL" FT CDS 1157814..1158989 FT /transl_table=11 FT /locus_tag="azo1075" FT /product="conserved hypothetical transferase protein" FT /function="predicted N-acetylglucosaminyl transferase" FT /EC_number="2.4.1.141" FT /note="Putative N-acetylglucosaminyl transferase. Enzyme FT that is involved in the catalysis of the reaction: FT UDP-N-acetyl-D-glucosamine + FT N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + FT N,N''-diacetylchitobiosyldiphosphodolichol. 36% FT Cas_TM1810_C.IPR001574; RIP.IPR001440; TPR.IPR008941; FT TPR-like.InterPro: TPR repeat TIGRFAMs:TIGR01870; FT cas_TM1810; 1. TMHx:1" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4D7" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR013026" FT /db_xref="InterPro:IPR019734" FT /db_xref="UniProtKB/TrEMBL:A1K4D7" FT /protein_id="CAL93692.1" FT /translation="MEIEFWWLLALPLFFALGWLAARIDIRQVVQESRALPRSYLAGLN FT FLLNEQPDKAIDAFIEAVRIDPQTVELHFALGSLFRRRGETDRAIRLHQLLVDRDDLNE FT DQRLQALGELGQDFLKAGLLDRAETVFLKLRDTRANDVALRYLLEIYQQEKDWAKAIEI FT ARALPDHEEAMWRKEVASFHCELATTALADSRFPDVRRHIDEALAINRSCVRASLIEGD FT LYAAQGRDEDALEAWKRIESQDPVYLSLAAERVMDAYGRLGRVEQGHMLLRSWLDRHAS FT LDLLDELFQWEIEKLGPKAAYDLVREELRRNPTLLGLDKLLEAALLAAPAEQRGDIELV FT KQLIHGHTRKVARYRCESCGFKARQFHWHCPACGGWETYPPRRTEEFDLEP" FT CDS 1159107..1160429 FT /transl_table=11 FT /gene="ugd" FT /locus_tag="azo1076" FT /product="UDP-glucose 6-dehydrogenase" FT /function="oxidation of UDPglucose to UDPglucuronate, a FT possible precursor of cell surface carbohydrates" FT /EC_number="1.1.1.22" FT /note="UDP-glucose 6-dehydrogenase (EC 1.1.1.22) (UDP-Glc FT dehydrogenase) (UDP-GlcDH) (UDPGDH)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4D8" FT /db_xref="InterPro:IPR001732" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR014026" FT /db_xref="InterPro:IPR014027" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR017476" FT /db_xref="InterPro:IPR021157" FT /db_xref="UniProtKB/TrEMBL:A1K4D8" FT /protein_id="CAL93693.1" FT /translation="MKVTVVGTGYVGLVSGACLADVGNDVLCLDVDPDKIRILEEGGIP FT IHEPGLLDVVRRNVAAGRLSFTTDVERAARHGVIQFIAVGTPPDEDGSADLQYVLAAAR FT NIGRHMDGYRVIVDKSTVPVGTGDKVRAAVAEELVVRGSTLAYSVVSNPEFLKEGAAVE FT DFMRPDRIIVGADDERAVELMRQLYGPFQRNHEKLLVMDVRSAELTKYAANAMLATRIS FT FMNELANLAETLGADIELVRQGIGSDPRIGWHFLYAGCGYGGSCFPKDVKALVRTGAEH FT GHDLLLLNAVEAVNDAQKLRLVDKVVSRFGENLAGRRFAVWGLAFKPNTDDMREAPSRV FT VLGELLGRGASVCVYDPVAMDEARRIFGVDARLSYAERPMDALEAADALVIVTEWKEFR FT SPDFERIRALLKQPVIFDGRNMYDPAVLRSEGIEYFGMGRR" FT CDS 1160583..1161473 FT /transl_table=11 FT /gene="cysM" FT /locus_tag="azo1077" FT /product="cysteine synthase B" FT /function="Cysteine synthase" FT /EC_number="2.5.1.47" FT /note="Cysteine synthase chloroplast precursor," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4D9" FT /db_xref="InterPro:IPR001216" FT /db_xref="InterPro:IPR001926" FT /db_xref="InterPro:IPR005856" FT /db_xref="InterPro:IPR005858" FT /db_xref="UniProtKB/TrEMBL:A1K4D9" FT /protein_id="CAL93694.1" FT /translation="MEFKTLEDYVGKTPLVRMKRITAGHNNVILAKLEGNNPAGSVKDR FT PALSMVVRAEARGDIKPGDTLIEATSGNTGIALAMAAAMRGYRMILVMPENQSVERRQT FT MRAFGAELVLTPKEGGMEMARDVAEKMRDEGKGIILDQFANPDNPLAHYEGTGPELWEQ FT TAGRITHFVSSMGTTGTIMGTSRFLKEMNPAIRIVGCQPEEGSQIPGIRKWPEAYLPAI FT YHRESVDSLEYVSQADAEEMTRRLAREEGLFAGISSGGAMHVALRIAAQVENAVIVSVI FT CDRGDRYLSTGVFPA" FT CDS 1161512..1162306 FT /transl_table=11 FT /locus_tag="azo1078" FT /product="conserved hypothetical protein" FT /function="predicted 3-5 exonuclease related to the FT exonuclease domain of PolB" FT /note="Probable DNA polymerase epsilon catalytic subunit A FT (EC 2.7.7.7) (DNA polymerase II subunit A). TIGR00099: FT conserved hypothetical protein." FT /note="Function unclear" FT /db_xref="GOA:A1K4E0" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR019288" FT /db_xref="UniProtKB/TrEMBL:A1K4E0" FT /protein_id="CAL93695.1" FT /translation="MRVPVLVFDIETIPDVAGIRVLNDLPPDLSDFEVAEFAFQQRRAT FT NGTDFLPHHLQRVVTISCAMRDADQFRVFSLSEPQANEAQIIQRFFDGVERFTPQLVSW FT NGGGFDLPVLHYRGMLHGVAAPRYWDLGDGDFGDSRDFKWNNYISRYHTRHLDLMDVLA FT LYQPRANAPLDDLAKLMGYPGKLGMDGGAVWQAWQEGRIAEIRDYCETDVVNTYLVYLR FT FQRMRGQLDLAAWEAEVRVVRDTLERLEGEHWKRFLAAWSAA" FT tRNA 1162391..1162467 FT /gene="tRNA-Val" FT /locus_tag="azo_tRNA_0021" FT /product="transfer RNA-Val" FT /anticodon=(pos:1162425..1162427,aa:Val) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 1162660..1164576 FT /transl_table=11 FT /locus_tag="azo1079" FT /product="ThrS protein" FT /function="Threonyl-tRNA synthetase" FT /EC_number="6.1.1.3" FT /note="Threonyl-tRNA synthetase (EC 6.1.1.3) FT (Threonine--tRNA ligase) (ThrRS)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4E1" FT /db_xref="InterPro:IPR002314" FT /db_xref="InterPro:IPR002320" FT /db_xref="InterPro:IPR004095" FT /db_xref="InterPro:IPR004154" FT /db_xref="InterPro:IPR006195" FT /db_xref="InterPro:IPR012675" FT /db_xref="InterPro:IPR012676" FT /db_xref="InterPro:IPR012947" FT /db_xref="InterPro:IPR018163" FT /db_xref="UniProtKB/Swiss-Prot:A1K4E1" FT /protein_id="CAL93696.1" FT /translation="MPNIKLPDGSVRSFDHPVTVAEVAASIGSGLAKAALAGRVDGKAV FT DLSYCIERDSELAILTDKSAEGVDVIRHSTAHLLAHAVKELFPEAQVTIGPVIENGFYY FT DFSYKRPFTPEDLEAIEKRMAELVKRELPVEREVWPRDKAVAFFKSIGEHYKAEIIASI FT PANEDVSLYRQGEFVDLCRGPHVPSTGRLKVFKLTKLAGAYWRGDAKNEMLQRVYGTAW FT AKKEDLESYLHMLEEAEKRDHRKLGRQLDLFHIQEEAPGMVFWHAKGWTLWQQVEQYLR FT GTISRHGYQEVRTPQIVDRSLWEKSGHWGMYSDLMFTTQSEKHDYAVKPMNCPCHIQIF FT NQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGIMRVRNFVQDDAHIFCTDEQVQEEAAAF FT IALLQKVYADFGFRDIQIKLSTRPEKRVGADEQWDAAEAALAAALKAQGLEYELQPGEG FT AFYGPKIEFSLKDCLNRVWQCGTLQLDFNLPVRLGAEYVAEDNTKKFPVMLHRAIVGSL FT ERFIGILIEHYAGAMPLWLAPVHAVVMNISEGQADYATEVVNRLREAGFRVEADLRNEK FT INYKIREHSVHKLPYQLVVGEKEKAAGVVAVRVRGGQDLGQLSLDKLIERWNGELASRS FT GPV" FT CDS 1164657..1165127 FT /transl_table=11 FT /gene="infC" FT /locus_tag="azo1080" FT /product="translation initiation factor IF-3" FT /function="Translation initiation factor 3 (IF-3)" FT /note="Translation initiation factor IF-3. IF-3 binds to FT the 30S ribosomal subunit and shifts the equilibrum between FT 70S ribosomes and their 50S and 30S subunits in favor of FT the free subunits thus enhancing the availability of 30S FT subunits on which protein synthesis initiation begins." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4E2" FT /db_xref="InterPro:IPR001288" FT /db_xref="InterPro:IPR019813" FT /db_xref="InterPro:IPR019814" FT /db_xref="InterPro:IPR019815" FT /db_xref="UniProtKB/TrEMBL:A1K4E2" FT /protein_id="CAL93697.1" FT /translation="MRLVGEDGEQLGIVSLNAALNAAEEAGLDLVEIAPMAKPPVCKIM FT DFGKFKYQEQKKAHEARLKQKQVQVKEVKLRPGTDENDYQIKLRNLKRFLEEGDKCKVT FT LRFRGREMAHQEFGLRQLERIKADLEELGQVEQMPKMEGRQMIMVIAPKKNR" FT CDS 1165275..1165472 FT /transl_table=11 FT /gene="rpmI" FT /locus_tag="azo1081" FT /product="50S ribosomal protein L35" FT /function="Ribosomal protein L35" FT /note="50S ribosomal protein L35." FT /note="Family membership" FT /db_xref="GOA:A1K4E3" FT /db_xref="InterPro:IPR001706" FT /db_xref="InterPro:IPR018265" FT /db_xref="InterPro:IPR021137" FT /db_xref="UniProtKB/Swiss-Prot:A1K4E3" FT /protein_id="CAL93698.1" FT /translation="MPKMKTKSSAKKRFKVRSSGGIKRSQAFKRHILTKKTTKSKRQLR FT GMTEVHASDEKLIRAMLPYA" FT CDS 1165485..1165844 FT /transl_table=11 FT /gene="rplT" FT /locus_tag="azo1082" FT /product="50S ribosomal protein L20" FT /function="Ribosomal protein L20" FT /note="50S ribosomal protein L20. This protein binds FT directly to 23s ribosomal RNA and is necessary for the in FT vitro assembly process of the 50s ribosomal subunit. It is FT not involved in the protein synthesizing functions of that FT subunit" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4E4" FT /db_xref="InterPro:IPR005813" FT /db_xref="UniProtKB/Swiss-Prot:A1K4E4" FT /protein_id="CAL93699.1" FT /translation="MPRVKRGVTARARHKKVLDQAKGYRGRRKNVYRIAKQAVMKAGQY FT AYRDRRQRKRQFRALWIARINAAARELGLTYSTFMNGLKKAAVEVDRKVLADLAVFDKP FT AFAALAEQARAKLAA" FT CDS 1165911..1166942 FT /transl_table=11 FT /gene="pheS" FT /locus_tag="azo1083" FT /product="phenylalanyl-tRNA synthetase alpha chain" FT /function="Phenylalanyl-tRNA synthetase alpha subunit" FT /EC_number="6.1.1.20" FT /note="Phenylalanyl-tRNA synthetase alpha chain (EC FT 6.1.1.20) (Phenylalanine--tRNA ligase alpha chain) (PheRS). FT InterPro: Phenylalanyl-tRNA synthetase alpha subunit pheS: FT phenylalanyl-tRNA synthetase a" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4E5" FT /db_xref="InterPro:IPR002319" FT /db_xref="InterPro:IPR004188" FT /db_xref="InterPro:IPR004529" FT /db_xref="InterPro:IPR006195" FT /db_xref="InterPro:IPR010978" FT /db_xref="InterPro:IPR022911" FT /db_xref="UniProtKB/Swiss-Prot:A1K4E5" FT /protein_id="CAL93700.1" FT /translation="MDNLDQLVQQAQADFAGVSDSAQLEQAKARYLGKSGALTEQLKGL FT GKLPPEEKREAGAAINRAKTAIEAALEARRNALREAALLAQLAAEALDVTLPGRGAQGG FT GLHPVSRTLERIEMLFRSIGFIVADGPEIETDWHNFTALNTPENHPARSMHDTFYLEGR FT DDVLLRTHTSPVQIRTMLAHVKRHAEAAAMPEIRVIIPGRVYRVDSDATHSPMFHQVEG FT LWVGEKVSFADLKGVIADFLRKFFETEDLQVRFRPSFFPFTEPSAEIDVAFMSGPLKGR FT WLEIAGCGMVHPNVLRFGGVDPERYTGFAFGMGPDRLTMLRYGVNDLRLFFEGDLRFLS FT QFR" FT CDS 1166949..1169339 FT /transl_table=11 FT /gene="pheT" FT /locus_tag="azo1084" FT /product="phenylalanyl-tRNA synthetase beta chain" FT /function="Phenylalanyl-tRNA synthetase beta subunit" FT /EC_number="6.1.1.20" FT /note="Phenylalanyl-tRNA synthetase beta chain (EC FT 6.1.1.20) (Phenylalanine--tRNA ligase beta chain) (PheRS)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4E6" FT /db_xref="InterPro:IPR002547" FT /db_xref="InterPro:IPR004532" FT /db_xref="InterPro:IPR005121" FT /db_xref="InterPro:IPR005146" FT /db_xref="InterPro:IPR005147" FT /db_xref="InterPro:IPR009061" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR020825" FT /db_xref="UniProtKB/TrEMBL:A1K4E6" FT /protein_id="CAL93701.1" FT /translation="MQFSEQWLRTFVNPPLDSDALGHLLTMAGLEVEEAQPVAPAFSGI FT VVASIIEAEKHPNADKLRVCKVDAGTGELLQIVCGAPNAAAGMKVPCALVGAQLPGDFA FT IKAAKLRGVESFGMLCSARELGISEDHGGLLELPADAPVGCDIRAYLALDDTLFTIKLT FT PNRADCLSLAGVAREVAAITAAELSLPAVQPVEPVTDARRAVALDVPAACPRYCGRVLR FT GVDARAQTPDWMKQRLQRSGLRPISALVDITNYVMLELGQPLHAFDDARISGSVHVRLA FT LPGEQLLLLNGQTVSLTPDSLVIADEDRVLALAGVMGGEECGVTLDTRDVFLESAFFAP FT AGIAGRARSYGFSSDAAHRFERGVDFALGPRAIERATRLILDICGGEAGPTVVAEVASA FT LPERPAVRLRPERARRLLGVTLDDGQMQALLERVHLNVVPSGSDLLVTPPSFRFDVEIE FT EDLIEELARLHGYDNIPAVPPQGQLMMLERSESARSPWTVRHLLAARGYQEVVNFAFVE FT EAWERDFCANEDPIRLANPIASQMSVMRSSLVPGLVANLATNRKRQQQRVRVFEVGRCF FT ERKADGEPVAGFHQPVRIAALAAGGVVPEQWGERERQVDFYDVKGDLEALFAPRLLSFE FT PLSHPALHPGRAAAVLLDGRRIGWLGEVHPVWVQRYDVGSAPVVFEVDLDSALESRLPS FT FGGVSRMPAVTRDLALVVAAEVPAARILEVLKAAAGPLVTEISLFDLYHGKGIDPDKKS FT LAFRVLMQDTHRTLEDAEVDAAVAALVQQAELVFGARLRGAVE" FT CDS 1169336..1169647 FT /transl_table=11 FT /gene="ihfA" FT /locus_tag="azo1085" FT /product="integration host factor alpha-subunit" FT /function="Bacterial nucleoid DNA-binding protein" FT /note="Integration host factor alpha-subunit (IHF-alpha). FT This protein is one of the two subunits of integration host FT factor a specific DNA-binding protein that functions in FT genetic recombination as well as in transcriptional and FT translational control (By similarity). InterPro: Bacterial FT histone-like DNA-binding protein." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4E7" FT /db_xref="InterPro:IPR000119" FT /db_xref="InterPro:IPR005684" FT /db_xref="InterPro:IPR010992" FT /db_xref="InterPro:IPR020816" FT /db_xref="InterPro:IPR023630" FT /db_xref="UniProtKB/Swiss-Prot:A1K4E7" FT /protein_id="CAL93702.1" FT /translation="MNVTLTKAELADLLFERVGLNKREAKDMVEGFFEEIRTALERGDS FT VKLSGFGNFQLRDKPQRPGRNPKTGEEIPITARRVVTFHASQKLKAAVEQLSDASKQP" FT CDS 1169628..1170008 FT /transl_table=11 FT /locus_tag="azo1086" FT /product="putative MerR-family transcriptional regulator" FT /function="predicted transcriptional regulators" FT /note="Putative MerR-family transcriptional FT regulator,similar toTREMBL: trembl|Q83C17 (51% Coxiella FT burnetii,cbu1319) Pfam: PF00376 MerR family regulatory FT protein. HTH reporting nucleic acid binding motif." FT /db_xref="GOA:A1K4E8" FT /db_xref="InterPro:IPR000551" FT /db_xref="InterPro:IPR009061" FT /db_xref="UniProtKB/TrEMBL:A1K4E8" FT /protein_id="CAL93703.1" FT /translation="MQASSPDVDDTELPPIPAKRYFTIGEVSELCAVKPHVLRYWEQEF FT TQLKPVKRRGNRRYYQHHEVLLIRRIRQLLYSEGFTISGARNRLCEGEILHQEETAELE FT RCQSQLRAVRAGLMEALAVLRA" FT tRNA 1170058..1170134 FT /gene="tRNA-Pro" FT /locus_tag="azo_tRNA_0022" FT /product="transfer RNA-Pro" FT /anticodon=(pos:1170092..1170094,aa:Pro) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 1170324..1171067 FT /transl_table=11 FT /gene="surE" FT /locus_tag="azo1087" FT /product="phosphoric-monoester phosphohydrolase" FT /function="predicted acid phosphatase" FT /EC_number="3.1.3.2" FT /note="Acid phosphatase surE (EC 3.1.3.2). sprot|SURE_NITEU FT (Q82VV9) Acid phosphatase surE -70% identity, 80% FT similarity. Interpro:Members of this family are acid FT phosphatases, EC: 3.1.3.2 [1]. In bacteria they may be FT involved in the stress response [2]. Escherichia coli cells FT with the surE gene disrupted are found to survive poorly in FT stationary phase surE: stationary-phase survival protein S FT TIGRFAM: taut (tautomerase), MIP (family of channel FT proteins), CynX (Cyanate transport system proteins) TMHMM FT predicted transmembrane helices" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4E9" FT /db_xref="InterPro:IPR002828" FT /db_xref="UniProtKB/Swiss-Prot:A1K4E9" FT /protein_id="CAL93704.1" FT /translation="MRILVSNDDGYFAPGIAALAAALGELGDVTVVAPERDRSGASNSL FT TLDRPLSLRRAANGFFFVNGTPTDCVHLAVTGMLDQLPDMVVSGVNHGANMGDDTLYSG FT TVAAATEGYLLGIPSIAVSLASWSATDFSVAAQVARDVAARLMRSPLPAPVLLNVNVPD FT CAGGAPKGTRVTRLGKRHKAEPVIRSQTPRGETVYWVGAAGAAADAGEGTDFHAVANGF FT VSVTPLQVDLTHTGQIAAVDTWLSA" FT CDS 1171112..1171717 FT /transl_table=11 FT /gene="pcm2" FT /locus_tag="azo1088" FT /product="protein-L-isoaspartate (D-aspartate) FT O-methyltransferase" FT /EC_number="2.1.1.77" FT /note="Protein-L-isoaspartate O-methyltransferase, 56% FT Identity to TrEMBL;Q7VXN1.51% Identity to FT TrEMBL;Q82VW0,Q7NRV0. SProt;Q886L4(52% Idnetity), FT Q87LQ6(51%),P24206(47%) Has PF01135, FT Protein-L-isoaspartate(D-aspartate) O-methyltransferase FT (PCMT);IPR000682, PCMT; Protein-L-isoaspartate(D-aspartate) FT O-methyltransferase (PCMT) MEDLINE: (which is also known as FT L-isoaspartyl protein carboxyl methyltransferase) is an FT enzyme that catalyzes the transfer of a methyl group from FT S-adenosylmethionine to the free carboxyl groups of FT D-aspartyl or L-isoaspartyl residues in a variety of FT peptides and proteins. The enzyme does not act on normal FT L-aspartyl residues L-isoaspartyl and D-aspartyl are the FT products of the spontaneous deamidation and/or FT isomerization of normal L-aspartyl and L- asparaginyl FT residues in proteins. PCMT plays a role in the repair FT and/or degradation of these damaged proteins; the enzymatic FT methyl esterification of the abnormal residues can lead to FT their conversion to normal L-aspartyl residues." FT /db_xref="GOA:A1K4F0" FT /db_xref="InterPro:IPR000682" FT /db_xref="UniProtKB/Swiss-Prot:A1K4F0" FT /protein_id="CAL93705.1" FT /translation="MVERLRAQGIQDEGALAAMMQVPRHLFVEEGLAYSAYDDTALPIG FT FQQTISQPYVVARMIELLRSGGRQLGRVLEIGAGCGYQAAVLSTLATEVYAVERIRPLL FT DKARANLRPLRLPNVRLKHADGTLGLPEAAPFESIIVAAAAGGVPNALKEQLAPGGRLI FT IPVGGGEQRLLLIERQGNVFRESGYEAVRFVPLLAGTE" FT CDS 1171714..1172622 FT /transl_table=11 FT /gene="nlpD" FT /locus_tag="azo1089" FT /product="conserved hypothetical lipoprotein" FT /function="Membrane proteins related to FT metalloendopeptidases" FT /note="Conserved hypothetical lipoprotein. Homology to nlpD FT of R. gelatinosus of 43% (trembl|Q9JP90) InterPro: FT Peptidase family M23/M37 (IPR002886); LysM motif FT (IPR002482) Pfam: LysM domain; Peptidase family m23/M27 FT signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4F1" FT /db_xref="InterPro:IPR002482" FT /db_xref="InterPro:IPR011055" FT /db_xref="InterPro:IPR016047" FT /db_xref="InterPro:IPR018392" FT /db_xref="UniProtKB/TrEMBL:A1K4F1" FT /protein_id="CAL93706.1" FT /translation="MNDSVNIKKRIAPYFLALGVLFLAGCASRAPVAVRDGNGVAPPPA FT AAPVADRAGVHVVRAGETLLGIARQYGQNVKDLVVWNGLTNPNQIHVGQEIRVLPPDAN FT AIPGGAVATPIPITSEPPVAVPVVPQPATAGALKLEPKGGKQPYSDELWARVRRSGEPA FT APVASEPRATQAPEQEPGDAEWLWPAKGKVLSGFNEATNKGIDISGNPGDAVVASAAGR FT VVYAGSGLRGYGKLVIIKHNQEYNSVYAHNQKLLVKEDDQVSQGQKIAELGSTDADRPK FT LHFEIRKQGRPVDPMKFLSAR" FT CDS 1172633..1173568 FT /transl_table=11 FT /gene="rpoS" FT /locus_tag="azo1090" FT /product="putative RNA polymerase sigma factor" FT /function="DNA-directed RNA polymerase sigma subunit FT (sigma70/sigma32)" FT /note="RNA polymerase sigma factor RpoS Sigma factors are FT initiation factors that promote the attachment of RNA FT polymerase to specific initiation sites and are then FT released. This sigma factor is involved in acid resistance. FT Belongs to the sigma-70 factor family 50% 1. PF04542 FT Sigma70_r2; 1. helixturnhelix HTH: reporting nucleic acid FT binding motif" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4F2" FT /db_xref="InterPro:IPR000943" FT /db_xref="InterPro:IPR007624" FT /db_xref="InterPro:IPR007627" FT /db_xref="InterPro:IPR007630" FT /db_xref="InterPro:IPR009042" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR012761" FT /db_xref="InterPro:IPR013324" FT /db_xref="InterPro:IPR013325" FT /db_xref="InterPro:IPR014284" FT /db_xref="UniProtKB/TrEMBL:A1K4F2" FT /protein_id="CAL93707.1" FT /translation="MEDPVSSDELESHEPDLPLEVEVFAEPHAPVFENDFLSDVTQIYL FT NEIGANPLLSAEEEAALARRVRAGDFDARQTMIERNLRLVVNIAKHYLNRGIPLLDLVE FT EGNLGLMHALEKFDPERGFRFSTYATWWIRQNIERAIMNQSRTIRLPVHVVKELNQVLR FT AQRVVEAASNGDFSLDEIARRLDKPIEEVRAILALSEHTASLDAPLDIDPTLSIGESLA FT DEHAETPESQIHNAEIEGLIRAWIDMLNDKQRLVIRHRYGIGECELMTLEELAARLELT FT RERVRQIQLEALGQLRRILKRRGISRDVLF" FT CDS complement(1173565..1174575) FT /transl_table=11 FT /gene="mltB" FT /locus_tag="azo1091" FT /product="putative membrane-bound lytic murein FT transglycosylase" FT /function="Membrane-bound lytic murein transglycosylase B" FT /EC_number="3.2.1.-" FT /note="Putative membrane-bound lytic murein FT transglycosylase. homology to mltb of E. coli of 38% FT (sprot|MLTB_ECOLI) Murein-degrading enzyme. Catalyzes the FT cleavage of the glycosidic bonds between N-acetylmuramic FT acid and N- acetylglucosamine residues in peptidoglycan. FT May play a role in recycling of muropeptides during cell FT elongation and/or cell division. no domains prediced signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4F3" FT /db_xref="InterPro:IPR011757" FT /db_xref="InterPro:IPR023346" FT /db_xref="UniProtKB/TrEMBL:A1K4F3" FT /protein_id="CAL93708.1" FT /translation="MKLRPTLFAALVALGAAVAHAAPPVRPEIRNFAAEMAQRHGFDQE FT TVERTLAEARYEARVINLIQPPTKPGTRSWQRYRSRFLDRTRIAGGLAFWEENNAALEA FT ASARFGVPPEIIVAVIGVETIYGRQTGNFQTLSALSTLAFDYPPRADLFRRELEHLFLL FT AREQGRPPGSYTGSYAGALGYPQFLPSSVRAYAVDFDGDGRVDFDTAPDDAIGSVANYL FT HVHGWIAQAPVAERARFNGVVEAAPLVAAGIEPVLSPDTLANAGVTTLDGSSAAAPATL FT VDLETPGEPTEYWLGYRNFYVITRYNRSSFYAMSVFELAETLRRERLQRTALQRG" FT CDS complement(1174572..1176551) FT /transl_table=11 FT /locus_tag="azo1092" FT /product="conserved hypothetical membrane protein" FT /function="Transglutaminase-like enzymes putative cysteine FT proteases" FT /note="Conserved hypotetical membrane protein. Homology to FT RSp0111 of R. solanacearum of 41% (trembl|Q8XTJ7(SRS)) FT Pfam: Transglutaminase-like superfamily signal peptide FT probable 4 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR002931" FT /db_xref="InterPro:IPR021878" FT /db_xref="UniProtKB/TrEMBL:A1K4F4" FT /protein_id="CAL93709.1" FT /translation="MTKLLRWRRSTVTPPAPPPRRDVGLWLVVTAALTLAPHAAYLPPW FT IAGLCTALLIWRTAALLRQHRSLPAAILLLMAVGAGFAVRQHFGHFFGQEPGVALLALL FT LCLKLFELRTLRDVRVAVMLSFFLQLGLFFDNETLPVAALALAGALCALACLVAAEDAH FT SHTRERLRTAGVLLAQSLPLMAVLFLLFPRIPAPLWGLPADANSASSGLSDAMSPGSIS FT SLGLSEEIAFRVEFLGAVPEPRLRYWRGPVLTEFDGRTWRPIARPTRDQPGYQLTGPRI FT DYRMTLEPHGQRWLLALDFPGADLAQVRYTPEFQAVLRAPLRDRTQFALTAHPGARVGL FT QDGGPLLEAALQLPPGNARSRALARELAGDTPNAERTIARTLDYLRGGHFLYTLEPPLL FT KQDFIDEFLFDTRQGYCEHFSAAFVFLLRAAGVPARVVAGYQGGELNPFDGTLIVRQSD FT AHAWAEAWIADKGWVRVDPTAAVAPSRISGESAARSATGGALPLMMQTRLDWLRQLRLR FT WEAVSHGWDLWVLGYNSERQADLLRRLGLSQTDWTVLAGVGSLAGLVFFALLFIWAQWR FT SNPADALDRAWGRFCGKLAKAGVPRHPFEGPLDYSTRAGAARPAESERIDRISRTYARL FT RYGRDCPPDQLRALLHDIDSLRIK" FT CDS complement(1176544..1177527) FT /transl_table=11 FT /locus_tag="azo1093" FT /product="conserved hypothetical membrane protein" FT /function="uncharacterized conserved protein (some members FT contain a von Willebrand factor type A (vWA) domain)" FT /note="Conserved hypothetical membrane protein. Homology to FT RS03012 of Ralstonia solanacearum of 40% (trembl|Q8XTJ8) FT InterPro: Protein of unknown function DUF58 This domain is FT found in a family of prokaryotic proteins that have no FT known function. Proteins belonging to this family include FT hypothetical proteins from eubacteria and archaebacteria. FT Some of these proteins also contain the Von Willebrand FT factor, type A domain InterterPro: IPR002881; DUF58. Pfam: FT PF01882; DUF58; Non-secretory with low signal peptide FT probability (Signal P predicted). TMHMM predicted 2 FT transmembrane helices." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR002881" FT /db_xref="UniProtKB/TrEMBL:A1K4F5" FT /protein_id="CAL93710.1" FT /translation="MPRFTPARIRARVEHWLFRIGAPEQAPIRLGQRRIYVLPTPAGLV FT FAAALVTMLIASINYGLSLGYMLTFLLASAGITSIVHAFRNLLHLEIAPARVTPVFCGE FT AAEFRLRINNARAERRPALRLRARGANTAFDAAAASATEIVLACRTTRRGLLELGRTVL FT ETTWPLGLIRAWSIFVPDIDCIVYPAPEHHPPPLPAEGAGNEGGTRSSIRGDDDFAGLR FT PTQPSDSPRHIAWKSLARGGPMLTKQFSASTGSAHVFDWAALPPALDDEARLSRLTAWI FT LAADAAGRPFSLRLPGAEIDIGRGPGHVHACCRLLALHGQVRVDHD" FT CDS complement(1177527..1178444) FT /transl_table=11 FT /gene="moxR1" FT /locus_tag="azo1094" FT /product="MoxR protein" FT /function="MoxR-like ATPases" FT /note="MoxR protein (MxaR protein). MAY BE INVOLVED IN THE FT REGULATION OF FORMATION OF ACTIVE METHANOL DEHYDROGENASE. FT TREMBL:Q883V0: 60% identity, 73% similarity SMART: SM00382; FT AAA InterPro: IPR003593; AAA_ATPase. IPR001270; FT Chaprnin_clpA/B. IPR003442; UPF0079. Pfam: PF02367; FT UPF0079; Pfam: Mg_chelatase:Magnesium chelatase, subunit FT ChlI ruvB: Holliday junction DNA helicase Ru No signal FT peptide and transmembrane helices" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4F6" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR011703" FT /db_xref="InterPro:IPR016366" FT /db_xref="UniProtKB/TrEMBL:A1K4F6" FT /protein_id="CAL93711.1" FT /translation="MPRHYVTRLLEAAGQIILGKEHELRLALACLVARGHLLIEDLPGV FT GKTTLAHVLARLIGLQFQRIQFTSDLLPADIVGVSIFDRESHGFRFHPGPIFAQLILAD FT EINRATPKTQSALLEAMEEHQVTADGETLALPAPFFVIATQNPAHQIGTFPLPEAQLDR FT FLMRIRLGYPEPAAERALLMGENRRELLERQQPVITPLQMVELQEAARAVSVADRLVDY FT LHALLIATRNSPEFASGLSPRAGLALLAAARAHAFIEEREHVLPEDVQRVFPFVAGHRL FT HLAGDGRPAPAAALDALLRSVPVR" FT CDS 1178599..1179525 FT /transl_table=11 FT /locus_tag="azo1095" FT /product="histone deacetylase family protein" FT /function="Deacetylases including yeast histone deacetylase FT and acetoin utilization protein" FT /note="Histone deacetylases, acetoin utilization proteins FT and acetylpolyamine amidohydrolases are all members of an FT ancient protein superfamily, TREMBL:Q7VZF1 (58% identity); FT TREMBL:Q7NRU4 (57% identity). InterPro (IPR000286): Histone FT deacetylase family Pfam (PF00850): Histone deacetylase FT domain." FT /note="Family membership" FT /db_xref="InterPro:IPR000286" FT /db_xref="InterPro:IPR023801" FT /db_xref="UniProtKB/TrEMBL:A1K4F7" FT /protein_id="CAL93712.1" FT /translation="MTTTAFITHRECWLHDMGTFHPECPDRLSAINDRLIAAGLDLYLS FT FYDAPYATEEQVTRVHPASYLGELMANVPEHGIRHLDPDTAMSPNTMKAALRSAGAGVL FT ATDLVLKGEVESAFCAVRPPGHHAEKAKAMGFCFLNNVAIAARHALEAHGLERVAIVDF FT DVHHGNGTEDIFRDDPRVMMVSIFQHPFYPYSGVENPPAHMCNVPVPAGTRGDAFRQIV FT SDIWVPALRNHNPQAIFVSAGFDAHYEDDMGSLGLVESDYVWATQQIKSVAEDCGHKRV FT ISVLEGGYSLSSLARSVVAHIKALADL" FT CDS 1179632..1180510 FT /transl_table=11 FT /gene="dapA" FT /locus_tag="azo1096" FT /product="dihydrodipicolinate synthase" FT /function="Dihydrodipicolinate synthase/N-acetylneuraminate FT lyase" FT /EC_number="4.2.1.52" FT /note="Dihydropicolinate synthase (DHDPS) is the key enzyme FT in lysine biosynthesis via the diaminopimelate pathway. It FT catalyzes the condensation of L-aspartate-beta- FT semialdehyde and pyruvate to dihydropicolinic acid via a FT ping-pong mechanism in which pyruvate binds to the enzyme FT by forming a Schiff-base with a lysine residue. Similar to FT trembl|Q82SD7 (63%) and to sprot|DAPA_ECOLI (51%). Pfam FT (PF00701): Dihydrodipicolinate synthetase family" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4F8" FT /db_xref="InterPro:IPR002220" FT /db_xref="InterPro:IPR005263" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR020624" FT /db_xref="InterPro:IPR020625" FT /db_xref="UniProtKB/Swiss-Prot:A1K4F8" FT /protein_id="CAL93713.1" FT /translation="MITGSIVAIVTPMHEDGSLDFPRLRSLIDWHVAEGTDGIVIVGTT FT GESPTVSVDEHCELIRVAVEHAAGRIPVIAGTGANSTAEAIALARYAQQAGAVAHLSVV FT PYYNRPSQEGLYQHFRSVAEAVELPLILYNVPGRTVADLSNDTALRLAEIPNIIGLKDA FT TGSIDRACDLIERAPEGFALYSGDDMTVAAFILLGGHGTISVTANVAPRAMHEMCAAAL FT AGDAAKARTINARLVGLHRHLFCEANPIPVKWAVQRMGLVEGGLRLPLTPLAESFHDRV FT LTAMRQAGIQA" FT CDS 1180537..1181676 FT /transl_table=11 FT /gene="nlpB" FT /locus_tag="azo1097" FT /product="putative lipoprotein" FT /function="uncharacterized lipoprotein" FT /note="Putative lipoprotein. Homology to nlpB of E. coli of FT 20% (sprot|NLPB_ECOLI) This family consists of a number of FT bacterial lipoproteins often known as NlpB or DapX. This FT lipoprotein is detected in outer membrane vesicles in FT Escherichia coli and appears to be nonessential. Pfam: FT NlpB/DapX lipoprotein singal peptide no TMHs" FT /note="Family membership" FT /db_xref="InterPro:IPR010653" FT /db_xref="UniProtKB/TrEMBL:A1K4F9" FT /protein_id="CAL93714.1" FT /translation="MNRFTRPSLSVIALSLMLAGCSGSLLESKRIDYKSASSQRVPQLE FT VPPDLVAPTRDDRFAVPDVSPRGVATYSAYSAERTQPTQRGATEVLPAQEKMRVERAGS FT QRWLVVPGTPDELWPQIKEFWLELGFILNIDNPEIGVMETDWAEDRAKIPQDFVRNALG FT KVLDGLFSTPERDKFRTRLETNKETGQVEIYISHRGMMEIYPTEAKDSTIWQPRPANPE FT LEAEMLRRLMVRLGADEARAQAALAVAPTAERAKISASPDGVVALRIDEPFDRAWRRVG FT LALDRIGFTVEDRDRAKGLYYVRYVDPEADNKGKEGEGFMSKLAFWRSSDKPQGGSEYR FT LQVKGQGDAALVNVLTREGGTDKSDTAKKMLGLLQAELR" FT CDS complement(1181789..1182073) FT /transl_table=11 FT /locus_tag="azo1098" FT /product="conserved hypothetical secreted protein" FT /note="Conserved hypothetical secreted protein. Homology to FT NMB1523 of N.meningitidis of 50% (tremble:Q9JYL7) No FT domains predicted. No TMHs Signal Peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K4G0" FT /protein_id="CAL93715.1" FT /translation="MKHSLLVAALVALAVSACGKKEETAPVTAPAPTAPAATAPAAPTE FT QAPAAEAAKEAADAAKDAAEAAKDAAAASVEAAKEGAAAATEAAKDAAK" FT CDS complement(1182332..1183447) FT /transl_table=11 FT /locus_tag="azo1099" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical protein. Homology to CV3581 FT of C.violaceum of 48% (tremble:Q7NS46) FT SM00558;JmjC:Probable enzymes, but of unknown FT functions,that regulate chromatin reorganisation processes. FT No signal peptide or TMH present. lytR_cpsA_psr: cell FT envelope-related fu" FT /db_xref="InterPro:IPR003347" FT /db_xref="InterPro:IPR013109" FT /db_xref="InterPro:IPR022777" FT /db_xref="UniProtKB/TrEMBL:A1K4G1" FT /protein_id="CAL93716.1" FT /translation="MITTLLGGMTPRQFLQEYWQKKPLLVRQAVPGFTGVLGREDIFDL FT ACDPDVESRHIRLHEGNWELNRGPQTRARLRGKRSPWTVLVQGINLWSEAADELLHRFN FT FIPQARLDDLMVSYAVDGGGVGPHFDNYDVFLLQGQGQRRWQIADQDDRSLVEGAPLRI FT LRNFVPAHDWILEPGDMLYLPPHWAHNGIAIGECTTYSIGFRSPTAQELGAEFLGWLQE FT RVCLDGLYSDPDLTEQDNSALIGDAMIDQVQRVIEGIRWSRADVAAFLGHYLTEPKPTV FT FFEPPEEPIPLKAFRRALGAGGLRLDARTLLLRSQGNFFLNGEAVDSVPAWQQALDTLA FT HARRLTGCADLPAALQDLFYEWYCDGFAHPM" FT CDS 1183539..1184840 FT /transl_table=11 FT /locus_tag="azo1100" FT /product="putative 23S rRNA (Uracil-5-) methyltransferase" FT /function="SAM-dependent methyltransferases related to tRNA FT (uracil-5-)-methyltransferase" FT /EC_number="2.1.1.-" FT /note="Putative 23S rRNA (Uracil-5-)-methyltransferase rumA FT (EC 2.1.1.-) (23S rRNA(M-5-U1939)-methyltransferase). FT Homology to ruma of E. coli of 39% (sprot|RUMA_ECOLI(SRS)) FT Catalyzes the formation of 5-methyl-uridine at position FT 1939 (M-5-U1939) in 23S rRNA. Tigrfam: ygcA: RNA FT methyltransferase, TrmA family Pfam: TRAM domain no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4G2" FT /db_xref="InterPro:IPR001566" FT /db_xref="InterPro:IPR002792" FT /db_xref="InterPro:IPR010280" FT /db_xref="InterPro:IPR016027" FT /db_xref="UniProtKB/Swiss-Prot:A1K4G2" FT /protein_id="CAL93717.1" FT /translation="MPTAVIESLDHEGRGIARVEGKAVFIEGGLPGETVEYRVLRSKPN FT YEQAEATRIVRRSALRVAPRCPHFGVCGGCSMQHLDTLAQAATKQRVLEDALWRIGKVK FT PGIIYSAIQGPAWGYRYRARLGVRLVPAKGGVLIGFHERRSSYIADLGVCPVLPAHVSA FT LLPALKVLVASLSIADRLPQIEVAVSEATTVLVFRNLLALKKADEAQLRSFAETHGVQV FT WLQPEGPDSIVPLHPRSGPGLTYTLPEFDVALDFRATDFTQVNVHINRLLIRRAMQLLQ FT PAPGERIADLFCGLGNFSLPIARRGATVVGVEGSEALVARALENARRNGLDSRTEFHAA FT NLFDATEDSLAALGPLDKLLIDPPREGAIAVVKAVGPAQQPARIVYVSCNPATLARDAA FT VLVHEKGYVLRGAGIANMFPQTSHVESIALFERP" FT tRNA 1184957..1185046 FT /gene="tRNA-Ser" FT /locus_tag="azo_tRNA_0023" FT /product="transfer RNA-Ser" FT /anticodon=(pos:1184991..1184993,aa:Ser) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 1185090..1185695 FT /transl_table=11 FT /locus_tag="azo1101" FT /product="pseudouridylate synthase" FT /function="16S rRNA uridine-516 pseudouridylate synthase FT and related pseudouridylate synthases" FT /EC_number="4.2.1.70" FT /note="Ribosomal large subunit pseudouridine synthase E (EC FT 4.2.1.70) (Uracil hydrolyase). Responsible for synthesis of FT pseudouridine from uracil-2457 in 23S ribosomal RNA" FT /note="Family membership" FT /db_xref="GOA:A1K4G3" FT /db_xref="InterPro:IPR000748" FT /db_xref="InterPro:IPR006145" FT /db_xref="InterPro:IPR018496" FT /db_xref="InterPro:IPR020103" FT /db_xref="UniProtKB/TrEMBL:A1K4G3" FT /protein_id="CAL93718.1" FT /translation="MSRLILLNKPYGVLCQFSGEPGRATLKDHVPIPEVYPAGRLDTDS FT EGLLLLTDDGALQARIADPRHKLPKTYLVQVEGEPDDAALAALRAGVDLGDFRTRPCSA FT RRVVEPDWLWPRDPPVRYRKSVPTSWVEIVLREGKNRQVRRMTAKVGFPTLRLLRVAIG FT PWRLDGLAPGAWREVEPRLPPAPEARSAGARPGGLRRR" FT CDS 1185730..1186185 FT /transl_table=11 FT /locus_tag="azo1102" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical secreted protein. Homology to FT rsc2494 of R. solanacearum of 48% (trembl|Q8XWI0(SRS)). FT Pfam: DUF192 signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR003795" FT /db_xref="UniProtKB/TrEMBL:A1K4G4" FT /protein_id="CAL93719.1" FT /translation="MSVRAVLLRAVFALALGAASAAHARAEMPLAELSAGMYRIPVEVA FT ATPQSRQLGLMNRKEMPQQQGMVFVFTEDARHCMWMKNTLLPLSVAFLDGQGRILNIED FT MQPQTEDSHCARGPARFALEMNQGWFRERGLRAGDQIRGVERLPAGY" FT CDS 1186321..1187466 FT /transl_table=11 FT /gene="flhB" FT /locus_tag="azo1103" FT /product="flagellar biosynthetic protein FlhB" FT /function="Flagellar biosynthesis pathway component FlhB" FT /note="Flagellar biosynthetic protein flhB. Required for FT formation of the rod structure in the basal body of the FT flagellar apparatus.The FlhB and FlhA together with FliI FT and FliH, may constitute the export apparatus of flagellin. FT The flhB gene encodes a highly hydrophobic polypeptide with FT several potential membrane-spanning segments, suggesting FT that it may be an integral membrane protein. InterPro: FlhB FT HrpN YscU SpaS Family flhB: flagellar biosynthetic protein FT Pfam: FlhB HrpN YscU SpaS Family 4 TMHs no signal peptide" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4G5" FT /db_xref="InterPro:IPR006135" FT /db_xref="InterPro:IPR006136" FT /db_xref="UniProtKB/TrEMBL:A1K4G5" FT /protein_id="CAL93720.1" FT /translation="MAEDSDLEKTEPASGRRLEQAREEGQVPQSRELSTFLVTMTGVVT FT LWLLGEWMAQRLLGMIRRSFAFEREMAFDHTLILAELQSLLGGALLTLMPLFLALLVAA FT VASPIALGGLVFAPKALGPNFGRMNPIQGLGRMFSVHGLAEMVKAILKALLVGGVGAAV FT LWYYKDHLFDLMVEPLEVGMPDFAETVVFTALLITASLGLLALLDVPFQLWQYHKRLRM FT TKEEVKREAKEQDGDPQLKGRIRAMQREMARGRMMAAVPKADVVVTNPTHFSVALKYDA FT ERMGAPVVVAKGRGELAMKIREIARENDVPLLEAPPLARALYAHCELEQAIPAALYTAV FT AEVMAYVYQLNHWMESGGLPPTTPSELPVPEGMDPGSPDEA" FT CDS 1187481..1189580 FT /transl_table=11 FT /gene="flhA" FT /locus_tag="azo1104" FT /product="flagellar biosynthesis protein flhA" FT /function="Flagellar biosynthesis pathway component FlhA" FT /note="Flagellar biosynthesis protein flhA. Required for FT formation of the rod structure of the flagellar apparatus. FT Together with FlhB, FliI and FliH may constitute the export FT apparatus of flagellin. Pfam: FHIPEP no signal peptide FT probable 7 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4G6" FT /db_xref="InterPro:IPR001712" FT /db_xref="InterPro:IPR006301" FT /db_xref="UniProtKB/TrEMBL:A1K4G6" FT /protein_id="CAL93721.1" FT /translation="MNALNLRELFSVSNLRQLSAPILIVMILSMMVLPLPVFLLDVFFT FT FNIAVSVMVMLVAMYSKKPLDFSVFPTVLLVTTLLRLSLNVASTRIVLLNGHSGPDAAG FT KVIEAFGHFLVGGNTAVGIVVFVILTIINFVVITKGAGRIAEVSARFTLDAMPGKQMAI FT DADLNAGLIDEKTAKARRKEIAQEADFYGAMDGASKFVRGDAVAGILILVINIIGGLFV FT GVVQHNMAAGDAAHTYTLLTIGDGLVAQIPALIISVAAGLVVSRVGDEGDIGGLVIGQL FT FSNPQVLALTAGIIGVLGLIPGMPNFVFLLLAAGLGWLAWSRNRKLMEPESVAQTQAAA FT AQAAAAAPQAEAQEASWNDVAPVDVLGLEVGYRLIPMVDKGQDGELLKRIRGLRKKFAQ FT EVGFLSAPVHIRDNLELKPNAYRIALKGVEIGSGEAYPGQYLAINPGRVSGPMSGRETK FT DPAFGLPAYWIDAGSREQAHGLGYTVVDASTVVATHLNHLILNHAAELLGRQETQALLD FT HIGKESPKLVDDLVPKLLPISAVQRVLQNLLDEGVNIRDMRTIIEVLAEFAPRNQDPVE FT LTSKVREALGRAIIQGLFPGTAEVQVMALEPSLERILMQAMSASGEGGAIEPGLADTLL FT RQTAQIAQRQEDIGLPPVLLVPAPLRMLLSRFLRRAVPTLKVISNAEVPESRTIRVTAM FT VGAAA" FT CDS 1189724..1191256 FT /transl_table=11 FT /gene="flhF" FT /locus_tag="azo1105" FT /product="putative flagellar biosynthesis protein FlhF" FT /function="Flagellar GTP-binding protein" FT /note="Putative flagellar biosynthesis protein flhF FT (Flagella associated GTP-binding protein). Necessary for FT flagellar priosinthesis. May be involved in translocation FT of the flagellum (by similarity). Belongs to the family of FT of subunits of the signal recognition particale in bacteria FT like FtsY, the pilA protein and the flagellar biosynthesis FT protein flhF. InterPro: AAA ATPase superfamily, GTP-binding FT signal recognition particell (SRP54) G-domain no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4G7" FT /db_xref="InterPro:IPR000897" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR020006" FT /db_xref="UniProtKB/TrEMBL:A1K4G7" FT /protein_id="CAL93722.1" FT /translation="MNVKRYFAPTAREALRALKEELGADAIVLSNRAVEGGVEILALPA FT DAVGALHNAARSARPAPAAPRQPAYPPAAPTGYPQAAARRDEPVEPRAPARPAPRFDDD FT DFHVSLSALAAGAVPRNAAAPAVRQPGDKVIRPFNPPRIETADYMLREEKPQPRSAPAP FT RRAVEEPAATAPAAAAAAPMVAPEAAVRDDGRVRELQETNARLMAELSGIRGMIERQLA FT GFAWGETRRQAPARAAMVGELLEAGFSAPSARKLAEAVGEDDSPQAARAAVRAELDRAL FT RARASDDDLIDRGGVFALVGPTGVGKTTTTAKLAARCVVRHGASKLALITTDGYRIGAQ FT EQLRIYGRILGVPVFSVRDAADLRQTLAELRNKHMVLIDTMGVSQRDRMVAEQAAMLTG FT AGEVRRLLLLNATCRGDTLDDVVRAYAGPDLAGVIFSKVDEAASLAPAIDVAVRRKLDL FT LYVTNGQRVPEDLHLPNRAYLLHRALREQSAESPWRMNGDEAGLMLAAGSGA" FT CDS 1191259..1192041 FT /transl_table=11 FT /gene="fleN" FT /locus_tag="azo1106" FT /product="hypothetical flagellar related protein FleN" FT /function="ATPases involved in chromosome partitioning" FT /note="Hypothetical flagellar related protein FleN. FT Homology to fleN of Pseudomonas fluorescens of 27% FT (AAN03366). No domains predicted. No signal peptide. No FT TMHs" FT /db_xref="GOA:A1K4G8" FT /db_xref="UniProtKB/TrEMBL:A1K4G8" FT /protein_id="CAL93723.1" FT /translation="MIPAREDQAAGLRRLFRRAPPTVVALYAAGRQRSYNAVRAAHRIA FT GQAERVLLLDEATGEDSLADALGLPPGGDLLQMLDGRMTLADLLQPVPGLMGRVPAAAA FT ALALPLLDDARRACLVEAVRVLHRHAGIVLIHAASAADPSPFVHAAPRRLLVAEVSASG FT ATEAYQAIKQLAAAGAGSLHVAVCRARSRTEAGAFFGSLEKLVRRHVGVPLAFVGEVER FT DDIAAGLQAPVAESSPREAEAAFLRRLGALAVPRSPGA" FT CDS 1192166..1192936 FT /transl_table=11 FT /gene="fliA" FT /locus_tag="azo1107" FT /product="RNA polymerase sigma factor" FT /function="DNA-directed RNA polymerase specialized sigma FT subunit" FT /note="RNA polymerase sigma factor for flagellar operon FT (Sigma-F factor) (Sigma-27) (Sigma-28). THE SIGMA FACTOR IS FT AN INITIATION FACTOR THAT PROMOTES ATTACHMENT OF THE RNA FT POLYMERASE TO SPECIFIC INITIATION SITES AND THEN IS FT RELEASED. THIS ALTERNATIVE SIGMA FACTOR IS SPECIFIC FOR FT CLASS 3 FLAGELLAR OPERONS. Similar to SWISSPROT: FT sprot|FLIA_PSEAE (46% Pseudomonas aeruginosa, RNA FT polymerase sigma factor for flagellar operon (sigma-f FT factor) (sigma-28)). InterPro: IPR000943 Sigma_70. Pfam: FT PF00140 Sigma-70 factor, region 1.2. HTH reporting nucleic FT acid binding motif. gatB_rel: aspartyl-tRNA(Asn) FT amidotrans" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4G9" FT /db_xref="InterPro:IPR000943" FT /db_xref="InterPro:IPR007624" FT /db_xref="InterPro:IPR007627" FT /db_xref="InterPro:IPR007630" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR012845" FT /db_xref="InterPro:IPR013324" FT /db_xref="InterPro:IPR013325" FT /db_xref="InterPro:IPR014284" FT /db_xref="UniProtKB/TrEMBL:A1K4G9" FT /protein_id="CAL93724.1" FT /translation="MYDAEGNLDKDHLVVAYAPLVKRIAFQLMAKLPASVEVEDLIQNG FT MMGLLDAIGRYEEGLGAQFETYAVQRVRGAMLDGLRENDWLPRSLRRDMRRIESAIHVL FT EQQHGRPPSETELAESLGVPLPEYQRMLQDARGHQLVYFEDFTDGEGEDFLDRHLGAHE FT SNPAELLEDADMRANLIRAIDDLPEREKLVMALYYEEELNLREIGEVLGVTESRVCQLH FT SQAVARLRARVMGARAPVSGGARRGRPPKRPPEA" FT CDS 1193004..1193744 FT /transl_table=11 FT /locus_tag="azo1108" FT /product="flagellar motor protein MotA" FT /function="Flagellar motor component" FT /note="Flagellar motor protein MotA (Chemotaxis motA FT protein). Required for rotation of the flagellar motor. FT Probable transmembrane proton channel (By similarity). FT Pfam: MotA/TolQ//ExbB proton channel family signal peptide FT probable 4 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4H0" FT /db_xref="InterPro:IPR002898" FT /db_xref="UniProtKB/TrEMBL:A1K4H0" FT /protein_id="CAL93725.1" FT /translation="MDSISLVGLTLGVAAILIGQAMEGGHIASLLQPTAFLIVIGGTLG FT AVMLQSPLRVFKEGMRMAKWVFITPATSHAQLIQQVTNWSHVARKEGLLALEAQIPRLP FT DPFMRKGLQMLVDGVEPGRLREVLEVEIGAWEAQLRQCARIWESAGGYAPTVGILGAVM FT GLIHVMENLSDPAKLGSGIAVAFVATIYGVGSANLIFLPIAKKLLAHIGTLVAQREMFV FT DGLVGIANGDNPRIIESRMQGYVV" FT CDS complement(1193801..1195465) FT /transl_table=11 FT /gene="tar" FT /locus_tag="azo1109" FT /product="putative aspartate chemoreceptor protein" FT /function="Methyl-accepting chemotaxis protein" FT /note="E. coli uses five MCP-family receptors to promote FT chemotactic movements toward different attractant FT compounds: Tar is the aspartate and maltose chemoreceptor. FT Methyl-accepting chemotaxis protein," FT /note="Specificity unclear" FT /db_xref="GOA:A1K4H1" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004089" FT /db_xref="UniProtKB/TrEMBL:A1K4H1" FT /protein_id="CAL93726.1" FT /translation="MSLQCRPRTPTGFIMDFIFNSVRNKLLLICGGGTALVLLAAGVGL FT FLQYRSIDDLTSGRLAELQQLRATTLESKVDYYDQLLAWKNTLLRITDAGAQEAHWKTF FT RTLEQQVEGKVAALKGVDAAEVRQLAEQFSAEHLALGAHYQQALNDYKVDFNIYDLEQN FT VRDSDAASDALLDRLVEAMVRHIDNQTDAIQRSSQRAISLSVALMAVACALAFGIFLWL FT LRQQVTRPAEELEASLHRLARGDFSAPIVAHTRDEIGRIATSAESIRRDLGALIQQVAR FT SIQQVDDAAGGMAHETRGVADATAGTADVAASTAATLDEVTASIQAISDNAGRVSALSR FT SGRDEARAAEARLAALAASVDESTSVMNAVTETARAFIQNAEKITAMTQQVREIADQTN FT LLALNAAIEAARAGEQGRGFAVVADEVRKLAEKSGHSASAIDAITSTLGEQAHALEQAL FT NHGLQALESSRDSMAGTSAAVGAASQSSSRAAEEVEQISQAVREQSAASTQIAQQVERI FT AQMVEDSHGALGRMADTADRLHRLADELKGSIDSFRL" FT CDS 1195645..1196484 FT /transl_table=11 FT /gene="motB1" FT /locus_tag="azo1110" FT /product="flagellar motor protein MotB" FT /function="Flagellar motor protein" FT /note="Flagellar motor protein MotB (Chemotaxis motB FT protein. Required for the rotation of the flagellar motor. FT Might be a linker that fastens the torque-generating FT machinery to the cell wall. Pfam: OmpA family no signal FT peptide probable 1 TMH" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4H2" FT /db_xref="InterPro:IPR006665" FT /db_xref="UniProtKB/TrEMBL:A1K4H2" FT /protein_id="CAL93727.1" FT /translation="MPRRRKLEDEHENHERWLVSYADFITLLFAFFVVMYSLSSINEGK FT YRVLSDSLVQAFRSININESGQQIVLPPVSVMSPAAPAPAASTRSPEEEAKRQQTAQRM FT RNMAEEIRRVLAPLTQDGQVSISEGAFGIAVEINASVLFAPGEATLGAPAVSALRAVAQ FT VLAGAEFPITIEGHTDNIPISNLRFPSNWELSAVRASSVVRLFIESGVRAERLTAAGYA FT DQRPVAGNDTDAGRARNRRVTIMIESRVGEMAPAAPGRIGADDPIRSILPDQAPPSQ" FT CDS 1196592..1197074 FT /transl_table=11 FT /gene="dcrH2" FT /locus_tag="azo1111" FT /product="putative hemerythrin-like protein" FT /function="Hemerythrin" FT /note="DcrH:hemerythrin protein, is transmembrane FT methyl-accepting protein probably involved in bacterial FT chemotaxis . 31% Hemerythrin. Pfam:PF01814; Hemerythrin; FT 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4H3" FT /db_xref="InterPro:IPR012312" FT /db_xref="InterPro:IPR012827" FT /db_xref="InterPro:IPR016131" FT /db_xref="UniProtKB/TrEMBL:A1K4H3" FT /protein_id="CAL93728.1" FT /translation="MAELFEWNDDYNVGVADIDEQHLELVALINQLHDAIRSHKASKQV FT RRTLDELAEYTRTHFAIEERLMRESNYPDYESHRSYHEALIDQIRALQAKLDGGEASIT FT FELLHFLRTWLIRHICDVDKQFGAYFIAHGSRPEWMVEAHAAMTSRRWWQFWKARA" FT CDS complement(1197195..1199600) FT /transl_table=11 FT /locus_tag="azo1112" FT /product="DNA topoisomerase IV subunit A" FT /function="DNA gyrase (topoisomerase II) A subunit" FT /EC_number="5.99.1.-" FT /note="Region start changed from 1199745 to 1199601 (-144 FT bases)" FT /db_xref="GOA:A1K4H4" FT /db_xref="InterPro:IPR002205" FT /db_xref="InterPro:IPR005742" FT /db_xref="InterPro:IPR006691" FT /db_xref="InterPro:IPR013758" FT /db_xref="InterPro:IPR013760" FT /db_xref="UniProtKB/TrEMBL:A1K4H4" FT /protein_id="CAL93729.1" FT /translation="MSNDTPDLFGENAAAPAAPEPTAATVAPEAAPPADTPPPPPAPPV FT LMPGSDGALPLDLYAERAYLAYAMSVVKSRALPQVEDGMKPVQRRILYAMNEMRLNATA FT KHVKSARVVGDVIGKYHPHGDSSVYDAMVRVAQDFSLRYPLVDGQGNFGSRDGDSAAAM FT RYTECRLTPIAELLLSEIDRGTVDFVPNYDGAFEEPQLLPARLPFVLLNGASGIAVGMA FT TEIPPHNLREVAEATCHLIRHPEAGLDDILPLLPGPDFPGGGQLISSPEAIRDAYAGGR FT GSLRMRARWRIEELARGQWRVIVEELPHGVSAAQVLSEIETLTNPQPRAGKKEVSQEQK FT QLKQLVLGVLDTVRDESSDKAPVRIVLEPKSSRQSRDEFMAVLLAHTSLETSVSVNMTM FT IGRDGRPQQKNLVQILREWIDFRYVTVERRTRHRLDEVDRRIHILEGRMIAFLHIEDVI FT RVIRESDEPKPALIAAFGLSDVQAEDILEIRLRQLARLEGFKIEKELNELKEEREGLQH FT VLDNRSAMTRLILKEIGEDTKKYGDDRRTLIETVAPIASAEISVADEPVTVILSKNGWI FT RSRQGHGLDAAAISYKAGDFAFALLETRTTWPLIVIDTHGRAYTVKVSDLPGGRGDGVP FT IATLVEFQDGGKPAQVVSDDPATTWLFANSGGYGFLCSVADATSRQRAGKAFMALEKGE FT KVLAPAKVFGEWIAAGSENGRILVFPRAEMKTQSGGRGVIVMALDEGEALSAVAVPADD FT AVLTIEGAGRGGKSTTVELKPAQREGLRHRRARKGAPLTPKVKPERMR" FT CDS complement(1199800..1200315) FT /transl_table=11 FT /locus_tag="azo1113" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT Bucepa03000705 of Burkholderia cepacia of 33% FT (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="GOA:A1K4H5" FT /db_xref="InterPro:IPR011990" FT /db_xref="UniProtKB/TrEMBL:A1K4H5" FT /protein_id="CAL93730.1" FT /translation="MARPTPKENLVDFGPLPAHVNALLQEGVGCHRSDPPRARALFRHA FT IEISPGSLPAYRCLLKLQNQQREFDEALSVAMEGLAEAAHQARVSQDWRDWTLAEVGDD FT KRRTVPQRFLLLFLKAMAFIELRRGNNDISRNLVAKLKELDPEDGCGHSVISAMLDDVD FT DDAETETD" FT CDS complement(1200393..1201181) FT /transl_table=11 FT /gene="lhpp" FT /locus_tag="azo1114" FT /product="putative inorganic pyrophosphate phosphatase" FT /function="predicted sugar phosphatases of the HAD FT superfamily" FT /EC_number="3.1.3.-" FT /note="Phospholysine phosphohistidine inorganic FT pyrophosphate phosphatase. Enzyme that hydrolyzes not only FT oxygen-phosphorus bonds in inorganic pyrophosphate but also FT nitrogen-phosphorus bonds in phospholysine,phosphohistidine FT and imidodiphosphate in vitro. 38% HAD_SF_IIA.IPR006355; FT HAD_SF_IIA_hyp2.IPR005834; Hydrolase. FT Pfam:PF00702;Hydrolase; 1. TIGRFAMs:TIGR01460; HAD-SF-IIA; FT 1.TIGR01458; HAD-SF-IIA-hyp3; 1. TMHelix:1" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4H6" FT /db_xref="InterPro:IPR002645" FT /db_xref="InterPro:IPR006355" FT /db_xref="InterPro:IPR006357" FT /db_xref="InterPro:IPR006402" FT /db_xref="InterPro:IPR023214" FT /db_xref="InterPro:IPR023215" FT /db_xref="UniProtKB/TrEMBL:A1K4H6" FT /protein_id="CAL93731.1" FT /translation="MTDPTPLSPRSPRAVLIDLAGVLYVGTSAIPGSVAALQRLRAAGL FT PLRFLTNSTRMPREPIAARLRAMGFTLQADEIQTAAHAALNLVRRRGLHPRYLVHPDLR FT DEVGPDAERPDAVVMGDMGPFLDYAQLNAAFRLLMDGHPLIAMARNRYFMDADGLSLDM FT GAFVTGLEFCSGTRAEIVGKPAPGFFHDAVAELGVEPEDAVLIGDDLHDDVGAARAAGL FT RAVLVRTGKFRAGDDAHPQVRPDLVADDFSAAVDHLLAHG" FT CDS complement(1201275..1203248) FT /transl_table=11 FT /gene="parE" FT /locus_tag="azo1115" FT /product="topoisomerase IV subunit B" FT /function="DNA gyrase (topoisomerase II) B subunit" FT /EC_number="5.99.1.-" FT /note="Topoisomerase IV subunit B (EC 5.99.1.-). FT TOPOISOMERASE IV IS ESSENTIAL FOR CHROMOSOME SEGREGATION. FT IT HAS RELAXATION OF SUPERCOILED DNA ACTIVITY. PERFORMS THE FT DECATENATION EVENTS REQUIRED DURING THE REPLICATION OF A FT CIRCULAR DNA MOLECULE. InterPro: DNA topoisomerase II" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4H7" FT /db_xref="InterPro:IPR001241" FT /db_xref="InterPro:IPR002288" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR013506" FT /db_xref="InterPro:IPR013759" FT /db_xref="InterPro:IPR013760" FT /db_xref="InterPro:IPR014721" FT /db_xref="InterPro:IPR018522" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/TrEMBL:A1K4H7" FT /protein_id="CAL93732.1" FT /translation="MTSKTYDESSFRVLKGLEPVRERPGMYTRTDSPAHIIQEVIDNAA FT DEALGGFAKKIHVTLHLDGSVTVADDGRGIPVGLHPEEGVPVVVLAYTRLHAGGKFDKR FT EGNGAYAFSGGLHGVGVAVTNALSTRVEVEVKRDGKIHRIDFSDGGENIGAVRIEGDCG FT RQTGTRVRVWPDPKYFEAPRVPMNELERLLRSKAVLLSGVSVRLDIEQAAGPALTKTWS FT YPEGLAGYLKELAGDVEPVAPIFTAEKYAGKDDASFAPGEGAAWALAWFESAVPSESYV FT NLIPTVNGGTHESGLRAGVFEAVKSFIEHHTLLPRGVKLQQEDVCGRMSFLLSARLLDP FT QFQGQVKEKLNSREAVKLVSTQLRDPFEIWLNNHVEAGKAIAELSIKQALARQKNAQKV FT EKKKTSGVAVLPGKLSDCESEDIAENELFLVEGDSAGGSAKMARNKETQAILPLRGKVQ FT NAWEIDPDRLLANAEIHDIAVALGVDAHRADSSPDLSGLRYGKIVIMSDADVDGSHIQT FT LLLTLFFRHFPKLIENGHIYVAQPPLYRVDVPAQGKKRPARRLYALDDGELAAIRDRLA FT QEGFKPDAIEIGRFKGLGEMNPDQLRETTMDPATRRVLPVQVRAEAIEQTLKMFTLLMG FT KGEASGRRAWMEEKGDTVEADV" FT CDS complement(1203341..1203955) FT /transl_table=11 FT /locus_tag="azo1116" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane FT protein,TrEMBL;Q8NSJ9(49% identity,73% FT similarity),TrEMBL;Q7VSN7(53% identity, 72% similarity). FT Has 2 PF03458(IPR005115 ):UPF0126 domain;Domain always FT found as pair in bacterial membrane proteins of unknown FT function. This domain contains three transmembrane helices. FT The conserved glycines are suggestive of an ion channel (C. FT Yeats unpublished obs.). signal peptide 6 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR005115" FT /db_xref="UniProtKB/TrEMBL:A1K4H8" FT /protein_id="CAL93733.1" FT /translation="MLTTIYLIAITAEAMSGALAAGRRSMDIFGVAVIAFVTALGGGTI FT RDMILGHFPIGWTQHPEYVYLVISAGLLTTLVARYMHHLKTVFLVLDAMGLIAFSLIGC FT GVALEMGYATPVVIMSGMITGIFGGILRDVLCNQVPVVFRHELYASVSLAVCALYLALH FT HFAVPEQINIAASFAAGLTLRLLAIWRGWRLPTFSYRERWE" FT CDS complement(1204519..1205832) FT /transl_table=11 FT /gene="aceA" FT /locus_tag="azo1117" FT /product="AceA protein" FT /function="Isocitrate lyase" FT /EC_number="4.1.3.1" FT /note="Isocitrate lyase. Homology to aceA of E. coli of 73% FT (sprot|ACEA_ECOLI). Isocitrate lyase is an enzyme that FT catalyzes the conversion of isocitrate to succinate and FT glyoxylate. This is the first step in the glyoxylate FT bypass, an alternative to the tricarboxylic acid cycle in FT bacteria, fungi and plants. InterPro: Isocitrate lyase FT (IPR000918) Pfam: Isocitrate lyase family no signal peptide FT no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4H9" FT /db_xref="InterPro:IPR000918" FT /db_xref="InterPro:IPR006254" FT /db_xref="InterPro:IPR015813" FT /db_xref="InterPro:IPR018523" FT /db_xref="UniProtKB/TrEMBL:A1K4H9" FT /protein_id="CAL93734.1" FT /translation="MTLTREQQIAALEKDWAENPRWKGIKRGYSAADVVRLRGSLPIEY FT TLAKRGAETLWAKVNGGAKKGYVNAFGAITAGQAMQQAKAGLEAVYLSGWQVAADGNTS FT ETMYPDQSLYAYDSVPTMVRRINNTFKRADEIQWSRGIEPGSKEFIDYFLPIVADAEAG FT FGGVLNAFELMKNMIAAGAAGVHFEDQLAAVKKCGHMGGKVLVPTQEAIEKLISARFAA FT DVMGVSTLILARTDAEAANLITSDHDANDKPFLTGERTQEGFYRVKNGLEQAISRGVAY FT APYADLVWCETGTPDLGFAREFAQAVHAACPGKLLSYNCSPSFNWKKNLDDATIAKFQD FT ELSALGYKYQFITLAGIHVNWYNTFKFAHAYARGEGMKHYVEMVQEPEFAAREQGYTFV FT SHQQEVGAGYFDDVTTVIQGGSSSVKALTGSTEEEQFH" FT CDS 1206325..1207365 FT /transl_table=11 FT /locus_tag="azo1118" FT /product="putative AraC-family transcriptional regulator" FT /function="AraC-type DNA-binding domain-containing FT proteins" FT /note="Putative AraC-family transcriptional regulator," FT /note="Family membership" FT /db_xref="GOA:A1K4I0" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR018060" FT /db_xref="InterPro:IPR018062" FT /db_xref="UniProtKB/TrEMBL:A1K4I0" FT /protein_id="CAL93735.1" FT /translation="MHPSANLDLSKVYRNCVFQSRSAVTSHAQLSRELSEHDLEWRRGS FT VDTALFRADVNRMSLLALRYGAEVEVRPEPFKDFALVQMPLRGAAEIECDGVRLTVAQG FT EAAVVAPRRQIRLVWQPGCEQLLLKVPFELLRQVSCHTCIRSRCPDDASDCGVGLEPAF FT VIERGFNLQWRALVQQLLNLLPAPGEAGLHPGWLNQFEQTVALFLLAHQPAAVGRDLDD FT DAGPAEAVIELTASSRLAERKLDAVEDYMRSRLFAPISLADLAKAAGVSARTLNILCHR FT YRGVAPMVLLRHVRLDAARARLLADPFASVTEVALEYGFGHLGRFSAYYRERFGELPRD FT TGAARH" FT CDS 1207554..1209134 FT /transl_table=11 FT /gene="crtI" FT /locus_tag="azo1119" FT /product="phytoene dehydrogenase" FT /function="Phytoene dehydrogenase and related proteins" FT /EC_number="1.14.99.-" FT /note="Phytoene dehydrogenase (EC 1.14.99.-) (Phytoene FT desaturase). Phytoene dehydrogenase (phytoene desaturase) FT is an enzyme of carotenoid biosynthesis that converts FT phytoene into zeta-carotene via the symmetrical FT introduction of two double bonds at the C-11 and C-11' FT positions of phytoene, TREMBL:Q8XYC4 (50% identity); FT SWISSPROT:P06108 (26% identity). InterPro (IPR008150): FT Bacterial-type phytoene dehydrogenase Pfam (Phytoene_dh): FT Phytoene dehydrogenase related enzyme." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4I1" FT /db_xref="InterPro:IPR006076" FT /db_xref="InterPro:IPR018203" FT /db_xref="UniProtKB/TrEMBL:A1K4I1" FT /protein_id="CAL93736.1" FT /translation="MSGYDAIIVGSGINSLVCAGVMSRRGKKVLVLEREAVLGGCIRSE FT QLTAPGYLHDTMSTAHPLFVTSPGYAELKDALHANGLDYGNNATPTGVLLPDGRSLILG FT RDRAANIAMMNALAPGDGDAYGAGMAFVEQNAQLIFALLGNELWSAGVAKTMLGRLWKQ FT GTHDTVGFFGPAMQSCRAWMETQLKSDLVRAMLAPWVLHTGLGPESAMSALMAQVIAFT FT LEAVGLPLVKGGNARTVDAFRAVVEGAGGRFETGADVAEILVEGGKARGVRTGDGRVFE FT AKQVICNVTPTQLYGRLLPAAHSPEPLRSQAAQYRYGKGNMQIHLALSEPPQWADPKLR FT EVIYLHLTSGLDGVSRAVNEAERGLLPAEGTICVAQPCAVDPSRAPAGGWVMWVQLPEC FT PRTVRGDAAGEIAAPADGSWTEDVRERYADRAIERIAAHVPNLKASIIGRKVISPADLE FT RLNINLVGGDPYSGECAIDQYLFWRPLRGVKNHATPVKGLYHIGASTHPGPGLSGASGF FT HVANALVKG" FT CDS complement(1209318..1210130) FT /transl_table=11 FT /locus_tag="azo1120" FT /product="Short-chain dehydrogenase family protein" FT /function="Dehydrogenases with different specificities FT (related to short-chain alcohol dehydrogenases)" FT /note="The short-chain dehydrogenases/reductases family FT (SDR) is a very large family of enzymes, most of which are FT known to be NAD- or NADP-dependent FT oxidoreductases,TREMBL:Q8XYC0 (36% identity); TREMBL:Q9EX74 FT (34% identity). InterPro (IPR002198): Short-chain FT dehydrogenase/reductase (SDR). InterPro (IPR002347): FT Glucose/ribitol dehydrogenase. Pfam (PF00106): Short chain FT dehydrogenase." FT /note="Specificity unclear" FT /db_xref="GOA:A1K4I2" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K4I2" FT /protein_id="CAL93737.1" FT /translation="MSTTETPRLAGKVAIVTGATQGLGADIARVLAGSGATVYIVGRGR FT EAGEAVAAGIGSPARYLEADITDDAAIERCIRTVIDDCGRLDLLVNNACSYNDRGLASS FT RAEWLATLNVNLVSGAIFTQKAAEVMRPGSVVINLGSTGGKFGADGRAVYPASKAAIIQ FT ITKNFAVSLAPLGIRVVSVSPAWTWSPSVESMTGGSIEKADAVGAHFHPLGRVGRGEEV FT GRAIAFAASADASWITGIDIPVDGGFSILGPDQGRSPREWFARLQPEG" FT CDS complement(1210127..1210732) FT /transl_table=11 FT /locus_tag="azo1121" FT /product="isochorismatase family protein" FT /function="Amidases related to nicotinamidase" FT /note="This is a family of hydrolase enzymes. FT Isochorismatase, also known as 2,3 dihydro-2,3 FT dihydroxybenzoatesynthase catalyses the conversion of FT isochorismate, in the presence of water, to FT 2,3-dihydroxybenzoate and pyruvate, TREMBL:Q9HZE2 (34% FT identity); TREMBL:Q8XSM9 (39% identity). Pfam (PF00857): FT Isochorismatase family." FT /note="Family membership" FT /db_xref="GOA:A1K4I3" FT /db_xref="InterPro:IPR000868" FT /db_xref="UniProtKB/TrEMBL:A1K4I3" FT /protein_id="CAL93738.1" FT /translation="MTTPVVLALHYQNDQLHPEGRIRVGLAEDDPARARLIAAAGRLLA FT GARARGWPIIHVRMAFRPDYADLARNTPIFRKTAEIGAVRDGHWGSEFFSELAPLDSPR FT EFAFKHNRISAFYGTELEALLRLLDAKQLVIAGIATHSVVESTVRDAADRGYEVTVAAD FT ACAAAGTAHDNALASMRLIAEVGDVDSAFAALAPKGHA" FT CDS complement(1210885..1211421) FT /transl_table=11 FT /gene="carBa1" FT /locus_tag="azo1122" FT /product="putative dioxygenase, hydroxylase small FT component." FT /note="Ring hydroxylating dioxygenases are multicomponent FT 1,2-dioxygenase complexes that convert closed-ring FT structures to non-aromatic cis-diols. The beta subunit is FT may be responsible for the substrate specificity of the FT enzyme. Putative 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, FT CarBa. Involved in the aerobic degradation of carbazole by FT P.resinovorans sp. strain CA10. XlyY: Benzene FT 12-dioxygenase beta subunit (EC 1.14.12.3), involved in FT benzoate degradation.Degradation of benzoate to FT 2-hydro-12-dihydroxybenzoate (dhb)." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4I4" FT /db_xref="InterPro:IPR000391" FT /db_xref="UniProtKB/TrEMBL:A1K4I4" FT /protein_id="CAL93739.1" FT /translation="MQLLDRTFDVSTVPVSGASLSAEAVRRVEQFLFHEARLLDERRFA FT EWLALWTEDGRYWVPRFHDQANPFEQISLFWEDKMLREVRVRRVENARNWSQQPLTRSA FT HLVGNITIEGLDAAGHLIVRSTLQLTEWRIDQRQLAGAVFHKLAATEDGGWKIVLKRVN FT LVNCDDVFANLEVFI" FT CDS complement(1211408..1212763) FT /transl_table=11 FT /gene="carBb1" FT /locus_tag="azo1123" FT /product="putative dioxygenase hydroxylase large component" FT /function="Phenylpropionate dioxygenase and related FT ring-hydroxylating dioxygenases large terminal subunit" FT /EC_number="1.14.12.-" FT /note="Ring hydroxylating dioxygenases are multicomponent FT 1,2-dioxygenase complexes that convert closed-ring FT structures to non-aromatic cis-diols. Hydroxylase large FT component of 1,2-dioxygenase protein complex, involved in FT aromatic compounds degradation. 81% simialr to a Putative FT 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase, CarBb. Involved FT in the aerobic degradation of carbazole by Pseudomonas FT resinovorans sp. strain CA10. TREMBL:Q8GI28 FT InterPro:IPR005806; Rieske_reg.IPR001663; Ring_hydroxyl_A. FT Pfam:PF00355; Rieske; 1. PF00848; Ring_hydroxyl_A; 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4I5" FT /db_xref="InterPro:IPR001663" FT /db_xref="InterPro:IPR015879" FT /db_xref="InterPro:IPR017941" FT /db_xref="UniProtKB/TrEMBL:A1K4I5" FT /protein_id="CAL93740.1" FT /translation="MTLSNEALAALVRADSVHKRVYTDPEIFALEMERIYGQAWIYVGH FT ESQVKKTGDYHTTRIGDQDVIMVRAADGKVHVVYNRCPHKGAKVVAEGDGCTGKFFRCP FT YHAWTFKLDGSHLSLPLKNGLEGTCYDPANPDFSMKAVARVDSYRGFVFASQSAEGPDL FT KTFLGGVASSIDNLCERSPVGEVEVAGGTFRVMQKSNWKVFYENLHDTMHARVTHESSF FT VAAREEAAALGEMPFELLIMDGNGEPYEFWEKLELRAYHNGHGYMEGIFDPTAATRDPV FT SRDHFAVLTEAYGEEKARQILGMNRHNTIIYGSGSPHTVFQQFRVIRPVSVDRTMIEIQ FT TFRLKGAPDAVFDRALTYANLINSPSSNVMPDDVEVYKRCQEGNQTRGGDWVSLHRYLG FT TDQETPDGMVSTNGTSELPMRNQFAAWKQYMLNPAPTRQRQAQEKEADRATA" FT CDS complement(1212783..1213730) FT /transl_table=11 FT /gene="vanB1" FT /locus_tag="azo1124" FT /product="probable vanillate O-demethylase oxidoreductase" FT /function="Flavodoxin reductases (ferredoxin-NADPH FT reductases) family 1" FT /note="Probable vanillate O-demethylase oxidoreductase FT (Vanillate degradation ferredoxin-like protein). Homology FT to vanB of P. sp HR199 of 40% (sprot|VANB_PSEUH). The FT vanillate demethylase (EC:1.14.13.82) consists of two FT proteins: an oxygenase and an oxygenase reductase (VanA and FT VanB). This enzyme is involved in the vanillate FT degradation, a key intermediate in the degradation of FT lignin. InterPro: NADH:cytochrome b5 reductase FT (CBR)(IPR001834); Ferredoxin (IPR001041); Oxidoreductase FT FAD and NAD(P) binding domain (IPR001433) Pfam: FT Oxidoredutase FAD-binding domain; Oxidoreductase FT NAD-binding domain; 2Fe-2S iron-sulfur cluster binding FT domain no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4I6" FT /db_xref="InterPro:IPR000951" FT /db_xref="InterPro:IPR001041" FT /db_xref="InterPro:IPR001433" FT /db_xref="InterPro:IPR006058" FT /db_xref="InterPro:IPR008333" FT /db_xref="InterPro:IPR012675" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:A1K4I6" FT /protein_id="CAL93741.1" FT /translation="MTALSMRVEQIDALTPLIRRLILRTADGSAIPAYTAGAHVELHVP FT RERPLRRAYSLVTPADGGDRVEIAVQLEAQGSGGSRWVHSLSEGETITVSPPKNLFPLE FT AAAEEHLLFAGGIGITPILCMARTLAAAGKRYALHYAARDPERAAYCAEVEALEHARCW FT FDGGDPARGMPLAEVIGAPAAGRHLYVCGPKGFIAAVLDTGRKLGWAEANLHCELFTGA FT LDEAGDRPFTVELTTSGITLEVPVGKTVMDVMEEAGLDPMFDCRRGECGICTAKVVAGE FT ADHRDICLSARERSEGGFCTCVSRARSERLVLEL" FT CDS 1214284..1215204 FT /transl_table=11 FT /locus_tag="azo1125" FT /product="ABC transporter permease protein" FT /function="Branched-chain amino acid ABC-type transport FT system permease components" FT /note="Branched-chain amino acid transport system typically FT composed of a periplasmic substrate-binding protein, one or FT two reciprocally homologous integral inner-membrane FT proteins and one or two peripheral membrane ATP-binding FT proteins that couple energy to the active transport FT system.The integral inner-membrane proteins translocate the FT substrate across the membrane. Similar to trembl|Q7W060 FT (64%) and to sprot|LIVH_ECOLI (24%). Pfam (PF02653): FT Branched-chain amino acid transport system / permease FT component TMHMM reporting eight Tmhelix." FT /note="Specificity unclear" FT /db_xref="GOA:A1K4I7" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:A1K4I7" FT /protein_id="CAL93742.1" FT /translation="MDSTFVIEQLINGIGYGLMLFLLAAGLTLVFGVMDTMNLAHGTLF FT MFGAYIAATVHEHSHSFIAAVLAAVVVTVAIGALMETVLMRRLYRRNHLNQVVATFGVI FT LLADDLVKWLWGAAPIMAPTPAALSGPVQLMAELPYPSYRLLILAAGVAAALLLYVVVN FT HTRLGMLVRAGASDRPMAELMGVRVQSVFTVVFVLGAALAGVAGALMGPLTAVQIGMGE FT AILIPALVVIVIGGIGSVRGAFVAALLVGLVDTAGRAFVPPALRAVMPPALAADVGPAL FT AGIAMYVLMAAILCFKPRGLFPARG" FT CDS 1215207..1216199 FT /transl_table=11 FT /gene="livM2" FT /locus_tag="azo1126" FT /product="putative branched-chain amino acid transport FT permease" FT /function="ABC-type branched-chain amino acid transport FT system permease component" FT /note="Putative branched-chain amino acid transport FT permease Homology to livM of S. typhimurium of 28%. Part of FT the binding-protein-dependent transport system for FT branched-chain amino acids. Probably responsible for the FT translocation of the substrates across the membrane. FT InterPro: Binding-system dependent bacterial transporters FT (araH livH/limM families) Pfam: Branched-chain amino acid FT transport system signal peptide probable 9 TMHs" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4I8" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:A1K4I8" FT /protein_id="CAL93743.1" FT /translation="MSSHNNAWLAPGLLLAALAAFPALAPHFGLDYYTGFVMRVLIVML FT IATSLNFLMGYGGMVALGHAGFVGVGAYALVAMTEAGITNAWALWGGAMLAASVAALLV FT GAVSLRTRGVYFIMITLAFAQMLYYLAVSLRAYGGDDGYNLMARPLLGFGLNADDDATL FT YWVVLAVCALCFLFFHHAIGSRFGQALIGVRDNESRMLALGYPVFLLKLQAFVIAAAVA FT GLGGALMVTQNSFISPSSMHWSQSAVLIVIVVLGGLGHRWGGVIGAAVWVSLEEVLRMS FT TEYWHWPLGALLIAIILFAPDGLGALCRRRAAGTGAGRVGFFHLLRRSA" FT CDS 1216196..1216945 FT /transl_table=11 FT /locus_tag="azo1127" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems ATPase component" FT /note="ATP-binding cassette (ABC) transporters are FT multidomain membrane proteins, responsible for the FT controlled efflux and influx of substances (allocrites) FT across cellular membranes. ATP binding domains are FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the ransmembrane domains. Similar FT to trembl|Q7W058 (49%) and to sprot|LIVG_ECOLI (39%). Pfam FT (PF00005): ABC transporter Smart (SM00382): AAA ATPase FT superfamily" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4I9" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A1K4I9" FT /protein_id="CAL93744.1" FT /translation="MTLFSTRGLVKQFGRLRATDEVSIEVAPNEVHALIGPNGAGKSTL FT VNLISGMLPADGGSIVLDGVDLTRMPPHKRVRAGLSRCFQVTNLFKGASVRSNLMLAVQ FT SHRGSSFVPLGRRDGEAELAERAAALAARVGLGGELDRIAGSLPHGAQRQLDVALALAA FT DPKLLLLDEPMAGMGPDESARMVELIQQLRRDMAILLIEHDMDAVFRLADRVSVLVYGK FT VLASGTAEQIKSHPEVQAVYLGSEAVA" FT CDS 1216942..1217658 FT /transl_table=11 FT /locus_tag="azo1128" FT /product="ABC transporter ATP-binding protein" FT /function="ABC-type branched-chain amino acid transport FT systems ATPase component" FT /note="ATP-binding cassette (ABC) transporters are FT multidomain membrane proteins, responsible for the FT controlled efflux and influx of substances (allocrites) FT across cellular membranes. ATP-binding protein is for FT coupling the energy of ATP hydrolysis to conformational FT changes in the transmembrane domains. Similar to FT trembl|Q7W057 (65%) and to trembl|Q84HI4 (49%). Smart FT (SM00382): ATPase superfamily Pfam (PF00005): ABC FT transporter ProSite (PS50101): ATP/GTP-binding site motif A FT (P-loop)" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4J0" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K4J0" FT /protein_id="CAL93745.1" FT /translation="MKHEALLSCSGLQAGYGASQVLFGLDFEIRPGEVIGLLGRNGMGK FT STTIKSIVGTLAPSRGDIRFLGKSIAGMRPDAIARMGVAIVPEGRHCFPNLSVREHLVA FT FADNRNDQRDGWTLERIYALFPRLKERADNLGNQLSGGEQQMLAIGRALSTNPRLLILD FT EATEGLAPVIRDEIWRCLAQLKAEGQTTLVVDKYVDRLVGLADRHLILERGRVVWSGPS FT SELAADRSLWHRYMGV" FT CDS 1217770..1218957 FT /transl_table=11 FT /locus_tag="azo1129" FT /product="probable ABC transporter substrate binding FT protein" FT /function="ABC-type branched-chain amino acid transport FT systems periplasmic component" FT /note="ABC transporter substrate binding proteins counts to FT the family of extracellular ligand binding proteins. It is FT a component of the high affinity amino acid transport FT system. Similar to trembl|Q83V39 (51%) and to trembl|Q7WF58 FT (49%). Pfam (PF01094): Receptor family ligand binding FT region SignalP reporting Signal peptide." FT /note="Function unclear" FT /db_xref="InterPro:IPR001828" FT /db_xref="UniProtKB/TrEMBL:A1K4J1" FT /protein_id="CAL93746.1" FT /translation="MKGTLTRTAAALLALGLLCAPAHAADEIRIGFMTTLSGPGAALGT FT EVRDGFLLALKHSGDKFGGLPVKMEVVDDQQNPQTGRQTVERFLKRDKVDLVTGGVFSN FT VVLPVLPSILQADTVYLSTNTGPRDYAADKCDPNFFALAWQNEDIPAAMGKFASDMGYK FT KVAMIAPNYPGGRESLEGFKHLYKGEIVEEIYTKLGQLDYAAELATIRVAKPDAVFFFL FT PGGMGVNFIKQFDGAGLSKTIPLLAPGFSADEDTIKAVGESITGLYNASQWAADLDNAA FT NKRFVADYIKTYGRIPTMYAAQAYDTAMLIDSAVKKVGGKIEDKAAFRKALRAADFQSV FT RGSFRFNTNQYPVQDIYMRAVAKNAQGQTTNKTVGVVIKAHADRFAAECKMAAGG" FT CDS complement(1219045..1219530) FT /transl_table=11 FT /locus_tag="azo1130" FT /product="S-adenosylmethionine:2-demethylmenaquinone FT methyltransferase" FT /function="Demethylmenaquinone methyltransferase" FT /EC_number="2.1.1.-" FT /note="Region start changed from 1219636 to 1219531 (-105 FT bases)" FT /db_xref="GOA:A1K4J2" FT /db_xref="InterPro:IPR005493" FT /db_xref="InterPro:IPR010203" FT /db_xref="UniProtKB/TrEMBL:A1K4J2" FT /protein_id="CAL93747.1" FT /translation="MSQSIQTADLCDANEGKVAVVAPMFRSFGGRSAFGGAIATLKLFE FT DNALVRKTLETPGNGRVLVVDGGGSMRCALVGDQLGELGVKNGWAGIVVYGCIRDSKAL FT SGMDIGVFALGTHPLKSIKRNTGEAELPVTFGGVTFVPGHYLYADEDGVIVSASALL" FT CDS complement(1219713..1220327) FT /transl_table=11 FT /locus_tag="azo1131" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT Daro03001685 of Dechloromonas aromatica of 46% FT (gi|41725028|ref|ZP_00151838.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K4J3" FT /protein_id="CAL93748.1" FT /translation="MLIAGQLGISQTKQEIYMLFDRYEQQGLLFNMNFKEASTTAGKAA FT YRGELVLVEGEVGDAAGRRKPPTEVMRGAVLLSDGDKLEMAAGMLNDVSEVPLFFEKYG FT EDLVPGAKLLFFVVNVAKPLFTEFGGQTSALIPLQDGMVWNELIDELKLEKGDFKGQSA FT ADKVLTVAGAFADYKPKYPTVGWDEVVATKTNAVREARGPV" FT CDS complement(1220421..1222703) FT /transl_table=11 FT /gene="clpA" FT /locus_tag="azo1132" FT /product="probable ATP-dependent Clp protease, ATP-binding FT subunit clpA" FT /function="ATPases with chaperone activity ATP-binding FT subunit" FT /EC_number="3.4.21.92" FT /note="ATP-dependent Clp protease ATP-binding subunit clpA. FT Homology to clpA of E. coli of 63% (sprot|CLPA_ECOLI). FT ATP-dependent specificity component of the clpP protease. FT It directs the protease to specific substrates. The primary FT function of the clpA-clpP complex appears to be the FT degradation of unfolded or abnormal proteins. InterPro: FT AAA-protein (ATPases associated with various cellular FT activities)(IPR003959); AAA ATPase superfamily (IPR003593); FT Clp amino terminus (IPR004176); chaperonins clpA/B FT (IPR001270); Bacterial typeII secretion system protein E FT (IPR001482) Pfam: Clp amino ternimal domain; ATPase family FT associated with cellular activites no signal peptide no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4J4" FT /db_xref="InterPro:IPR001270" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003959" FT /db_xref="InterPro:IPR004176" FT /db_xref="InterPro:IPR013093" FT /db_xref="InterPro:IPR013461" FT /db_xref="InterPro:IPR018368" FT /db_xref="InterPro:IPR019489" FT /db_xref="InterPro:IPR023150" FT /db_xref="UniProtKB/TrEMBL:A1K4J4" FT /protein_id="CAL93749.1" FT /translation="MIAQELEVSLHMAFVEARQKRHEFITVEHLLLALLDNPSAAEVLR FT ACAANLDELRRELTNFINEHTPKVEGSEEIDTQPTLGFQRVIQRAILHVQSSGKKEVTG FT ANVLVAIFGEKDSHAVYFLQRQNISRLDVVNFISHGIAKTPQQGGGTQGRGAGEQGEQG FT EQEAEEKQSAGALENYTQNLNQQALVGKIDPLIGREKEVERVIQTLCRRRKNNPLLVGE FT AGVGKTAIAEGLARRIVEGRVPEILENAQVYALDMGALLAGTKYRGDFEQRLKAVLKQL FT VENQDAILFIDEIHTLIGAGAASGGTLDASNLLKPALSSGQLKCIGATTYNEYRQIFEK FT DHALSRRFQKVDVTEPSVSETVEILKGLKSRFEEHHGVKYSASALSSAAELSAKYINDR FT HLPDKAIDVIDEAGAAQRILPKSKQKKTIGKNEIEEIVAKIARIPPRTVSNDDKAALKT FT LERDLKNVVFGQNAAIEALAKAIKMSRSGLGNPAKPIGSFLFSGPTGVGKTEVARQLAY FT TLGIELVRFDMSEYMERHAVSRLIGAPPGYVGFDQGGLLTEQITKKPHCVLLLDEIEKA FT HPDIYNILLQVMDHGTLTDNNGRQADFRNVIMIMTTNAGAETMQKSVIGFSAKREAGDE FT MSEIKRMFSPEFRNRLDATISFKALDSEIILRVVDKFLMQLEAQLHEKKVEAHFSDELK FT AWLAERGFDPLMGARPMARLIQDTIRSALADELLFGRLANGGKVTIDIDDEQKVKLTFD FT ETEVATV" FT CDS complement(1222704..1223012) FT /transl_table=11 FT /gene="clpS" FT /locus_tag="azo1133" FT /product="ClpS protein" FT /function="ATP-dependent Clp protease adaptor protein clpS" FT /note="ATP-dependent Clp protease adaptor protein clpS FT [clpS],65% identity (82% similarity) to FT SwissProt;Q7NRW1,64% identity to SwissProt;Q8XWK9. Has FT PF02617;ATP-dependent Clp protease adaptor protein FT ClpS(IPR003769); In the bacterial cytosol, ATP-dependent FT protein degradation is performed by several different FT chaperone-protease pairs, including ClpAP. ClpS directly FT influences the ClpAP machine by binding to the N-terminal FT domain of the chaperone ClpA. The degradation of ClpAP FT substrates, both SsrA-tagged proteins and ClpA itself, is FT specifically inhibited by ClpS. ClpS modifies ClpA FT substrate specificity, potentially redirecting degradation FT by ClpAP toward aggregated proteins." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4J5" FT /db_xref="InterPro:IPR003769" FT /db_xref="InterPro:IPR014719" FT /db_xref="InterPro:IPR022935" FT /db_xref="UniProtKB/Swiss-Prot:A1K4J5" FT /protein_id="CAL93750.1" FT /translation="MATQKQDGFVLEAKRTRTRPPPLYKVLLLNDDFTPMDFVIVVLQK FT YFSMDRERATRVMLQVHREGMGVCGVFPRDIASTKVEQVVSFARQHQHPLACVMEEN" FT CDS 1223446..1223649 FT /transl_table=11 FT /gene="cspE" FT /locus_tag="azo1134" FT /product="cold-shock protein" FT /function="Cold shock proteins" FT /note="Cold-shock protein cspE, (When Escherichia coli is FT exposed to a temperature drop from 37 to 10 degrees FT centigrade, a 4-5 hour lag phase occurs, after which growth FT is resumed at a reduced rate. During the lag phase,the FT expression of around 13 proteins, which contain specific FT DNA-binding regions, is increased 2-10 fold. These FT so-called 'cold shock' proteins are thought to help the FT cell to survive in temperatures lower than optimum growth FT temperature.)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4J6" FT /db_xref="InterPro:IPR002059" FT /db_xref="InterPro:IPR011129" FT /db_xref="InterPro:IPR012156" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR019844" FT /db_xref="UniProtKB/TrEMBL:A1K4J6" FT /protein_id="CAL93751.1" FT /translation="MATGTVKWFNDSKGFGFITPDDGSEDLFAHFSAINMNGFKTLKEG FT EKVSFEVTQGPKGKQASNIQRA" FT CDS complement(1223918..1224085) FT /transl_table=11 FT /gene="rpmG" FT /locus_tag="azo1135" FT /product="50S ribosomal subunit protein L33" FT /function="Ribosomal protein L33" FT /note="50S ribosomal protein L33." FT /note="Family membership" FT /db_xref="GOA:A1K4J7" FT /db_xref="InterPro:IPR001705" FT /db_xref="InterPro:IPR011332" FT /db_xref="InterPro:IPR018264" FT /db_xref="UniProtKB/Swiss-Prot:A1K4J7" FT /protein_id="CAL93752.1" FT /translation="MAKGIREKIKLESTAGTGHFYTTSKNKRTTPEKLEFNKYDPVARK FT HVPYKEVKLK" FT CDS complement(1224147..1224383) FT /transl_table=11 FT /gene="rpmB" FT /locus_tag="azo1136" FT /product="50S ribosomal protein L28" FT /function="Ribosomal protein L28" FT /note="50S ribosomal protein L28." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4J8" FT /db_xref="InterPro:IPR001383" FT /db_xref="UniProtKB/Swiss-Prot:A1K4J8" FT /protein_id="CAL93753.1" FT /translation="MARVCQVTGKAPMVGNHVSHANNKTKRRFLPNLQNRRFWSEAENR FT WIRLRVSNAALRTIDKKGIDVVVAELRARGDKI" FT CDS complement(1224488..1225165) FT /transl_table=11 FT /gene="radC1" FT /locus_tag="azo1137" FT /product="DNA repair protein radC homolog" FT /note="DNA repair protein radC homolog, 64% Idnentity to FT SwisProt;Q82UL9,(58%) to Q8XWN0. TrEMBL;Q7NTH5(60% FT Identity) Signal Peptide Present Has PF04002, RadC, DNA FT repair protein;IPR001405: RadC plays a role in repair of FT DNA damage after UV and X-ray irradiation in prokaryotes. FT The E. coli radC gene encodes a RecG-like DNA FT recombination/repair function. RadC may function FT specifically in recombinational repair that is associated FT with the replication fork." FT /db_xref="InterPro:IPR001405" FT /db_xref="InterPro:IPR010994" FT /db_xref="InterPro:IPR020891" FT /db_xref="UniProtKB/Swiss-Prot:A1K4J9" FT /protein_id="CAL93754.1" FT /translation="MAITDWPEDERPREKLLSRGANALSDAELLALFLRVGIRGRTAVD FT LARDLIARFGTLTRLCSATSSEFAAIPGMGLAKYAQLQAVMELARRALSETLCARDLFD FT SPEAVRDWLRLRLGHLPHETFCVLLLDARNTLIDAVDLFRGTLTQTSVYPREVVKLALD FT RNAAAVIFAHNHPSGAAEPSSADEQLTRHLKDALALVDIRVLDHFVVPAHGKPTSFAER FT GLI" FT CDS 1225220..1226419 FT /transl_table=11 FT /gene="dfp" FT /locus_tag="azo1138" FT /product="phosphopantothenoylcysteine decarboxylase / FT Phosphopantothenate--cysteine ligase" FT /function="Phosphopantothenoylcysteine FT synthetase/decarboxylase" FT /EC_number="4.1.1.36" FT /note="DNA/pantothenate metabolism flavoprotein homolog. FT includes: phosphopantothenoylcysteine decarboxylase (ppcdc) FT (coac); phosphopantothenate-- cysteine ligase FLAVOPROTEIN FT AFFECTING SYNTHESIS OF DNA AND PANTOTHENATE METABOLISM (BY FT SIMILARITY)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4K0" FT /db_xref="InterPro:IPR003382" FT /db_xref="InterPro:IPR005252" FT /db_xref="InterPro:IPR007085" FT /db_xref="UniProtKB/TrEMBL:A1K4K0" FT /protein_id="CAL93755.1" FT /translation="MTSLQGKRIVLGVTGGVAAYKAAELVRLLGKAGVDVHVVLTEAGA FT RFVGAVTFQALSGNPVWSDLWDPRMPNNMAHIDLGREADAVLVAPASADFIARIAGGRA FT DDLLTTLCLARDCPLLVAPAMNRQMWEHPATQRNVGQAVADGVTMLGPAAGDQACGETG FT MGRMEEPEALLEGLEAFFVAKTLAGRRVVLTAGPTFEAIDPVRGITNSSSGKMGYALAR FT ACAQAGAEVVLVSGPVALPVPRGVRRVDVRSALEMRGAVLDALPGTDVFIAVAAVADYR FT PAQTAEHKIKKSGDTLHLSLTPNPDILAEVAARPDAPFCVGFAAESRDLDAYAEGKRRN FT KRLPLLVGNLVGDGLGGDDNLVVLYDDRGKHPLPRAPKTELARQIVDHLAALLPPSNSR FT " FT CDS 1226436..1226885 FT /transl_table=11 FT /gene="dut" FT /locus_tag="azo1139" FT /product="dUTP diphosphatase" FT /EC_number="3.6.1.23" FT /note="dUTP diphosphatase (Deoxyuridine-triphosphatase) FT (dUTPase)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4K1" FT /db_xref="InterPro:IPR008180" FT /db_xref="InterPro:IPR008181" FT /db_xref="UniProtKB/Swiss-Prot:A1K4K1" FT /protein_id="CAL93756.1" FT /translation="MHRIDVKLLDPRLKTHPPAYASAGAAGLDLRACLDAPVLLHPGET FT TLVPSGLAIHLADPGLAAMVLPRSGLGHKHGIVLGNLVGLIDSDYQGQVFVSVWNRGRD FT VFTIQPMERIAQLVVVPVLQVGFNVVDDFAASERGEGGFGSTGKH" FT CDS 1226887..1227312 FT /transl_table=11 FT /locus_tag="azo1140" FT /product="conserved hypothetical mutT family protein" FT /note="Conserved hypothetical MutT family protein. Homology FT to AGR_C_3368 of Agrobacterium tumefaciens of 33% FT (tremble:Q7CYF2). Pfam: NUDIX domain MutT is a small FT bacterial protein (~12-15Kd) involved in the GO system FT MEDLINE:1328155 responsible for removing an oxidatively FT damaged form of guanine (8-hydroxy- guanine or FT 7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. FT 8-oxo-dGTP is inserted opposite dA and dC residues of FT template DNA with near equal efficiency, leading to A.T to FT G.C transversions. MutT specifically degrades 8-oxo-dGTP to FT the monophosphate, with the concomitant release of FT pyrophosphate. A short conserved N-terminal region of mutT FT (designated the MutT domain) is also found in a variety of FT other prokaryotic, viral and eukaryotic proteins. No signal FT peptide. No TMH" FT /note="Family membership" FT /db_xref="GOA:A1K4K2" FT /db_xref="InterPro:IPR000086" FT /db_xref="InterPro:IPR015797" FT /db_xref="InterPro:IPR020084" FT /db_xref="InterPro:IPR020476" FT /db_xref="UniProtKB/TrEMBL:A1K4K2" FT /protein_id="CAL93757.1" FT /translation="MQAKGIPTGVHIVCERGGRVLLMRRAGTGFFDGLYSLPGGHVEEG FT ESVRAAAVRELREETGLSVDEAALDWLGVVHRRSDSNRIDFFLRAAAWMGEPAIREPEK FT CDAIGWFAPDDLPAAMVPYVRHALGQAHTPWMLELGW" FT CDS complement(1227315..1228592) FT /transl_table=11 FT /gene="soxF" FT /locus_tag="azo1141" FT /product="probable sulfide dehydrogenase, flavoprtein FT subunit" FT /function="uncharacterized NAD(FAD)-dependent FT dehydrogenases" FT /EC_number="1.8.2.1" FT /note="Probable sulfide dehydrogenase, falvoprotein subunit FT (Flavocytochrome C flavoprotein subunit). Homology to fccB FT of C. vinosum of 40% (sprot|DHSU_CHRVI). Pfam: Pyridine FT nucleotide-disulphide oxidoreductase signal peptide no FT TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4K3" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR015323" FT /db_xref="InterPro:IPR015904" FT /db_xref="InterPro:IPR016156" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K4K3" FT /protein_id="CAL93758.1" FT /translation="MFPRRRFLQGIAALAGAPALALPLSGCVSAPGRAAPHVVVVGGGF FT GGATAARYLRLWSEGTVRVTLIERDARFVSCPLSNLVLGGSIGLDDLTRSYDRLRDDWG FT VTVVRDEVTAVDAAGRTVTTASGARFNYDRLVLSPGVDFIPGAIEGLSPGDERVPHAWK FT AGPQTALLRRQLVAMRAGGVYALHVPKAPYRCPPGPYERACVIADYLRHANPRAKVLVL FT DANPEIQSKKALFTAAFAEYKGLIEYRPNSDLRAVDGATRTAELEFERIAADVLNVLPP FT MRAGDLARRAGLPLINERWVDIDWLSYEARGVPGVHVLGDAVFAAPGMPKSGHMATQHA FT RVAAAAILRLLAGEAPDPAPVVMNTCYSFVDARRVIHVASVHPFDPEKRQPVPVAGAGG FT VSAVASEAEGEIAWTWARNTWRDMLG" FT CDS complement(1228607..1228906) FT /transl_table=11 FT /gene="soxE" FT /locus_tag="azo1142" FT /product="putative sulfide dehydrogenase, cytochrome FT subunit" FT /function="Cytochrome c553" FT /note="Putative sulfide dehydrogenase, cytochrome subunit. FT Homology to fccA of C. limicola of 26% FT (sprot|CYSD_CHLLT(SRS)) InterPro: Cytochrome c class I FT (IPR003088); cytochrome c class IC (IPR008168) Pfam: FT Cytochrome C signal peptide no TMHs" FT /db_xref="GOA:A1K4K4" FT /db_xref="InterPro:IPR003088" FT /db_xref="InterPro:IPR009056" FT /db_xref="UniProtKB/TrEMBL:A1K4K4" FT /protein_id="CAL93759.1" FT /translation="MKSRATLTALFCLGLAQSALAAAPPPGRSLAATCFNCHGSDGRSQ FT GAIASLAGMPSDTLLATLEEFRSGARPATIMHQIVRGYTPQQLELIARYFAQLK" FT CDS 1229108..1229551 FT /transl_table=11 FT /gene="soxY" FT /locus_tag="azo1143" FT /product="sulfur covalently-binding protein" FT /db_xref="InterPro:IPR016568" FT /db_xref="UniProtKB/TrEMBL:A1K4K5" FT /protein_id="CAL93760.1" FT /translation="MKAGGGFGLLGLLVGAGLVSPQVARAAWDKAAFDSRGVEAVFAAL FT GAGKPAPSTEIRINAPEIAENGAVVAVSVVSNLPQTEQIALLVDRNPYTLAAHFVIPPG FT TAPDIQTRIKMAESANVYALVKAGGRFHVARREVKVTLGGCGA" FT CDS 1229562..1229873 FT /transl_table=11 FT /gene="soxZ" FT /locus_tag="azo1144" FT /product="phosphodiesterase I" FT /EC_number="3.1.4.1" FT /note="Gene Function" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4K6" FT /db_xref="InterPro:IPR014756" FT /db_xref="InterPro:IPR014880" FT /db_xref="UniProtKB/TrEMBL:A1K4K6" FT /protein_id="CAL93761.1" FT /translation="MSNPTRIRATAKDGYTEVRVLMSHVMENGQRKDAGGVVVPAHFIT FT EVSVTHNERVVLAAQFGPSVSANPYLAFRFQGGASGDRIAVRWTDNGGDSRSDEARIG" FT CDS complement(1229883..1231652) FT /transl_table=11 FT /gene="aceK" FT /locus_tag="azo1145" FT /product="[Isocitrate dehydrogenase (NADP+)] kinase" FT /function="Isocitrate dehydrogenase kinase/phosphatase" FT /EC_number="2.7.11.5" FT /note="Isocitrate dehydrogenase kinase/phosphatase, WHEN FT BACTERIA ARE GROWN ON GLUCOSE IDH IS FULLY ACTIVE AND FT UNPHOSPHORYLATED BUT WHEN GROWN ON ACETATE THE ACTIVITY OF FT IDH DECLINES DRASTICALLY CONCOMITANT WITH ITS FT PHOSPHORYLATION AT MULTIPLE SITES (BY SIMILARITY)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4K7" FT /db_xref="InterPro:IPR010452" FT /db_xref="UniProtKB/Swiss-Prot:A1K4K7" FT /protein_id="CAL93762.1" FT /translation="MDAQVGDNPVAQAIAHALVEGFNKHYRIFRGTSRRAKEYFEAGDW FT RAQLDAVRDRVQFYDDRVDETVRRLLEEFDADSLDDATWQQVKLHFIGALINHKQPELA FT ETFFNSVGCKILHRTYFNNDYIFARPAISTEYIESYPPVYSSYYPQDGGLRATIRRIIE FT DFDWQRPFEDLDRDIDCIMRAALAHLGEWPAMEVNCQLQVLYSAFYRNKTAYIIGKVIN FT GWQDYPFTLAVRHGASGRLVIDTILLDPWRISVLFSLSRAYFMVDMEVPSGYVQFLRSI FT MPNKPRSELYTMLGLGKQGKTMFFRDLVAHLRHSNDQFIIAPGIRGLVMLVFTLPSYPY FT VFKIIKDVFGSSKNMDRATVKRKYLMVKQVDRVGRMADTLEFSYAALPLSRFHPELLEE FT LRTLAPSAFEIDGDALVLKHFYIERRMTPLNIHLEKASDGEVEAAVHEYGNAIRELAIA FT NIFPGDMLWKNFGVTRYGRVVFYDYDEIEYMTSMNFRRIPPAPHEDMELSGEPWYSAGP FT MDVFPEEFATFLLGSPRVRKAFMKYHRDLLEPAFWQAAQQGVRDGHVEDFFPYPAELRF FT SVMFPATPVAAQD" FT CDS 1232133..1234370 FT /transl_table=11 FT /gene="icd2" FT /locus_tag="azo1146" FT /product="isocitrate dehydrogenase[NADP]" FT /function="Monomeric isocitrate dehydrogenase" FT /EC_number="1.1.1.42" FT /note="Isocitrate dehydrogenase [NADP]. Homology to icd2 of FT A. eutrophus of 80% (trembl|Q8KLU4) This monomeric type of FT isocitrate dehydrogenase is NADP-specific. It is an FT important enzyme of the TCA. Interpro: Isocitrate FT dehydrogenase NADP-dependent, monomeric type (IPR004436) FT Tigrfam: monomer-idh: isocitrate dehydrogenase FT NADP-dependent no singal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4K8" FT /db_xref="InterPro:IPR004436" FT /db_xref="InterPro:IPR024084" FT /db_xref="UniProtKB/TrEMBL:A1K4K8" FT /protein_id="CAL93763.1" FT /translation="MPSQQPTIIYTITDEAPMLATAAFLPVIRSFTKPAGIQIEEADIS FT LAGRILAEFPDFLSDAQKVPNTLAELGALTLKPEANIIKLPNISASVAQLKAAIKELQG FT KGYKIPDFPEDPKNDEEKAIKTRYSKCLGSSVNPVLREGNSDRRAPAAVKNYAKKHPHS FT MGDWKQWSRTHVSHMEHGDFYHGEKSMTLDKARDVKMELLTKSGKAIVLKPKVALLDGE FT VIDSMFMSKKALLEFYEQQLEDCREAGILFSLHVKATMMKVSHPIVFGHCVKIYYKEAF FT EKHGKLFDELGINVNNGMVDLFDKIKTLPESKRDEIIRDLHACHEHRPELAMVDSAKGI FT TNFHSPNDVIVDASMPAMIRAGGKMYGADGKPYDCKAVMPESTFARIYQEMINFCKWHG FT NFDPRTMGTVPNVGLMAQKAEEYGSHDKTFEIPEDGVANITDLATGEVLLSQNVEAGDI FT WRMCQVKDAPIRDWVKLAVTRARNSGMPAVFWLDPYRPHENELIKKVEKYLKDHDTSGL FT EIRIMSQVRAMRFTLERVVRGLDTISVTGNILRDYLTDLFPIMELGTSAKMLSIVPLMN FT GGGMYETGAGGSAPKHVQQLVEENHLRWDSLGEFLALAVSLEELGIKTGNAKAKVLAKT FT LDEATGKLLDLDKSPSRRTGELDNRGSQFYLSLYWAQALAAQTDDAELAAQFGPLAKTL FT AENEQKIVDELKAVQGKPAEIGGYYRVDVEKCTAVMRPSATFNAAIASIAG" FT CDS 1234547..1235824 FT /transl_table=11 FT /gene="icd1" FT /locus_tag="azo1147" FT /product="isocitrate dehydrogenase [NADP]" FT /function="Isocitrate dehydrogenases" FT /EC_number="1.1.1.42" FT /note="Isocitrate dehydrogenase [NADP]. Homology to icd1 of FT A. eutropus of 75% (trembl|Q8KLU5) Isocitrate dehydrogenase FT is an important enzyme of the TCA which catalyzes the FT reaction: isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH + FT H+ Pfam: Isocitrate/isopropylmalate dehydrogenase Tigrfam: FT prok_nadp_idh: isocitrate dehydrogenase no signal peptide FT no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4K9" FT /db_xref="InterPro:IPR001804" FT /db_xref="InterPro:IPR004439" FT /db_xref="InterPro:IPR019818" FT /db_xref="InterPro:IPR024084" FT /db_xref="UniProtKB/TrEMBL:A1K4K9" FT /protein_id="CAL93764.1" FT /translation="MVESNNQEGVDMSTSHIKVPAGGQKIVPGQPIPDNPIIPYIEGDG FT IGIDITPVMIKVIDAAVDKAYGGGRKIHWMEVFAGEKSTRLYGPDEWLPKETFDALKEY FT SVSIKGPMTTPVGGGIRSLNVALRQELDLYQCVRPVRYFNGVPSPLKDPSKVDMVIFRE FT NTEDIYAGIEWAAESDSAKKVIRFLQEEMGVKKIRFPATSGIGIKPISREGTTRLVRAA FT LRYAIDNDRRNLTIVHKGNIMKFTEGAFRDWAYEVAQKEFGAEPIDGGPWCRFKNPKTG FT REIVVKDAIADAFLQQILLRPAEYDVIACCNLNGDYISDALAAQVGGIGIAPGANISDQ FT YACFEATHGTAPKYAGLDKVNPGSIILSAEMMLRHLGWTEAADLVIRSMEAAIGDKVVT FT YDFARLMEGAQEVSCSAFGDAMIARM" FT CDS 1236048..1236302 FT /transl_table=11 FT /locus_tag="azo1148" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT ws0602 of W. succinogenes of 63% (trembl|Q7MSB5(SRS)) no FT domains predicted no singal peptide 2 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR019886" FT /db_xref="UniProtKB/TrEMBL:A1K4L0" FT /protein_id="CAL93765.1" FT /translation="MENNSAAYWKATLALLTKILIIWFLVSFGAGILFAPALNSIHLGG FT YPLGFWFAHQGSIYVFVILIFYYAKKMAQIDERFDVHED" FT CDS 1236315..1238120 FT /transl_table=11 FT /locus_tag="azo1149" FT /product="conserved hypothetical sodium:solute symporter" FT /function="predicted symporter" FT /note="Conserved hypothetical sodium:solute symporter. FT Homology to to ws0601 of W. succinogenes of 68% FT (trembl|Q7M9X9). Sodium/substrate symport (or co-transport) FT is a widespread mechanism of solute transport across FT cytoplasmic membranes of pro- and eukaryotic cells. Thereby FT the energy stored in an inwardly directed electrochemical FT sodium gradient (sodium motive force, SMF) is used to drive FT solute accumulation against a concentration gradient. The FT solutes transported may be sugars, amino acids, FT nucleosides, inositols, vitamins,urea or anions, depending FT on the system. InterPro: Sodium:solute symporter family FT (IPR001734) Tigrfam: sss: SSS sodium solute transporter FT superfamily no signal peptide 12 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4L1" FT /db_xref="InterPro:IPR001734" FT /db_xref="InterPro:IPR019899" FT /db_xref="UniProtKB/TrEMBL:A1K4L1" FT /protein_id="CAL93766.1" FT /translation="MDLQTITYLVVGASFALYIGIAIWARAGSTSEFYVAGGGVHPVTN FT GMATAADWMSAASFISMAGLIANMGYGGGLFLMGWTGGYVLLAMLLAPYLRKFGKFTVP FT QFIGDRFYSKSASTVAVVCLLTASITYVIGQMTGVGVAFSRFLGVSNDMGIYIGMGIVF FT MYAVFGGMKGITYTQVAQYIVLILAYTIPAIFIALQLTGNPIPQLGLGSDLSGTDVSLL FT QRLNQVVTDLGFGEYTTSVPGSTLNMFVYTVSLMIGTAGLPHVIVRFFTVPKVKDARSS FT AGWALVFIAILYTTAPAVAAMAKYNLHATVNSAVTTGGDLYATEASIKAEERPDWMKRW FT EKTGLLKFEDKNGDGRIQYYNDATKNADAKAKAEAAGWKGNELSVNADIIVLANPEIAL FT LPNWVIALIAAGGLAAALSTAAGLLMAISSAVSHDLVKNVFMPGISEKGELMAGKLSMA FT VAIVIAGYLGLNPPGFAAGTVALAFGIAASSLFPAIMMGIFSKKMNKEGAIAGMLAGLF FT VTCFYVFAHKGLFFIKGTEFVDMIGGPNAFFGITPEAFGAIGALVNFGVAFAVDKVTKE FT PPEHIQHLVESVRIPRGAKAVDGAH" FT CDS 1238249..1238617 FT /transl_table=11 FT /locus_tag="azo1150" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. No singal peptide 3 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K4L2" FT /protein_id="CAL93767.1" FT /translation="MIFDVSVALTWILFLALFPVSFYWLRRAWRIVVRRDFSEVALKRG FT ESPPNPARFAPYAAAINLVGAGVLIAAIIGVVTGEYAYETWSAMAGSTLWFKVLADFIL FT ARHAHPVRSRKRAAPAGQ" FT CDS complement(1238632..1238925) FT /transl_table=11 FT /locus_tag="azo1151" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT vv11244 of V. vulnificus of 42% (trembl|Q8DCZ3(SRS)) no FT domains predicted no signal peptide 2 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR019886" FT /db_xref="UniProtKB/TrEMBL:A1K4L3" FT /protein_id="CAL93768.1" FT /translation="MTEPVEIPLAPSRLTRRHRAYWRWTQVLTAVLLTLWFAVTFVSGF FT YASDLNAHTFLGFPLGFYLLAQGSLIAYVAIIGIYVLAMNWLDRHYGVGERR" FT CDS complement(1238922..1240967) FT /transl_table=11 FT /gene="fusA1" FT /locus_tag="azo1152" FT /product="putative elongation factor EF-G" FT /function="Translation elongation factors (GTPases)" FT /EC_number="3.6.5.3" FT /note="Putative elongation factor EF-G. Homology to FusA of FT E. coli of 29% (sprot|EFG_ECOLI(SRS)) This protein promotes FT the GTP-dependent translocation of the nascent protein FT chain from the A-site to the P-site of the ribosome. FT Interpro: Elongation factor G, C-terminus (IPR000640); FT Elongation factor Tu domain 2 (IPR004161); GTP-binding FT elongation factor (IPR000795); ATP/GTP-binding site motifA FT (P-loop) (IPR001687) Tigrfam: EF-G: translation elongation FT factor G Pfam: Elongation factor Tu domain 2; Elongation FT factor Tu GTP binding domain; Elongation factor G FT C-terminus no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4L4" FT /db_xref="InterPro:IPR000640" FT /db_xref="InterPro:IPR000795" FT /db_xref="InterPro:IPR004161" FT /db_xref="InterPro:IPR005517" FT /db_xref="InterPro:IPR009000" FT /db_xref="InterPro:IPR009022" FT /db_xref="InterPro:IPR014721" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/TrEMBL:A1K4L4" FT /protein_id="CAL93769.1" FT /translation="MTPSSVHDIRNLTLLGHAGCGKTTLLEALLAAAGVIGAPGSVERG FT DTVSDFDPQEKASGHSLNATLAHLEWSGHWINVLDTPGLPDLAGRALATLPAVETAAIV FT INAAAGIETGSRRMMAASEGKCRLIIVTKIDAAGANCGALMDAISAEFGRECLPLNLPA FT PASDGVVDCFFRPAPAATAFGDVASAHDGIVDQVVELDEALMARYLEQGQSLDPEQLHA FT PFEQALREGHLIPVCFVSARTGAGVRELLEVMGRLLPDPTEGNPPAFLKGEGADAQPVS FT VSPDPARHAVAHVFQVSNDPYRGKLALFRLHQGTVTPNSTLFIGNGRKPFKVSHLLRPQ FT GRNAVETPLAVPGDICALARVEELHRDAVLHDSHDEDHFHLVPPRYPQPVFGLALTATK FT PADEQKLAEALARLVDEDPCLEVSNDAHGRQTVVRGLGAQHLKVVLEQLAARWNLRPAT FT ATPAIPYRETIGAVGESRYRHKKQSGGAGQFGEVALRVEPLPRGSGLAFGDEVKGGAIP FT IQFMPAVEKGVRQALAEGALAGYPLQDLRVVVTDGKHHAVDSNEVSFITAARHALMEAV FT LAARPQVLEPLLRVSVKVADSHFGEVSAELAGRRGRVVGTDSPAGGWTLISAIVPMAEL FT EGFESRLKAISAGDSEFVLEAAGYDSAPGDTQNRLAQAHRSQGAAQ" FT CDS complement(1241063..1242703) FT /transl_table=11 FT /locus_tag="azo1153" FT /product="putative permeases of the major facilitator FT superfamily" FT /function="Permeases of the major facilitator superfamily" FT /note="Permease,member of the Major Facilitator FT Superfamiliy (MFS)transporters. MFS are single-polypeptide FT secondary carriers capable only of transporting small FT solutes in response to chemiosmotic ion gradients. 61%" FT /note="Function unclear" FT /db_xref="InterPro:IPR004324" FT /db_xref="UniProtKB/TrEMBL:A1K4L5" FT /protein_id="CAL93770.1" FT /translation="MLAALQQNAFYRWLDRNILELGREMRLAYLPPLMVYCAAGVSGLT FT GIVGTFFIKDYLGLSAAFLAALGFWAGIPWALKMPIGHLVDLLWRYKAGLVYLGALLIA FT ASIAIMIGLIGSPEAMRAVMPAEAWFVLSVLLSPVGYVMQDAVADAMTVEAVPHFDERG FT ERIGEDQVRLMHTTMQMLGRVAIIGGTVLVSFANVVMFQGAENLPESAKVEIYLHIYQL FT ALVIPLMSVSGVLLAGVLKRREARRLAALGREHAEIDRLLHEPAEKTAPNWWILGGSAV FT FVAFTLAIGLSGIEYGQEIIFAGSFAIIGFMITRLLRELSPEAARTLLGTVIVIFVFRA FT MPGPGAGASWWMIDELGFDQSFLSRLDLITSLLTLAGLFMFRRFMAEKSIAQIVIFLTL FT AATVLSLPIIGMYHGLHEWTARLTGGVVDARFIAIANTALESPLGQVSMVPMLAWIANS FT APPHLKATFFAVMASFTNLALSAAQLGTKYLNEIYVVSREVRDAATRAITTPADYSQLG FT VLLLVVTVVGFVVPLLAILLTRVAGLRSA" FT CDS complement(1243088..1243822) FT /transl_table=11 FT /locus_tag="azo1154" FT /product="conserved hypothetical membrane protein" FT /function="Putative effector of murein hydrolase" FT /note="Conserved hypothetical membrane protein. Homology to FT rsc2670 of R. solanacearum of 64% (tremble: Q8XWO5) Pfam: FT LrgB-like family The two products of the lrgAB operon are FT potential membrane proteins, and LrgA and LrgB are both FT thought to control of murein hydrolase activity and FT penicillin tolerance. no signal peptide 6 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007300" FT /db_xref="UniProtKB/TrEMBL:A1K4L6" FT /protein_id="CAL93771.1" FT /translation="MSPRLDEIWVYLSTTPLLGLTLTLLAYQGAFWLYKRCGFHPLANP FT VLISVVILAGILLATGMPYQRYFDGAQFVHFLLGPATVALAIPLYAQWPRLKAMALPLC FT IALVVGSLTAALSAYGLGALFGASRESLISLAPKSVTTPIAMGIAERLGGLPSLTAVLV FT ITTGILGAVGARYLYRLLRIHDPAVRGFAIGIASHGIGTARAFQVSEQTGAFAALAMGL FT NGLATAVSLPWILPWIERLFGE" FT CDS complement(1243819..1244181) FT /transl_table=11 FT /locus_tag="azo1155" FT /product="conserved hypothetical membrane protein" FT /function="Putative effector of murein hydrolase LrgA" FT /note="Conserved hypothetical membrane protein. This family FT is uncharacterised. It contains the protein LrgA that has FT been hypothesised to export murein hydrolases FT TREMBL:Q8XW06: 56% identity, 73% similarity FT InterPro:IPR005538; LrgA. Pfam: PF03788; LrgA; 1. ProDom: FT PD009239; LrgA Signal peptide present (Signal P predicted) FT TMH's 3 (TMHMM predicted)" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4L7" FT /db_xref="InterPro:IPR005538" FT /db_xref="UniProtKB/TrEMBL:A1K4L7" FT /protein_id="CAL93772.1" FT /translation="MLAALTLLLLFQLAGEVIARALALPIPGPVIGMALLFLALLVRGG FT PGDDLRSTAGTLLQHLSLLFVPAGTGVVLYGSRIADEWLPLGVALVGSTALAIAVTALV FT LQALLRRREPPAEDRR" FT CDS complement(1244251..1245189) FT /transl_table=11 FT /locus_tag="azo1156" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT Daro03002578 of Dechloromonas aromatica of 75% FT (gi|41723981|ref|ZP_00150871.1|(NBCI ENTREZ)). Has PF07670, FT Nucleoside recognition; This region in the nucleoside FT transporter proteins are responsible for determining FT nucleoside specificity in the human CNT1 and CNT2 proteins. FT In the FeoB proteins, which are believed to be Fe2+ FT transporters, it includes the membrane pore region, so the FT function of this region is likely to be more general than FT just nucleoside specificity. This family may represent the FT pore and gate, with a wide potential range of specificity. FT Hence its name 'Gate'. no signal peptide. 2 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K4L8" FT /protein_id="CAL93773.1" FT /translation="MDQLTDIILRAGRSAVELSLFVLLPIMVVMLSLMRMLEARGVIDW FT VVARLAPVLRPVGLTGLGVFAALQINFVSFAAPVATLTMMEGRGASDRHLAATLAMVMA FT MAQANVTFPMAAMGLAFGPALALSLLGGLIAAAATYHGFGRGLSALEGRLDETLHHQVA FT DNAKGVLDVINRAGAEAFKIAVGSIPMLVLALVAVMALRATGSIDALTAALTPLLAAIG FT IDPAMILLTLTKYIAGGTAMMGVMDEMLRNGVTTVATLNHGAGFLIHPLDVAGVAILMS FT AGRRVATVWKPAALGAAVGIAARTVGHALLR" FT CDS complement(1245583..1245789) FT /transl_table=11 FT /locus_tag="azo1157" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. Signal Peptide FT present. No good homolgous hits in the PDB. No TMHs No FT domains predicted." FT /db_xref="UniProtKB/TrEMBL:A1K4L9" FT /protein_id="CAL93774.1" FT /translation="MTRWNRITDFLAHGTLVLPLVLGLGMRSFDTFALTLAPMLLLLIG FT VTLGAPAVVVPTEEDEGSDGDRR" FT CDS 1246197..1247258 FT /transl_table=11 FT /gene="ncd2" FT /locus_tag="azo1158" FT /product="probable 2-nitropropane dioxygenase" FT /function="Dioxygenases related to 2-nitropropane FT dioxygenase" FT /EC_number="1.13.11.32" FT /note="TREMBL:Q9HWH9: 45% identity, 52% similarity FT 2-nitropropane dioxygenase (EC 1.13.11.32) (Nitroalkane FT oxidase) (2-NPD). CATALYZES THE OXYGENATIVE DENITRIFICATION FT OF VARIOUS ANIONIC NITROALKANES. InterPro: 2-nitropropane FT dioxygenase InterPro:IPR004136; 2nprop_dioxygen. IPR003009; FT FMN_enzyme. Pfam PF03060; NPD thiE: thiamine-phosphate FT pyrophosphoryl No transmembrane helices (TMHMM predicted)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4M0" FT /db_xref="InterPro:IPR004136" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:A1K4M0" FT /protein_id="CAL93775.1" FT /translation="MSATADFLNRVAVRHPIIQAPMVGVSTPALAAAVSNAGGLGSIGL FT GGGGVDEARAAIGATRALTSAPFNVNLFCHRPAVADPAREAAWLAELRPLFAEFGAQPP FT TVLREPYQSFIGQRAMLDMLLAERPAVVSFHFGLPSQEWIRELRASGSVTLASATTLAE FT AQAVEAAGIDIIVAQGVEAGGHRGMFEPEAGDALLGTVALLRLLAGKVKAPVVAAGGIM FT DGAGIAAALQLGAAAVQLGTAFVLAPESAANAAYRAAMKSAAAYRTRLTAAISGRAARG FT LPNRFDDLPGTAVLPDYPIAYDAAKALHAAASARGCSDFAPHWAGQGAPLAREMPAAQI FT VAELVREWQAVSR" FT CDS complement(1247367..1248971) FT /transl_table=11 FT /gene="aceB" FT /locus_tag="azo1159" FT /product="AceB protein" FT /function="Malate synthase" FT /EC_number="2.3.3.9" FT /note="Malate synthase. Homology to aceB of A. eutropus of FT 73% (trembl|Q8VM95). CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O FT + glyoxylate = S-malate + CoA. Acts in the glyoxylate FT bypass. Pfam: Malate synthase no TMHs 1 HTH" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4M1" FT /db_xref="InterPro:IPR001465" FT /db_xref="InterPro:IPR006252" FT /db_xref="InterPro:IPR011076" FT /db_xref="InterPro:IPR019830" FT /db_xref="UniProtKB/TrEMBL:A1K4M1" FT /protein_id="CAL93776.1" FT /translation="MTATLDLPQGMQINAPLHPRFDQILTRDALELVAKLHRAFEPRRQ FT ELLKARVARQARIDAGELPDFLPETKHIREGDWKVAPLPKALECRRVEITGPVERKMII FT NAFNSGADSYMTDFEDSNSPNWYNQIQGQVNLFDAIRREISYTNEAGKVYKLNDKIATL FT QIRPRGWHLDEKHVLVDGQRVSGGIFDFALVFFHNAKEQIARGAGPFYYLPKMESHLEA FT RLWNDIFVMAQDHIGLPQGTIKATVLVETILATFEMEEILYELRNHSAGLNAGRWDYIF FT SCIKKFKKNKDFCLANRGAITMEVPFMRSYALALVQACHKRGAPAMGGMSALIPIKSDP FT VANEKALAGIRHDKTRDANDGYDGGWVAHPGLVPIAMEEFVKVLGDKPNQWEKQVSGSF FT GPKDWMNFQPEQPITEVGVRNNINVGIHYLGSWLAGNGCVPIHNLMEDAATAEISRSQI FT WQWVVSPKGKLDDGRKVTADMVRAMIPEELAKVKATVTAQGENTATYDQAATIFEEMSL FT SENFPEFLTLPLYEAME" FT CDS complement(1248990..1249772) FT /transl_table=11 FT /locus_tag="azo1160" FT /product="conserved hypothetical membrane protein" FT /function="predicted permeases" FT /note="Conserved hypothetical membrane protein. Homology to FT mlr4286 of M. loti of 43% (trembl|Q98EE2) InterPro: FT IPR002781; DUF81.This domain is found in integral membrane FT proteins of prokaryotes which are uncharacterized FT Pfam:PF01925; DUF81 Signal peptide present and presence of FT 6 transmembrane helices" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4M2" FT /db_xref="InterPro:IPR002781" FT /db_xref="UniProtKB/TrEMBL:A1K4M2" FT /protein_id="CAL93777.1" FT /translation="MTSLALIDIVIIGIAALAAGAVNSIAGGGTFFSFPALLAVGVPPV FT VANASNSVSLWPGSLAGAWAFRRELARFSRSLPLLSAVAFVGGIAGGLLLLATSNAAFS FT KLIPWLLLVATVLFAFSAQISALVKKLKPAPAHADERHVGPAGYVFQLAVSVYGGFFGA FT GMGILMLAALAIQGFKDVHEINALKNWLSAVIYSVAVGTFVIANAVSWPHTIVMLLTGT FT AGGYLGAAFARRIPARLLRYCIIATGSVLTAYYFSKTL" FT CDS 1249955..1250920 FT /transl_table=11 FT /locus_tag="azo1161" FT /product="putative transcriptional regulator,LysR family" FT /function="Transcriptional regulator" FT /note="Transcriptional regulator, LysR family This protein FT activates the transcription of the lysA gene encoding FT diaminopimelate decarboxylase. LysR is also a negative FT regulator of its own expression. 29% 1 helixturnhelix FT PF03466 LysR_substrate; 1. HTH reporting nucleic acid FT binding motif" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4M3" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K4M3" FT /protein_id="CAL93778.1" FT /translation="MDQLKQIETFVAVASRGSLSAAARAEGVTPAVIGRRLDGLEARLG FT VRLLVRTTRSITLTFEGSAFLEDCQRILNDLSNAEASVSLGGVKPSGHLRVSAPAGFGR FT RHVAPLVREFLLANPDVSCSLDLSDRLVDLVNEGLDCAVRIGDMADSSLVSVKLADNRR FT VVVASPDYLARHGVPRTPEDLPRHVCLTLVQQRGWQFADGRGGAVSAKVAGRLECNDGA FT VLHEWALAGQGLAWRSLWEVSEDLAAGRLVSVLDEFAARPTGIYAVFPYRRNLALRVRY FT FIDYLKQRYGDTGYWNSAAGEPLTPPTPPESHSRSSASAR" FT CDS complement(1250865..1252127) FT /transl_table=11 FT /gene="ttuD" FT /locus_tag="azo1162" FT /product="probable hydroxypyruvate reductase" FT /function="hydroxypyruvate reductase" FT /EC_number="1.1.1.81" FT /note="Putative hydroxypyruvate reductase. Degrades an FT unidentified toxic product from the first step of tartrate FT degradation. Involved in the second step of the tartrate FT degradation pathway. 59% MOFRL.IPR005346; UPF0125. FT Pfam:PF05161; MOFRL; 1.PF03658; UPF0125; 1. Signal peptide FT present." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4M4" FT /db_xref="InterPro:IPR007835" FT /db_xref="UniProtKB/TrEMBL:A1K4M4" FT /protein_id="CAL93779.1" FT /translation="MTTPPRELLAQMFAAAVNAAQPEHCIPPHLPAPPRGRTVVIGAGK FT ASAAMAQALERHWAGPLSGVVVTRYGYAVPCERIEIVEAAHPVPDAAGHGAAARVLTLV FT DGLSADDLVICLISGGGSALLPLPGAGVTLADKQAINRALLKSGATISEMNCVRRHLSA FT IKGGRLAAACHPARVVNLLISDVPGDNPIDIASGPTVADPTTCADALEIVRRHGIELPA FT GARALLESGAGETVKPGDPRLAGVSTHLVATPQQALEAAARVAEAAGVRALILGDSIEG FT EARDVGKVIAAIALQVKRHGQPVAAPCVLLSGGETTVTVRGQGRGGRNVEFLLALAIAL FT DGAPDIHAVAGDTDGVDGLEDIAGAFVTPDTLARAWAAGLRPRDRLDDNDGHGFFEALG FT DSLVTGPTLTNVNDFRAVWVG" FT CDS complement(1252153..1252941) FT /transl_table=11 FT /gene="gip" FT /locus_tag="azo1163" FT /product="putative hydroxypyruvate isomerase" FT /function="Hydroxypyruvate isomerase" FT /EC_number="5.3.1.22" FT /note="Hydroxypyruvate isomerase (EC 5.3.1.22).Catalyzes FT the reversible isomerization between hydroxypyruvate and FT 2-hydroxy-3-oxopropanoate (also termed tartronate FT semialdehyde).Belongs to the hyi family. 52%" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4M5" FT /db_xref="InterPro:IPR012307" FT /db_xref="InterPro:IPR013022" FT /db_xref="InterPro:IPR017643" FT /db_xref="UniProtKB/TrEMBL:A1K4M5" FT /protein_id="CAL93780.1" FT /translation="MPKLAANLTLLFTELDFLDRFQAAAAAGFKAVEFQFPYAWPAARI FT AERLDAAGLPVVLHNLPAGDWAAGERGIACHPDRVGEFRDGVGRAIDYAVVLGCKQLNC FT LAGIVPAGVTAQAAHETFIANLRFAADALKSAGIRLLVEPINTFDIPGFYLSRTAQAAA FT ILDEVGADNLHIQYDIYHAQRMEGDLANTIARHLPRIAHMQIADNPGRHEPGTGEINYG FT WLFRHIDRLGYDGWIGCEYLPAAGTREGLGWMTALAAMAQ" FT CDS 1253717..1254214 FT /transl_table=11 FT /locus_tag="azo1164" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ORF153 FT of Rubrivivax gelatinosus of 48% FT (gi|55832787|gb|AAV66902.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K4M6" FT /protein_id="CAL93781.1" FT /translation="MRVGVSAPDLYASQTSRAASQAGSRSGSTPFAAILDAMTTQAAAA FT PQTSRTSTAAPTDSGTAKEATQLDFTSMTRQELFDWMNSQLRAGKMTLDESTCFLGMTL FT KISAATGQQVDMATDTTRENFLERARLGIEGALWRHDQDLARRLGETVDIMLRRQGEAA FT GV" FT CDS complement(1254523..1256169) FT /transl_table=11 FT /gene="lctP" FT /locus_tag="azo1165" FT /product="LctP protein" FT /function="L-lactate permease" FT /note="L-lactate permease. Homology to lctP of E. coli of FT 72% (sprot|LLDP_ECOLI) Transports L-lactate across the FT membrane. Can also transport D-lactate and glycolate. Seems FT to be driven by a proton motive force (By similarity). FT Tigrfam: lctP: L-lactate transport Pfam: L-lactate permease FT signal peptide 12 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4M7" FT /db_xref="InterPro:IPR003804" FT /db_xref="UniProtKB/TrEMBL:A1K4M7" FT /protein_id="CAL93782.1" FT /translation="MQPWMQIYDPLGNLWLSALVAALPIIFFFVALAVLRMKGHVAGTI FT TVAIALAVAILFYQMPVPMALAAAGYGFLYGLWPIAWIIIAAVFLYKITVKTGQFDIIR FT ASVVSITDDQRLQMLLVGFSFGAFLEGAAGFGAPVAITAALLVGLGFNPLYAAGLCLIA FT NTAPVAFGAMGIPIIVGGQVTGIDPFKIGQMAGRQLPLLSMIVPFWLVAMMDGWRGIKE FT TWPAVIVAGGSFAVTQFFTANYIGPELPDITSALVSLICLTIFLKNWKPKNIFRFDQQH FT HAELGEDRHYSFGQIAKAWSPFVILTAIVTVWSLKPFKALFASGGALYSTVFQFPVPML FT DKLVIKMEPIVAQATPYAAVYKLDILSATGTAIFISALVSMVVLGMRGGEAAKALKETV FT VELKRPIYSIGMVLAFAFVANYSGLSATLALLLAGTGALFPFFSPFLGWLGVFLTGSDT FT SSNALFCSLQATTAHQVGVSDTLLVAANTTGGVTGKMISPQSIAVACAAVGLVGKESDL FT FRFTVKHSLMFAAMVGVITTLQAYVFTWMIP" FT CDS complement(1256528..1259305) FT /transl_table=11 FT /locus_tag="azo1166" FT /product="conserved hypothetical iron-sulfur bindinding FT oxidase" FT /function="FAD/FMN-containing dehydrogenases" FT /note="Conserved hypothetical iron-sulfur binding oxidase. FT Homology to pa4772 of P. aeruginosa of 53% (pir|H83050) FT InterPro: FAD linked oxidase C-terminal (IPR004413) Pfam: FT FAD binding domain ; Fad linked oxidase, C-terminal domain FT Tigrfam: glcD: glycolate oxidase subunit GlcD no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4M8" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR004113" FT /db_xref="InterPro:IPR006094" FT /db_xref="InterPro:IPR009051" FT /db_xref="InterPro:IPR012285" FT /db_xref="InterPro:IPR016164" FT /db_xref="InterPro:IPR016166" FT /db_xref="InterPro:IPR016167" FT /db_xref="InterPro:IPR016168" FT /db_xref="InterPro:IPR016171" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K4M8" FT /protein_id="CAL93783.1" FT /translation="MSALIDALRLRLPAERVITDELRRLAYGTDGSFYRLIPEVVAVVQ FT DEDEVREVTRIARAHQRSVTFRAAGTSLCGQAVTDGVLVLLGEGLATCRIGDGGNTVEV FT GPAIVGAEVNRRLAPLGRKIGPDPASINAAKIGGIAANNSSGMCCGTAQNSYNTLASLR FT VMLADGTVLDTGDAASVAAFRHSHGELLDRLNALAHGVRADAALAGRIRSKYKIKNTTG FT YSLNALVDYHDPVDILAHLMIGSEGTLGFISRVTYNTVPEHAHKASALAFFEDMESACR FT AVVGLKARPVAAVELLDRASLRCVAHKPGMPPLLKTLSEGATALLIETRAPSAAELRQQ FT TDSILEELQAYTLIEAPAFTTDPAEIERLWNVRKGTFPAVGAVRKPGTTVIIEDVAVAV FT PDLAACCLDLQHLFAKHGYHEAIIFGHALEGNVHFVFTQDFGIDTEVARYAAFMDELCA FT TLVKKYDASLKAEHGTGRNMAPFVELEWGAQAYGLMKEIKQLFDPEGLLNPGVIINDDA FT EAHLKHLKPMPAAGQLYAAVDRCIECGFCEPQCPSHGLTLSPRQRIVGWRELSRREAAG FT EAPGQLGEDYLYMGLDTCAACGLCATACPVGIETGALTRAVRGEKLSGVARSLGRVAAN FT HFGATQALARTALKAGHFAEAIVGSRALNRLSGGAWKEGMPHPQPLRYQVSRSAGDPIV FT YFPTCAGRMFGADSAEQALSATVIRVLERAGYRPIVPDGVNSLCCGQSFASKGLAAEAD FT AKSAEVEAALMKASNYGEYPIVLDASACTLRMKTFLAERLKVFDLVEFAHDALLPRLML FT QKKADPVLVHLNCSARRMGFEAKLKQLAAACAEQVVMPPEVKCCGFGGDRGFAVPELNA FT HALRKLEVPSGCCGGYSSNQTCEIGLTHASGVPYRSIVHLLDECSAEAARMASC" FT CDS complement(1259517..1260968) FT /transl_table=11 FT /locus_tag="azo1167" FT /product="conserved hypothetical iron-sulfur protein" FT /function="uncharacterized conserved protein containing a FT ferredoxin-like domain" FT /note="Conserved hypothetical iron-sulfur protein. Homology FT to cv3028 of C. violaceum of 68% (trembl|Q7NTM6) Tigrfam: FT TIGR00273: iron-sulfur cluster binding protein Pfam: 4Fe-4S FT binding domain no TMHs no signal peptide" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4M9" FT /db_xref="InterPro:IPR003741" FT /db_xref="InterPro:IPR004452" FT /db_xref="InterPro:IPR012285" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="InterPro:IPR024185" FT /db_xref="InterPro:IPR024569" FT /db_xref="UniProtKB/TrEMBL:A1K4M9" FT /protein_id="CAL93784.1" FT /translation="MSGQTHTTSGQPIAIVSAQALRERMHAAVNDPHLRQSFRGAMDFL FT MAKRLAQFPDESELVSLRSLSEAIRQYSLSKLPDLLEQLEANLTRNGVKVHWAETPEEA FT NAIMLGIAQAHQARLIVKGKSMVSEEIEFNHAMEAAGVGALESDMGEYIVQLAGEKPSH FT IIMPAIHQTKQQIAKLFAEKIPGVDYTDNVDALIQIGRRVLREKFEVADIGLSGVNFAV FT AETGTLCLVENEGNGRMCTTVPKVHIAITGIEKVVEKLEHVAPLYSILTRSATGQAVST FT YFNMISGPRRGEDKDGPEEVHLVLLDNGRSQAYADEQLRKTLQCIRCGACMNHCPVYTR FT IGGHAYGTTYPGPIGKIVSPHMTGLEQTHLLPTASSLCGACGEVCPVKIPIPELLIRLR FT GEANSAPHAHPAMVGQGAAYDPKISLLWRMWARVYGHPAAYRAFSWLATRFRALTPRKQ FT GGWTVARTPLQPAPRRLRDMLKERP" FT CDS complement(1260965..1261639) FT /transl_table=11 FT /locus_tag="azo1168" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to DVU1781 FT of D.vulgaris of 45% (tremble:Q72B57). Has PF02589 DUF162 FT domain:Uncharacterized ACR, YkgG family. No signal peptide FT or TMH reported present." FT /db_xref="InterPro:IPR003741" FT /db_xref="InterPro:IPR024185" FT /db_xref="UniProtKB/TrEMBL:A1K4N0" FT /protein_id="CAL93785.1" FT /translation="MSARDRILAKLRAAQPAQPNALPDPAEHYATRARNESKADRLARF FT RTGIEGFHAEVHLSTATDWPDLLASLCAQKQVGTLMYGADTPAGARLHATGFGATALRP FT WQGEFEQLKADLFHTVDAGFTQTRGAIAETGSLIVWASAAEPRTLSLVPPIHFALLDAN FT HIHPTFFDALRAENWAAGLPTNALLISGPSKTADIQQTLAYGAHGPKELVVIVINAEGD FT AQ" FT CDS complement(1261636..1262442) FT /transl_table=11 FT /locus_tag="azo1169" FT /product="conserved hypothetical protein" FT /function="Fe-S oxidoreductases" FT /note="Conserved hypothetical protein. Homologyt to nma1648 FT of N. meiningitidis of 55% (trembl|Q825P5) InterPro: Domain FT of unknown function DUF224 (IPR004017) Pfam: Domain of FT unknown function no signal no TMHS" FT /db_xref="InterPro:IPR004017" FT /db_xref="UniProtKB/TrEMBL:A1K4N1" FT /protein_id="CAL93786.1" FT /translation="MSHPAAGAPARTYPPRPQAVYFYGTCLVDMFVPEAGMDAIALLER FT EGIRVIFPENQTCCGQPAFTSGFPGEARQVVASQLDLFPGDYPIVVPSGSCGGMLRWHW FT EKAVGDDPALKAKAAAISERTYEFAEFLLHVVGFNRQDQGPATTVTLHTSCSARREMGT FT HLVGRELLARLGNVTLAHHDHESECCGFGGTFSLKHPDVSTAMVSDKVASLKATGAAQM FT VTADCGCMLNITGRAAKEDQDAGRAKPSLPGEHLATFLLRRTGGKA" FT CDS 1262710..1263492 FT /transl_table=11 FT /gene="lldR" FT /locus_tag="azo1170" FT /product="probable L-lactate dehydrogenase operon FT regulatory protein" FT /function="Transcriptional regulators" FT /note="Putative L-lactate dehydrogenase operon regulatory FT protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4N2" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K4N2" FT /protein_id="CAL93787.1" FT /translation="MATGKLVVQRLSDTIAHELERRILDGVLKPGDRLQPERELAAELG FT VSRPSLREAIQKLVSKGLLHSRQGGGTYVTDQLEAGFTDPWHEMLRQHPNIQDDLLEFR FT GMLEKEAAILAAQRATAADLQRIGEAYARVDALFDQGTSPAVLEQQVKADLAFHQTIAE FT AAHNVMIGHLTASLLKVINDHIDRNLRHLRRSEDDWAHLREQHRAVWEAIRDADPVAAA FT RAVQGHIEFVHESMKARARQEERENRARARQSGAEAEG" FT CDS 1264770..1265240 FT /transl_table=11 FT /locus_tag="azo1171" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No homology to the FT data bank. No domains predicted. signal peptide. no TMH" FT /db_xref="UniProtKB/TrEMBL:A1K4N3" FT /protein_id="CAL93788.1" FT /translation="MTMAINPKQLGVSFMRTVLLVFLVGCATVRTDVVGGGDLNNYKRA FT YVEALTEDEFQIYGALFSELTDMGIQVVAAPFKEPEGTDLLVKYTYEGGWDMTRYLQSF FT QFQFVDAKTGRVVAIQSYKSHGLWRGVRDGRLKTAFNELRAKNGYPPSKQFP" FT CDS 1265498..1265653 FT /transl_table=11 FT /locus_tag="azo1172" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to the FT N-terminus of NE0717 of Nitrosomonas europaea of 56% FT (tremble:Q82WG3). Pfam: Cold shock protein domain FT RNA-binding domain that functions as a RNA-chaperone in FT bacteria and is involved in regulating translation in FT eukaryotes. Contains sub-family of RNA-binding domains in FT the Rho transcription termination factor. No signal FT peptide. No TMHs" FT /db_xref="GOA:A1K4N4" FT /db_xref="InterPro:IPR002059" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="UniProtKB/TrEMBL:A1K4N4" FT /protein_id="CAL93789.1" FT /translation="MRHQGHISSWKDDKGFGFITPAAGGEKVFVHISAFANRRGRPEVD FT DRVPTS" FT CDS 1265650..1266129 FT /transl_table=11 FT /locus_tag="azo1173" FT /product="conserved hypothetical membrane protein" FT /function="unknown" FT /note="Conserved hypothetical membrane protein. Homology to FT the C-terminus of ne0717 of N. europaea of 57% FT (trembl|Q82WG3). Pfam: Protein of unknown function FT (DUF1294). No signal peptide. 3 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR010718" FT /db_xref="UniProtKB/TrEMBL:A1K4N5" FT /protein_id="CAL93790.1" FT /translation="MRADAQGRAQAGEVAFLDRRRTSSFRPRRLLPLLVAASFLGVLAY FT AVNSGRVPALVLVVYLGASVVAFVAYALDKWAAVKGRWRTQESTLHFFALVGGWPGALA FT AQGLLRHKSSKVSFQVTFWVTVIVNCGALGWLLSASGAVALRSALRLFRTAVGAF" FT CDS 1266287..1266538 FT /transl_table=11 FT /locus_tag="azo1174" FT /product="hypothetical protein" FT /note="Hypothetical protein. No homology to the data bank. FT No domains predicted. No signal peptide. No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K4N6" FT /protein_id="CAL93791.1" FT /translation="MHCCGASSPRRKCPHPPKTLGFRAIHRLVRNLLYLPRPLAKTLAG FT KPPPTTVGSGRCDSYRCSPAIRTYIEPRSAEAFMHVRG" FT CDS 1266596..1269127 FT /transl_table=11 FT /gene="nirB" FT /locus_tag="azo1175" FT /product="nitrite reductase (NAD(P)H) large FT subunit,probable." FT /function="NAD(P)H-nitrite reductase" FT /EC_number="1.7.1.4" FT /note="Nitrite reductase [NAD(P)H] large subunit (EC FT 1.7.1.4). 76% EGF_like.IPR001327; FAD_pyr_redox. FT IPR007419;Fer2_BFD.IPR006066; Nir_Si.IPR006067; FT Nir_Sir_4Fe4S. IPR005117; NiR_SiR_beta_fer. IPR001100; FT Pyr_redox. Pfam: PF04324; Fer2_BFD; 1.PF01077; NIR_SIR; FT 1.PF03460; NIR_SIR_ferr; 1. PF00070; Pyr_redox; 1. In FT E.coli, the NADH-dependent nitrite reductase catalyzes the FT six-electron reduction of nitrite to ammonia and also FT catalyzes the two-electron reduction of hydroxylamine to FT ammonia. The enzyme is a FAD-flavoprotein, and also FT contains a siroheme and one 2Fe-2S center." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4N7" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR005117" FT /db_xref="InterPro:IPR006066" FT /db_xref="InterPro:IPR006067" FT /db_xref="InterPro:IPR007419" FT /db_xref="InterPro:IPR012744" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR017121" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K4N7" FT /protein_id="CAL93792.1" FT /translation="MKIVLVGHGMVGHKFLEELQQLQIPGAEVTVLCEEPRTAYDRVHL FT SEFFSGKTAEDLSLVAPGFFDDTGFALRLNSRAAAIDRRAKTVTTQDGVTLSYDKLVLA FT TGSYPFVPPVKGNDREQCFVYRTIEDLEAMKAAGAISRKGVVVGGGLLGLECAKALRDL FT GLETHVVEFAPRLMAVQVDDDGGRILREKIEQLGVQVHTSRNTTEITDGMTARHRMVFA FT DGSHLETDMIVFSAGIRPRDELARQNALAVGARGGIAVDDHCRTSDPDIYAIGECAAWR FT DQTFGLVAPGYDMARLVARHLAGETKAAFAGADMSTKLKLMGVDVASIGDAHGKTAGCR FT SFRYSDEVKQVYKKIVVSEDGKRLLGAVLVGNADEYGTLLQMALNGIAPPAEPEFLILP FT SSDGKAKPGLGPDALPDSAQICSCNNVSKGQICAAVGEGATSIGEIKSCTKAGATCGGC FT VPLVTQIMKAEMAKRGMAVNNHLCEHFPYSRQELFHLVRVGGIKSFEDLLARHGQGHGC FT DICKPTAASIFASCWNDFVLQGELASLQDSNDYFLGNIQKDGTYSVVPRMPGGEVTPDG FT LIAVGQVAKKYGLYTKVTGGQRVDLFGARVEQLPAIWEELIAAGFESGHAYGKALRTVK FT SCVGSTWCRYGVDDSVGLAVELENRYKGLRAPHKIKFGVSGCTRECAEAQGKDVGIIAT FT ERGWNLYVCGNGGMKPRHAELIASDLDRAALIRLIDRFLMFYVRTADRLQRTSTWRENL FT EGGLDYLKDVLIADSLGLAAELEAQMQHVVDTYQCEWKTAVTDPDVRKRFRTFVNDPQA FT DKRIVFVKERGQIRPARAEERDAATADPLAV" FT CDS 1269149..1269487 FT /transl_table=11 FT /gene="nirD" FT /locus_tag="azo1176" FT /product="nitrite reductase small subunit, probable." FT /function="Ferredoxin subunits of nitrite reductase and FT ring-hydroxylating dioxygenases" FT /note="Nitrite reductase [NAD(P)H] small subunit (EC FT 1.7.1.4). REQUIRED FOR ACTIVITY OF THE REDUCTASE. 66% FT simialr to the nirD protein from R. solanacearum,a probable FT nitrite reductase NADPH (small subunit) oxidoreductase FT protein [EC:1.7.1.4]. TREMBL:Q8XQK3. InterPro: Rieske FT iron-sulfur protein 2Fe-2S subunit In E.coli, the FT NADH-dependent nitrite reductase catalyzes the six-electron FT reduction of nitrite to ammonia and also catalyzes the FT two-electron reduction of hydroxylamine to ammonia. The FT enzyme is a FAD-flavoprotein, and also contains a siroheme FT and one 2Fe-2S center." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4N8" FT /db_xref="InterPro:IPR012748" FT /db_xref="InterPro:IPR017881" FT /db_xref="InterPro:IPR017941" FT /db_xref="UniProtKB/TrEMBL:A1K4N8" FT /protein_id="CAL93793.1" FT /translation="MTTETLNWTAVCKVGDILPGTGVCALVDERHVAVFRLGKDNFYAI FT DNIDPRSGVSVLSRGLIGNLGEHIVVASPIYKNHFDLRTGACLEAPEHSVRAHRVQISG FT DDVLVALG" FT CDS 1269519..1270331 FT /transl_table=11 FT /gene="nirC" FT /locus_tag="azo1177" FT /product="putative nitrite transporter" FT /function="Formate/nitrite family of transporters" FT /note="76% For/Nit_transpt. Pfam: PF01226; Form_Nir_trans; FT 1. In E. coli, NirC is a putative nitrite transporter which FT is a member of the FNT family of formate and nitrite FT transporters. The nirC gene is located in the nir operon FT which codes for a NADH-dependent nitrite reductase. NirC FT may function to import nitrite as a substrate for this FT enzyme complex. The nir operon is anaerobically expressed FT and is repressed by oxygen. TMhelix:6" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4N9" FT /db_xref="InterPro:IPR000292" FT /db_xref="UniProtKB/TrEMBL:A1K4N9" FT /protein_id="CAL93794.1" FT /translation="MAYLAPAEFVTKMIDAGESKLLMSTRDTLIRAYMAGAILALAAAF FT AVSITVNTGNPLIGALLFPVGFCMLYLLGFDLLTGVFTLAPLAVLDRRPGATWSGVMRN FT WSLVFTGNFAGALTVAVFMAIIFTNGFSEAPNAIGQKIGHIGEGRTVGYAAHGAAGMLT FT LFVRAVMCNWMVSTGVVAAMMSTSVSGKVIAMWMPILVFFYMGFEHSIVNMYLFPSGLM FT LGGQFTFMDYLIWNEIPTVLGNLVGGLTFVGATLYSTHYKTAPKRKVA" FT CDS 1270372..1272093 FT /transl_table=11 FT /locus_tag="azo1178" FT /product="putative serine/threonine protein kinase" FT /function="Serine/threonine protein kinase" FT /note="Putative serin/threonin protein kinase," FT /note="Family membership" FT /db_xref="GOA:A1K4P0" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR001932" FT /db_xref="InterPro:IPR008266" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:A1K4P0" FT /protein_id="CAL93795.1" FT /translation="MSVGQHSLAGAHDTNQDFHGAVLPGGHLLAAKGIALALADGISSS FT SVSHLASQTAVGSFLEDYYATSEAWTVRRAAQRVLGATNAWLHGQTQRGEGRFDKDRGY FT VCTFSALVLKGRDLHLLHVGDSRIYRLHPQSLEQLTEDHRVRHSSVESYLARALGTGPH FT VEIDYRSWEAEAGEIYVLATDGAYAQLDAAAIHRAIAHHADDLDAAAAALVAQARAAGS FT DDDATLQLLRIDELPQDDAPQAQLRREGLALPPALTPRSEFEGFTIVRELQVSARSHVL FT LATDKDSGRPVVLKAPSVDLRGDAAYLDSFVLEEWVARRVDSPHVIKAWPGERRRRHLY FT VAMEYIEGQTLAQWMTDHPAPPLEAVRAIVEQLAQGVQALHGRDMLHRDLRPENVMIDR FT DGTVKLIDLANVHVAGLAEGRGGAEQGAPPGTLQYMAPECLLGQPASTAADLFSLAAIT FT YQMLCGQLPYGLSVTRVRTQQDLRNLRYVPLRHHRPDLPAWLDGVLAKALQVAPAKRQE FT AVSEFVHDLRTPGARFQRAQRTPLVERDPVLFWKCLSAVLGALVVGLLFYIRWRLA" FT CDS complement(1272191..1272715) FT /transl_table=11 FT /gene="allA" FT /locus_tag="azo1179" FT /product="ureidoglycolate hydrolase" FT /EC_number="3.5.3.19" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4P1" FT /db_xref="InterPro:IPR007247" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR023525" FT /db_xref="InterPro:IPR024060" FT /db_xref="UniProtKB/TrEMBL:A1K4P1" FT /protein_id="CAL93796.1" FT /translation="MPPRPAMSDTARALAVEPLSRAAFAPFGDVIEASDAVRHFTINAG FT NTERYHDLAQVEPGPEGRAILSIFRGQPRALPFAVTMMERHPLASQAFIPMSGKPYLVV FT VAPAGAAPAVADLRVFLARGDQGVNYAPGVWHHPLLALDTVCDFLVVDRAGPGHNCDEV FT AVAPPGLILSV" FT CDS complement(1272715..1273755) FT /transl_table=11 FT /gene="alc" FT /locus_tag="azo1180" FT /product="Allantoicase" FT /EC_number="3.5.3.4" FT /note="Allantoicase (Allantoate amidinohydrolase)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4P2" FT /db_xref="InterPro:IPR005164" FT /db_xref="InterPro:IPR008979" FT /db_xref="InterPro:IPR015908" FT /db_xref="UniProtKB/TrEMBL:A1K4P2" FT /protein_id="CAL93797.1" FT /translation="MASIPGTPVFAPPADLPEWARRSVDLASVRLGAKALYASDDFFAP FT VERMLDPAPAQFVPGKYDANGKWMDGWESRRKRVAGHDWALVKLGVRGVIRGFDVDTSH FT FTGNYPPAVSIEACVSVSDDVEALKAAAWTEILPATPLGPNSHHLLECASTAAWTHLRV FT NIYPDGGIARLRVYGRPLGALANVPADATVDLVAMENGGRAVSWNDASFGSSASALLLP FT GRGLDMGDGWETRRRREPGNDWCVLELGTPGIIERVEVDTAFYKGNYPDRCSLQAAFVS FT GGTDRSITTQSMFWATLLPEHKLEMDAVHSFTALAPLGPVTHVRFNIFPDGGVSRLRLW FT GKVAPR" FT CDS complement(1274116..1275063) FT /transl_table=11 FT /locus_tag="azo1181" FT /product="conserved hypothetical deacetylase protein" FT /function="predicted xylanase/chitin deacetylase" FT /EC_number="3.5.1.-" FT /note="Polysaccharide deacetylase family protein.This FT family of polysaccharide deacetylases includes FT NodB(nodulation protein B from Rhizobium) which is a FT chitooligosaccharide deacetylase.It also includes chitin FT deacetylase from yeast,and endoxylanases which hydrolyses FT glucosidic bonds in xylan. 62% Polysac_deacet. FT Pfam:PF01522; Polysacc_deac_1. TIGR:PP4286." FT /note="Function unclear" FT /db_xref="GOA:A1K4P3" FT /db_xref="InterPro:IPR002509" FT /db_xref="InterPro:IPR011330" FT /db_xref="InterPro:IPR017625" FT /db_xref="UniProtKB/TrEMBL:A1K4P3" FT /protein_id="CAL93798.1" FT /translation="MTAPSAPSTPYPRDLIGYGRTPPHANWPGRARIAVQFVLNYEEGG FT ENSVLHGDPGSEQFLSELFNPASYPDRHLSMEGIYEYGSRVGVWRFLREFERRGLPLTV FT FGVAMALERHPELTAAFRELGHEIACHGWRWIHYQDTPEEIEREHMRIGMEIIERLTGE FT RALGWYTGRDSPNTRRLVADYGGFLYDSDYYGDDLPFWTEVQKTDGTTVPHLIVPYTLD FT TNDMRFALPQGFSHGDPFFQYLRDAFDVLYAEGDERPAMLSIGMHCRLLGRPGRFRALQ FT RFLDHVEKHDRVWVCRRVDIARHWIEEHPYGRKA" FT CDS complement(1275084..1275611) FT /transl_table=11 FT /locus_tag="azo1182" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to RS01483 FT of R.solanacearum of 55% (tremble:Q8XXJ2). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="GOA:A1K4P4" FT /db_xref="InterPro:IPR017580" FT /db_xref="InterPro:IPR018020" FT /db_xref="UniProtKB/TrEMBL:A1K4P4" FT /protein_id="CAL93799.1" FT /translation="MSTLPTPGTTVAALSALPRADFVAALGGIFEHSPWVAERAWAARP FT FATADALHAAMVAAVDGAARGEQLALIRAHPELAGKEAAAGTLTAASTGEQRGAGLDQC FT SAAELQRLRELNAAYRARFGFPFVIAVKGLGREQIIAALAQRLTHDSDAEFRTCLAEIG FT KIARFRLDALLA" FT CDS complement(1275648..1276844) FT /transl_table=11 FT /locus_tag="azo1183" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT RS01489 of Ralstonia solanacearum of 50% FT (trembl|Q8XXJ8(SRS)) Has PF06181:Protein of unknown FT function (DUF989);This family consists of several FT hypothetical bacterial proteins of unknown function. no FT signal peptide 8 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4P5" FT /db_xref="InterPro:IPR003088" FT /db_xref="InterPro:IPR009056" FT /db_xref="InterPro:IPR010389" FT /db_xref="UniProtKB/TrEMBL:A1K4P5" FT /protein_id="CAL93800.1" FT /translation="MIETYLLDWANLLLRWLHLITGIAWIGASFYFVMLDTSLKPPKKA FT EDARRGVFGELWAVHGGGFYCSQKFLTGPKGEPLSNDLHWSKWEAYTTWMSGFALLVVI FT YWIGASSYLIDSQVLALTPAAAIGISIAVLVAGWVVYDLLCRTLIGRDRLLAALVFVFV FT MAMNWALHQVFSARGAYIHVGAMLGTMMVANVFFHIIPGQKRMVEQIRAGQDVDGRPGI FT VGKQRSVHNTYFTLPVLFIMISNHYPMTYASKHGWLVLAVLMVAGVLIRQFFVLRHRGQ FT LKWWLPASGAALIAALVVAMAPRPADAGAAAVSFAAVKAVIDSRCVACHAAQPSWEGFA FT QPPKGVTLQSAEQIGQHAAKIAETVSNGYMPLGNLTHITADERALIATWAAQGARLAD" FT CDS complement(1276863..1277213) FT /transl_table=11 FT /locus_tag="azo1184" FT /product="conserved hypothetical transthyretin" FT /function="Transthyretin-like protein" FT /note="Conserved hypothetical transthyretin. Homology to FT pa1518 of P. aeruniosa of 62% (sprot|YF18_PSEAE) InterPro: FT Transthyretin precursor (IPR000895) Pfam: Transthyretin FT precursor no signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4P6" FT /db_xref="InterPro:IPR000895" FT /db_xref="InterPro:IPR014306" FT /db_xref="InterPro:IPR023416" FT /db_xref="InterPro:IPR023418" FT /db_xref="InterPro:IPR023419" FT /db_xref="UniProtKB/TrEMBL:A1K4P6" FT /protein_id="CAL93801.1" FT /translation="MGRLTTHVLDTATGRPGAGIAVRVFRLDGERREVARAVTNHDGRC FT DAPLLNGTAFEAGRYEIVFAAGNYFRASGQVLPEPPFVDEVVLRFGIASPEQHYHVPLL FT VSPWSYSTYRGS" FT CDS complement(1277327..1278304) FT /transl_table=11 FT /gene="pip" FT /locus_tag="azo1185" FT /product="probable proline iminopeptidase" FT /function="predicted hydrolases or acyltransferases FT (alpha/beta hydrolase superfamily)" FT /EC_number="3.4.11.5" FT /note="TREMBL:Q8PC98: 42% identity, 54% similarity. Proline FT iminopeptidase (EC 3.4.11.5) (Prolyl aminopeptidase) (PAP). FT SPECIFICALLY CATALYZES THE REMOVAL OF N-TERMINAL PROLINE FT RESIDUES FROM PEPTIDES (BY SIMILARITY). InterPro:IPR000073; FT A/b_hydrolase. IPR003089; AB_hydrolase. IPR002410; FT Peptidase_S33. IPR005944; Pept_S33. IPR000379; Ser_estrs. FT Pfam PF00561; Abhydrolase_1; TIGRFAMs: TIGR01249; FT pro_imino_pep_1 TIGR00149: conserved hypothetical protein" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4P7" FT /db_xref="InterPro:IPR002410" FT /db_xref="InterPro:IPR005944" FT /db_xref="UniProtKB/TrEMBL:A1K4P7" FT /protein_id="CAL93802.1" FT /translation="MGDSMSLMATQPSSPPPPCRDGLLDVGDSHTLWFEQCGNPAGIPL FT LFLHGGPGSGCSPRHRDLFDLTRFRVILFDQRGCGRSTPRGGLDANTTAHLVADIERLR FT AHLGIARWLVSGGSWGSTLALAYCARYPAACLGAVLRGIFLARREDIDWFFEGAAPRLP FT EAHAAFAACAPGPGRLATRVFDAVLGADDARALQVVRHWMQWEESLTLGRAAPLPVLGD FT DDAARMLDKYRVQAHYLRHDCFLGHDGWRGLAQQIAAAGLPVTVLHGQDDRICQPAAAQ FT LLRATIPHSRLTMVAAGHDPFAPAMRRALLAACADPLPPLPGPK" FT CDS 1278781..1279233 FT /transl_table=11 FT /locus_tag="azo1186" FT /product="hypothetical protein" FT /function="unknown" FT /db_xref="UniProtKB/TrEMBL:A1K4P8" FT /inference="nucleotide motif:Gismo" FT /protein_id="CAL93803.1" FT /translation="MTRNLLRRMTVVIAASIGAAGCTHIDVTKMDARKHPLSLVCIEEN FT PNASATDIVSVIEDGFQRRGILTAVYSGNAPSECEYSVWYLDEWGWDLAPYMRRAEIRL FT RRKAVTVARATYVHSGGLALNKWAGTKSKLEPVIDQLLAGYEPVLK" FT CDS 1279714..1280628 FT /transl_table=11 FT /gene="pqqB" FT /locus_tag="azo1187" FT /product="probable coenzyme PQQ synthesis protein B" FT /function="Metal-dependent hydrolases of the beta-lactamase FT superfamily I" FT /note="Coenzyme PQQ synthesis protein B (Pyrroloquinoline FT quinone biosynthesis protein B) (Coenzyme PQQ synthesis FT protein D)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4P9" FT /db_xref="InterPro:IPR011842" FT /db_xref="UniProtKB/Swiss-Prot:A1K4P9" FT /protein_id="CAL93804.1" FT /translation="MKVRVLGSAAGGGFPQWNCNCPNCDGLRRGTVRARARTQSSIAVT FT GDDENWVLFNASPDVLQQLREAPELQPARALRDTAIRAIVLIDAQIDHTTGLLMLREHR FT QPHALWCTAPVREDLSTGNPLFGVLGHYCGLDLNEIPLQGGFDIAGVPGVGFAALPLTS FT NAPPYSPRRDKPVPGDNIGVTLTDTRSGRRLFYAPGLGEMEPHVWAAMQAADCVLVDGT FT LWTDDEMIRLGASSKTSRAMGHLPQSGPGGMLEWLDRLPASTRKVLIHINNTNPILDED FT SPQRAELAAHGVEVAWDGMVLSL" FT CDS 1280664..1281455 FT /transl_table=11 FT /gene="pqqC" FT /locus_tag="azo1188" FT /product="coenzyme PQQ synthesis protein C" FT /note="Coenzyme PQQ synthesis protein C .is a member of six FT genes, constituting the pqqABCDEF operon, which are FT required for the synthesis of the cofactor pyrroloquinoline FT quinone (PQQ).This family consists of several bacterial FT coenzyme PQQ synthesis protein C or PQQC proteins. FT Pyrroloquinoline quinone (PQQ) is the prosthetic group of FT several bacterial enzymes,including methanol dehydrogenase FT of methylotrophs and the glucose dehydrogenase of a number FT of bacteria. PQQC has been found to be required in the FT synthesis of PQQ but its function is unclear. Shares 60% FT identity(75% similarity) with pqqC gene from Klebsiella FT pneumoniae. pfam05312, Q88QV6 mazG: MazG family protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Q0" FT /db_xref="InterPro:IPR004305" FT /db_xref="InterPro:IPR011845" FT /db_xref="InterPro:IPR016084" FT /db_xref="UniProtKB/TrEMBL:A1K4Q0" FT /protein_id="CAL93805.1" FT /translation="MEAELLAAPAARTLAPNAGTHDRPPMSREEFEAQLRAKGTSYHIY FT HPFHVMMAEGRLTPAQLRGWVANRFYYQIAIPVKDAAIMSNCPDREIRREWIQRILDHD FT GYEIGGVSDPGGIEAWIRLGEAVGLSRDDVTSLRFVAPAARFAVDAYINFARQRPWEEA FT VASSLTELFAPHIHQQRIDTWPQVYPWVKTEGLQYFRNRLTQARRDVAHGLRFTLEHFS FT QTRALQERALEILQFKLDVLWALADAIMLSQCEIEIKGPKA" FT CDS 1281634..1281900 FT /transl_table=11 FT /gene="pqqD" FT /locus_tag="azo1189" FT /product="PqqD protein" FT /note="Coenzyme PQQ synthesis protein D .This family FT contains several bacterial coenzyme PQQ synthesis protein D FT (PqqD) sequences. This protein is required for coenzyme FT pyrrolo-quinoline-quinone (PQQ) biosynthesis. 65% FT similarity with Klebsiella pneumoniae and 80%" FT /note="Family membership" FT /db_xref="GOA:A1K4Q1" FT /db_xref="InterPro:IPR008792" FT /db_xref="InterPro:IPR022479" FT /db_xref="UniProtKB/TrEMBL:A1K4Q1" FT /protein_id="CAL93806.1" FT /translation="MNQRPRVSRRFRLQWEDAQQAWVLLYPEGMVKLNRSAGEILARCN FT GERTLAEVVQDLEQAFGASNLAAEVVAFIDMARKQQWVEAQDA" FT CDS 1281902..1283056 FT /transl_table=11 FT /gene="pqqE" FT /locus_tag="azo1190" FT /product="pyrroloquinoline quinone synthesis protein E" FT /function="predicted Fe-S oxidoreductases" FT /note="Coenzyme PQQ synthesis protein E (Pyrroloquinoline FT quinone biosynthesis protein E).PART OF THE PQQ OPERON. FT Q88QV8: 58% identity, 74% similarity with Klebsiella FT pneumoniae InterProIPR000385, FT InterProIPR007197,PfamPF04055, SMARTSM00729, FT InterProIPR006638 cofactor:iron-sulfur cluster (potential). FT pathway:pyrroloquinoline quinone (pqq) biosynthesis. FT similarity: belongs to the radical sam superfamily, pqqE FT family TIGR PP0376; HAMAP MF_00660; Pfam PF04055; FT Radical_SAM; PROSITE: PS01305; MOAA_NIFB_PQQE" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Q2" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR011843" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR017200" FT /db_xref="InterPro:IPR023885" FT /db_xref="UniProtKB/TrEMBL:A1K4Q2" FT /protein_id="CAL93807.1" FT /translation="MNAAQPPSPASTLGPPLWLLAEVTYRCPLHCAFCYNPVDFARDDT FT ELSTEDWLRVLREARAAGSVQCGFSGGEPLMRDDLEVLVAEAHRLGYYTNLLTSGVGLT FT AERAQALKAAGLDHIQLSFQDSTRELNDFLSHTRTFDLKQRVAGIIKDNGWPMVMNCVI FT HRLNIDYIDRIIEMAVELGAEYLELANSQYYSWALLNRDQLMPSREQLERAERITNEYR FT QRLGDRIRIFFVVPDYYEKRPKKCMNGWGNVFLTVTPDGTALPCHTARMLPGLEFPNVR FT DMDVKSIWYDSEGFNRYRGDSWMKDPCRTCPDKEKDHGGCRCQAYMLAGDPAAADPVCD FT KSPDHHKVVEAVERANTPGWKGAEQPLIFRDPARSRELAACGKR" FT tRNA 1283196..1283271 FT /gene="tRNA-Thr" FT /locus_tag="azo_tRNA_0024" FT /product="transfer RNA-Thr" FT /anticodon=(pos:1283229..1283231,aa:Thr) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS complement(1283387..1283563) FT /transl_table=11 FT /locus_tag="azo1191" FT /product="Hypothetical protein" FT /note="Hypothetical protein. Has very bad homology with FT hits in the database. No Signficant motifs, domains or FT Signal peptide known to be present." FT /db_xref="UniProtKB/TrEMBL:A1K4Q3" FT /protein_id="CAL93808.1" FT /translation="MERRNNPLLRARIDLLLLAVKAGRLSIGDAGRRMDQLGVPFAVAC FT RVLTRSPVQAAPH" FT CDS complement(1283668..1284468) FT /transl_table=11 FT /locus_tag="azo1192" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to XAC0112 FT of X.axonopodis of 44% (trembl:Q8PR54). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="InterPro:IPR024787" FT /db_xref="UniProtKB/TrEMBL:A1K4Q4" FT /protein_id="CAL93809.1" FT /translation="MNTPLDAAALEELAAARAKLEAQSLALRLSALVGSPLEKGLRYLP FT APWRNKLDGLAHDALGRAMGIAARSLVLQPRASPRLHKVLGSVSGGAGGAFGLPGLALE FT IPVSTVLIMRAILATAREAGEDIDDPQVRLAALEVFALGGPGSADDSVDTGYYAVRAAL FT AGAVSEATRHVASSGLAGLGERGAPAIARLIALVAARYKVQLTQKAASMVVPGLGAAAG FT VAVNLMFMSHFQAVSEGHFAVRRLERHHGAEVVRAAYQGLGAGT" FT CDS complement(1284477..1285598) FT /transl_table=11 FT /gene="hppD" FT /locus_tag="azo1193" FT /product="probable 4-hydroxyphenylpyruvate dioxygenase" FT /function="4-hydroxyphenylpyruvate dioxygenase and related FT hemolysins" FT /EC_number="1.13.11.27" FT /note="Probable 4-hydroxyphenylpyruvate dioxygenase (EC FT 1.13.11.27) (4HPPD) (HPD) (HPPDase). Homology to hppD of FT Pseudomonas sp. of 56% (pir|S21209) Catalysis of the FT reaction: 4-hydroxyphenylpyruvate + O2 = homogentisate + FT CO2. Pfam: Glaxolase/Bleomycin resistance protein no signal FT peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4Q5" FT /db_xref="InterPro:IPR004360" FT /db_xref="InterPro:IPR005956" FT /db_xref="UniProtKB/TrEMBL:A1K4Q5" FT /protein_id="CAL93810.1" FT /translation="MSSTDLWDNPMGIDGFEFIEYAAPNPAELAAVFTRLGFKPIARHR FT AKDVTLYRQGGINFIINAEPDSFGQRFARLHGPSICAMAFRVADARKAYKRAVELGAWG FT YDSHSGPMELNIPAIKGIGDSLIYLVDRWRGKNGRQGGIGDISIYDVDFEPIVDADGVT FT DEYPVGHGFNLIDHLTHNVHRGRMNEWADFYERLFNFREARYFDIEGKVTGVKSKAMTS FT PCGKIHIPINEEGNDTKGQIQEYLDKYHGEGIQHIALGTDDIYTAVDRLRASGIQLLDT FT PDTYYELLDGRIPGHGEPLEALRARRILVDGAPGDLLLQIFSENQLGPVFFEFIQRKGN FT KGFGEGNFKALFESLELDQMRRGVLSGAADKAA" FT CDS 1286022..1287257 FT /transl_table=11 FT /locus_tag="azo1194" FT /product="putative integral membrane efflux protein" FT /function="Permeases of the major facilitator superfamily" FT /note="Permease member of the Major Facilitator FT Superfamiliy (MFS)transporters. MFS are single-polypeptide FT secondary carriers capable only of transporting small FT solutes in response to chemiosmotic ion gradients. 2A0121: FT H+ Antiporter protein 24% similarity to NorA who confer FT relatively high resistance to hydrophilic quinolones such FT as norfloxacin, enoxacin, ofloxacin, and ciprofloxacin in FT S. aureus. 20% similarity to TapA a multidrug efflux pump FT wich confers low level of resistance to aminoglycosides and FT tetracycline in Mycobaterium fortuitum and M. FT tuberculosis." FT /note="Specificity unclear" FT /db_xref="InterPro:IPR010290" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:A1K4Q6" FT /protein_id="CAL93811.1" FT /translation="MRALRHRNFRFYFGGQAVSVLGSWIQQVALAWLIYRLTGSVALLG FT VTAFAALLPMLIVGPLAGAWIDRRDKRRLLILVQGLLAGQAALLAVLTALDAIGPTLIV FT VMSVVLGVLNAFDTPLRQAQISVFVDDRADLPNALALNAMVFNSGRFIGPPLAGLILGL FT TSEAVCFALNAVSFAALAFGVAMIRVEATPRAKGSMGAVFREGLKFVWDVYTIRMLILT FT LATVNVTASSYAVLLPVFAKDVFVGDARMLGWLWGAAGAGAFVGTIFLATRKHLPGLVR FT VILSGASASALAMLVFSYNREMPVALAAMAVVGFGISVCNVAINMLLQSLAPDHLRGRV FT VSFFSSTRFGFDAIGGLVAGLIAAQIGVQAAVLLEGVLLLAFIAWAWRLRGRLHGDIAL FT HAGSGHAPATPR" FT CDS 1287319..1288497 FT /transl_table=11 FT /gene="argM" FT /locus_tag="azo1195" FT /product="probable acetylornithine transaminase" FT /function="Ornithine/acetylornithine aminotransferase" FT /EC_number="2.6.1.11" FT /note="Probable acetylornithine transaminase. Homology to FT argM of E. coli of 45% (sprot|ARGM_ECOLI). Catalyzes the FT transmination of n(2)-succinylornithine and FT alpha-ketoglutarate into n(2)-succinylglutamate FT semialdehyde and glutamate. Can also act as a FT acetylornithine aminotransferase. Tigrfam: argD: FT acetylornithine and succinylornithine aminotransferases FT Pfam: Aminotransferse class-III no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Q7" FT /db_xref="InterPro:IPR004636" FT /db_xref="InterPro:IPR005814" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:A1K4Q7" FT /protein_id="CAL93812.1" FT /translation="MKYGEFDSASLMYITNRPEILFERGEGSWLYDAQGKAYLDFVQGW FT AVNCLGHSPAEVRDAIVAQAGKLINPSPAFYNGPMIELAGLLTAHCSLDRVFFANTGAE FT ANEGAIKLARKWGRLHRNGAYQIITFEHSFHGRTLATMSASGKAGWDTLFAPQVPGFPK FT ARLNDLESVKALIGPETVAVMLEPVQGEGGVIPAAPEFLQALRALTREHGILLIVDEVQ FT SGMGRTGRLFAHQHAGIEPDIMTLGKGIGGGVPLSALLATEAVSCFEAGDQGGTYNGNP FT LMTAAGIAVMRRLTAPGFLDEVLARGDYLAARLRELVAKRHLVGERGSGLLRALVLDSD FT RAPAIVKAALEGAPTGLLLNAPRPNLLRFMPSLTVSEAEIDQMVEMLDALLG" FT CDS complement(1288769..1289806) FT /transl_table=11 FT /locus_tag="azo1196" FT /product="conserved hypothetical protein" FT /function="Coenzyme F420-dependent N5N10-methylene FT tetrahydromethanopterin reductase and related FT flavin-dependent oxidoreductases" FT /note="Conserved hypothetical protein. Homology to ypo3484 FT of y. pestis of 60% (trembl|Q8ZBD2). Pfam: Luciferase-like FT monooxygenase. no signla peptide no TMHs" FT /db_xref="GOA:A1K4Q8" FT /db_xref="InterPro:IPR011251" FT /db_xref="InterPro:IPR019949" FT /db_xref="UniProtKB/TrEMBL:A1K4Q8" FT /protein_id="CAL93813.1" FT /translation="MTAAPPQPAVGRAVARLSVLDLAPITEGSTAARALANTRDLARVA FT ERCGYTRYWVAEHHNMTGIASAATAVVIGHIAAATSTIRVGAGGIMLPNHAPLVIAEQF FT GTLESLFPGRIDLGLGRAPGTDQRTARALRRSLVGSDDSFPQDVVELQGWFADPQPGQA FT IQAVPGAGLKVPIWLLGSSLFSAGLAAQLGLPFAFASHFAPRFLKQAIALYRREFQPSA FT ALAEPYVMVGANAIAADSDAQAAFLFRSLRLRFAAMARGVRGQLPPPERFNEADWSPNE FT LAFADESLSCSAVGSPHTVRQRLMEIVEDTGADELMLTAQIFDHGARLRSFELIARAWQ FT LKPGD" FT CDS complement(1289811..1290620) FT /transl_table=11 FT /locus_tag="azo1197" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical protein. Homology to NE1163 FT of N.europaea of 76% (tremble:Q82VD1) Has FT PF02649,Uncharacterized ACR, DUF198 Domain; No signal FT peptide or TMH reported present." FT /db_xref="GOA:A1K4Q9" FT /db_xref="InterPro:IPR002042" FT /db_xref="InterPro:IPR003801" FT /db_xref="InterPro:IPR022838" FT /db_xref="UniProtKB/Swiss-Prot:A1K4Q9" FT /protein_id="CAL93814.1" FT /translation="MNSPLAHAIPDVQNSEDSRQIAINKVGIKSIRHPVKVSDKNGGVQ FT HTVANFNMYVGLPHNFKGTHMSRFIEILNSNEREISVESFEPMLREMVKRLEAETGHVE FT MTFPYFINKSAPVSGVQSLMDYEVTFTGEIHEGGRYEFTMKVVVPVTSLCPCSKKISAY FT GAHNQRSHVTVTATLNDHLWIEDVVQLVEGQASCEVYGLLKRPDEKYVTERAYDNPKFV FT EDMVRDVAGLLNKEVRIDAYAVESENFESIHNHSAYALIERDKRIEA" FT CDS complement(1290707..1292566) FT /transl_table=11 FT /gene="dxs" FT /locus_tag="azo1198" FT /product="probable 1-deoxy-D-xylulose 5-phosphate synthase" FT /function="Deoxyxylulose-5-phosphate synthase" FT /EC_number="2.2.1.7" FT /note="The enzyme 1-deoxy-D-xylulose 5-phosphate (DXP) FT synthase, probably a Dxs homodimer [ Kuzuyama00 ] , acts in FT the mevalonate-independent pathway of isopentenyl FT diphosphate biosynthesis, in thiamin biosynthesis, and FT pyridoxal biosynthesis [ Sprenger97 ].Overproduction of Dxs FT affects flux through the pathway under some FT circumstances.Dxs has similarity to transketolases [ Lois98 FT ] Entry name SWISSPROT:DXS_ECOLI Prim. accession # P77488 FT Identities = 358/614 (58%) InterPro:- IPR005477; Dxs_synth. FT IPR009014; Transketo_C_like. IPR005476; Transketolase_C. FT IPR005475; Transketolase_CR. IPR005474; Transketolase_N. FT Pfam PF02779; transket_pyr; 1. PF02780; transketolase_C; 1. FT Number of predicted TMHs: 0" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4R0" FT /db_xref="InterPro:IPR001017" FT /db_xref="InterPro:IPR005474" FT /db_xref="InterPro:IPR005475" FT /db_xref="InterPro:IPR005476" FT /db_xref="InterPro:IPR005477" FT /db_xref="InterPro:IPR009014" FT /db_xref="InterPro:IPR015941" FT /db_xref="InterPro:IPR020826" FT /db_xref="UniProtKB/Swiss-Prot:A1K4R0" FT /protein_id="CAL93815.1" FT /translation="MSPYPHLERIGSPADLRATERRELAQVASELRAFLIESVSKTGGH FT LSSNLGTVELTIALHYVFNTPDDRIVWDVGHQTYGHKILTGRREAMSGLRHWGGISGFP FT RRCESEYDTFGTAHSSTSISAALGMAVAARDRGEDRRAIAVIGDGAMSAGMAFEALNNA FT GDMDANLLVILNDNEMSISPPVGALTKILARLMSGSTYNAARRVGEKVLGTVPPMAELA FT RKVEEYAKGMIAPGTLFEEFGFHYYGPIDGHDLDALIPTLQNIRKLKGPQFLHVITKKG FT QGYKLAEADPILYHGVSKFDHTAGIQTGKSGGKLTYTQVFSDWLCDIAAADPRIVGITP FT AMREGSGLVEFAQRFPDRYYDVGIAEQHALTFAAGLACEGLKPVVAIYSTFLQRAYDQL FT IHDIALQNLPVVLAIDRGGLVGADGATHHGAFDLSFLACVPNLVVMAPADENECRQMLY FT TAVCHDGPTAVRYPRGGGSGVVPLEPMTALPIGKGEIRRHGTRIAVLAFGSMLGVALEV FT GEALDASVANMRFVKPLDEALIAELAANHALLVTVEENAVIGGAGSEVARFVDTLPQRP FT RVLRLGLPDRFIDHGDQAQLLASVGLDKTGILAAIEAVYPHNS" FT CDS complement(1292594..1293496) FT /transl_table=11 FT /gene="ispA" FT /locus_tag="azo1199" FT /product="Geranyltranstransferase" FT /function="Geranylgeranyl pyrophosphate synthase" FT /EC_number="2.5.1.10" FT /note="Geranylgeranyl pyrophosphate synthetase chloroplast FT precursor (GGPP synthetase) (GGPS) [Includes: FT Dimethylallyltransferase (EC 2.5.1.1); FT Geranyltranstransferase (EC 2.5.1.10); FT Farnesyltranstransferase (EC 2.5.1.29)]. catalyzes the FT trans-addition of the three molecules of ipp onto dmapp to FT form geranylgeranyl pyrophosphate. InterPro: Polyprenyl FT synthetase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4R1" FT /db_xref="InterPro:IPR000092" FT /db_xref="InterPro:IPR001849" FT /db_xref="InterPro:IPR008949" FT /db_xref="InterPro:IPR017446" FT /db_xref="UniProtKB/TrEMBL:A1K4R1" FT /protein_id="CAL93816.1" FT /translation="MTALSPQDFAAWMGAIQQRTEAALAGVLPEPTIAPERLHEAMRYA FT VLGGGKRVRPLLVHAAGAIGGAQPERLDRIACAVELIHAYSLVHDDMPCMDDDVLRRGK FT PTVHVEYDDATALLVGDALQTLAFQVLASAPVTDMPTRQLGMIGLLAMASGSRGMAGGQ FT AIDLAAVGRQLDLRELEFMHIHKTGALIRCSVLLGAQAGTVDGETLERLDRYAKLTGLL FT FQVVDDILDAEADTATLGKTAGKDADHDKPTYVSLLGVADARRLAQDMLAEALAALEPL FT GARAGHLAALANYIVHRPF" FT CDS complement(1293493..1293747) FT /transl_table=11 FT /gene="xseB" FT /locus_tag="azo1200" FT /product="Exodeoxyribonuclease VII" FT /function="Exonuclease VII small subunit" FT /EC_number="3.1.11.6" FT /note="Probable Probable exodeoxyribonuclease VII small FT subunit . InterPro: Exonuclease VII small subunit." FT /note="Function unclear" FT /db_xref="GOA:A1K4R2" FT /db_xref="InterPro:IPR003761" FT /db_xref="UniProtKB/Swiss-Prot:A1K4R2" FT /protein_id="CAL93817.1" FT /translation="MPKPASSPTSFEAAVAELETIVQQMESGQLSLEDALARYQRGVGL FT LKFCQETLSGAEQRIRQLEGGELVELRIDTNADGSQECA" FT CDS 1293877..1294977 FT /transl_table=11 FT /gene="alcE" FT /locus_tag="azo1201" FT /product="putative iron-sulfur protein" FT /function="Phenylpropionate dioxygenase and related FT ring-hydroxylating dioxygenases large terminal subunit" FT /note="AlcE: iron-sulfur-containing dioxygenases, probably FT involved in alcaligin biosynthesis pathway in Bordetella FT species. Putative iron-sulfure protein involved in aromatic FT compounds degradations. Choline monooxygenase chloroplast FT precursor (EC 1.14.15.7). Catalyzes the first step of the FT osmoprotectant glycine betaine synthesis. InterPro: Rieske FT iron-sulfur protein 2Fe-2S subunit hypA: hydrogenase FT expression/formation pr" FT /note="Function unclear" FT /db_xref="GOA:A1K4R3" FT /db_xref="InterPro:IPR017941" FT /db_xref="UniProtKB/TrEMBL:A1K4R3" FT /protein_id="CAL93818.1" FT /translation="MSDIASTARLAPAVSQLPVSSYFDEKVFELEKKLLFDAGPGYVGH FT ELMVPEVGNYRSLEWLDHSKLLFRTEAGVHQLSNICRHRQAIMLQGAGKTEHIVCPIHR FT WTYDQQGSLLGAPHFPDNPCLNLKRDVLENWHGLLFKGPRSANADLAGMQVAQELDFSG FT YKLDRVEIHQCNYNWKTFIEVYLEDYHVVPYHPGLGNFVTCDDLTWQFGDWYSVQRVGV FT TSLAKPGSATYAKWHKAVQEYYGEKKPAHGAIWLTYYPNIMVEWYPHVLVVSTLIPTDV FT DKTTNVVEFYYPEDIVEFEREFVEAEQAAYMETAIEDDDIGERMDRGRLALLKEGRNEV FT GPYQSPYEDGMQHFHEFYRRIMEPNV" FT CDS complement(1295352..1296290) FT /transl_table=11 FT /gene="lytB" FT /locus_tag="azo1202" FT /product="probable 4-hydroxy-3-methylbut-2-enyl diphosphate FT reductase" FT /function="Penicillin tolerance protein" FT /EC_number="1.17.1.2" FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase FT (EC 1.17.1.2). Function:- Converts FT 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into FT isopentenyl diphosphate (IPP) and dimethylallyl diphosphate FT (DMAPP) (By similarity). InterPro: LytB protein lytB: FT penicillin tolerance protein LytB SWISSPROT:ISPH_ECOLI FT Prim. accession # P22565 Identities = 185/308 (60%) FT InterPro IPR003451; LytB. Pfam PF02401; LYTB; 1. TIGRFAMs FT TIGR00216; ispH_lytB; 1. TMHMM 0.0, Signal peptide FT probability: 0.000 Prediction: Non-secretory protein" FT /note="Family membership" FT /db_xref="GOA:A1K4R4" FT /db_xref="InterPro:IPR003451" FT /db_xref="UniProtKB/Swiss-Prot:A1K4R4" FT /protein_id="CAL93819.1" FT /translation="MDNNEILLANPRGFCAGVERAIEIVERALQRFGAPIYVRHEVVHN FT KFVVDDLRAKGAVFVEELDEVPTGNTVIFSAHGVSQAVREEADKRGLRVFDATCPLVTK FT VHIEVGRMREQGRELVMIGHKGHPEVEGTMGQVKDGIHLVETAADVANLQVADPDKLAY FT VTQTTLSVDDAAAIVTALRERFPNIMGPKKDDICYATQNRQDAVKFMTPHADVVFVVGS FT KNSSNSNRLREVAELRGVPAYLVDNAAGIDPAWIVGKRRIGVTAGASAPEVLVAEVIER FT LKALSGASVRNLDGVPEKVTFPLPKELQEAR" FT CDS complement(1296320..1296748) FT /transl_table=11 FT /gene="slpA" FT /locus_tag="azo1203" FT /product="putative peptidyl-prolyl cis-trans isomerase" FT /function="FKBP-type peptidyl-prolyl cis-trans isomerases FT 2" FT /EC_number="5.2.1.8" FT /note="Putative peptidyl-prolyl cis-trans isomerase. FT Homology to slpA of E. coli of 39% (sprot|FKBX_ECOLI) FT Accelerate protein folding by catalyzing the cis-trans FT isomerization of proline imidic peptide bonds in FT oligopeptides. InterPro: FKBP-type peptidyl-prolyl FT cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type FT peptidyl-prolyl cis-trans isomerase no signal peptide no FT TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4R5" FT /db_xref="InterPro:IPR001179" FT /db_xref="InterPro:IPR023566" FT /db_xref="UniProtKB/TrEMBL:A1K4R5" FT /protein_id="CAL93820.1" FT /translation="MSQTVAANSLVTLHYRITLPNGQPLISTFEATPATLQLGAGEMLP FT AMEQLIIGLEIGSNHVFELEPENAFGPHRAELVERVKREHMPNEEIEPMSIMEFTAPDG FT SRYSGLVREIDEQSALIDFNHPLAGKAIRFEVKVIGTS" FT CDS complement(1296745..1297275) FT /transl_table=11 FT /gene="lspA" FT /locus_tag="azo1204" FT /product="probable signal peptidase II" FT /function="Lipoprotein signal peptidase" FT /EC_number="3.4.23.36" FT /note="Probable signal peptidase II (EC 3.4.23.36) FT (Prolipoprotein signal peptidase) (Signal peptidase II) FT (SPase II). This protein specifically catalyzes the removal FT of signal peptides from prolipoproteins (By similarity). FT lspA: lipoprotein signal peptidase Pfam: Peptidase_AS FT probable 5 TMH no signal peptide" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4R6" FT /db_xref="InterPro:IPR001872" FT /db_xref="UniProtKB/Swiss-Prot:A1K4R6" FT /protein_id="CAL93821.1" FT /translation="MPDLQAGQRPAFVAMLPWLVLAAAVMGLDQLTKQVVLATMQYGEV FT IPVTGFFDLVLVFNRGAAFSFLAEHSGWQRWFFTGLAVVICGWLLALMHQHREERLLPA FT AFALIIGGAIGNVVDRLLHGAVVDFLYFHAGRYGWPAFNLADSAITLGVGLMLWAQLRA FT GKHKPEAGPERPS" FT CDS complement(1297268..1300066) FT /transl_table=11 FT /locus_tag="azo1205" FT /product="IleS protein" FT /function="Isoleucyl-tRNA synthetase" FT /EC_number="6.1.1.5" FT /note="Isoleucyl-tRNA synthetase (EC 6.1.1.5) FT (Isoleucine--tRNA ligase) (IleRS)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4R7" FT /db_xref="InterPro:IPR001412" FT /db_xref="InterPro:IPR002300" FT /db_xref="InterPro:IPR002301" FT /db_xref="InterPro:IPR009008" FT /db_xref="InterPro:IPR009080" FT /db_xref="InterPro:IPR010663" FT /db_xref="InterPro:IPR013155" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR023585" FT /db_xref="UniProtKB/Swiss-Prot:A1K4R7" FT /protein_id="CAL93822.1" FT /translation="MADYRKTLNLPDTAFPMRGDLPKREPGWIAAWQQQKLYQKIRKAA FT AGRPKFVLHDGPPYANGNLHLGHALNKILKDIIVRSKTLAGFDAPYVPGWDCHGLPIEH FT KVEVTHGKNLPADKVRELCRAYAAEQVEIQKKEFIRLGVLGDWDNPYLTMNFANEAGEV FT RALAEMVKAGYVFKGLKPVNWCFDCGSALAEAEVEYADKVSPAVDVGFPCAEPDRLADA FT FGLAPLTKPALAVIWTTTPWTIPANQALNMHPEFDYALVDTGERYLVLAHDLVGACLER FT YGLNGRIVATCKGAALDRVAFRHPFYDRLSPVFLGDYVTLDAGTGVVHSAPAYGLEDFQ FT SCRANGMQSDDILTPVMGDGRYAPDLPFFGGMNIWKANPEITAKLREVGCLLAEAKITH FT SYMHCWRHKTPLIYRATAQWFVGMDKPVADGSTLRERALRGVEATRFFPAWGQSRLHAM FT IANRPDWCISRQRNWGVPIPFFLHKETGELHPRTVELMEEVAKRIEQEGIEAWFKLDAA FT ELLGAEAAQYEKISDTLDVWFDSGTTHWHVLRGSHNDGHVEGPRADLYLEGSDQHRGWF FT HSSLLTGCAIDGHPPYNALLTHGFTVDQQGRKMSKSLGNTILPQEVSEKMGAEILRLWV FT ASTDYSGELSISKEILDRVVEVYRRVRNTLRFLLANTADFDIAKDAVPLEQWLDIDRYA FT LAFTRQLAQQAEADYARFEFHRIVQALQVFCAEDLGAFYLDILKDRLYTTAAGSQARRA FT AQTALWHITQTLLKLMAPILSFTAEEAWAVLNPGKEDSVMLHTFHALPAQEGEAGLVAR FT WETIRAVRAEALKVIEALRTEGKVGASLQAELELRLTADKYTAMQSLGEDLRFVTMTSR FT ATLLEAASAEAEAIVATPSARTKCERCWHYTDDVGHNAEHPTLCARCADNLYGAGETRT FT HA" FT CDS complement(1300081..1301079) FT /transl_table=11 FT /gene="ribF" FT /locus_tag="azo1206" FT /product="riboflavin kinase / FMN adenylyltransferase." FT /function="FAD synthase" FT /EC_number="2.7.1.26" FT /note="Riboflavin biosynthesis protein ribF [Includes: FT Riboflavin kinase (EC 2.7.1.26) (Flavokinase); FMN FT adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) FT (FAD synthetase)]. ribF: riboflavin biosynthesis protein R" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4R8" FT /db_xref="InterPro:IPR002606" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR015864" FT /db_xref="InterPro:IPR015865" FT /db_xref="InterPro:IPR023465" FT /db_xref="InterPro:IPR023468" FT /db_xref="UniProtKB/TrEMBL:A1K4R8" FT /protein_id="CAL93823.1" FT /translation="MQVSRGIPDHAARQPSVLTIGNFDGVHRGHQALLKLLTDKARALG FT LPAVVLTFEPHPREYFAPDAAPARLASLREKLLLLAAAGVDRVHVCRFDARLAQLSPTA FT FIDDLLVRGLGVRHLYIGDDFRFGARRAGDFAMLQQAGAAHGFAVESMATLDVEGERVS FT SSAVRAALADGDMAHAERLLGRPYSIAGRVIHGDKIGRRIGYPTANVQMKHRKPPFTGV FT YAVRVEGLTDGLVDGVASMGIRPTINSAGSLRLEVNLFDWNSDCYGAHLRVHFLHRLRG FT EARFDSLDALTAQIGRDADDARAWLAAHPTAGPRLPRPQDHSTITLPRPRG" FT CDS 1301459..1301782 FT /transl_table=11 FT /locus_tag="azo1207" FT /product="hypothetical protein predicted by FT Glimmer/Critica" FT /note="Hypothetical protein predicted by Glimmer/Critica. FT No homology to the data bank. No domains predicted. No FT signal peptide. No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K4R9" FT /protein_id="CAL93824.1" FT /translation="MSANLLTAAVLGRENDQYRGTAGVSSGNRDRGFRPAFLDGETGRV FT FLSCHADGRPAPFHLLDGLPAELTIRDPAGRVRGAKASLRSGFVLDDRFYSREEAAQLA FT VAE" FT CDS 1301779..1302555 FT /transl_table=11 FT /gene="gloB1" FT /locus_tag="azo1208" FT /product="probable hydroxyacylglutathione hydrolase" FT /function="Zn-dependent hydrolases including glyoxylases" FT /EC_number="3.1.2.6" FT /note="Hydroxyacylglutathione hydrolase (EC 3.1.2.6) FT (Glyoxalase II) (Glx II). Thiolesterase that catalyzes the FT hydrolysis of S-D- lactoyl-glutathione to form glutathione FT and D-lactic acid. Zn dependent Hydrolase belonging to FT glyoxalase II family of proteins. Presence of KOW motif,and FT PA domain.Presence of signal peptide. probably functioning FT as Carbamoylphosphate synthase L chain. 50% identity and FT 60% similarity to Bordetella pertussis hydrolase. InterPro: FT Metallo-beta-lactamase superfamily gidA: glucose-inhibited FT division protein" FT /note="Family membership" FT /db_xref="GOA:A1K4S0" FT /db_xref="InterPro:IPR001279" FT /db_xref="InterPro:IPR017782" FT /db_xref="UniProtKB/TrEMBL:A1K4S0" FT /protein_id="CAL93825.1" FT /translation="MRPLPLRVRPIPAFQDNYIWLLTRGDEAVVVDPGTAGPVLAVLTA FT ERLRLRAVLITHHHDDHVGGVAEVLRHAAVPVYGPAGEDIAVLTHRVADGERVAVLDDH FT PGFEVLALPGHTAGHIGYFDGTHLFCGDVLFPCGCGRVFEGTPAQMHAALARLAALPPA FT TQVYCAHEYSLANARFALAAEPGNRLLQGRQRWMEARRAAGEPTVPSSLRDELDTNPFL FT RCTEPALRRAAADWRGHPIEDEAEVFAALRDWKNHF" FT CDS 1302969..1303301 FT /transl_table=11 FT /locus_tag="azo1209" FT /product="hypothetical protein predicted by FT Glimmer/Critica" FT /note="Hypothetical protein predicted by Glimmer/Critica. FT No homology to the data bank. No domains predicted. No FT TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K4S1" FT /protein_id="CAL93826.1" FT /translation="MLSAAELEDCIPHALDFTGRARWRVRVVAELVELNSRHLRAETRR FT AGADIELQGALEQGLRLETALSVADLRHALLEAEAELDALDDQRTQLLVVLDALNAAEA FT GPGALQ" FT CDS 1303298..1304290 FT /transl_table=11 FT /locus_tag="azo1210" FT /product="putative GTPase" FT /function="Putative GTPases (G3E family)" FT /note="TREMBLnew:CAE26305: 46% identity, 65% similarity. FT sprot:YJIA_ECOLI, 33% identity, 55% similarity Hypothetical FT protein. Pfam:cobW: Cobalmine synthesis protein; ABC_tran FT TIGRFAM: MMR_HSR1- GTPASE of unknown function InterPro: FT Cobalamin synthesis protein/P47K mobB: FT molybdopterin-guanine dinucleotid" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR003495" FT /db_xref="InterPro:IPR011629" FT /db_xref="UniProtKB/TrEMBL:A1K4S2" FT /protein_id="CAL93827.1" FT /translation="MNAAPSRLPVTVLTGFLGAGKTTLLNHLLRESGGRYAVIVNEYGE FT IGIDGELVVGAEEEVLELNNGCICCKVRGDLIRVVSGLLKRRGRFDGILIETTGLADPA FT PVVQSFMADDEIRQQARVDGVVCVVDACHFLTGLERSREAGVQLAHASLVVINKAELAD FT EAVVAQVEREIARLNPGATVLRSARGAVPAAALLDQGAYELPRLELPAAPAAARARYVP FT VPQGRHTDGLACVSLVLQRPLERGRFLAWLQRLVTERGEKLLRTKGIVALAGADRRFVF FT QGVHMMVDSDFDRPWRTEETRDSRLVFIGHGLDDSELRAGLDACQVSPA" FT CDS 1304287..1305360 FT /transl_table=11 FT /locus_tag="azo1211" FT /product="conserved hypothetical protein" FT /function="FOG: WD40 repeat" FT /note="Conserved hypothetical protein. Homology bll7767 of FT B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta FT repeat no signal peptide no TMHs" FT /db_xref="InterPro:IPR001680" FT /db_xref="InterPro:IPR015943" FT /db_xref="UniProtKB/TrEMBL:A1K4S3" FT /protein_id="CAL93828.1" FT /translation="MNAPLGGLPPLVALCGAHWRLEAPVVAVAWSRRGGPAAFAMGDGG FT VVFARPPTRPGGQGAPGLVRMEAHAGACLALAADPAGGFVSGGDDGRLLHLDPAAGAAS FT APAVLADHRGEWLDHVAVGARGLRACASGRRVWLHGPGSEAVLELASGVTALAFDPAGG FT RLAIAGHGGVELWSAADGARRRLEAPGYHRALAWSPDGRYLASGMQENALCCWRLGDGQ FT RHLFEGYPGQPRALGFAARGHLLASNGGPRVVSWDLDHPRPASTRSESGYPGRVPVSAL FT AWHPSRALLAAGYHNGAVLLCRPGSDQHLFVQGSGAGPVTALAWAADGAALALGTQHGE FT LAVVAIPAQILSMARAA" FT CDS 1305397..1305612 FT /transl_table=11 FT /locus_tag="azo1212" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT Rsph03000178 of Rhodobacter sphaeroides of 37%. No domains FT predicted. No signal peptide. No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K4S4" FT /protein_id="CAL93829.1" FT /translation="MSNETQASTEIDPAEAAAKDGFFERIAAVSEDMIQAYGREFAMGT FT LLLAARYIAQSRAAEAEPAPQIITQP" FT CDS 1305750..1306688 FT /transl_table=11 FT /gene="qbdB1" FT /locus_tag="azo1213" FT /product="conserved hypothetical secreted protein" FT /function="Protein involved in meta-pathway of phenol FT degradation" FT /note="Conserved hypothetical secreted protein. Homology to FT qbdB of Pseudomonas putida of 50% FT (gi|22779360|dbj|BAC15558.1|(NBCI ENTREZ)). No domains FT predicted. No TMHs. Signal peptide present." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4S5" FT /db_xref="InterPro:IPR011250" FT /db_xref="UniProtKB/TrEMBL:A1K4S5" FT /protein_id="CAL93830.1" FT /translation="MAAKHSQGEVAPVARRSRDSRRARRRFGAALASALAAASTSAWAL FT EMDAGDDTPLPEGTNLAVLYYQHVERDRLYVDGDRVPGRNRLDSDIGIARFVHYTKFAG FT MTINPQFLLPFGNLHAKGDLSPLGSASGVGDLILASVFWLVEKPETNTYFAITPYVYLP FT TGSYDKNEALNLGENRWKGTLQLGYITGLTDKLLLDLYADVTVFGNNNDYGPTSATLKQ FT DPLYQVQGWLRYKLTDAWDVRAGYFYTWGGETKVNGVSGDDRQRNTKYQVGTAWFYEPS FT AQVVFTYGQDISVESGFRERNRLNFRWLKVF" FT CDS 1306817..1307347 FT /transl_table=11 FT /locus_tag="azo1214" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT Rgel02003151 of Rubrivivax gelatinosus of 37% FT (gi|47572524|ref|ZP_00242567.1|(NBCI ENTREZ)). FT PF06496,Protein of unknown function FT (DUF1097);IPR009476;This family consists of several FT bacterial putative membrane proteins. signal peptide. 4 FT TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR009476" FT /db_xref="UniProtKB/TrEMBL:A1K4S6" FT /protein_id="CAL93831.1" FT /translation="MSQLAALSLSIALLGGFATWLFLTVGGVLIWAAFVAWGCYFQAGG FT NAPALRNTLVCNTFGAAVAWLAAVVILSVPLAATLTLPGWAAVVVFATAWLVCMAANVP FT ALSTIPASFYGYASTFAFLLQTPERMNLAALTSPGLDNAFIVTALSMAIGALFGYVSGA FT LGGALMTRTARAG" FT CDS 1307593..1308540 FT /transl_table=11 FT /gene="mntC2" FT /locus_tag="azo1215" FT /product="putative periplasmic solute binding protein" FT /function="ABC-type metal ion transport system periplasmic FT component/surface adhesin" FT /note="Part of the ABC transporter complex mntABC involved FT in manganese uptake. 28% Similar to the putative FT periplasmic-binding protein MntC precursor in N FT gonorrhoaeae, also involved in the resistance to oxidative FT stress. TREMBL:Q9F4F6 InterPro:IPR006128; FT Lipoprotein_4.IPR006127; SBP_bac_9. Pfam:PF01297; FT SBP_bac_9; 1. Signal peptide present.TMHelix:1 This operon FT probably is also involved in other cations uptake like FT Fe,Cu and Zn.This protein also could act as an adhesin FT which is involved on adherence to extracellular matrix." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4S7" FT /db_xref="InterPro:IPR006127" FT /db_xref="InterPro:IPR006128" FT /db_xref="InterPro:IPR006129" FT /db_xref="UniProtKB/TrEMBL:A1K4S7" FT /protein_id="CAL93832.1" FT /translation="MPRRLLYCILLCLSVFAAPGRAAPPLDVVTTLAQIAEPLSVIAGP FT RARVSSLLGPGVDPHLYRLTRSDVARLTRADLVFYNGLHLEAQMEEMLQSLATRKPVVA FT IAAGVDPARLRGGAGQARDPHIWMDPALWRSALEAAVAALAAADPEGAEGYRSRARDYF FT QRLNRLQTYVGEVLASVPASARVLVTAHDAFGYFGHAFGLEVLAIQGISTESEAGLRRI FT EELVETLVRRRIGAVFVESSVSPRSVRALVDGAAARGHTVRIGGELYSDAMGKPGGYTG FT TYIGMLDHNASTIARGLGGRVPAGGMLGELADLH" FT CDS 1308560..1309357 FT /transl_table=11 FT /gene="mntA2" FT /locus_tag="azo1216" FT /product="putative manganese transport system ATP-binding FT protein" FT /function="ABC-type Mn/Zn transport systems ATPase FT component" FT /EC_number="3.6.3.35" FT /note="Manganese transport system ATP-binding protein mntA. FT This protein is probably a component of a manganese FT permease a binding protein-dependent ATP-driven transport FT system (mntABC). Probably responsible for energy coupling FT to the transport system. 40% AAA_ATPase.IPR003439,AAA FT ATPase superfamily; ABC_transporter. Pfam: PF00005; FT ABC_tran; 1. This operon probably is also involved in other FT cations uptake like Fe,Cu and Zn." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4S8" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:A1K4S8" FT /protein_id="CAL93833.1" FT /translation="MVTLLKFRPRSRPLPADSDSPLAVHGLTVAYGQQTVLREVDFVAP FT AASLVAVVGPNGAGKSTFIKAVLGLQPRLAGAVSCYGRAVERQRHLIGYVPQRSSVDWD FT FPASALDVVTMGLYGRIGWCRPVRARHREQALDCLEQVGMADFARRQIGQLSGGQQQRV FT FLARALAQDAMLYLMDEPFAGVDAATERAIVDVLRTLKGRGRTVLCVHHDLQTAPDYFE FT HLLLLAGRVVAAGPINETFTAAALEAAYGVGLPPVAAAVARAG" FT CDS 1309369..1310265 FT /transl_table=11 FT /gene="mntB2" FT /locus_tag="azo1217" FT /product="putative manganese transport system permease FT protein" FT /function="ABC-type Mn2+/Zn2+ transport systems permease FT components" FT /note="Part of the ABC transporter complex mntABC involved FT in manganese import. Probably responsible for the FT translocation of the substrate across the membrane. 28% FT IPR001626; ABC_transpt3. Pfam; PF00950; ABC-3; 1. TmHelix:8 FT This operon probably is also involved in other cations FT uptake like Fe,Cu and Zn." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4S9" FT /db_xref="InterPro:IPR001626" FT /db_xref="InterPro:IPR001991" FT /db_xref="UniProtKB/TrEMBL:A1K4S9" FT /protein_id="CAL93834.1" FT /translation="MGEFIDLLLLRAGYNSAVVVAGAALLGLAAGVIGAFVLLRKRVLI FT SDAISHATLPGVGLAFLAGVALTGNGRHFGLLLLGAGASGALGVLLVQAIKDHTRLPED FT SAIATVLSLFFGAGVVLLSHIQTLPVGGQAGMNGFLLGAAATMSLDEAQLVGAAALAVL FT ALAALLGKEFGLVCFDAGYAAALGWPVRRLDLALLVLLLAVVAIGLKTVGLILVVALVT FT IPPVAARFWTERLGAMVALAGGFGALAAWLGAAVSSLLPGLPTGAVIVLVAAALLVLSL FT LCGPARGLPARLRRVTA" FT CDS 1310262..1311221 FT /transl_table=11 FT /gene="mntB3" FT /locus_tag="azo1218" FT /product="putative manganese transport system permease FT protein" FT /function="ABC-type Mn2+/Zn2+ transport systems permease FT components" FT /note="Part of the ABC transporter complex mntABC involved FT in manganese import. Probably responsible for the FT translocation of the substrate across the membrane. Similar FT to the permease protein, MntB in Synechocystis 6803. 30% FT IPR001626; ABC_transpt3. Pfam; PF00950; ABC-3; 1. This FT operon probably is also involved in other cations uptake FT like Fe,Cu and Zn." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4T0" FT /db_xref="InterPro:IPR001626" FT /db_xref="UniProtKB/TrEMBL:A1K4T0" FT /protein_id="CAL93835.1" FT /translation="MNPGVEDFLLIDLPAVLAAVLAALACALPGSFLVLRRQALMGDAM FT SHVVLPGIVCAYLAVGDIAPLAMVAGALGAALVAVLLINALQRVGGLEPGAAMGVVFTV FT MFAAGLVLLEQSGAGNAHLDAEHALYGNLEGTLWPGPRDWADLLDPESYRTLPRVLVTL FT AVVTAAMVLLLVLFFKELAVTTFDPGLAAGLGISTRAVGTGLLAMTAVAAVAAFEAVGS FT IIVIAMFVCPAATARMLTDRLAAQVWLSALFAVLAGAGGYWLAAFLPPLLGHDNALNAA FT GMVAVAAGAMQCLAMLLAPRYGVLPRAWRARRRLAAAG" FT CDS 1311744..1313414 FT /transl_table=11 FT /locus_tag="azo1219" FT /product="conserved hypothetical aromatic/alkene FT monooxygenase, subunit alpha" FT /EC_number="1.14.13.-" FT /note="Conserved hypothetical aromatic/alkene FT monooxygenase, subunit alpha Homology to blr3677 of B. FT japonicum (trembl|Q89P06(SRS) Bacterial aromatic/alkene FT monooxygenase is a multicomponent enzyme that catabolises FT phenol and some of its methylated derivatives (like methane FT and toulene). InterPro:IPR003430 Pfam: FT Methane/Phenol/Toluene hydroxylase (PF02332) no signal FT peptide no TMHs" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4T1" FT /db_xref="InterPro:IPR003430" FT /db_xref="InterPro:IPR009078" FT /db_xref="InterPro:IPR012348" FT /db_xref="UniProtKB/TrEMBL:A1K4T1" FT /protein_id="CAL93836.1" FT /translation="MTAGLTLNKITSQRGVSIGEAARRIADLGWNPSYVQEAMTFPTDY FT KIGRQPKDPMKQVLRSYFPMQEEKDNRVYGALDAALRGDMFRNVEARWVEWMKLFLAII FT PFPEISAARSMSMLGRLAPGEELRTGFTMQMVDEFRHSTIQMNLKKWYMENYIDPAGFD FT ITEAAFGKCYATTIGRQFGEGFLTGDAITAANVYLQVVAETAFTNTLFVAMPSEAARNG FT DYALPTVFLSVQSDESRHIGNGHSLLMSILNDPDNHLLLERDLRYAFWQNHCIIDAAVG FT TLIEYGTTNRDKNKESYVELWHRWIYEDYYRTYMLPLEKYGIKVHHDDVAAAWDRLVKK FT NYHHKVAQFFAVGWPVNFWRIEAQTEKDFEWFEHKYPGWYAEFGDFWKWYGKKSVPGET FT NMLFDQENGYVYPHRCWSCMVPCLIREDFVVDEVDGKLYTYCSDLCRWTHKVAFSAEYE FT GRATPAMGRFSGRREWEECYHGWDLADCIKDLGFVRSDGKTLVSQPHLRFDNKDMWTLD FT HVKGHTIQSPLVLLRNMTPEQREKHIADYRAGFKINPFQ" FT CDS 1313496..1314539 FT /transl_table=11 FT /locus_tag="azo1220" FT /product="conserved hypothetical aromatic/alkene FT monooxygenase, subunit gamma" FT /function="2-polyprenylphenol hydroxylase and related FT flavodoxin oxidoreductases" FT /note="Conserved hypothetical aromatic/alkene FT monooxygenase, subunit gamma. Homology to blr3678 of B. FT japonicum of 60% (trembl|Q89P05(SRS) Bacterial FT aromatic/alkene monooxygenase is a multicomponent enzyme FT that catabolises phenol and some of its methylated FT derivatives (like methane and toulene). Interpro: Phenol FT hydroxylase reductase family (IPR001221); Oxidoredutase FAD FT and NAD(P)-binding domain (IPR000134); NADH:cytochrome b5 FT reductase (CBR) (IPR000134) Pfam: 2Fe-2S iron-sulfur FT cluster binding domain; oxidoreductase FAD-binding domain; FT Oxidoreductase NAD-binding domain no signal peptide no FT TMHs" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4T2" FT /db_xref="InterPro:IPR001041" FT /db_xref="InterPro:IPR001221" FT /db_xref="InterPro:IPR001433" FT /db_xref="InterPro:IPR001709" FT /db_xref="InterPro:IPR006058" FT /db_xref="InterPro:IPR008333" FT /db_xref="InterPro:IPR012675" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:A1K4T2" FT /protein_id="CAL93837.1" FT /translation="MSETPVHIVRFEPVGVEMEVAEGETVLDAAFRQGVAVMHGCKEGQ FT CSSCKALLIDGDVEMLKYSTFALPDYERDANHVLLCRTLAHTDITVELLNYDEDLMRRS FT IAVKEFAGKVVGISALTHDIRRLDVELEQPIRFWAGQFVDITLPEKGITRSYSMASVPS FT SPGQVSFIIKKYPNGAFSTALDTELKPGDPVLVKGPYGGCFRREERPGPMVLIGGGSGM FT SPLWSILNDHIESGEQRPIRFFYGARTRRDLFYLEQFAEFEQKVPDFRFIPALSAAEPE FT DGWTGETGYIHEVVARTLKEEGFDGASIDAYTCGPAPMIDAITPVLHMAGVPPDQMYFD FT KFTQAVR" FT CDS 1314604..1315695 FT /transl_table=11 FT /locus_tag="azo1221" FT /product="conserved hypothetical aromatic/alkene FT monooxygenase, subunit beta" FT /note="Conserved hypothetical aromatic/alkene FT monooxygenase, subunit beta Homology to blr3679 of B. FT japonicum of 53% (trembl|Q89P04(SRS) Bacterial FT aromatic/alkene monooxygenase is a multicomponent enzyme FT that catabolises phenol and some of its methylated FT derivatives (like methane and toulene). Interpro: FT Methane/Penol/Toluene hydroxylase (IPR003430) Pfam: FT Methane/Penol/Toluene hydroxylase (PF02332) no signal FT peptide no TMHs" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4T3" FT /db_xref="InterPro:IPR003430" FT /db_xref="InterPro:IPR009078" FT /db_xref="InterPro:IPR012078" FT /db_xref="InterPro:IPR012348" FT /db_xref="UniProtKB/TrEMBL:A1K4T3" FT /protein_id="CAL93838.1" FT /translation="MNAFTQEAVAQPVKSGAAGAAQFVGWDSRKYNYYTPKGRHATHYE FT DVTVDVQPDPKRYLLQDFIISFPDGTPTYSEHWTEARSSDWHKFRAVDEEWERTHYQRQ FT STICGMITNVIENARRAGATKRLDRAWVKVLEQYLGAYKHAEFGLGMATMHAQRYGYSQ FT MINSAILTNASYKLRFAQDLTLYLAELALDQPDLNLDLGKQHWMENPAWQGTRHAIEAI FT NGTSDYLEKYFAVNLVFEPVVAELVRSGFFMQVAAAQGDFTTPTVISAAEGDYQRNLAN FT TVELVHVLAQDPEHGAHNRALFNRWLADHGKRALTAAQQLQPMWSLPHHKVAQFPDALA FT RALSRIRSITGELGLDLPAELKA" FT CDS 1315744..1316100 FT /transl_table=11 FT /gene="dmpM" FT /locus_tag="azo1222" FT /product="phenol 2-monooxygenase" FT /EC_number="1.14.13.7" FT /note="Phenol hydroxylase P2 protein (Phenol FT 2-monooxygenase P2 component)68% similarity to FT SWISSPROT:P19731,Pseudomonas sp DmpM or Phenol hydroxylase FT protein component P2, this protein lacks redox co-factors FT and is required for optimal turnover of Phenol hydroxylase FT . Phenol hydroxylase catabolises phenol and some of its FT methylated derivatives in the first step of phenol FT biodegradation, and is required for growth on phenol. The FT multicomponent enzyme is made up of P0, P1, P2, P3, P4 and FT P5 polypeptides. Pfam:PF02406, InterPro:IPR003454 91% FT similarity with hypothetical protein Rgel01002820 FT [Rubrivivax gelatinosus PM1] NO Signal Peptide No TMH's. FT MmoB/DmpM family" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4T4" FT /db_xref="InterPro:IPR003454" FT /db_xref="UniProtKB/TrEMBL:A1K4T4" FT /protein_id="CAL93839.1" FT /translation="MSNYHGDNIFQSIKDMKFEQTISHQCGVTMNDSVEARAIAELMAT FT KPGIKVTYLPAMIRIDGEGKIEFSMPEISEALGREMTPHLFEIFTSTHYGRMVMLDDDT FT VVLFGDMDAALAYE" FT CDS 1316323..1317960 FT /transl_table=11 FT /gene="groEL2" FT /locus_tag="azo1223" FT /product="probable chaperonin GroEL" FT /function="Chaperonin GroEL (HSP60 family)" FT /EC_number="3.6.4.10" FT /note="Probable chaperonin GroEL. Homology to groEL of B. FT japonicum of 43% (SWISSPROT:CH61_BRAJA). Prevents FT misfolding and promotes the refolding and proper assembly FT of unfolded polypeptides generated under stress conditions FT (By similarity). InterPro: TCP-1 (Tailless complex FT polypeptide)/cpn60 chaperonin family (IPR002423); FT chaperonin cpn60 (IPR001844) Pfam: TCP-1/cpn 60 chaperonin FT family no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4T5" FT /db_xref="InterPro:IPR001844" FT /db_xref="InterPro:IPR002423" FT /db_xref="InterPro:IPR018370" FT /db_xref="UniProtKB/TrEMBL:A1K4T5" FT /protein_id="CAL93840.1" FT /translation="MPNIMLHDDEARAALARGVAKMARAVRGTLGPRGMNAIIDRPIGT FT PIISRDGVSIAAEIELEDPFENIGAQVLREVSRQTNEVAGDGTTTATVLADALVQEGLA FT CVQAGVKPVELVKGLELAVDETVAALKSMAIPVRGREDVFSVAVVAANEESTGALVAEA FT LERVGPDGIVDVEYGTTVETTLDVLDGMAFDRGYLSHHMVTDVEKMQVVLDDPWILMTD FT QRLQSQEEVAVLQSLLAGSKRPLLIIADEVAPACVVSLMAWREKSGVPVAAIHPPEYGH FT WRKAMLDDIAIVTGGKVIARDLGGSLKDVSLAELGSARQVRISSNQTVISGGGGTHEAI FT AARRKQVQRQYELAPQNIERDKFQERLAKLTGGTALILAGGATPVEQKRRLLLIEDAIH FT AARAAIEEGIVPGGGITLLQAAGRLEHLVAQTSGGVQQGVRLLQRALSRPLYHLAGNAG FT LDSEQVVDRAMRAEPGHGLDVRSGAFVDLVAEGVIDPVRVSYTAVRNAASVAGLILTTQ FT TLVAKKPEIIDPTAGPATGGGAELYGRQ" FT CDS 1318051..1318197 FT /transl_table=11 FT /locus_tag="azo1224" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domains predicted. No signal peptide. 1 TMH" FT /db_xref="UniProtKB/TrEMBL:A1K4T6" FT /protein_id="CAL93841.1" FT /translation="MNEISGRRDPAPFNSLCPRSPARRLQRLFGVLIWAAGLMVWLSDS FT LVR" FT CDS 1318385..1320445 FT /transl_table=11 FT /locus_tag="azo1225" FT /product="Sigma-54 dependent transcriptional regulator" FT /function="Transcriptional activator of acetoin/glycerol FT metabolism" FT /note="Some bacterial regulatory proteins activate the FT expression of genes from promoters recognized by core RNA FT polymerase associated with the alternative sigma-54 factor. FT These have a conserved domain of about 230 residues FT involved in the ATP-dependent interaction with sigma-54, FT TREMBL:Q8RM05 (41% identity); TREMBL:Q880V5 (32% identity). FT Pfam (PF02954): Bacterial regulatory protein,Fis family. FT Pfam (PF00158): Sigma-54 interaction domain. HTH reporting FT nucleic acid binding motif." FT /note="Family membership" FT /db_xref="GOA:A1K4T7" FT /db_xref="InterPro:IPR002078" FT /db_xref="InterPro:IPR002197" FT /db_xref="InterPro:IPR003018" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR020441" FT /db_xref="UniProtKB/TrEMBL:A1K4T7" FT /protein_id="CAL93842.1" FT /translation="MRELSYRKSGVRFSAELRPNPAAQCSGRELVSIDRATYAAWERFV FT TGEALPPSTIESPVLDSWRRSRDAGVNPVGRAAPVAARGDDMELLRRRHRELMAAASNL FT FAHTGDLLAGSHSIMLLTSPEGVVLDAAGDAATLDAARDIHLMTGGNWCEAVVGTNGIG FT TAIATRCPAQIHGAEHFCEGIQGWTCAAAPIFEPGTQDILGVLDISGPPQTFQRNNLLL FT AVSVARQIEMALSHSALGERLRLLEHCMNRLSLADAAGMVAIDRQGRLIHSAGRVPLPV FT GVGERLPGFRPHADLEEWAAHLPEGLRPEWLHPVVAGGRTVGAVVLVPGRGVRNSPVAR FT LAEQSSEADPRRSCFDNILGRSPAMREATDLGRRLATKRVPVLVEGETGVGKELFARAL FT HGGEHLGGPFITYNCGAASKELIAADLFGHVRGAFTGATNDGRPGRFELANGGTLCLDE FT IGEMPLDLQPVLLRALEEGIVYRLGDTQPRRVDVRLIAMTNRNLREEVAAGRFRRDLYY FT RIGVTRLRIPPLRERDGDIPLLASHFCTQLAERHGVPRREFGPEVLDALQAYCWPGNVR FT ELRNVVESLLLMDSTPQVRVDELPEEILASVPQAARPAAEGAEPECPSLEAAERRAIQK FT AVINFQGNLAQAARLLGISRSTLYRKVERYALEDFVRAAGGNLEGEGGAGD" FT CDS 1320918..1321319 FT /transl_table=11 FT /gene="lguL" FT /locus_tag="azo1226" FT /product="lactoylglutathione lyase" FT /function="Lactoylglutathione lyase and related lyases" FT /EC_number="4.4.1.5" FT /note="Glyoxalase I catalyzes the first step of the glyoxal FT pathway. S-lactoylglutathione is then converted by FT glyoxalase II to lactic acid. Similar to trembl|Q8YEJ0 FT (61%), to trembl|Q8DB12 (58%) and to trembl|Q8UCM7 (52%). FT Pfam (PF00903): Glyoxalase/Bleomycin resistance FT protein/Dioxygenase" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4T8" FT /db_xref="InterPro:IPR018146" FT /db_xref="UniProtKB/TrEMBL:A1K4T8" FT /protein_id="CAL93843.1" FT /translation="MPKPKLIHTMIRVLDLDKSLAFYRDALGLEEAYRLDFPDFALAYL FT RNAENDFELELTLNKGRSEAYTHGSGYGHIAVCVDDVEAEHRRLAGLGLGPTDVKRFAD FT GDALIARFFFIQDPDGYKVEVLERHGHYQ" FT CDS 1321373..1321966 FT /transl_table=11 FT /locus_tag="azo1227" FT /product="conserved hypothetical secreted protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical secreted protein. Homology to FT blr7490 of B. japonicum of 31% (trembl|Q89DE9(SRS)). No FT domains predicted. No TMHs Signal peptide present" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR019546" FT /db_xref="UniProtKB/TrEMBL:A1K4T9" FT /protein_id="CAL93844.1" FT /translation="MSEQSVVLGALAAPRVTRRAFLKGSGILVGTLWASSSALLALAPS FT PAWALELKSLDQATGEALLGFCRRIFPHDKLDDAVYALVVKELDQAAAKSADTRKLLTE FT GVAALNKAAGGNWAGAPLAKKDAIVAGLATTPFFLKVHGTAVVALYNNELAFAHFGYEG FT NAFQQGGGYLLRGFNDLKWLPNPSAQASPAPFGA" FT CDS 1321992..1323557 FT /transl_table=11 FT /gene="gdhAlpha1" FT /locus_tag="azo1228" FT /product="putative glucose dehydrogenase alpha subunit" FT /function="Choline dehydrogenase and related flavoproteins" FT /EC_number="1.1.-.-" FT /note="Putative glucose dehydrogenase alpha subunit. FT Homology to gdhAlpha of B. cepacia of 29% (trembl|Q8GQE7) FT InterPro: NAD binding site (IPR000205) Pfam: GMC FT oxidoreductase no signal peptide no TMHs" FT /note="Function unclear" FT /db_xref="GOA:A1K4U0" FT /db_xref="InterPro:IPR000172" FT /db_xref="InterPro:IPR007867" FT /db_xref="UniProtKB/TrEMBL:A1K4U0" FT /protein_id="CAL93845.1" FT /translation="MATYKHDDNSVVVIIGSGAGGGTLANELCQKGIKVVVLEAGKRQS FT PATFINDEWAAFGQLSWTDKRTTSGSWRVAKDFPNLPAWICKTVGGTTTHWAGASLRFQ FT EHEFRTRTVYGDIAGANLLDWPLTLAELEPYYARAEDKMGVTRTHDIPGLPGNNNFKVF FT YNGATKMGYGATTGRMAINSEPRAGRGSCQQYGFCFQGCKSGAKWSTLYTEIPAAEKTG FT KLELRTECHVARIEHDAAGKATGVVYFDKDGKEQRQKARVVCVAGNAIETPRLLLMSAS FT SKFPDGLANSSGQVGRNYMRHTTGSVYATFNDPVHMYRGTTMAGIVQDEAHHNTKRGFA FT GGYELETLSLGLPFMAAFLNPGGWGKDFAEAMDNYVNMAGLWIVGEDMPQETNRVTLHA FT TEKDQWGLPVPNVHYDDHPNDIALRKHAYQQASALYQSVGAKKVYEVPPYPSTHNLGTC FT RMSAKASDGVLNKWGQTHDIKNLFVSDGSQYTTGATENPTLTIVTLAIRQADYIAGQMQ FT ARAL" FT CDS 1323688..1324407 FT /transl_table=11 FT /locus_tag="azo1229" FT /product="hypothetical secreted protein" FT /note="Hypothetical secreted protein. No good homology with FT hits in the database. Signal peptide present. No TMHs. No FT domains predicted" FT /db_xref="UniProtKB/TrEMBL:A1K4U1" FT /protein_id="CAL93846.1" FT /translation="MKIVDAPAPRAGRADRAALLSLALLSGPALADRPLTVDDAATLVV FT GEGKLEAGWLRDDTLRGVEVNGGYSPLQGLELEAGAGRGEARGKRDWRRAHAEGVAVKW FT VPLQAPVGLSAGLRYAYVRDRVELSGGGRLHGHLHDATALASLASEAGNALHLNLGRRW FT GRFDGERSAVTHWGLAAEHPLTETLTLTAEIVRDADARPERALGVRYLVTDDLALSAAC FT GRGDGRNFWTAAVSWTF" FT CDS complement(1324442..1324726) FT /transl_table=11 FT /locus_tag="azo1230" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical membrane protein, 40% FT identity (49% Similarity) to TrEMBL;Q6D7F7. Signa P FT reporting Signal peptide present. TMHMM2 reporting 2 TMH's FT present." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR011846" FT /db_xref="UniProtKB/TrEMBL:A1K4U2" FT /protein_id="CAL93847.1" FT /translation="MLPAPERRTPGIRLLPLVAALAIMLGVTAWPRVLAGAQGGADHLA FT ALALFWAMSAGFVAGVGFRPRGWIWRALFGAPACALGLALAVLRAWAAG" FT CDS complement(1324874..1326016) FT /transl_table=11 FT /gene="cydB" FT /locus_tag="azo1231" FT /product="probable cytochrome bd type terminal FT oxidase,subunit II" FT /function="Cytochrome bd-type quinol oxidase subunit 2" FT /note="Cytochrome D ubiquinol oxidase subunit II (EC FT 1.10.3.-) (Cytochrome BD-I oxidase subunit II). Cytochrome FT bd type terminal oxidases catalyse quinol dependent, Na+ FT independent oxygen uptake. Members of this family are FT integral membrane proteins and contain a protoheame IX FT center B558. It may play an important role in microaerobic FT nitrogen fixation. Tigrfam: cydB: cytochrome d ubiquinol FT oxidase subunit II Pfam: cytochrome oxidase subunit II no FT signal peptide 8 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4U3" FT /db_xref="InterPro:IPR003317" FT /db_xref="UniProtKB/TrEMBL:A1K4U3" FT /protein_id="CAL93848.1" FT /translation="MIFDYPTLKLIWWLLVGVLLIGFAIMDGHDMGVGTLLPFVGRNDE FT ERRVIINTVGPHWDGNQVWFITGGGAIFAAWPLVYATAFSGFYWAMLAVLWALFFRPVG FT FDYRSKIHHAGWRRTWDWGLFVGGAVPPLIFGVAFGNLLQGVPFHFDANLVPYYTGSFF FT GLLNPFALLTGVVGSAMLTFHGAIYLAHRTEGEIQRRALRAALIFGVLMLAGFSAAGLW FT LAYGDFGYVLVTAPDPAALPNPLTKSAVHAAGAWLANYGRQPATLALPALAYAGGLAAL FT ALAARRRTLAAFVASALALTGVIGTAGVSMFPFVLPSSTVPGASLTVWDAVSSQRTLSI FT MFWATLIFMPLIIAYTGWAYRVMAGKVTAAYIREHEHSAY" FT CDS complement(1326028..1327596) FT /transl_table=11 FT /gene="cydA" FT /locus_tag="azo1232" FT /product="probable cytochrome bd type terminal FT oxidase,subunit I" FT /function="Cytochrome bd-type quinol oxidase subunit 1" FT /note="Probable cytochrome bd type terminal oxidase,subunit FT I. Homology to cydA of A. vinelandii of 67% FT (sprot|CYDA_AZOVI). Cytochrome bd type terminal oxidases FT catalyse quinol dependent, Na+ independent oxygen uptake. FT Members of this family are integral membrane proteins and FT contain a protoheame IX center B558. It may play an FT important role in microaerobic nitrogen fixation. InterPro: FT Cytochrome bd ubiquinol oxidase subunit I (IPR002585) Pfam: FT Bacterial cytochrome ubiquinol oxidase no singal peptide 9 FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4U4" FT /db_xref="InterPro:IPR002585" FT /db_xref="UniProtKB/TrEMBL:A1K4U4" FT /protein_id="CAL93849.1" FT /translation="MVTDQLVDLSRLQFAATAMYHFLFVPLTLGMVWLLVIMESAYVMT FT GKPVYKDMTRFWGKLFGINFALGVTTGITLEFQFGTNWAYYSHYVGDVFGAPLAIEGLM FT AFFLESTFIGLFFFGWDRLSRRQHLLVTLLMAVGTNLSALWILIANGWMQHPVGAEFSY FT ETMRMELTDFWAVVFNPVAQGKFVHTVSAGYVTGAMFVLSVSAYYLLRRRDVEFAKRSF FT RIAAAFGFASICSVIVLGDESGYALGEAQQTKLAAIEAMWETEPAPASFNLIALPNDAA FT MRNDFALHVPWLMGLIGTRSVDKTLPGLKEILARNRERVVSGTEAVKLLDALRRSPDDA FT ALRSRFAAVQGDLGFGLLLRKYVADVNDATPALIDQAARDTLPRVAPLFWTFRAMVGLG FT FAMLVLFGLALWHSVRGDFARRPGLLKWALWFLPAPWIACEMGWFVAEYGRQPWTIYGV FT LPTHLSVSTLTVESLYGSLAGFVGFYTVLLVVELYLMVKFARQGPGSLGTGRYANEAHP FT AALPA" FT CDS complement(1327586..1327813) FT /transl_table=11 FT /locus_tag="azo1233" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. no homology to to the FT data bank. no domains predicted. no signal peptide. 1 TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K4U5" FT /protein_id="CAL93850.1" FT /translation="MHTTDRRLVRELVLIVLLKLALLAGLWFAFVREARVAVDGAAMGG FT HVLAAPAGVHPAPHPTPNPNRTIPGEPDGH" FT CDS 1327954..1329348 FT /transl_table=11 FT /locus_tag="azo1234" FT /product="probable transcriptional regulator" FT /function="Transcriptional regulator containing PAS FT AAA-type ATPase and DNA-binding domains" FT /note="Probable ranscriptional regulator," FT /note="Specificity unclear" FT /db_xref="GOA:A1K4U6" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR002078" FT /db_xref="InterPro:IPR002197" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K4U6" FT /protein_id="CAL93851.1" FT /translation="MASIPPWMAVMCPDARSLPELVSFLETLPEPHILCDRDYRIVAAN FT AAYRASCAGGGEVIGRTCYEVSHRYSVPCDRAGESCPLARSLASGQRERVLHLHHTPRG FT EDYVNIELSPLRDASGEIAWFIEKMEPLAVARGEAGGHGLIGRAPAFQRMLELVMRVAP FT AEASVLLQGESGTGKELVAAAVHRASRRAERPFVVVDCSGLPETLFESELFGHERGAFT FT GAVSRKPGLVEAAAGGTLFLDEVGDIPLGMQVKLLRLLETGTYRRVGATELRRADVRLV FT SATHRPLQRMVREGAFRQDLYFRINTFPITVPALRERVEDLPLLVDSLLERVAPRRGLT FT VSAAAMRVLAAYPFPGNVRELRNVLERASLMCDGEVIGPAHLAEEVRAPGGPAVDDDAL FT LAPAAEPPLDLAEVQRQTLLRAARSHRGSRRELARKLGLSERTLYRRLRALSADEDSAL FT PEQDSD" FT CDS 1329607..1330194 FT /transl_table=11 FT /gene="petA2" FT /locus_tag="azo1235" FT /product="probable ubiquinol-cytochrome C reductase FT iron-sulfur protein" FT /function="Rieske Fe-S protein" FT /note="Ubiquinol-cytochrome C reductase iron-sulfur FT protein. Homology to petA of R. gelantinosus of 60% FT (trembl|Q93SY7). Component of the ubiquinol-cytochrome c FT reductase complex (complex III or cytochrome b-c1 complex) FT which is a respiratory chain that generates an FT electrochemical potential coupled to ATP synthesis. Pfam: FT Riedke [2Fe-2S] domain no TMHs signal peptide" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4U7" FT /db_xref="InterPro:IPR005805" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR006317" FT /db_xref="InterPro:IPR014349" FT /db_xref="InterPro:IPR017941" FT /db_xref="InterPro:IPR019470" FT /db_xref="UniProtKB/TrEMBL:A1K4U7" FT /protein_id="CAL93852.1" FT /translation="MSATCQDRRLLLLATSGAGAVAAAATAVPFVASLTPSARARASGA FT PVEVDVGKLPAGEMMTVEWRGKPVWILHRDAAMLAALEAHAARLADAGSAVTQQPDYAR FT NAHRSIRPEFLVVVGICTHLGCSPSEKFAAGAAAGMPADWPGGFLCPCHGSTFDLAGRV FT FLGQPAPTNLEVPPHAWLSDTLLRIGEAEDSA" FT CDS 1330265..1332022 FT /transl_table=11 FT /locus_tag="azo1236" FT /product="ABC transporter permease and ATP-binding protein" FT /function="ABC-type multidrug transport system ATPase and FT permease components" FT /note="ATP-binding cassette (ABC) transporters form a large FT family of proteins responsible for translocation of a FT variety of compounds across biological membranes. They are FT composed of two transmembrane domains responsible for FT binding and transport and two nucleotide-binding domains FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the TMDs. Similar to FT TREMBL:Q88H94 (52% identity); TREMBL:Q9RXZ1 (29% identity); FT SWISSPROT:Q9WYC4 (25% identity). Pfam (PF00664): ABC FT transporter transmembrane region. Pfam (PF00005): ABC FT transporter. TMHMM reporting six transmembrane helices. TC FT (3.A.1): The ATP-binding Cassette (ABC) Superfamily." FT /note="Family membership" FT /db_xref="GOA:A1K4U8" FT /db_xref="InterPro:IPR001140" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR011527" FT /db_xref="InterPro:IPR017871" FT /db_xref="InterPro:IPR017940" FT /db_xref="UniProtKB/TrEMBL:A1K4U8" FT /protein_id="CAL93853.1" FT /translation="MLQSHAVAATSTRLAAVPSAPAAHAAAPARELAWLYGFVRPQRGA FT IAGLMALSLLASALALLQPWLTKLLIDDGLLAGDRRALLLIAAAMIVAGLAGTLLAGAN FT RLLHTRLSGRILFALRSDLYGHLQTLSPAFYARQRLGDLIARLDGDVAEIQRFAVDSLF FT AALSSVLGLVGTVALMLTLSWKLSLLLLVLVPLEVLWLRRMRRRLEGEVRATRERAADV FT SSFLVETLPAMKFIQASGQQARERQRLDALGVRYLDDLLRLQRSEFLTAAVPGTLTSWT FT RAAAFLVGGWWVIDGDWQLGALIAFSTYLGMATGPVNTLLGLYVAVRRMRVSLARVGEL FT RAAAADVRDAGGAPLFAPRGELRLEGVGFRHRDRADVVLADAEALIPAGAKVALSGPSG FT VGKSTLIDLLQRHYDPDTGTLRLDGRDLRSLALGDLRRAVAVVSQDIVLFRGTLADNIR FT YAAPDAADDAVRAAARRARLDELIAALPAGLDTPLGERGQQLSGGQRQRIAIARALLQN FT PCVLILDEATSAVDEATEAQVIAAVDELFAARTRIYVSHRATTLAGCELHLVLEQGGRL FT RCASPGAAA" FT CDS 1332019..1332723 FT /transl_table=11 FT /gene="subC" FT /locus_tag="azo1237" FT /product="Subtilisin" FT /EC_number="3.4.21.62" FT /note="Subtilisin Savinase precursor, 36% identity to FT SwissProt; P29600. Has PF00082, Subtilase family;IPR000209, FT Pept_S8_S53;Subtilases are a family of serine proteases. FT They appear to have independently and convergently evolved FT an Asp/Ser/His catalytic triad, like that found in the FT trypsin serine proteases (see Trypsin). Structure is an FT alpha/beta fold containing a 7-stranded parallel beta FT sheet, order 2314567. PROSITE;) PS00136; SUBTILASE_ASP; 1. FT PS00137; SUBTILASE_HIS; 1. PS00138; SUBTILASE_SER; 1." FT /db_xref="GOA:A1K4U9" FT /db_xref="InterPro:IPR000209" FT /db_xref="UniProtKB/TrEMBL:A1K4U9" FT /protein_id="CAL93854.1" FT /translation="MNAPPQGPLRLRVGIVDSGCGAAHPLAAAAAFVLTPDGVHQAAAQ FT PDRLGHGSRVADIVAHLAPSAALCIAQVFDARPATSALQVAAAIDWLVAQGARVINLSL FT GLRAPRAQLADACARALAAGCVLCASAPALGAAVYPAAFDGVLRVTGDARCGRGEFSAL FT ASAQADFGACVHPLDAAFRASGASMGCAHLSGHIAAHLAGGGDAAPAALRAWLGAQARY FT GPQRPGSPGDAR" FT CDS 1332713..1334038 FT /transl_table=11 FT /locus_tag="azo1238" FT /product="conserved hypothetical secreted protein" FT /function="Dehydrogenases (flavoproteins)" FT /note="Conserved hypothetical secreted protein. Homology to FT ebA2217 of Azoarcus sp. EbN1 of 32% FT (gnl|keqq|eba:ebA2217(KEGG)). C-terminus is not homolog to FT COG0644. signal peptide present. no TMHS." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4V0" FT /db_xref="InterPro:IPR003042" FT /db_xref="InterPro:IPR006905" FT /db_xref="UniProtKB/TrEMBL:A1K4V0" FT /protein_id="CAL93855.1" FT /translation="MRARRIAVLGAGPAAIAAAIGLRRAGEDVMLIGEPRRFAAVEGVS FT ARVLEALRRAGFSRALACFAAPSRRCATWNGTLTQANWESLVERERFDRAALEDARAAG FT VRVVVGRALDVRTTAAGHQIHVEGEGGAECEADFLIEARGRAAPGLGMPRMRGAETVSL FT LQYWQGPRGAVHSAVESCADGWMWMAALADGRRYLQLTLDVAGAALPPKAELGAFCRAR FT FAASAAAAPFVRDAQPVGEPCARTSTPVLHGELAGENWLRVGDAAAAVDPLSGNGIFLS FT LSSALQAPAVVGTLLHDPARAALAQRFHRERVAHLFYRFARIGRDFYAQEQRWLHSPFW FT QARRGWPDDLPAEGDAAGGGARIERRPVVAHGRVVEDEVVVTAAQPLGIWHLDGIGLAP FT LLRAVQGAAPAAAEAALRAELGGEGARAARIAAWMREQGWIA" FT CDS 1334490..1336076 FT /transl_table=11 FT /gene="qhpA" FT /locus_tag="azo1239" FT /product="probable quinohemoprotein amine FT dehydrogenase,alpha subunit" FT /EC_number="1.4.99.3" FT /note="Probable quinohemoprotein amine dehydrogenase,alpha FT subunit. Homology to qhpA of P.putida of 50% FT (gi|18655859|pdb|1JMZ|A(PDB (RCSB))). Quinoproteins are a FT class of amine-oxidising enzymes that catalyse the FT oxidation of biological amines, using quinone as a redox FT cofactor to store reducing equivalents. Quinohemoprotein FT amine dehydrogenase (QH-AmDH) from bacteria represents a FT new class of quinoproteins that contains both quinone and FT one or two hemes as redox active groups. The presence of FT extra redox active groups allows for intramolecular FT electron transfer. QH-AmDH is a heterotrimeric enzyme FT containing alpha, beta and gamma chains encoded by separate FT genes. The alpha chain makes contact with both the beta and FT gamma chains. The small gamma chain forms three intra-chain FT cross-links via thioester bonds between cysteine and FT aspartic or glutamic acid residues, thereby encaging the FT cysteine tryptophylquinone cofactor. The largest chain, FT alpha, contains two heme c groups. The alpha chain is FT folded into four domains, domain 1 forming a diheme FT cytochrome. Domains 2, 3 and 4 are antiparallel beta-barrel FT structures. Has PF00034, Cytochromes c (cytC). Interpro FT (IPR009111) Quinohemoprotein amine dehydrogenase, alpha FT chain, domain 3. Signal peptide present. No TMHs." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4V1" FT /db_xref="InterPro:IPR009056" FT /db_xref="InterPro:IPR009111" FT /db_xref="InterPro:IPR013783" FT /db_xref="InterPro:IPR014756" FT /db_xref="InterPro:IPR015182" FT /db_xref="InterPro:IPR015183" FT /db_xref="InterPro:IPR015184" FT /db_xref="InterPro:IPR023887" FT /db_xref="UniProtKB/TrEMBL:A1K4V1" FT /protein_id="CAL93856.1" FT /translation="MKMKSMARLLGTGMAALGIALGAAPAGAAGDALIAEKCLVCHADA FT QGGSGRIAQQRKTPEGWLMTVARMQLTHGLQVTDAERREIVKYLADTQGLAPSESAGAR FT YAIERRLNTVEQFESAEFTQMCARCHSGARVLLQRRTASEWEHLIHFHLGQFPTAEYQA FT LGRDRDWFGVALKDIAPMLARTQPFESAAWKQWRARAPQAVAGEWSVSGRMAGRGAFTA FT TMRVAPAAGKDQYTLALAGRWDDGAPLQGEGAAVIYTGYEWRADLQLDGQPMRQVFALD FT KGVLRGRMFLRDQDEVGADVVAGRVEGGAARVLAVHPAHLRSGEETELRIVGTGLDGAV FT RLPAGVRTLKVVARTPTEVVLRVRAEAGAQGVHPVAVGKARGASLALYDRIAAVKVVPA FT FAVARIGGNGTPSPKVEGRFEAEAWAAGRDGKPGTADDYRIGIVPAKWSVAPHDEVAAR FT DEDVRFAGVMQPDTGIFVPGGAGPNPARRMSANNVGNLKVVAEVVQGGERVQGEGHMIV FT AAQRWNNPPLP" FT CDS 1336144..1337574 FT /transl_table=11 FT /gene="qhpX" FT /locus_tag="azo1240" FT /product="conserved hypothetical qinohemoprotein amine FT dehydrogenase, unknown subunit" FT /function="Arylsulfatase regulator (Fe-S oxidoreductase)" FT /note="Conserved hypothetical qinohemoprotein amine FT dehydrogenase, unknown subunit. Homology to P. putida of FT 71% (gi|16950513|dbj|BAB72009.1|(NBCI ENTREZ)). FT InterPro:IPR000385; MoaA_NifB_PqqE. IPR007197; Radical_SAM. FT Pfam:PF04055; Radical_SAM. No signal peptide. No TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4V2" FT /db_xref="InterPro:IPR000385" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR023404" FT /db_xref="InterPro:IPR023885" FT /db_xref="InterPro:IPR023886" FT /db_xref="UniProtKB/TrEMBL:A1K4V2" FT /protein_id="CAL93857.1" FT /translation="MAAVLNLIHHNLHEVRVDDTRMLFHIPSSSLFALDELTAAVIDRI FT RRDSLTAEALVAGLRPRFAAAAVSEALDELAALELVSDGRPRAEAAALRAPAQFPLSTV FT VLNVNTGCNLSCTYCYKEDLDTPSAGRKMSLDTARASIELLLRESPDEPRYTVVFFGGE FT PLSNLPLIKAVVEYCEARFAGLGKVVDFVMTTNATLLNDDTIAWLDAHRFGLSVSMDGP FT EAIHDRNRRTVGGHGTYRTVSDKAGRLLARYRSRPVGARVTLTRGTTEVERIWDHLFNE FT LGFAEVGFAPVTAGDIETFNLTGEELAEVFAAFKRLGRRYLDAALAGRNIGFSNLHQLI FT TDLHEGHKKSLPCGAGLKMLAVDHQGGLNLCHRFTGSALPTFGDVTSGVRHQQLGDFLA FT QRLDRSGTGCESCRIRNLCAGGCYHESYARYGDPAHPTYHYCELMRDWVDFGIEVYSRI FT MAGNPAFIEQHISPRRAN" FT CDS 1337576..1337902 FT /transl_table=11 FT /gene="qhpC" FT /locus_tag="azo1241" FT /product="probable quinohemoprotein amine FT dehydrogenase,gamma subunit" FT /note="Probable quinohemoprotein amine dehydrogenase,gamma FT subunit. Homology to qhnDH of P. putida of 54% FT (sprot|QADG_PSEPK(SRS). Quinoproteins are a class of FT amine-oxidising enzymes that catalyse the oxidation of FT biological amines, using quinone as a redox cofactor to FT store reducing equivalents. Quinohemoprotein amine FT dehydrogenase (QH-AmDH) from bacteria represents a new FT class of quinoproteins that contains both quinone and one FT or two hemes as redox active groups. The presence of extra FT redox active groups allows for intramolecular electron FT transfer. QH-AmDH is a heterotrimeric enzyme containing FT alpha, beta and gamma chains encoded by separate genes. The FT alpha chain makes contact with both the beta and gamma FT chains. The small gamma chain forms three intra-chain FT cross-links via thioester bonds between cysteine and FT aspartic or glutamic acid residues, thereby encaging the FT cysteine tryptophylquinone cofactor. The largest FT chain,alpha, contains two heme c groups. The alpha chain is FT folded into four domains, domain 1 forming a diheme FT cytochrome. Domains 2, 3 and 4 are antiparallel beta-barrel FT structures. no domains predicted. no signal peptide. no FT TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4V3" FT /db_xref="InterPro:IPR015084" FT /db_xref="UniProtKB/TrEMBL:A1K4V3" FT /protein_id="CAL93858.1" FT /translation="MKHLKAINQKARLLEQAAGEGRAEEVVAMSAVVGCTATVDPGWEV FT DAFGGVGSLCQPMEADLYGCADPCWWPAQVPDVMNTYPDWGKDAPDLTQDWRKLGSVFP FT GDKR" FT CDS 1337920..1339065 FT /transl_table=11 FT /gene="qhpB" FT /locus_tag="azo1242" FT /product="probable quinohemoprotein amine dehydrogease,beta FT subunit" FT /function="uncharacterized conserved protein" FT /note="Probable quinohemoprotein amine dehydrogenase,alpha FT subunit. Homology to qhpB of P.putida of 50% FT (gi|34809688|pdb|1PBY|B(PDB (RCSB))). Quinoproteins are a FT class of amine-oxidising enzymes that catalyse the FT oxidation of biological amines, using quinone as a redox FT cofactor to store reducing equivalents. Quinohemoprotein FT amine dehydrogenase (QH-AmDH) from bacteria represents a FT new class of quinoproteins that contains both quinone and FT one or two hemes as redox active groups. The presence of FT extra redox active groups allows for intramolecular FT electron transfer. QH-AmDH is a heterotrimeric enzyme FT containing alpha, beta and gamma chains encoded by separate FT genes. The alpha chain makes contact with both the beta and FT gamma chains. The small gamma chain forms three intra-chain FT cross-links via thioester bonds between cysteine and FT aspartic or glutamic acid residues, thereby encaging the FT cysteine tryptophylquinone cofactor. The largest chain, FT alpha, contains two heme c groups. The alpha chain is FT folded into four domains, domain 1 forming a diheme FT cytochrome. Domains 2, 3 and 4 are antiparallel beta-barrel FT structures. Interpro (IPR0011044) Quinoprotein amine FT dehydrogenase, beta chain-like. Signal peptide present. No FT TMHs.," FT /note="High confidence in function and specificity" FT /db_xref="InterPro:IPR011044" FT /db_xref="InterPro:IPR015943" FT /db_xref="InterPro:IPR023879" FT /db_xref="UniProtKB/TrEMBL:A1K4V4" FT /protein_id="CAL93859.1" FT /translation="MAHTTPALRCAALLATLAAALPAAAQNAPTALNTDRALQSGHEYL FT VVANRPNNLHVVDLQSNTLYKTCPLPDAFGPGTAQISPDRRTAYILNNRFEDIYGIDLD FT TCEVRFRAHMAQADNERAKAIFSFAISADGKSLYAVQNPTTLHRDHYRVGEPRFVVYDT FT AAGLDAKPVRSFPAPRQATVMQAALDGSGAVYMAGANLYRVDPATGTFTTTLPIRDWQR FT PGYAPPDVLYAWPIQTPTKDFTLLYTTARVADASKPESAEYRYGLLNVNLQTGEAEAPE FT FGPLTEIYFSGVRWPKDRNIMFGLLHRLAKYDIKAQKLLEAVELEHTYYALLTNASGSR FT LYLTGTFNDIAVYDAETLKKVTNVQLPGGDMSLGTGQVFMR" FT CDS complement(1339138..1340523) FT /transl_table=11 FT /locus_tag="azo1243" FT /product="conserved hypothetical N-acetylmuramoyl-L-alanine FT amidase" FT /function="N-acetylmuramoyl-L-alanine amidase" FT /EC_number="3.5.1.28" FT /note="Conserved hypothetical N-acetylmuramoyl-L-alanine FT amidase. Homology to amiC of R. solanaceraum of 50% FT (trembl|Q8XWD5) CELL-WALL HYDROLASE PROBABLY INVOLVED IN FT CELL-WALL HYDROLYSIS SEPTATION OR RECYCLING (BY FT SIMILARITY). Pfam: N-acetylmuramoyl-L-alanine amidase no FT signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4V5" FT /db_xref="InterPro:IPR002508" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR021731" FT /db_xref="UniProtKB/TrEMBL:A1K4V5" FT /protein_id="CAL93860.1" FT /translation="MRDRTDQPAAPGADDAARLNDSDDLPAPRRRLSRRELLKFSGAAL FT TLLVTRTGHAAASLLAVRVWPAEEYTRITLEGTAEPRFTHMLVKDPERLVVDLEGVELN FT SVLQSLPSKVLDSDPYIRLIRAGQNRPGVVRVVIELKAEINPQVFTLQPVGDYRHRLVL FT DLYPTQPADPLLALIQKPSPMDAAAGDSGSGAQQPTRDTRATTPQQDAQQTARRNAPKV FT NRLFTVVLDPGHGGEDPGAVGRAGSYEKNVTLSIGRRLKRKIDADPNMRAVLTRDDDFF FT VPLAQRVTRARKVQADLFVSIHADAFVRPEARGSSVFVLSESGASSSAARWLAQKENDA FT DLIGGVNLAKQDGHLARTLLDLSQTATINDSLKLGKAVLSELGDINTLHKAHVEQAGFA FT VLKAPDIPSILVETAFISNPEEERRLNDDAYQDKMADAILRGIKRYFEENPPNPRVKVA FT QLG" FT CDS complement(1340466..1340987) FT /transl_table=11 FT /locus_tag="azo1244" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein having FT uncharacterised P-loop hydrolase, 47% Identity to FT TrEMBL;Q82WL4,Q63WN1. Has PF02367, Uncharacterised P-loop FT hydrolase UPF0079;IPR003442; This signature is found in a FT family of bacterial proteins, which contain a P-loop." FT /db_xref="InterPro:IPR003442" FT /db_xref="UniProtKB/TrEMBL:A1K4V6" FT /protein_id="CAL93861.1" FT /translation="MISIVHAAHDSEAQLDLPAEADTLALGAALAGVVRAGLHVWLQGD FT LGSGKTTLTRGLLRALGHEGKVKSPTYTLIEPYALSRLDLYHFDFYRFNAPEEYLDAGL FT DEYFAGDGVCIVEWPDKALPYLPAPDLELRLDRAGEGRRASITAHSEPGRTCVIELTSL FT LRQGRTTPPA" FT CDS 1341000..1342058 FT /transl_table=11 FT /locus_tag="azo1245" FT /product="conserved hypothetical electron transport FT protein" FT /function="uncharacterized Fe-S protein" FT /note="Conserved hypothetical electron transport protein. FT Homology to pa4950 of P. aeruginosa of 63% (trembl|Q9HUL4). FT Pfam: 4Fe-4S- binding domain Tigrfam: TIG00276: iron-sulfur FT cluster binding protein, putative no TMHs no signal peptide FT TIGR00276: iron-sulfur cluster binding pr" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4V7" FT /db_xref="InterPro:IPR004453" FT /db_xref="InterPro:IPR011989" FT /db_xref="InterPro:IPR013542" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K4V7" FT /protein_id="CAL93862.1" FT /translation="MTGADAEHLAGLVQRIREWGKALGFSAVTIGGVDLADAEPGLMDW FT LAAGFHGEMDYMARHGLKRARPAELLPGTLRVISARMDYLPDAADARAALDDPARAYVS FT RYALGRDYHKVLRKRLQQLADRIAAEVPHGYRVFVDSAPVLEVELASRSGAGWRGKHTL FT LLDRTGSWFFLGELFTDLPLPVDAPVQPHCGSCSACIGACPTGAIVAPYQVDARRCISY FT LTIELQGAIPEALRPLLGNRIYGCDDCQLACPWNRFAQLSAEPDFAPRHRLDEATLCEL FT FAWSAEDFATRTAGSAIHRIGHERWLRNIAVALGNAPATPEVIAALRSRADDESALVRE FT HVAWALAQHGVG" FT CDS complement(1342145..1343311) FT /transl_table=11 FT /locus_tag="azo1246" FT /product="conserved hypothetical mandelate racemase" FT /function="L-alanine-DL-glutamate epimerase and related FT enzymes of enolase superfamily" FT /EC_number="5.1.2.2" FT /note="Conserved hypothetical mandelate racemase. Homology FT to bll6730 of B. japonicum of 76% (trembl|Q89FH0) Mandelate FT racemase and muconate lactonizing enzyme are two bacterial FT enzymes involved in aromatic acid catabolism. They catalyze FT mechanistically distinct reactions yet they are related at FT the level of their primary, quaternary (homooctamer) and FT tertiary structures. InterPro: Mandelate racemase/muconate FT lactonizing enzyme family (IPR001354) Pfam: Mandelate FT racemase/muconate lactonizing enzyme, N-terminal domain; FT Mandelate racemase/muconate lactonizing enzyme, C-terminal FT domain" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4V8" FT /db_xref="InterPro:IPR001354" FT /db_xref="InterPro:IPR013341" FT /db_xref="InterPro:IPR013342" FT /db_xref="UniProtKB/TrEMBL:A1K4V8" FT /protein_id="CAL93863.1" FT /translation="MKIIDIREVTKPIKSNIRNAYIDFSKMTLSLVAVVTDVIRDGKPV FT IGYGFNSNGRYGQGSLIRERFRPRLLEAAPETLINDAGDNLDPHRIWATMMTNEKPGGH FT GERSVAVGTIDMAVWDAVAKIAGKPLYQLLAEQYGNGTPDRKVFVYAAGGYYHPGQDLE FT ALKNEMRGYLDRGYKVVKKKIGGAPLAEDLRRIEAILSILPAGCKLAVDANGRFDLPTA FT VEYAKALSQYDLFWYEEAGDPLDYALQAELANHYEGPMATGENLFSMQDARNLIRYGGM FT RADRDWLQFDCALSYGLVEYLRTLEMLKENGWSPSRCIPHGGHQMSLNIAAGLGLGGNE FT SYPDLFQPYGGFPDGVKVVDSVIEMPELPGIGFEGKSDLIAEMRALAS" FT CDS 1343604..1344530 FT /transl_table=11 FT /locus_tag="azo1247" FT /product="putative transcriptional regulator, LysR family" FT /function="Transcriptional regulator" FT /note="Transcriptional regulator, LysR family This protein FT activates the transcription of the lysA gene encoding FT diaminopimelate decarboxylase. LysR is also a negative FT regulator of its own expression. 29% 1 helixturnhelix FT PF03466 LysR_substrate; 1. HTH reporting nucleic acid FT binding motif" FT /note="Specificity unclear" FT /db_xref="GOA:A1K4V9" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K4V9" FT /protein_id="CAL93864.1" FT /translation="MDAVASELAFFLLLADKGSFTAAARELNLTPPAVSKRLAQIEQRL FT GVRLLNRSTRRVSLTDEGELYLEHARRIVADIEDMEASLGSRRAAPKGLLRVNATLGFG FT RTTIAPIVSAFARQHPEVEVQLQLTDAPIDLVATGFDLAIRFGELPDSRLSARKLMSNR FT RFLCASPAYLDAHGTPQTPAELARHACILHRQNDDAYGIWRLARGRHVETVKVRGTLSS FT NDGDVVLGWALDGHGILIRSEWDLAKYLESGRLRAVLPDYTLPTADLYAVYPARRNQPA FT RVRAFIDFLLARFAPAGGAPGAQLSSV" FT CDS 1344671..1345414 FT /transl_table=11 FT /gene="nifY2" FT /locus_tag="azo1248" FT /product="NifY protein" FT /function="unknown" FT /note="NifY-like protein. Homology to Daro03003760 of FT Dechloromonas aromatica of 65% FT (gi|46140358|ref|ZP_00203574.1|(NBCI ENTREZ)). Pfam: FT Dinitrogenase iron-molybdenum cofactor. This family FT contains several NIF (B, Y and X) proteins which are FT involved in the synthesis of an iron-molybdenum cofactors FT (FeMo-co) in the dinitrogenase enzyme which catalyses the FT reduction of dinitrogen to ammonium. No signal peptide FT predicted. No TMHs." FT /note="Family membership" FT /db_xref="InterPro:IPR003731" FT /db_xref="UniProtKB/TrEMBL:A1K4W0" FT /protein_id="CAL93865.1" FT /translation="MQQSQAPITRDAALRVALAARAMPGITLPQLIDVLQNRIGSDQID FT VDELRTVTVTDLKTAFASADGEEDGEDIGIGLEAMKLAVRILWGDTEGEVLPEVLPYND FT GDMPGSVRVALASDSGEALNGHFGSCVRYLVYQVSATDTRLVGIRDALEADFAEDKNGF FT RVQLISDCHVLYVVSVGGPAAAKVIKGGIYPIKRIQGGEAAEVLAEFQQMMTDSPPPWL FT AKILGVAAGQRLKNYNAELVEDQAE" FT CDS 1345528..1345794 FT /transl_table=11 FT /locus_tag="azo1249" FT /product="hypothetical protein predicted by FT Glimmer/Critica" FT /note="Hypothetical protein predicted by Glimmer/Critica. FT No homology to the data bank. No domains predicted. No FT signal peptide No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K4W1" FT /protein_id="CAL93866.1" FT /translation="MADKDYHAIITDLIANAIKTSKVAGENGRITRLVAGSIGRFAAEL FT KVGKQEDEAAALIEHARELLDAGDGAEVVPALTAAVAAMAVTR" FT CDS 1345875..1346084 FT /transl_table=11 FT /locus_tag="azo1250" FT /product="Conserved Hypotheitcal protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved Hypotheitcal protein. Very strong FT consideration to be a homolog for SlyX protein. TrEMBL: FT Q7WMX4, 32% identity. Has PF04102|SlyX;(IPR007236):The SlyX FT protein has no known function. It is short less than 80 FT amino acids and is found close to the slyD gene. The SlyX FT protein has a conserved PPH(Y/W) motif at its C-terminus. FT The protein may be a coiled-coil structure. No Signal FT peptide present. No TMH present." FT /note="Family membership" FT /db_xref="InterPro:IPR007236" FT /db_xref="UniProtKB/TrEMBL:A1K4W2" FT /protein_id="CAL93867.1" FT /translation="MEDSAERIERLEAKLMLAEDLLDELNRTVYRQQQQIDLLQQHLRQ FT LAQQVQSGMPAARLRPEDEIPPHY" FT CDS complement(1346107..1348047) FT /transl_table=11 FT /locus_tag="azo1251" FT /product="conserved hypothetical peptidase" FT /function="Collagenase and related proteases" FT /note="Conserved hypothetical peptidase. Homology to cv0266 FT of C. violaceum of 58% (cvi:CV0266). InterPro: Peptidase FT family U32 Pfam: Peptidase family U32 no signal peptide no FT TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4W3" FT /db_xref="InterPro:IPR001539" FT /db_xref="InterPro:IPR020988" FT /db_xref="UniProtKB/TrEMBL:A1K4W3" FT /protein_id="CAL93868.1" FT /translation="MIHHRKVLELLAPAKTADIGIEAINHGADAVYIGGPSFGARSAAE FT NTVADIARLCTHAHRYRAKIFVALNTILRDDELEAARQLVWQVYEAGADALIVQDMGLL FT ELDLPPIQLHASTQTDIRDAAKARFLQDVGFSQIVLARELTLQQVQKIAAATDCQLEYF FT VHGALCVAYSGQCYISHAHTGRSANRGECSQACRLPYDLADKDGNLVASDQHMLSMKDN FT NQSANLRALAEAGVSSFKIEGRYKDLAYVKNITAHYRVLLDEIIDGSNGEYRRASSGRC FT EFLFTPRPEKTFNRGYTDYFANERQHGIEAFESPKFVGEAIGRVTKIDSRKGRFFEVER FT TEPIHNADGLAYYDPKGDLVGLRINTAEEIADGVDRLFPADPLPPALVPGTAVFRNHDH FT AFERLLEKKSAERRVKVDLRLFDTGDGYGLALADEDGVAVEARVACKREAAQNVERALA FT GLREHLGKLGNTTFSAGDVRLDLAGAPFIPASVINGLRRDACEKLEAARIASHPRPPRA FT APVEPPAPYPQEALSYLANVLNQKAADFYAKHGVKLIDAAYEANLEHDEVSLMITKHCL FT RYSFNLCPKEVKGIRPEPMTLINGKEKLTLRFDCKRCEMHVVGKLKPHAVGLPPVPPAQ FT KLQFFASRPTA" FT CDS complement(1348202..1348510) FT /transl_table=11 FT /locus_tag="azo1252" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT XCC3430 of Xanthomonas campestris of 38% (trembl:Q8P5B1). FT Has PF04892, VanZ like family;IPR006976 ; This family FT contains several examples of the VanZ protein,but also FT contains examples of phosphotransbutyrylases. VanZ confers FT low-level resistance to the glycopeptide antibiotic FT teicoplanin (Te). Analysis of cytoplasmic peptidoglycan FT precursors, accumulated in the presence of ramoplanin, FT showed that VanZ-mediated Te resistance does not involve FT incorporation of a substituent of D-alanine into the FT peptidoglycan precursors. no signal peptide. 2 TMHs." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR006976" FT /db_xref="UniProtKB/TrEMBL:A1K4W4" FT /protein_id="CAL93869.1" FT /translation="MRAAFALALIVVFWLAVQPAPDIVQLFSWQDKAEHALLFAALAAL FT GFAAWPQRAAAVVVGLLAYGAAMEVAQSFTAFRVGDPWDWLADAVGTLAALPLRRRC" FT CDS 1348736..1349905 FT /transl_table=11 FT /locus_tag="azo1253" FT /product="conserved hypothetical protein" FT /function="Glucose/sorbosone dehydrogenases" FT /EC_number="1.1.5.2" FT /note="Similar to the GdhB protein, a putative glucose FT dehydrogenase-B, periplasmic protein [EC:1.1.5.2], from FT Synechocystis. SPTR: P73001. Signal peptide:present" FT /db_xref="GOA:A1K4W5" FT /db_xref="InterPro:IPR011041" FT /db_xref="InterPro:IPR011042" FT /db_xref="InterPro:IPR012938" FT /db_xref="UniProtKB/TrEMBL:A1K4W5" FT /protein_id="CAL93870.1" FT /translation="MTATFSRLALAAFAAALVFAPHPAQPPAGAQPAPVVPANPMLRVT FT EVARGLENPWSLAFLPDGRMLVTERPGRMRLVAANGELSPPLAGVPAVQARGQGGLLDV FT VLAPDFASSRQIFFSFTQPTAGGARTAVASALLDFPGNRLTDVRVIFAQRDDPPGGNHW FT GSRLVFARDGTLFVTLGDRFDHRDRAQDLGSHLGKIVRIRSDGSVPPDNPFVGRPGVLP FT EIWSYGHRNVQGAALHPITGELWITEHGPQGGDELNRVLPGRNYGWPVITHGREYVSGF FT RIGDGTTRADVEPSVLQWTPSIAPSGLAFYTGDAYPEWKGNLFAGALKFRLLTRLELDG FT NTVRREERLLNDPGIRIRDVRQGPDGRLWLLDDGDGRVLRLDIVRPATR" FT CDS complement(1349902..1351638) FT /transl_table=11 FT /locus_tag="azo1254" FT /product="conserved hypothetical signaling protein" FT /function="FOG: GGDEF domain" FT /note="Conserved hypothetical signaling protein. Homology FT to Bcep02001865 of Burkholderia fungorum of 44% FT (gi|48787085|ref|ZP_00283167.1|(NBCI ENTREZ)). InterPro: FT IPR003660 HAMP. IPR000160 GGDEF. Pfam: PF00672 HAMP. FT PF00990 GGDEF domain. TIGRFAM:TIGR00254 putative FT diguanylate cyclase (GGDEF) domain. Signal P reporting FT signal peptide. TMHMM reporting 1 transmembrane helices (in FT signal peptide)." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4W6" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR003660" FT /db_xref="UniProtKB/TrEMBL:A1K4W6" FT /protein_id="CAL93871.1" FT /translation="MSTALRGSLGLKFSVLLAGFALLAGGLTGYSTYAASRRMLVEAAE FT HAQLTATQVLARRFSAAVAEAADDALQLAQQPLAERLATAGDAAGEADAGLLAEQFEAL FT LDVNPEYFQIRLISAGLNGLELVRVDRAEERVTRVAPAELQEKGHYPYVFKTLALGKGQ FT VYLSDIAINHERGAHAGLGQPSLVVATPVRGRDMRTLGLVVINLSLDNLFALLRRDLPD FT SYEVYLANQGGDFLVHPDTGKTFGFEQGRRILVQDSFAATDAIVHGSATQVVAAPARSA FT SGQPVVASFVRHPYGHDGRQFVVFGLTQPLEDVLRESRSLRTTVVESVLLFSLLAVLLA FT AVTSRAVTRPLQRMLAAIRQFPDEAAVRALPLARTDEIGVLARSFRDMQAQIRAYLDDL FT HDSRAELARQASHDALTGLANRRHFEERLEQALARCRRNGQSLALIYIDLDGFKQVNDR FT HGHATGDKLLQAVARRLQQAVREIDTVARLGGDEFVILFDQVSSHESVVLIAEKLLLML FT RMPVEIDALTLPVRASIGISMYPDDAPDAHALLNHADCAMYRAKTHGRDSYRFFGATGD FT GA" FT CDS complement(1351635..1352795) FT /transl_table=11 FT /gene="potD" FT /locus_tag="azo1255" FT /product="bacterial extracellular solute-binding protein" FT /function="Spermidine/putrescine-binding periplasmic FT protein" FT /note="Bacterial high affinity transport systems are FT involved in active transport of solutes across the FT cytoplasmic membrane. Similar to trembl|Q986V8 (37%). Pfam FT (PF01547): Bacterial extracellular solute-binding protein" FT /note="Family membership" FT /db_xref="GOA:A1K4W7" FT /db_xref="InterPro:IPR001188" FT /db_xref="InterPro:IPR006059" FT /db_xref="UniProtKB/TrEMBL:A1K4W7" FT /protein_id="CAL93872.1" FT /translation="MSRRPRRELGHGADLLSNKHIPSDLSSMPLPGNAALLSRASRTRL FT GAVLALVIGLLAATAANAEILRVVTWPGYADRDLVQTFELKHRVRVEVSYVGTDDVLWD FT KLAARGGADFDVFAVNTAELQRYIDGGLAAPVDPARIPNTARQLPRFRDVGAIAGLVRD FT GKVYGIPYTWSAMGLIYDRQRFASPPDSIKVLWDTGFRGQVLAFNGSSHNFSLAAQALG FT LPAPFAIGETDMPAVIDKLLALRRNVLTFYTLPEESVALFREQRVAVMFANYGSQQVQQ FT LREAGINIGYVMPREGAFAWLDCWAISAGARNRRLAEAWINHMLDHAASRALRERQGLA FT NTTDEANAPAAADRIIWLQPVEDVHRRAALWDQILSGDRRVSGRAP" FT CDS 1352950..1355322 FT /transl_table=11 FT /locus_tag="azo1256" FT /product="putative serine/threonine protein kinase" FT /function="Serine/threonine protein kinase" FT /note="Putative serin/threonine protein kinase, only very FT low similarity to SWISSPROT: sprot|PKSC_STRCO (13% FT Streptomyces coelicolor, serine/threonine protein kinase FT PksC (EC 2.7.11.1)) / TREMBL: trembl|Q9S478 (13% Myxococcus FT xanthus, Pkn4). Pfam: PF00069 Pkinase. SMART:SM00221 STYKc FT (Protein kinase; unclassified specificity). SM00065 GAF FT (Domain present in phytochromes and cGMP-specific FT phosphodiesterases)." FT /note="Family membership" FT /db_xref="GOA:A1K4W8" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR003018" FT /db_xref="InterPro:IPR008271" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR013976" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:A1K4W8" FT /protein_id="CAL93873.1" FT /translation="MADRVGRFEIRGELGRGAQSVVYRAFDPQLEREVAVKTLHFTEHK FT PGQNETLLAEARIVSPLRHPGIVPIFEAGEADGDVYLVFEYVRGESLAAHMQREGALPP FT VRAGEILVQILAAVGQAHAEGIIHRDLKPTNVLMDESGAVRVMDFGIACRTAGKGGQAG FT FAGTPSYMAPEYITTREVSERIDVFAAGVIFIELLTGRRLFAGDDVDQVMQRIVARQVV FT LPTDLSLDERVAGIALRAVARDPAERFESAAAFRQALEAWLQPDEAVQSAEARQSTVDF FT LLRRMRHKSDFPALSESVSAINRIASSESESVSKLSVSILRDFSLTNKILRLVNSVAYR FT QAGGGSISTVSRAVIVLGFDTVRNIAITVLLFEHLQNKANASQLKEDFLRANLAGILAR FT DIASKARTRDLEQSFICAIFHNLGRLLTQFYFPEESEEIRRMMAQKSCTEEVAALRVLG FT LSFEDLGIGIARSWGFPTLIVDSMHKLPAGKVRKPATQEDRLRVVSALSNEISTAIATL FT SPEERAKEMQRIAARFAEAQPLDDTELKDAIKHAIEEITEFARIIRINLGQTHFGQQLR FT RYSGGETGGEGGGSDGSMGSAVLEQNRSPALETGNFGEEGRKAADAQAVLTAGIQDISN FT TLVEEFKLNDILRIILETMYRAMGFRRVLLCIRDARSNTMQGRFGFGPEVTELAKQFRF FT TLSFTPDIFHAATSKGVDILISDVDDAKIAERIPAWFRKGVTAKTFVLFPLTIKNAPVA FT LIYADKEHAGEIEITEKELSLLRTLRNQAVLAIKQST" FT CDS 1355479..1356123 FT /transl_table=11 FT /locus_tag="azo1257" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to CV1784 FT of C.violaceum of 40% (tremble:Q7NX45). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K4W9" FT /protein_id="CAL93874.1" FT /translation="MATIPSSLPPPSSTAAERAGGRGAGAARGEGVATLSVAAEVRSQQ FT NNRILQASLEVSISVGNDSQALLFRSAIEKINEMLGTEQVPDALQKAASQDNSPEATAD FT RILSFATGLFASYSTQHPGADQATLAADFVELVRGGFQQGFDEAVDILKGLKVFEGGIA FT EGIQKTYDLVMKGFDDFLASLTGSSGTAAAPEAATAADAADAAGGASSTKT" FT CDS 1356239..1358347 FT /transl_table=11 FT /locus_tag="azo1258" FT /product="hypothetical membrane protein" FT /note="hypothetical membrane protein no homology to entire FT proteins seven transmembrane domains predicted, no signal FT peptide predicted" FT /note="Family membership" FT /db_xref="GOA:A1K4X0" FT /db_xref="InterPro:IPR001096" FT /db_xref="UniProtKB/TrEMBL:A1K4X0" FT /protein_id="CAL93875.1" FT /translation="MALPPDSDPAPQPAPAVVADAPAALHYSLDAATACAAHVLASRRV FT SHRFGGRGGAWLLQLLVWICIGAAAGIAAQGWRTGTAVSVWVLGGLLLGAGLFGAVLRR FT RLFDQLGRTHAAATGNVRLALEADGLHMLSGMGEAWVPWARVVEVAEQTGWVAVTLGPV FT PQVLAVPFAAFPDAAARSRWIAALEARIASACGQSGAHPSAASAAAPRAGSRAGAAVTA FT GEHEGATLPGALGQLGRLLAFRAPRPGALGFSPAVLLGCVVLYAALTLGVQVWEANGEG FT ELWWYEASGLLSPFAAAAIAAALAALVAPGQLPAGRLLVALTLLLLPLPLVGLWAAPEV FT GNFLRALAPGEADGPLMTLMFFLPQAWLLGAAGVVAWRLAAAEPAVRARVALVAVLASG FT ANLWLHNDPPMLWYAAVNEEARPRLNIDERVLYGQPRLLDQALAGLQPGRPGVAELYFL FT GVGGYGQQDVFLREVRTVESLFADRYGTTGRSALLVNNAATVHELPVANAESLGAALRA FT IGARMNHGEDLLFLFLTSHGSRDHRFSLAFWPFRFNDITPEMLRRALDDAGIDQRVVVV FT SACYSGGFIPALADARTLVITAAAADRNSFGCADQNELTDFGRAYFAEALHETRSFTAA FT FELARTRIAERETAEGLTPSLPQMQGGEALNAVLQRLAAPDAAPARAVPVGAAPARREA FT NALSSITH" FT CDS 1358370..1359830 FT /transl_table=11 FT /gene="pepD" FT /locus_tag="azo1259" FT /product="probable aminoacyl-histidine dipeptidase" FT /function="Di- and tripeptidases" FT /EC_number="3.4.13.3" FT /note="Probable aminoacyl-histidine dipeptidase (EC FT 3.4.13.3) (Xaa-His dipeptidase) (X-His dipeptidase) FT (Beta-alanyl-histidine dipeptidase) (Carnosinase) FT (Peptidase D). Homology to pepD of E. coli of 44%. THIS FT DIPEPTIDASE HAS SPECIFICITY FOR THE UNUSUAL DIPEPTIDE FT BETA-ALANYL-L-HISTIDINE. InterPro: Peptidase family FT M20/M25/M40 (IPR002933) Pfam: Peptidase family M20/M25/M40 FT no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4X1" FT /db_xref="InterPro:IPR001160" FT /db_xref="InterPro:IPR002933" FT /db_xref="InterPro:IPR011650" FT /db_xref="UniProtKB/TrEMBL:A1K4X1" FT /protein_id="CAL93876.1" FT /translation="MDLNLLPPAAVWRHFATLCRIPRPSGHEHALREEILGWARQRGLG FT AVVDATGNLILSKPASPGHEDRPGVVLQGHLDMVCQKNAGSAHDFLRDPIRAELRDGWL FT VADDTTLGADNGIGVAMALAVLEADDIAHPALEVLLTVDEEAGMTGARGLQADALRGRL FT LINIDTEDWGEFYLGCAGGADVVVDAVLDTVAAPAGGVALRLTVEGLKGGHSGVDIHLQ FT RGNAIKLLVRALQGLRAAGAGFALATLEGGTARNALPREAQAVIVVDAGDVAPLHEALA FT RIGAEIADELAGVDDGFRLHAGPAPLPARVCADEAGRRALAALHAAPHGVRRLSSRVPG FT VVETSDNLGVVRLAEGRLQATLMVRSLLDAGTRELAAEIVGLFGLAGMAATVSEPYPGW FT APNPRSGLLALFQQVYQREFGGEAAVKVIHAGLECGIFTATWPDMDMISFGPSIRGAHA FT PGERVEVASVERAWRLLVAVLAAVPAAR" FT CDS complement(1359827..1360354) FT /transl_table=11 FT /locus_tag="azo1260" FT /product="conserved hypothetical protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical protein. Homology to RPA1575 FT of R.palustris of 41% (tremble:Q6N9H4). Has FT PF04536:(IPR007621)Domain of unknown function (DUF477);This FT is a family of uncharacterised proteins. They are found in FT both eukarya and eubacteria. No TMHs. No signal peptide." FT /db_xref="InterPro:IPR007621" FT /db_xref="UniProtKB/TrEMBL:A1K4X2" FT /protein_id="CAL93877.1" FT /translation="MNALLRLLRHRWRDADDARRAIGPDALQRLEERITASERQHSGEI FT CLCIEASLPTSYLLRQWRSGVAIEAVVRERALAQFGKLRVWDTELNNGVLIYLQLAEHQ FT IEIVADRGLARHVPPGEWAALVGDMGAAFRAGRYEEGLGRAVDGVGAALARHFPPDAAA FT RENQLPDRPLVG" FT CDS complement(1360403..1361335) FT /transl_table=11 FT /locus_tag="azo1261" FT /product="conserved hypothetical membrane protein" FT /function="Beta-propeller domains of methanol dehydrogenase FT type" FT /note="Conserved hypothetical membrane protein. Homology to FT Bll7266 of B. japonicum of 45% (trembel:Q89E21) FT InterPro:IPR007621; DUF477. Pfam:PF04536; DUF477 Signal FT peptide present (Signal P predicted). Presence of 2 FT transmembrane helices." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007621" FT /db_xref="UniProtKB/TrEMBL:A1K4X3" FT /protein_id="CAL93878.1" FT /translation="MRARPALVHLRSLQWLVACALALALAAMLGALPALAQQLVPVPAL FT TARVIDQTATLAPAERQALEDRLAQFEAERGTQIVVLVVPTTAPEDIAAFAFRVADAWK FT IGRREVGDGLLLVVAKNDRTVRIEVARALEGAVPDLAAFRIIDGIIVPAFRRGDFAGGL FT QGGVDALMRLVRGEDLPLPEPRRAAADKGASLADLAVFLFIGVPVVGGILNTLLGRKLG FT TLATGCATGLLVQLLTGSLLLAVVGGVLALIFVLAMGGGGGGRGGRGGGGFGGPIIWGG FT GRGGGGGFGGGFGSGGGGSFGGGGASGRW" FT CDS complement(1361353..1361979) FT /transl_table=11 FT /gene="lemA1" FT /locus_tag="azo1262" FT /product="conserved hypothetical LemA family protein" FT /function="uncharacterized conserved protein" FT /note="Putative lipoprotein [lemA],57 % identity (75% FT similarity) to TrEMBL;Q72TG3,TrEMBL;Q6N9H6(60% identity). FT No signl peptide or TMH present. Has PF04011:LemA FT family(IPR007156,lemA);The members of this family are FT related to the LemA protein. LemA contains an amino FT terminal predicted transmembrane helix. It has been FT predicted that the small amino terminus is extracellular FT [1]. The exact molecular function of this protein is FT uncertain." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR007156" FT /db_xref="InterPro:IPR023353" FT /db_xref="UniProtKB/TrEMBL:A1K4X4" FT /protein_id="CAL93879.1" FT /translation="MPISLFRLARLAAIAAFAALLSGCGYNDFQRLDEQSKAAWAEVLN FT QYQRRADLIPNLVNTVKGEASFEQETLTRVIEARSRATAIQVTPEMLDDPDAMARFQQA FT QGQLGSALSRLLAVAENYPNLKANQGFQDLRVQLEGTENRITVARNKYIQSIQEYNVLA FT RSFPTNLTAMVFSYKPKAGFTVANEAEISRPPTVDFGTPPAQPAR" FT CDS 1362162..1362374 FT /transl_table=11 FT /locus_tag="azo1263" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="Conserved yhpothetical protein. Homology to BP1565 FT of B.pertussis of 66% (tremble:Q7VY02) Has PF07311:Protein FT of unknown function (DUF1458)(IPR009923 );This family FT consists of several hypothetical bacterial proteins as well FT as one archaeal sequence Q9HPW4. Members of this family are FT typically of around 70 residues in length. The function of FT this family is unknown. No signal peptide or TMH present." FT /db_xref="InterPro:IPR009923" FT /db_xref="UniProtKB/TrEMBL:A1K4X5" FT /protein_id="CAL93880.1" FT /translation="MSDHVYKLVELVGSSQTGVDDAIRNAIEAAGRTVRHIDWFEVTET FT RGHVVDGRVAHFQVTLKVGFRIENE" FT CDS 1362410..1363681 FT /transl_table=11 FT /locus_tag="azo1264" FT /product="putative transmembrane sensor protein" FT /function="predicted transmembrane sensor domain" FT /note="Putative transmembrane sensor protein, no similarity FT to other bacterial proteins. Best hits to mus musculus and FT homo sapiens. Domains (LCCL_dom and TIR) are found in FT proteins (animal and plants) involved in protection against FT bacterial infection. InterPro: IPR004043 LCCL_dom. FT IPR000157 TIR. TMHMM reporting 1 transmembrane helices." FT /db_xref="GOA:A1K4X6" FT /db_xref="InterPro:IPR000157" FT /db_xref="InterPro:IPR001283" FT /db_xref="InterPro:IPR004043" FT /db_xref="UniProtKB/TrEMBL:A1K4X6" FT /protein_id="CAL93881.1" FT /translation="MSRKAFISHASEDARIATALCAFLEGAGVPCWIAPRDVTPGREYA FT EEILDGIEGCAVFVLLLSAQANRSPFVRRELERAASKDKPLFLVRIEEVQPDRSLELFV FT SSEHWIDAWAPPLETHWARLANAIRGERAVAPPAQAARRPSAATKMVGLGAGLGVLMSL FT LAVGVWSWLTPAHEEAGGSTSAAQPSATLVTPAGPLVATATGPAAPPAGSAAPEASAAA FT ADDGAEPCPGYYAINPQLPSPYACTCGTVVSSQGSVWGSDIYTADSALCKAAVHAGVIP FT RSGGRVVVERVDGRELYVGTSRNGIGTSDYGPHHPAIHFVGSAQPAQPEPCPTFLAINP FT NLATPHVCRCAAGDTLQGSVWGSDPYTADSRLCRAAVHAGRIGTEGGTVTVVYADGRAM FT YSGSERNGVRSSDYGAYPLSIRFQ" FT CDS complement(1363688..1363981) FT /transl_table=11 FT /locus_tag="azo1265" FT /product="Hypothetical protein" FT /note="Hypothetical protein, 26% identity(49% similarity) FT to TrEMBL;Q8XT66. TrEMBL;Q7P1L8(34% identity). No FT domains,repeats, motifs or features present." FT /db_xref="UniProtKB/TrEMBL:A1K4X7" FT /protein_id="CAL93882.1" FT /translation="MNLHSIESLMADIEEEDPLDLGDLAIDETEARRLMASHFCEIDER FT LSEHGLDAEARLEIMAAIAAHTMTENMILHLGRLRASSGDDFHAWMRRHGIG" FT CDS complement(1364049..1365062) FT /transl_table=11 FT /gene="dnaJ2" FT /locus_tag="azo1266" FT /product="putative chaperone protein DnaJ" FT /function="DnaJ-class molecular chaperone with C-terminal FT Zn finger domain" FT /note="Putative chaperone protein dnaJ. homology to dnaJ of FT E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. FT Stimulates jointly with grpE the ATPase activity of dnaK FT (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 FT repeats), DnaJ Cterminal region no singal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4X8" FT /db_xref="InterPro:IPR001305" FT /db_xref="InterPro:IPR001623" FT /db_xref="InterPro:IPR003095" FT /db_xref="InterPro:IPR008971" FT /db_xref="UniProtKB/TrEMBL:A1K4X8" FT /protein_id="CAL93883.1" FT /translation="MDPYSLLDIAPGADAAEIKRAFRRLAMRWHPDRNPAPEAHDHFNA FT LRAAHDSLLAELAAGTAAGDDEDLADTDDEAPAPAPSRRGPDRRQTLEIRIEDACLGGE FT KIVVVADESVCGHCHGSGETALAHTRLCATCHGSGRLRAARGLVQCAVCGGRGFVSKAA FT CAHCGGSGRERTERRLAVQLPPGLLTGDELRLAGEGEAAADASAQPGDLRLTIALAPHP FT LYRAEGRDLHLRRPLSVFRLLAGGDIDIPLPGGCRTATLPPGGATRQLRLEGAGIPGRG FT GRPGGAAIIELAPLLPEAVDAATREALDAADLLMKRRFYAELPELADWEARWLDAD" FT CDS 1365220..1365705 FT /transl_table=11 FT /locus_tag="azo1267" FT /product="probable acyl-CoA thioester hydrolase" FT /function="Acyl-CoA hydrolase" FT /EC_number="3.1.2.-" FT /note="Entry name TREMBL:Q7W380 Prim. accession # Q7W380 FT Identities = 111/150 (74%) InterPro IPR006683; FT Thioestr_supf. Pfam PF03061; 4HBT; 1. Prediction: FT Non-secretory protein Signal peptide probability: 0.179 FT Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K4X9" FT /db_xref="InterPro:IPR006683" FT /db_xref="UniProtKB/TrEMBL:A1K4X9" FT /protein_id="CAL93884.1" FT /translation="MQLPNHQLAMTVLMTPDMANFSGKVHGGAILKLLDQVAYACASRY FT AGEYVVTLSVDQVMFREPINVGELVTFLASVNYTGKTSMEIGIKVLAENIRGKRVRHAN FT SCFFTMVAVDENGRATTVPQLQPSTPDEERRYQAAKLRRELRQEFEARQQALKPASA" FT CDS 1365702..1365947 FT /transl_table=11 FT /locus_tag="azo1268" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to FT PBPRB0126 of Photobacterium profundum of 54% FT (trembl:Q6LL06). No domains predicted. No TMHs. No signal FT peptide." FT /db_xref="GOA:A1K4Y0" FT /db_xref="InterPro:IPR003034" FT /db_xref="InterPro:IPR018668" FT /db_xref="UniProtKB/TrEMBL:A1K4Y0" FT /protein_id="CAL93885.1" FT /translation="MSGTTDAGAQAASRDPLHGVTLERLLNELVAHYGWSELGRRVDIR FT CFNLDPSIASSLKFLRRTPWARAQVEALYVELVRRR" FT CDS complement(1365959..1367140) FT /transl_table=11 FT /gene="purT" FT /locus_tag="azo1269" FT /product="phosphoribosylglycinamide formyltransferase 2" FT /EC_number="2.1.2.-" FT /note="Phosphoribosylglycinamide formyltransferase 2 (EC FT 2.1.2.-) (GART 2) (GAR transformylase 2) FT (5'-phosphoribosylglycinamide transformylase 2) FT (Formate-dependent GAR transformylase)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Y1" FT /db_xref="InterPro:IPR003135" FT /db_xref="InterPro:IPR005862" FT /db_xref="InterPro:IPR011761" FT /db_xref="InterPro:IPR013815" FT /db_xref="InterPro:IPR013816" FT /db_xref="InterPro:IPR013817" FT /db_xref="InterPro:IPR016185" FT /db_xref="UniProtKB/Swiss-Prot:A1K4Y1" FT /protein_id="CAL93886.1" FT /translation="MPRIGTPLSPTATRVLLCGSGELGKEVVIELQRLGCEVIAVDRYP FT NAPAMQVAHRNHVISMLDGAALRAVIEQEKPHYIVPEIEAIATATLVELEAEGYTVIPT FT ARAAQLTMNREGIRRLAAEELGLPTSPYRFADSYEDYAAAVAALGFPCVVKPIMSSSGK FT GQSLLRGPDDVKKAWDYAQEGGRAGKGRVIVEGFIDFDYEITLLTVRHAGGTTFCAPVG FT HRQEKGDYQESWQPQPMSAKAIAESERIALAVTGALGGRGLFGVELFIKGDMVWFSEVS FT PRPHDTGLVTLISQDLSEFALHARAILGLPIPAIRQVGPSASAVILVEGESTQPSFSNL FT GAALAEPDTALRLFGKPEVKGQRRMGVALARDESIEAARAKALRAAQAVKVEL" FT CDS 1367335..1368981 FT /transl_table=11 FT /locus_tag="azo1270" FT /product="conserved hypothetical protein" FT /function="predicted polymerase most proteins contain PALM FT domain HD hydrolase domain and Zn-ribbon domain" FT /note="Probable Branched-chain amino acid aminotransferase FT (EC 2.6.1.42) (Transaminase B) (BCAT). thrC: threonine FT synthase." FT /note="Function unclear" FT /db_xref="InterPro:IPR005646" FT /db_xref="UniProtKB/TrEMBL:A1K4Y2" FT /protein_id="CAL93887.1" FT /translation="MNTLDTRGAGLSLQLDATGRVLLASLVPQPEVAAIDAAWLEERIA FT EAGAGRFRRDAAACELLLQQYAGGAAVAGLALATAVDAALAVRIAPDALLATLDITPAQ FT GGTPISKEAVLAELGAKGITEGIALDAINQAIADGAAQDVEIARGRAPVAGEDGRLECL FT LPAARDRRPQLDASGHIDYRDLGEIQVVRAGEALMRRHPPTPGTPGITVRGAAIPPRAG FT KDIAFAPGLAGVAPAADDPNLLIAACAGQPVQVRGGIMVEPVFSVEAVNMASGNIRFDG FT SVKIRGDVAAGMLVSATGDIEIGGVVESATLEAGGSIVVKGGVIGRLGRKDAGDHHISC FT GGDFSAAYAQQVRVEAGDSIFIDDIAMQCDLLAANHIRVGQRRRGHVIGGRLQATLSVT FT ARVLGSPNRIETRFEIGTPPALHKQLAELARQRDGEETQLLEVSKLLAFADHNPGRLPP FT ATVEKAAHTAARLSAEIAALRETESALAQKADLARNARVVAEQAMYDGVVVTLGIQRYR FT VSGEHGAGAIGLGEQGLALLPAEDAVPAAPA" FT CDS complement(1368995..1369639) FT /transl_table=11 FT /locus_tag="azo1271" FT /product="conserved hypothetical secreted protein" FT /function="ABC-type uncharacterized transport system FT auxiliary component" FT /note="Conserved hypothetical secreted protein. Homology to FT pa3214 of P. aeruginosa of 52% (trembl|Q9HZ26). Pfam: FT DUF330 signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR005586" FT /db_xref="UniProtKB/TrEMBL:A1K4Y3" FT /protein_id="CAL93888.1" FT /translation="MTASPAPRRLHRLRPLATALLVAALASACSILPKPEPVDVYLLPA FT TRTPPAASPALALALRVAKPETSLHLAGQRIVVLPEGDRVSVYKGASWSDPAPLLVRNR FT LLDAFHGDGRIAALSSDDRSLHADLELDSDLRAFHSEYRDGRPEAVVRLDARLVAPASL FT RILASRRFEVRHPAASADVKDVVRAFGAAADALSAEVVAWTLENAAAPAAR" FT CDS complement(1369636..1370577) FT /transl_table=11 FT /locus_tag="azo1272" FT /product="conserved hypothetical secreted protein" FT /function="ABC-type transport system involved in resistance FT to organic solvents periplasmic component" FT /note="Conserved hypothetical secreted protein. Similar to FT TREMBL:Q9HZ27 (53% identity); TREMBL:Q88RI9 (46% identity); FT TREMBL:Q8PGP4 (33% identity). Pfam (PF02470): mce related FT protein. SignalP reporting signal peptide. No TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR003399" FT /db_xref="UniProtKB/TrEMBL:A1K4Y4" FT /protein_id="CAL93889.1" FT /translation="METRAHHVLIGLFTVLVVGAALSFALWLGKVDSDTQFNLYDVVFE FT EAVNGLSKGSTVEFNGIKIGEVSNLRLDPKDPRRVLARIRVDSAAPIRSDTRARLAPQG FT ITGIYTIRLSSGNDPGSVALEPRQGEVPVIIADPSPLSRLLANGEDVMVNVNELLMQAR FT VLFSAENAASLGRTLGHLEQTTGALAAQREDMGRALRELARASEQANAALAEATKMMSA FT TNRLIDTQGKETLQSAQRSMAAFEQAMQTVDKLVADNRGQLDSGMRGIADLGPALSELR FT RTLASLRTITRQLEDRPADYLLGLEPTREFQP" FT CDS complement(1370579..1371361) FT /transl_table=11 FT /locus_tag="azo1273" FT /product="putative ABC transporter ATP-binding protein" FT /function="ABC-type transport system involved in resistance FT to organic solvents ATPase component" FT /note="ATP-binding cassette (ABC) transporters form a large FT family of proteins responsible for translocation of a FT variety of compounds across biological membranes. They are FT composed of two transmembrane domains responsible for FT binding and transport and two nucleotide-binding domains FT responsible for coupling the energy of ATP hydrolysis to FT conformational changes in the TMDs, TREMBL:Q8PGP5 (60% FT identity); TREMBL:Q9PDS7 (57% identity). InterPro FT (IPR003593): AAA ATPase. InterPro (IPR003439): ABC FT transporter. InterPro (IPR001687): ATP/GTP-binding site FT motif A (P-loop). Pfam (PF00005): ABC transporter. TC FT (3.A.1): The ATP-binding Cassette (ABC) Superfamily." FT /note="Specificity unclear" FT /db_xref="GOA:A1K4Y5" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A1K4Y5" FT /protein_id="CAL93890.1" FT /translation="MSADHIIEVRGLRNQFGSQVVHDQLDLDVRRGEILSIVGGSGTGK FT SVLLRTIVGLNRPAAGSVRVFGEDLLTLAPAARSRLERRFGVLFQQGALFSSLTVAENV FT AVPLIEHAGLARKEALRLAGLKIALAGLPQSACAKYPADLSGGMVKRAALARALALDPD FT ILFLDEPTAGLDPIGAAAFDQLILTLRDALGLTVFIVTHDLDTIYTITDRVAVLARRQV FT LVNDRLAVVAATDDPWIQDYFHGPRGRAAQVAAAQPEN" FT CDS complement(1371358..1372500) FT /transl_table=11 FT /locus_tag="azo1274" FT /product="putative ABC transporter permease protein" FT /function="ABC-type transport system involved in resistance FT to organic solvents permease component" FT /note="TREMBL:Q88RI7 (56% identity); TREMBL:Q8PGP6 (42% FT identity). Pfam (PF02405): Domain of unknown function FT DUF140. TIGRFAM (TIGR00056): Conserved hypothetical FT protein. TMHMM reporting six transmembrane helices." FT /note="Specificity unclear" FT /db_xref="InterPro:IPR003453" FT /db_xref="UniProtKB/TrEMBL:A1K4Y6" FT /protein_id="CAL93891.1" FT /translation="MSDTSSSGRAELLAAAGGGVLRLSGDWTLAHYRSIADTVSALRAN FT VQHGTAVDASGLGALDTAGASLLVQLLGHDGLQALSTDPALAPERRALLRAVADALATP FT PEPEPADTGSALGDVLEHIGIAMGVFWRHAVGLLGFIGLTLESAFRIIAQPARWRLTAL FT AANLEKTALDAVPIVALLTFLVGAVVAFLGATVLADFGASIFTVDLVAFSFLREFGVLL FT TAILVAGRTASAFTAQIGSMKANEEIDAIRVLGLDPVELLVLPRVYALLLALPMLTFVA FT MLSGIVGGMLVCALTLDISPVMFLSIFENDVGLRHFIVGIAKAPIFAFLIAVIGCLEGF FT KVSGSAQSVGEHTTSAVVQSIFVVIVVDAVAALLCMELGW" FT CDS complement(1372520..1374184) FT /transl_table=11 FT /gene="yjjK" FT /locus_tag="azo1275" FT /product="probable ABC transporter, ATP-binding protein" FT /function="ATPase components of ABC transporters with FT duplicated ATPase domains" FT /EC_number="3.6.3.-" FT /note="ABC transporter ATP-binding protein yjjK. Presence FT of typical NB-ARC, KH, FolB and GAD domains. Occurence of FT Hydrolase like P-loop and C terminal alpha/beta chains like FT ATP synthease. Presence of Signal peptide and TM FT helices.85% identity and 92% similarity to Dechloromonas FT aromatica.ATPase of ABC transporter with duplicated ATPase FT domain. InterPro: AAA ATPase superfamily uvra: excinuclease FT ABC A subunit" FT /note="Family membership" FT /db_xref="GOA:A1K4Y7" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="InterPro:IPR022374" FT /db_xref="UniProtKB/TrEMBL:A1K4Y7" FT /protein_id="CAL93892.1" FT /translation="MAQYVMSMLRVSKIVPPKRQIIKDISLSFFPGAKIGLLGLNGSGK FT STVLRIMAGADKEYDGEVQHLAGQRIGYLPQEPELDPAKTVKEEVESGLGEILEARQKL FT EEIYAAYAEPDADFDKLAEEQARYENILATAGADIETQMEIAADALRLPPWDAVIGNLS FT GGEKRRVALCKLLLSRPDMLLLDEPTNHLDAESVEWLEQFLTRFPGTVVAVTHDRYFLD FT NAAEWILELDRGHGIPWKGNYSSWLEQKGQRLEQEAKQEAAHMKAMKTELEWARSNPKA FT RQAKSKARLARYEEMASVEYQRRNETQEIFIPPGERLGDKVIEFHNVSKAFGDKLLMDN FT VNFSIPPGAIVGVIGPNGAGKSTLFKMIEGLDKPDSGEVVVGPTVKLAAVDQSRAGLAN FT DKTVFEAISDGADILTVGRFEMPSRAYIGRFNFKGGDQQKIVGNLSGGERGRLHLAKTL FT IAGGNVLLLDEPSNDLDVETLRALEDALLEFAGCAMIISHDRWFLDRICTHILAAEGDS FT QWTFFAGNYQEYEEDKKKRLGEEGAKPKRIRYKPITR" FT CDS 1374585..1375484 FT /transl_table=11 FT /locus_tag="azo1276" FT /product="putative O-methyltransferase" FT /function="SAM-dependent methyltransferases" FT /EC_number="2.1.1.-" FT /note="Putative methyltransferase Rv0089/MT0098/Mb0092 (EC FT 2.1.1.-). Methyl transfer from the ubiquitous FT S-adenosyl-L-methionine (AdoMet) to either nitrogen, oxygen FT or carbon atoms is frequently employed in diverse organisms FT TREMBL:AAS95087-36%identity,50% similarity InterPro: SAM FT (and some other nucleotide) binding motif rrmJ: ribosomal FT RNA large subunit methylation TIGRFAM:Transcription FT regulator, AsR family, Ubi/COQ family." FT /note="Family membership" FT /db_xref="GOA:A1K4Y8" FT /db_xref="InterPro:IPR013216" FT /db_xref="InterPro:IPR023576" FT /db_xref="UniProtKB/TrEMBL:A1K4Y8" FT /protein_id="CAL93893.1" FT /translation="MPSPALLLNLFLDLVARGEQPRVPEPALVMDDPAAAEAFMRAGRE FT DGMLAHTYVYHAIQASAVIPAGGTVLDLGCGPANQLVQVARLNPDARFIGVDASPAMLA FT LARETLARCDVGNVTLREAQMQALADIPDASVDAVISTMSLHHLTDFAALAATLAEVKR FT VLRPGGGVYLVDFGRLRRAAGQHFFAHERAASQPQLFTTDYHHSLRAAFSLAELQAAAR FT VLGAAVRVRRTFLVPFLVAIRSRQPNRLRRESRAAARALYLALSPRQRFELRDLARFFG FT HGGFPLAYRPWWPWHRGR" FT CDS complement(1375505..1375996) FT /transl_table=11 FT /locus_tag="azo1277" FT /product="conserved hypothetical glutathione peroxidase" FT /function="Glutathione peroxidase" FT /EC_number="1.11.1.9" FT /note="conserved hypothetical glutathione peroxidase. FT Homolgy to pp1874 pf P. putida of 66% (trembl|Q88LQ5) FT Glutathione peroxidase (GSHPx), an enzyme whose principal FT function is to protect against damage from FT endogenously-formed hydroxyperoxides, catalyses the FT reduction of hydroxyperoxides by glutathione Pfam: FT Glutatione peroxidase no signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K4Y9" FT /db_xref="InterPro:IPR000889" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:A1K4Y9" FT /protein_id="CAL93894.1" FT /translation="MTTPLYDIPLQRLDGSAATLADYAGKVLLIVNTASQCGFTPQYAG FT LEMLYRNYKDRGLVVLGFPCNQFGAQEPGDASEIADFCERNYGVSFPMFAKLDVNGDNA FT HPLYVALKQQAPGVLGTEAIKWNFTKFLVDRHGEVIERYAPTTTPQDLAGDIEAQLARA FT " FT CDS complement(1376095..1378737) FT /transl_table=11 FT /locus_tag="azo1278" FT /product="EAL/GGDEF/PAS/PAC-domain containing signalling FT protein" FT /function="predicted signal transduction protein containing FT a membrane domain an EAL and a GGDEF domain" FT /note="EAL/GGDEF/PAS/PAC-domain containing signalling FT protein," FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K4Z0" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001633" FT /db_xref="InterPro:IPR013767" FT /db_xref="UniProtKB/TrEMBL:A1K4Z0" FT /protein_id="CAL93895.1" FT /translation="MIQPLPAPNPFAGLARWPLLRAALLMLAATLLLGWLFRQADTLTS FT PEPQHYGRELRRLLNIDAELDTAVLASGEGLQRDFDGITTSMREFTELGASVATVPAFL FT GEADRRRLGAEIAALRAVVAEKAELVDRFKRETSVLRNSLAYFPAATDRLIEEGMLPPA FT VSRQTGIVARNVMGFVLDAQPMRAAEMWERLDQLAIVALTLPPAQRERVVNLIAHGRII FT LDRKPVLDTITRDILALPTGARAESVIHAYVDGYQHATDRAHTYRVLLFVVALGLAGYL FT MIAILRLQRTSLALAGANEHLEERIQTLRLTESELHLYANVFTNASEGMAITDAQARIV FT AVNPAFTDITGYSIEEIHGRTPAVLASGRQDAAFYREMWATLGKRGQWQGEIWNRRRSG FT EIYPEWLSITAITEGDGGVSHYIGIFSDITDRKESEARIRHLAHHDALTGLPNRLLLQD FT RLGQAILKARRNSTQAAVLFLDLDRFKTINDTLGHEIGDGLLRQVTQRCLGAVRETDTV FT ARQGGDEFVIVLPDLEHGQDAGTIARKILAALTEPCRLGPHELTVTGSIGIALYPGDGA FT DPSMLLRNADAAMYRAKADGRNGFQFYAADMNTHSLGELLLEHQLRGALDRNELRLYFQ FT PKVNAADGCIEGCEALLRWQHPDLGLLAPGRFVPAAEESGLIVPIGEWVLREACRQLRA FT WIDAGLAPVPVAVNLSGQQFAHQDIVALVREALAEHRLPAPMLELELTETMLMRDLERT FT IATLAELRAMGVTLAIDDFGTGYSSLAYLRQFDVNALKIDRSFVHDIRPGSSDGKIATA FT VIALAHNLGLTVTAEGVETAAQQHFLARHGCDQLQGFLFGQPEPAEAFAQRLADDDRRA FT PHVRLVSAH" FT CDS complement(1378734..1379822) FT /transl_table=11 FT /locus_tag="azo1279" FT /product="putative cytochrome C peroxidase" FT /function="Cytochrome c peroxidase" FT /EC_number="1.11.1.5" FT /note="Probable cytochrome c peroxidase (EC 1.11.1.5), an FT electron-transfer proteins having one or several haem c FT groups, bound to the protein by one or, more generally,two FT thioether bonds involving sulphydryl groups of cysteine FT residues. CytC possess a wide range of properties and FT function in a large number of different redox processes. FT Similar to yhjA from E.coli." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Z1" FT /db_xref="InterPro:IPR003088" FT /db_xref="InterPro:IPR004852" FT /db_xref="InterPro:IPR009056" FT /db_xref="UniProtKB/TrEMBL:A1K4Z1" FT /protein_id="CAL93896.1" FT /translation="MTRLKTLFSATVKMPPVKRRALHLSIIGLLALLAVALVGLAWHDP FT LPELAASPTPATAIPSNEPLLPLPPRQPPAHPARVALGQRLFHEPLLSRDRTLACASCH FT NLSLGGTDRRPRSIGTGGALGQLNSPSVLNVALNFAQFWDGRVETLEAQVAGPLHNPVE FT MASNWAEAISRLRAQPEYRQAFALAYAGEGISETTIADALASFERSLLPVDSPFDRYLR FT GDRDAIDPDAREGYTRFKALGCASCHQGAGIGGNMFQRFGVMGDYFGARGDITVADLGR FT YNVTGRDADRHVFKVPSLRNVALTAPYFHDGNAATLDEAVAIMGRYQLGLELSAEDRRL FT IIAFLDTLTGQPPALAPAEPRR" FT CDS complement(1379865..1380641) FT /transl_table=11 FT /gene="fpr1" FT /locus_tag="azo1280" FT /product="ferredoxin-NADP+ reductase" FT /function="Flavodoxin reductases (ferredoxin-NADPH FT reductases) family 1" FT /EC_number="1.18.1.2" FT /note="Ferredoxin-NADP+ reductase (EC 1.18.1.2) Homology to FT fpr of A. vinelandii of 79% (sprot|FENR_AZOVI). CATALYTIC FT ACTIVITY: Reduced ferredoxin + NADP(+) = oxidized FT ferredoxin + NADPH. Pfam: Oxidoreductase FAD-binding FT doamin; Oxidoreductase NAD-binding domain no signal peptide FT no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Z2" FT /db_xref="InterPro:IPR001433" FT /db_xref="InterPro:IPR001709" FT /db_xref="InterPro:IPR008333" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:A1K4Z2" FT /protein_id="CAL93897.1" FT /translation="MSNLNEERVLSVHHWNDSLFSFRTTRNPGLRFENGQFVMIGLEVD FT GRPLTRAYSIASPNYEEHLEFFSIKVPDGPLTSRLQHLREGDPIVISKKPTGTLVLHDL FT NPGKHLYLLSTGTGLAPFMSVIQDPETYERFEKVVLIHGVRYVSELAYTDFLTRHLPDN FT EFFGDAVREKLIYYPTVTREPFRNQGRLTALLDSGKLNADIGLPPLDPATDRAMICGSP FT AMLQDCCDLLDSRGFKISPRIGEPGDYVIERAFVEK" FT CDS 1380741..1381667 FT /transl_table=11 FT /locus_tag="azo1281" FT /product="probable transcriptional regulator, LysR family" FT /note="Probable transcriptional regulator, LysR family FT proteins.57% Identity to TrEMBL;Q9HYK6, Q87XZ5, Q88MD6. Has FT PF03466, LysR substrate binding FT domain;IPR005119,LysR_subst; The structure of this domain FT is known and is IPR000847, HTH_LysR; Numerous bacterial FT transcription regulatory proteins bind DNA via a FT helix-turn-helix (HTH) motif. These proteins are very FT diverse, but for convenience may be grouped into FT subfamilies on the basis of sequence similarity. One such FT family, the lysR family,groups together a range of FT proteins, including ampR, catM,catR, cynR, cysB, gltC, FT iciA, ilvY, irgB, lysR, metR,mkaC, mleR, nahR, nhaR, nodD, FT nolR, oxyR, pssR, rbcR,syrM, tcbR, tfdS and trpI. The FT majority of these proteins appear to be transcription FT activators and most are known to negatively regulate their FT own expression. All possess a potential HTH DNA-binding FT motif towards their N-termini." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Z3" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K4Z3" FT /protein_id="CAL93898.1" FT /translation="MRFTLRQLEIFVSVARGENVSRAAEMMNLSQSATSAALAELEHQF FT EQQLFDRSGRRLRLNERGRLLLPRAVEFLDRAQEIEALLRGERGLGDLRIGATLTIGNY FT LLPLIAAGFLQRHPESRVHLLVENTESVVAKVARYEIDFGLVEGRVDDPDVEVAEWVGD FT ELSVFCAPTHPLAQRGKARWEELAGEPWILRERGSGTRQTLEQALRHQTKAIVPRLELE FT HTEAVKRAVESGLGIGCISRLALRDAFRRGSLVRIETPDLDLRRKFLFVWHRGKYHTAA FT IRTFLDDCRALTGGAGFSHEIPLPAVP" FT CDS complement(1381825..1384443) FT /transl_table=11 FT /gene="ndvB" FT /locus_tag="azo1282" FT /product="putative Beta-(1-3)-glucosyl transferase" FT /function="Glycosyltransferases probably involved in cell FT wall biogenesis" FT /note="Beta-(1-3)-glucosyl transferase, involved in the FT synthesis of the cyclic beta-(1,3),(1,6)-D-glucan. 36% FT Glyco_trans_2. Pfam:PF00535; Glycos_transf_2. Signal FT peptide: present. TMhelix:9." FT /note="Function unclear" FT /db_xref="GOA:A1K4Z4" FT /db_xref="InterPro:IPR001173" FT /db_xref="InterPro:IPR013781" FT /db_xref="InterPro:IPR017853" FT /db_xref="UniProtKB/TrEMBL:A1K4Z4" FT /protein_id="CAL93899.1" FT /translation="MKNAASLAYRMTIALAVASLVALAQYWIWEHFNRGSEFIGASQSI FT KGFAYNGFQRDQSPLRGTYPTDAQIGADLDLLARSADGLRTYGVNDLPGLLELAGQRDM FT LVTAGAWLDTDKEKNEKEINALLEVARKQRYIERVLVGNEAILRGDLKPDEMIVYLDRV FT RKSLRKPVSTAEPWHVWLKYPELAKHVDYITVHLLPYHEGVPVEAAVEYALQRYDELVK FT TFPKKKIVIGEIGWPSRGPVIGAAEPTLDNEARFIREFLAHPRTARLDYFLMEAIDQPW FT KVDVEGWAGAYWGMFNADRQPKFALEGLVERDPHWAKKASNAAALAFIPMLLIAFFLSD FT WNIAGRIFLAGLIQACVSTLIVSLNVPVDYYLTQRDLVGLTMLIAATCLTAAVLLSHGF FT EFGEILFKRKWQRRFMPLPPHAPEEQPFVSIHLACHNEPPEMVIATIDSLAKLNYSNFE FT VLILDNNTKDEAKWKPLEARCAELGPRFRFFHLMDWPGFKAGALNYGLEVTDPRAEVVG FT VVDADYVVDPDWLAVLIPHFDKPDVAVVQAPQAHRDWETHPFRRMCNWEFDGFFRIGMH FT HRNERNALIQHGTMTLVRRLALEEVGGWSEWCICEDTELGLRLIEKGYDTRYVDHILGR FT GLTPSDFAAIKSQRFRWAFGAMQILKAHLPQMVGKSTLNLAQRYHFLTGWFAWLGDALQ FT LVFAFGSLLWTLGILLFPKAFGLPVTALALPILGFMAFKAALGPILYRRTMECPWKDIL FT GASILSVGLAHAIARGVFTGLVKRKGVFVVTPKGWKAKGALAFFGPIREELGMLFALIL FT GAVALVTLRGANDLETQLWVGILALQCIPYVAAIACQIAAYMPERPAALPAGVKTLGAA FT G" FT CDS 1384729..1385121 FT /transl_table=11 FT /locus_tag="azo1283" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT PP1739 of P. putida of 30% (trembl|Q8EA80) No domains FT predicted. signal peptide 2 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K4Z5" FT /protein_id="CAL93900.1" FT /translation="MSRNNSQKYGWWPVVLGGALVLALALGARYGLIENGVLPRDCTVP FT EAQGAGAACALKWALVQLFHEQRLGIFSLVCGGLGFALTCRRLAWPGWLAGLAGLVLYN FT YDYAAVGALLALLVLTAGEHQRQAQG" FT CDS complement(1385065..1386660) FT /transl_table=11 FT /gene="ndvC" FT /locus_tag="azo1284" FT /product="putative glucan 1,3-beta-glucosidase" FT /function="Exo-beta-13-glucanase" FT /EC_number="3.2.1.58" FT /note="Glucan 1-3-beta-glucosidase FT precursor.(Exo-13-beta-glucanase).Glucanases possibly play FT a role in cell expansion during growth in cell-cell fusion FT during mating and in spore release during sporulation. This FT enzyme may be involved in beta- glucan degradation and also FT function biosynthetically as a transglycosylase. 47%" FT /note="Function unclear" FT /db_xref="GOA:A1K4Z6" FT /db_xref="InterPro:IPR013781" FT /db_xref="InterPro:IPR017853" FT /db_xref="UniProtKB/TrEMBL:A1K4Z6" FT /protein_id="CAL93901.1" FT /translation="MSRRSPWAALLAVHLIALAALVAWLALQSRPVQMHDLQLADGEKL FT KCVSYAPYHFPGQTPFDKDLRITREQIAADLAALSHITRCVRLYSVDQGLDQVPSVARE FT IGLKVLLGAWIGYDRKKNAAELDHAISIANEYPDVVRALIVGNEVLLRRERSEDEMRAL FT IRDAKSKSQVPVTYADVWEFWMRHDSLAREVDFVTVHILPFWEDEPVDIQHALQHVAAI FT HEEVQTHFGKPILIGETGWPSEGRQREASRPSPANQARYIREFVHQAHDRGWDYNLIEA FT IDQPWKRRLEGTVGGYWGMLDADLKPKFPLAGPVADRTSMQLPLLGAALGAALAAAVAL FT ARRGAGGRLRVAACASIGAVGGMLAVLNWEHGRVAYRDELEWILLGGLTALAATLAVLV FT SAWDGVMLPGARSAWRDLRHGWAPTPARLLALARGTLVFAAAVAALLLFVDARYRDFPT FT LLYLTPALIFGTLAALGRGAARAERICAAIIVLCGIGRWLPEPANPQAIAWLATTLALG FT LPLMLARGEHQQGE" FT CDS complement(1386740..1389619) FT /transl_table=11 FT /gene="gcvP" FT /locus_tag="azo1285" FT /product="glycine cleavage system P-protein" FT /function="Glycine cleavage system protein P FT (pyridoxal-binding) C-terminal domain" FT /EC_number="1.4.4.2" FT /note="Glycine cleavage system P-protein. Homology to gcvP FT of E. coli of 63% (CAA52146). The glycine cleavage system FT catalyzes the degradation of glycine. The P protein binds FT the alpha-amino group of glycine through its pyridoxal FT phosphate cofactor; CO(2) is released and the remaining FT methylamine moiety is then transferred to the lipoamide FT cofactor of the H protein (By similarity). Tigrfam: gcvP: FT glycine cleavage system P protein Interpro: glycine FT cleavage system P protein (IPR003437) Pfam: glycine FT cleavage system P protein no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Z7" FT /db_xref="InterPro:IPR003437" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015424" FT /db_xref="InterPro:IPR020580" FT /db_xref="InterPro:IPR020581" FT /db_xref="UniProtKB/TrEMBL:A1K4Z7" FT /protein_id="CAL93902.1" FT /translation="MPQTLLSAPLAQLEQRDAFIHRHLGPNPDEIARMCATIGVPDIDT FT LIAQTVPASIRLPQALPLAGPRPEHEALELLRGLAERNAVKKSMIGMGYYGTHTPAVIL FT RNVMENPGWYTAYTPYQAEIAQGRLEALLNFQQMVIDLTGLELANASLLDEATAAAEAM FT AMARRVSKSKSNAFFVDAACFPQTLDVVRTRAEYFGFNLVLGDAAEAAEHDVFGALLQY FT PNVHGTVGDLGAVIAALKGRGAITALATDLMALVLLKSPGAMGADIALGSAQRFGVPMG FT FGGPHAAFFATREAYVRSMPGRIIGVSRDARGKTALRMTLQTREQHIRREKANSNICTS FT QVLLANMAGFYAVYHGPQGLRTIAARIHRLAALLDAGLRAAGFAVRSSAYFDTLEVDAD FT ERAAAILSAADQAGFNLRDAGHGRIGLSVDETTTRADIAAVLACFGANVDLETLTPASA FT LPAGLLRDDAILAHPVFNTHHTEHEMLRYLKKLQNRDLALDHSMISLGSCTMKLNATSE FT MIPVTWPAFANLHPFAPPAQTQGYMAMIDGLADYLKAVTGFDAICMQPNSGAQGEYAGL FT VAIRRYHASRGEAHRDVCLIPRSAHGTNPATAQMCGMEVVVVDCDGSGNVDLENLQSKA FT AQYADRLAAMMITYPSTHGVFEENIREICAAVHAHGGQVYMDGANLNAQVGLTSPAIIG FT ADVSHMNLHKTFCIPHGGGGPGMGPIGLKAHLAPFMADHAVAATGDAERVNKGQGAVSA FT APFGSASILPISWMYITMMGGEGLKRATEVAILNANYLASRLAPHYPVLYTGSRGRVAH FT ECILDIRPIKAATGISEVDIAKRLMDYGFHAPTMSFPVAGTIMVEPTESEDLAELDRFI FT EAMVAIRGEILRIERGEWPADDNPLRNAPHTQGEIAAAQWERPYSREQAVFPLPWVADN FT KFWPSVNRIDDVYGDRNLFCACVPMEAYS" FT CDS complement(1389681..1390064) FT /transl_table=11 FT /gene="gcvH" FT /locus_tag="azo1286" FT /product="glycine cleavage system H protein [gcvH]" FT /note="Glycine cleavage system H protein [gcvH], 70% FT identity to SProt;Q8XU99, Q82WQ5. TrEMBL;Q62FN0(67% FT Identity). Has PF01597, Glycine cleavage H-protein; FT IPR002930, GCV_H; This is a family of glycine cleavage FT H-proteins, part of the glycine cleavage multienzyme FT complex (GCV) found in bacteria and the mitochondria of FT eukaryotes. GCV catalyses the catabolism of glycine in FT eukaryotes. A lipoyl group is attached to a completely FT conserved lysine residue. The H protein shuttles the FT methylamine group of glycine from the P protein to the T FT protein." FT /db_xref="GOA:A1K4Z8" FT /db_xref="InterPro:IPR002930" FT /db_xref="InterPro:IPR003016" FT /db_xref="InterPro:IPR011053" FT /db_xref="InterPro:IPR017453" FT /db_xref="UniProtKB/Swiss-Prot:A1K4Z8" FT /protein_id="CAL93903.1" FT /translation="MSTIPNDLKYTKSHEWIRLEADGTLTVGVTDHAQAALGDVVFLEL FT PEAGRVVSAGEACAVIESVKAASDIYAPVAGEVIARNDSVTDAPESVNADAYAAWLFKL FT KPANAGDTSALLDAAGYATEIAD" FT CDS complement(1390115..1391122) FT /transl_table=11 FT /gene="gcvT" FT /locus_tag="azo1287" FT /product="glycine cleavage system T protein" FT /function="Glycine cleavage system T protein FT (aminomethyltransferase)" FT /EC_number="2.1.2.10" FT /note="Glycine cleavage T proteins are part of the glycine FT cleavage multienzyme complex (GCV) found in bacteria and FT the mitochondria of eukaryotes. The T-protein is an FT aminomethyl transferase that catalyses the following FT reaction: (6S)-tetrahydrofolate + FT S-aminomethyldihydrolipoylprotein = FT (6R)-5,10-methylenetetrahydrofolate + NH3 + FT dihydrolipoylprotein Similar to sprot|GCST_NITEU (60%). FT Pfam: Glycine cleavage T-protein (aminomethyltransferase) FT TIGRfam (TIGR00528): Glycine cleavage T-protein FT (aminomethyl transferase)" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K4Z9" FT /db_xref="InterPro:IPR006222" FT /db_xref="InterPro:IPR006223" FT /db_xref="InterPro:IPR013977" FT /db_xref="UniProtKB/TrEMBL:A1K4Z9" FT /protein_id="CAL93904.1" FT /translation="MPVNYGSQIEEHHAVRRHAGMFDVSHMLALDLTGPDATAWLRRLL FT ANDVAKLRTAGKALYACMLNPTGGVIDDLIVYRLSDNQYRIVVNAGTADKDVQWMRRQI FT GEMPANVTLTPRRDLAMIAVQGPHAREASWKAFPELRAGSESLPPFSGAQLGDYFVGRT FT GYTGEDGFEIAVPADKAEAAWAQLLAAGVQPCGLGARDTLRLEAGMNLYGQDMDESTSP FT LDTGLGWTIDLKDEQRDFVGKTALLAAPATRQVLGLVLEDKGVLRAHMAVFTPDGEGET FT TSGTFSPTLQRAIAFARLPPGVAAGDTVEVDVRGKRLKARCVKLPFVRNGKALV" FT rRNA 1391911..1393444 FT /locus_tag="azo_rrn5" FT tRNA 1393517..1393593 FT /gene="tRNA-Ile" FT /locus_tag="azo_tRNA_0025" FT /product="transfer RNA-Ile" FT /anticodon=(pos:1393551..1393553,aa:Ile) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT tRNA 1393621..1393696 FT /gene="tRNA-Ala" FT /locus_tag="azo_tRNA_0026" FT /product="transfer RNA-Ala" FT /anticodon=(pos:1393654..1393656,aa:Ala) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT rRNA 1393962..1396848 FT /locus_tag="azo_rrn6" FT CDS 1397768..1398982 FT /transl_table=11 FT /gene="narK" FT /locus_tag="azo1288" FT /product="putative nitrate transporter" FT /function="Nitrate/nitrite transporter" FT /note="Probable nitrate transporters are involved in FT excretion of nitrite produced by the dissimilatory FT reduction of nitrate. NarK is polytopic membrane protein FT with 12 transmembrane domains which is involved in nitrate FT uptake and nitrite excretion and is thought to function as FT a nitrate/nitrite antiporter. At low concentrations of FT nitrate, NarK mediates the electrogenic excretion of FT nitrite rather than nitrate/nitrite exchange., 90% FT similarity to a probable nitrate transporter protein in FT Azoarcus sp. EbN1., InterPRo:04737: nitrate FT transporter,Signal peptide no present, TMHx:12 ," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K500" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:A1K500" FT /protein_id="CAL93905.1" FT /translation="MDKKSFLQAGHTPTLFAAFMYFDLAFMVWVMLGPLGVQIATDLGL FT THAQKGMMVATPVLAGALLRFVMGMLVDHLKPKLTGAIGQVIVIAALAYAWQHGIHSFE FT ETLILGLFLGVAGASFAVALPLASRWYPPEHQGTALGIAGAGNSGTALAALFGPGLAAS FT FGWVNVFGLALIPLGLVFVAYLLMAKDAPECPPPKRLGEYLAVLKDKDAWWFMFFYSVT FT FGGFVGLASSLTIYFNTQYGLDAKMAGYFTAACVFAGSLVRPIGGNLADRIGGIKSLSV FT VYIAAAVALSIVSVGLPSSWLALAVFVCAMLSLGMGNGAVFQLVPQRFRKEIGVMTGLV FT GMAGGVGGFYLASSLGYSKQVSGSYMPGFLIFAGLALAALVGLTAVKRRWRTTWGAPHL FT TTAKI" FT CDS 1399088..1400770 FT /transl_table=11 FT /locus_tag="azo1289" FT /product="putative serine/threonine protein kinase" FT /function="Serine/threonine protein kinase" FT /note="Putative serine/threonine protein kinase," FT /note="Family membership" FT /db_xref="GOA:A1K501" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR001932" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:A1K501" FT /protein_id="CAL93906.1" FT /translation="MNQLSVRIGYTSLTGARVANEDFGGYVTPAGAELMDKGILLAVAD FT GLGGHENGREAAERTVRGLLADYYATPATWSVNSSLERVIQSLNQWVLSQARKYRQTAG FT MATTLSAMVARGTRYYLAHVGDTRIYRLRGGGLEQLTTDHTWVHPELDSVLSRAVGLDS FT KLSVDFADGDLMVGDVYALMSDGVWATLGDERIRKILEDETDPEAAAADLAMAATRAGS FT PDNCTALVMKVDGLPPARLPEIIASGSALPLPPPLKPGQVIDGLTVEEVLHHSLVTLLY FT RVADAQGRQRVLKTLRNGAGDVENCQALVYEEWLARRVVDSRFPEVIDWPGRHHLYYLM FT SWHEGATLKARLAAGHRFSPAQVVELGGEILRGVGALHRLAIVHRDIKPDNLHLDAHGR FT LRILDLGVAASDGHAFNEINNPGTPSYMAPELFAGERANEASDLYAVGVTLYELLARRY FT PYGEIEPFQKPRFGDPVAVTRYRPDTPDWLEAILLKAVAPTPAERFETAEEFLLALELG FT AHRPLRTPRRRPLMQRDPALGLKLLAVSSVVLNVFLALLLFAR" FT CDS complement(1400786..1401718) FT /transl_table=11 FT /locus_tag="azo1290" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ebA98 of FT Azoarcus sp. EbN1 of 67% (gnl|keqq|eba:ebA983(KEGG)). No FT domains predicted. No signal peptide. No TMHs" FT /db_xref="UniProtKB/TrEMBL:A1K502" FT /protein_id="CAL93907.1" FT /translation="MNPEIPNGTLDTIDGVPRVYYDGYWIKVYDPPADSLQAKKTLIQA FT LTRRLFNHVEHGINIPGKRLNDARRSFETEQDPEHKRVKGAMLAGALFNRATDIFTKLV FT ELQALGIEIETDNALMRECGVCLQEALNLGRMVLHRSGEEGIDELWGEPFRAFSIPVEA FT FYESRYVKIAQALRDIDRLAATMIATFRGNPLFEGADVLIQDFAAISKVKCETLRTDDA FT IFDIWAEFVVTSERLAAFAPKLSCTPTPDEQQRAEDGQRLILQGRDLLTYIVRARVTMP FT KSAREYMERCAQYANLQHTPPAKPALPRI" FT CDS complement(1401860..1402312) FT /transl_table=11 FT /gene="sixA" FT /locus_tag="azo1291" FT /product="putative phosphohistidine phosphatase" FT /function="Phosphohistidine phosphatase SixA" FT /note="Putative phosphohistidine phosphatase, SixA. FT TIGRFAM: TIGR00249; sixA. Phosphohistidine phosphatase sixA FT (EC 3.1.3.-) (RX6). EXHIBITS PHOSPHOHISTIDINE PHOSPHATASE FT ACTIVITY TOWARDS THE HPT DOMAIN OF THE ARCB SENSOR INVOLVED FT IN THE MULTISTEP HIS- ASP PHOSPHORELAY." FT /note="Specificity unclear" FT /db_xref="InterPro:IPR013078" FT /db_xref="UniProtKB/TrEMBL:A1K503" FT /protein_id="CAL93908.1" FT /translation="MDLLLWRHAEAAEGSPDHSRELTERGHRQARRMAEWLHKNRPKKL FT RVLVSPTVRTRQTAAAFTQDFEIVPALAPDCGVADLIGATGWPDASGAVLIVGHQPGLG FT RLASLLLAGVEADWTIKKGALWWFTNRVRDDETQTVLRTVLPAELA" FT CDS complement(1402375..1403868) FT /transl_table=11 FT /locus_tag="azo1292" FT /product="adenylate cyclase" FT /function="uncharacterized conserved protein" FT /EC_number="4.6.1.1" FT /note="Conserved hypothetical protein,40% identity to FT TrEMBL;Q88AR4 Has PF01928|CYTH domain(IPR008172);These FT sequences are functionally identified as members of the FT adenylate cyclase family, which catalyses the conversion of FT ATP to 3',5'-cyclic AMP and pyrophosphate. Has PF05235:CHAD FT domain(IPR007899);The CHAD domain is an alpha-helical FT domain functionally associated with the CYTH domains. It FT has conserved histidines that may chelate metals." FT /db_xref="GOA:A1K504" FT /db_xref="InterPro:IPR007899" FT /db_xref="InterPro:IPR008172" FT /db_xref="InterPro:IPR023577" FT /db_xref="UniProtKB/TrEMBL:A1K504" FT /protein_id="CAL93909.1" FT /translation="MSQEIELKLALPPSALPALRRHPLVAGAAREGKAETLDNTYFDTP FT DLTLKANRVAVRTRRQGRKWLQTVKCAATSSGGLSSRPEWEGPYNGRFDFSAVDHPEAA FT RLLHKHGGKLTPLFSTRFRRETRLYSPREGVRILLMTDSGRIEAGGRELPICELELELV FT DGDPLDLLELACTLARDLPLVPNDISKAQRGYQLFHDQPVTPVRSEPPRLEADAGISEA FT FRALAFATLRAWQANAVAIAEGHQDPEFIHQLRVALRRLRALLRTFAPVLPADFHETWS FT ARLREHAALLAEARDLDVLYTELLEPVRTEEVNRDEIDVHGLAALADDARTEARKHALK FT GLAKAGEGLAMLEFTAALHRLPDIEGDLASFARERLDRLRKRARRRFDAATDLAPARLH FT ALRIAFKHLRYAVEFFTPLLARKAGARYLAALVKAQDTLGYLNDVDVARARLARWADDI FT RALQTAAAFVSGWHAPRYARYRRRVLDEARPLLWGRKPW" FT CDS complement(1403946..1406627) FT /transl_table=11 FT /gene="glnE" FT /locus_tag="azo1293" FT /product="probable [glutamate-ammonia-ligase] FT adenylyltransferase" FT /function="Glutamine synthetase adenylyltransferase" FT /EC_number="2.7.7.42" FT /note="Probable glutamate-ammonia-ligase FT adenylyltransferase (glutamine-synthetase FT adenylyltransferase) protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K505" FT /db_xref="InterPro:IPR005190" FT /db_xref="InterPro:IPR013546" FT /db_xref="InterPro:IPR023057" FT /db_xref="UniProtKB/TrEMBL:A1K505" FT /protein_id="CAL93910.1" FT /translation="MLNESAPLPDAVASAAELSRYLARMLASRPWLADRLAASIGAPVD FT EPAMLAFIAEQGADEARLRPTLRHLRTWVMCHLIVRDLAGLAPLAEVTETMTVLAEVAV FT RHAHHVLREGLVQRYGAPLSPTGWEQELLVIGMGKLGGRELNVSSDIDLIFIYPEDGDT FT GGKKVISNFEFFERLGKQLIQALAELTEHGQVFRVDMRLRPNGDSGPLVGSFDMLENYF FT ISQGREWERYAWIKARVLCGERWQELERIARPFVFRKYLDFGAVNAMRELHAQIRREVM FT RRDRVHNVKLGPGGIREIEFIAQVFQLIRGGRDTELQVRPTLTVLDRLAARGILGADTV FT GELSRAYDFLRRLEHRLQYLDDAQTHDIPDNDADRALIARAMGFAGFAELDTALAAHRE FT VVSRHFEAVFGDPTDEDHDLTATWAAANDCDRVTAKLAELGYRDAPAAASRLAAIHGSA FT RYQQLPNHIRQRFDALMPRVLEVAAATMDADETLARCLDLLETISRRGAYLALLQQYPQ FT ALRRVADLVGISRWAAQYLGRHPILLDELLDDRNHELEPDWVRFRADLSDRLDAIEPDM FT ERQMDLMREQHHAQVFRLLTRDIAGLLSVEKLADHLSALADVMLSLTLPLCWRKIKIRH FT REAPKFAVISYGKLGGKELGYASDLDIVFLYDDDAPESAEVYSRLAQRTNTWLSSQTAA FT GMLFETDLRLRPNGDSGLIACSLESFRKYQLESAWVWEHQALTRARCSAGDPAIGEAFE FT RIRCEVLRLPRDLDTLRAEVAAMRRKMRDAHGGKSALFDLKHDRGGLIDVEFLVQYLVL FT GHAHAHPELTGNLGNIALLHIAAGLGLIPAELAEACADSYRTFRRLQHRQRLNDQPSRV FT EPEEAAEARKPVEALWSHVFGD" FT CDS 1406776..1410699 FT /transl_table=11 FT /locus_tag="azo1294" FT /product="conserved hypothetical membrane protein" FT /function="predicted membrane protein" FT /note="Conserved hypothetical protein. Homology to cv2096 FT of C. violaceum of 32% (trembl|Q7NW94(SRS) no domains FT predicted no signal peptide 1 TMHs" FT /db_xref="InterPro:IPR011836" FT /db_xref="UniProtKB/TrEMBL:A1K506" FT /protein_id="CAL93911.1" FT /translation="MSDEADSPLSSVPPARARACALLRLWGGRLAVAGLCVWIAFAALF FT LVLREFVLPNVDAYRAEVEAGLTEALGAPVAIEHLSGDWSGMRPRLHLTGLALRDAEGR FT PALRLERVDATLGWLSLAQLRPFFHRLEIDGPDVAITRRADGRLEIAGMTMDDGPSDGS FT FLDWLLAQRQIVVRDAALTWTDELRGAPPLRLSQVQFRLERSFHRHRFALQAQPPAQLA FT SALDLRGELQQLVPQTPAASVGKLYVALDHADLGGWRQWVDYPVALSGSGGLRAWIDLE FT ADGRQAITTDVSLAGVETRLGDSLPVLQLARLGGRLTGRRLAHGFEVGAQGLSLLTGDG FT IRLAPTDFHLQVRHDGDSGGAGGFVRANQLDFAALAALAAHLPFDDSVRARLAAFDPRG FT RVDDLRLDWRGELDALQDWSVAAHFNDIGLAARDGIPGLGGLSGQVEGNLRGGRFRLDG FT RDTHLDLPEVFVESRLLFSTFRAEGGWSRADQRLEITLDSAGFDNPDAAGTASGRFWPG FT SEGAGEIDLQARLTRAEGTAVWRYLPRVVNRDTHDWVRNAIRQATVPDTRLRLKGRLAD FT FPFRKGEGQFLVAIQVADAVLDYAPGWPSIEGIFGEVRFEGPGLRIAANRGRIFGVALS FT DVVAQVPDLDAPPSEVMTLTGKAAGSTADFLRFVSESPVAERIDRFTDAMRAEGTGTLD FT LKLVMPLRHARDTSVQGEYRFSGNRMWVVDGLPALEDAVGRLRFTADELVIPEVRARLF FT GEPMALAARTSADGAVSFSASGKVTAAGVQRAYGWPVLNHFAGASPWQAEIAVRREGTR FT VDVRSALDGIASSLPYPLNKTTADAWPLHLALDYPAGTPGSTLKLTLADRVQVELERRE FT GDARPGGVVRGGVGVFQPVRVAERGVLVAATLDELDVDGWRRALGLSGGDEGAEGTAAA FT LPLAGVALQAKHAQVFGQRFSDLSLRAVADAGGWRARLDSTQAQGEFDWREAGNGTLVA FT RFARLAVGDKDDVSTSAADEAPTDPPPRSLPGLDVTVAQLSLRGQPLGRLEVLALNRDR FT QWVLERFALSRAEGRLAGHGLWRPGNDPRTELDFRLESADAGRLIHALGYPDAVRGAPA FT ELRGKLAWRGAPTRIDYPTLAGNMTVEVEKGQFNKLEPGVGRLLGILSLQSLPRRITLD FT FRDVFSEGFAFDRISGSIDVRAGVMRTEDLEIRGPAARVLMRGSADVSSESQDLRVTVQ FT PTLSESVAIGAAAALINPVAGAVTYLAQKALSDPIEKLFAYEYAVTGAWDDPKVEKLGS FT PAENLIPQLPRAQPAPRSGSTAP" FT CDS 1410696..1411553 FT /transl_table=11 FT /locus_tag="azo1295" FT /product="conserved hypothetical carbon-nitrogen hydrolase" FT /function="predicted amidohydrolase" FT /note="conserved hypothetical carbon-nitrogen hydrolase. FT Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). FT InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: FT Carbon-nitorgen hydrolase no signal peptide no TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K507" FT /db_xref="InterPro:IPR001110" FT /db_xref="InterPro:IPR003010" FT /db_xref="UniProtKB/TrEMBL:A1K507" FT /protein_id="CAL93912.1" FT /translation="MNSSSPRSAPQTARPPVRVAAVQTVSGPDVAANLRVVAELVAAAA FT DDGAKLVALPEYFALISAVETDKVRLRERDGEGPLQHFLRETAARHRVWLVGGTVPLVA FT ASDQKVRNTTLVYDDRGERVARYDKIHLFGFQRGAERYDEAATIEPGREVVCFDSPAGR FT TGLSVCYDLRFPELFRAMAEPDLIVLPAAFTHTTGRAHWEVLLRARAIENQCYVMAPAQ FT GGCHPSGRVTWGHSMIVDPWGEILACREEGPGFVAADLHPERIASVRASLPALEHRCLP FT GAAS" FT CDS 1411624..1413069 FT /transl_table=11 FT /gene="tldD" FT /locus_tag="azo1296" FT /product="probable TldD protein" FT /function="predicted Zn-dependent proteases and their FT inactivated homologs" FT /note="Probable TldD protein. Homology to tldD of E. coli FT of 59% (sprot|TLDD_ECOLI). Suppresses the inhibitory FT activity of the carbon storage regulator (csrA). Pfam: FT putative modulator of DNA gyrase no signal peptide no TMHs" FT /note="Function unclear" FT /db_xref="InterPro:IPR002510" FT /db_xref="UniProtKB/TrEMBL:A1K508" FT /protein_id="CAL93913.1" FT /translation="MSKSTNPLKIAEKYLLSPYQLGEAEIEKVFRKLMRHRIDYADLYF FT QYHRAEAWSLEEGIVKSGSFDIEQGVGVRAISGEKTAFAYSDDISLDALVDAATATRAI FT AEAGSRRSVGIEPKKSRIRLYRADDPLASLDDTAKVKLLERLEGFARAEDPRVTQVMAH FT IAGSWEVVMVARNDGHMAADVRPLVRVSITVIMEENGHREQGSAGGGGRYDYGYFSDER FT LQGYARAAVHQARVNLAAEPAPAGTMTVVLGSGWPGILLHEAIGHGLEGDFNRKGSSAF FT SGRIGQQVAARGVTVVDDGTLPDRRGSLTIDDEGNPTERTVLIEDGILAGYMQDTMNAR FT LMGMAPTGNGRRESYAHLPLPRMTNTYMLNGDKDPQEIIKSVKKGLYAVNFGGGQVDIT FT SGKFVFSTAEAYLIENGKVTRPVKGATLIGNGPDVLTRVSMIGNDMALDPGVGTCGKDG FT QSVPVGVGQPTLRVDGLTVGGTA" FT CDS complement(1413077..1413520) FT /transl_table=11 FT /locus_tag="azo1297" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to CV3985 FT of C.violaceum of 42% (tremble:Q7NR00). Has FT PF07025:(IPR010745)Protein of unknown function FT (DUF1316);This family consists of several hypothetical FT bacterial proteins of around 150 residues in length. The FT function of this family is unknown. No signal peptide or FT TMH present." FT /db_xref="GOA:A1K509" FT /db_xref="InterPro:IPR007048" FT /db_xref="InterPro:IPR015801" FT /db_xref="InterPro:IPR017737" FT /db_xref="UniProtKB/TrEMBL:A1K509" FT /protein_id="CAL93914.1" FT /translation="MPSLIDRLMATGGGAGTTAPTADTLRTALARDLEALLNTRATCAL FT DATSEFPRASGSLLTFGLPDFDSLNLHGAPDRRRLTDEVRRAIERNEPRLARVQVSMVA FT SPANGQPIRLRIAAELRSDARRRTPVSFDATLQLSSNAYRVKP" FT CDS complement(1413533..1414231) FT /transl_table=11 FT /locus_tag="azo1298" FT /product="conserved hypothetical membrane protein" FT /note="Conserved hypothetical membrane protein. Homology to FT cv3984 of C. violaceum of 47% (trembl|Q7NR01(SRS)) no FT domains predicted no signal peptide 1 TMH" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR017732" FT /db_xref="UniProtKB/TrEMBL:A1K510" FT /protein_id="CAL93915.1" FT /translation="MAIASTTSAAAVPDRSPGATPLIELLDDGFHLLALLRQRARPRHY FT DSFVDRVLALLRDFERNALAAGKAPPEIEQARYAFCAALDEVVLSSDFPLRAEWERQPL FT QLRLFGEHLAGEGFFERLAALRLAPHENIECLEVFHACLLLGFRGKYLLDDSDRIRYLQ FT RTLAQELQRVRGDPQTPPALWKLPEEELTPPRPGLPTRFYAGILLVVGLAFFALYQVLL FT DQRAQALFGV" FT CDS complement(1414245..1415591) FT /transl_table=11 FT /locus_tag="azo1299" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Hypothetical protein,50% identity (67% similarity)to FT TrEMBL;Q7NR02. TrEMBL;Q88IA6(39%),Q8XRU1(37%). Has FT PF05936(IPR010263):Bacterial protein of unknown function FT (DUF876);This family consists of a series of hypothetical FT bacterial sequences of unknown function. No Signal Peptide FT or TMH reported present." FT /note="Function unclear" FT /db_xref="InterPro:IPR010263" FT /db_xref="UniProtKB/TrEMBL:A1K511" FT /protein_id="CAL93916.1" FT /translation="MLKTRRVLWGEGMFLRPQHFQQQALQHEAALAGSLQGLYRHAWGA FT RAVVVDETGLAAGVLRFDNLSIWFRDGTRYCAPEHDPLPPSRDLAGISADGNTVLVYAC FT LPELHPHGGNVGDHERNPAQRVRFLKRHAASCDLYSGALEAELTLLDLNVQLRLEDENR FT DGFESLPVARLRRDGQGQWSVDASYLPPSLDLALDGAAARLLRRLLDILQVKSGLLAAR FT QREHATHLLEYGSSDIAAFWLLHTVNRNYARLQHLERARPLHPEALYLALAELYGELVT FT FSRSHTLADLPPYRHENLAGSLTPLDDRIRDLLDTVVSNRHQVITLRNPKPSFHIGHLD FT NERLLEADFYLSVQSSMPAAAVIDAVPSKLKIGAPDDVEKILNSAVRGVAVVHATQTPS FT SVPVRIGNHYFALEPNSEVYQRMVQARSVCVYVPQTLADLKLELIAVFR" FT CDS complement(1415603..1416217) FT /transl_table=11 FT /locus_tag="azo1300" FT /product="Hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Hypothetical protein,34% identity (52% similarity) FT to TrEMBL;Q7NR03. No domains, repeats, motifs or features FT were predicted with confidence." FT /note="Function unclear" FT /db_xref="InterPro:IPR017734" FT /db_xref="UniProtKB/TrEMBL:A1K512" FT /protein_id="CAL93917.1" FT /translation="MNFLDWPALPIFQGCKARRRPSSTRAFIARVPSPAGRILYVCASL FT FLAGCAVTSTPPRLVLSAETALNRDGSGASLSVVVRTYQLRDRRAFDRLGFDVFGGGRS FT DTEIFGAELLSSQEFVLTPGARLSDALPLHAEASYVGIVGLFMQPDGELWRGLVDAQAT FT RKLGLQVRLQECYLRIESPAPLKIPGQTEGRTPSCPAGRPS" FT CDS 1416388..1417059 FT /transl_table=11 FT /locus_tag="azo1301" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology of the FT entire protein with the data bank. Pfam: D-alanyl-D-alanine FT carboxypeptidase (101-209 aa) no signal peptide 1 TMHs" FT /db_xref="InterPro:IPR003709" FT /db_xref="InterPro:IPR009045" FT /db_xref="UniProtKB/TrEMBL:A1K513" FT /protein_id="CAL93918.1" FT /translation="MVPVPVCSRLRSESGRRRNPGAFWMAGWTLLGLSLAVLVAVLGSG FT WEPGAQAGVTSVTSQSTPLSRGFADDTLALLLPQSAARGPAAAAWIPGEGEVDRDWAKL FT DARFRERLQRVVERLRGRGQHFVLVEGYRSPERQDQLFALPTKVTAARAWESRHQYGLA FT ADLAPVRDGAASFETDGLGMEAYRLLGEEAEAAGLTWGGRWDIRDYGHVEMPDRPTRHA FT G" FT CDS 1417056..1420748 FT /transl_table=11 FT /locus_tag="azo1302" FT /product="conserved hypothetical membrane protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical membrane protein. Homology to FT CV3712 of Chromobacterium violaceum of 35% (trembl|Q7NR05) FT Signal P reporting Signal Peptide Present. TMHMM2 reporting FT 2 TMH's present. Has PF06761:(IPR009612)ImcF-related;This FT family represents a conserved region within several FT bacterial proteins that resemble ImcF, which has been FT proposed [1] to be involved in Vibrio cholerae cell surface FT reorganisation, resulting in increased adherence to FT epithelial cells and increased conjugation frequency. Note FT that many family members are hypothetical proteins. Has FT PF06744,(IPR010623)Protein of unknown function FT (DUF1215);This family represents a conserved region FT situated towards the C-terminal end of several hypothetical FT bacterial proteins of unknown function. A few members FT resemble the ImcF protein, which has been proposed to be FT involved in Vibrio cholerae cell surface reorganisation FT that results in increased adherence to epithelial cells FT line and increased conjugation frequency." FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR009612" FT /db_xref="InterPro:IPR010623" FT /db_xref="UniProtKB/TrEMBL:A1K514" FT /protein_id="CAL93919.1" FT /translation="MNPRFRRLMRISGPALLLLAAVLVLVQTLPPGWDRGGEGVVRVLA FT AFSVVLLAGVALWAFSRRWRMRGATGAAAQARPGPASAEPGSVLRSGLRAAVESIRASD FT LGRRAGRNALGQLPWYGVIGAEGAGKTALIKQSGLSFPFEHLPGCPDDGDCGWFLATEA FT VVLDLGGRYLSDSLGDSSWLEFWRELKRLRPAQPLDGLVAAVSAAELLGGDERALHAHA FT TRVRACIDEIQDAVGVRLPVYLVVTQLDLIGQGALPSERDAPRSPFGFAIPAVPADRTI FT DSVAERFALFRAGLRHHVLAAAEMHDPLTQSEQLSFSVEFDGLGARLNSFVRVLLGNNP FT YHVQPALRGVYFSSLPAGGGHTVLGPRTDALAQRFELDLRDTRSSGFSHDRQDAPSPAR FT LFHDVVLPDRFFARRLRSASASQGRWAWMATSLAVVCLAVGLMTASFTGNHQLLTELAA FT SQQAAQTSGDGVPLAVELERLVALQHQLERLRRYRLAQPPWRLRFGLYQGDKVEAMLRA FT RYFAGVRQLMLEPVAREIERELGATASAPVRRAGAGRPAGAVTANDRPPAGLPIIPLGE FT GAAAQPLRAAGIPPGGPALSARVRRSAGESAGIEGQYNALKTYLMLADPSRIEAEHLAD FT QLPRFWRRWLQAERGQTPLPDIYALAQRMVDFYIEERAAPDLPVIAAEGALVARSRSAL FT IGAMRRLPPEERIYRALLAAANVRFEPVSVTGVLRDHASDLVGGSVVVPGAFTRKAYDE FT YLRSAFGLSGRDLDTGTDWVLDDHAGNLAESSSGAVDPGALERRYREDFEIAWLGFLQG FT LTVPVFADLAAATDALGQLGDPARSPLLPLLQRAGHELGGRGRAVEGERGRMETVLARA FT RGVLDAGRSEAVADAGPASEASPLPGVVALAGGPVEAGDPRLDGALREYLARLLKLRDR FT LAVVAAAGSDAEPAIRLVRATFDGRESEFPASLSFVDNELLGAMDSASRTALRPVLTQP FT VLRAFDALIPLVSRDLDLAWQREVLPHWRRLAETFPFSDSEHDVVPSELAEFAAQGGVL FT DRFVERRLEGLVSRRGQGLATRNWGDRSIALNPAFLPALERLLAFGAALPRQGELARFE FT LQPMPTPGLTEIVIEIDGQSLRYRNGPQTWASFSWPGTAVQEAAVRVVDVSGAPGAVLH FT RRGRMALIRLLAEASVQGATPGPLQFAWNGAGAAVRFNFRSLSGASPLDLLALRKLTLP FT DRISR" FT CDS 1420836..1421360 FT /transl_table=11 FT /locus_tag="azo1303" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Hypothetical protein,50% identity (66% Similarity) FT to TrEMBL;Q8XRT8. TrEMBL;Q7NR06(60% identity,74% FT similarity). Has PF05591;Protein of unknown function FT (DUF770)(IPR008312)This family consists of several proteins FT of unknown function from various bacterial species. No FT Signal peptide or TMH present." FT /note="Function unclear" FT /db_xref="InterPro:IPR008312" FT /db_xref="UniProtKB/TrEMBL:A1K515" FT /protein_id="CAL93920.1" FT /translation="MVRESTQKKLSRVRPPRVQITYDVEVGDAIETKELPFVLGVLGDY FT TGHAREQLPRLKERKFVAIDRDNFDDVMKALAPRLGLRVPNRLSAEGGLLGVELGFAAM FT EDFEPQNVVAQFTPLRRLLEARQRLAELRNKLVGSERFEALLNEAVADRDALQALKGEL FT DARGGMHDGAR" FT CDS 1421344..1422837 FT /transl_table=11 FT /locus_tag="azo1304" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Hypothetical protein,63% identity (81% similarity) FT to TrEMBL;Q8XRT7. TrEMBL;Q7NR07(73% identity,86% FT similarity). Has (IPR010269 )PF05943:Protein of unknown FT function (DUF877);This family consists of a number of FT uncharacterised bacterial proteins. The function of this FT family is unknown. No Signal peptide or TMH present." FT /note="Function unclear" FT /db_xref="InterPro:IPR010269" FT /db_xref="UniProtKB/TrEMBL:A1K516" FT /protein_id="CAL93921.1" FT /translation="MTARDEHLVRTSASPQVEAEGAGLLDSLIARSRVAVDEAEHDRTR FT DLIGELVQEVMSGALPLTCDLAASIDARIAELDELISAQLNEIMHDPEFQRLEGSWRGL FT KYLVDAAETGPMLKLRMLNVSKKELIKDFRQAAEFDQGALFKKVYEEEYGTFGGAPFAA FT LVGDYEFSRHPEDLYLLEELAHVAAAAHAPFIGAVAPAMFGLDNFAELGRPRDLSRIFE FT TVEYAKWKSFRASDDSRYVGLVLPHVLGRLPYGRDTHPVDAFNFEEDVDGSDHAKYLWT FT SAVYSYASRLTAAFAQFGWLAAIRGVEGGGLVEDLPLHTFRTDDGEIGAKCPTELAITD FT RNEKLLADLGFIALTHCKNSDYAAFFSGQSVQRPRTYNTDAANANARLSAQLPYIFASS FT RIAHYLKAMMRDKVGSFASRQNVQDFLNAWLAQYVLLDDAASQEAKSKYPLREARVEVV FT EVPGRPGAYRAAAFLRPHFQLDELTISLRLVAELPQPAR" FT CDS 1422881..1423378 FT /transl_table=11 FT /locus_tag="azo1305" FT /product="conserved hypothetical protein" FT /function="Hemolysin-coregulated protein (uncharacterized)" FT /note="Conserved hypothetical protein. Homology to CV3977 FT of C.violaceum of 77% (tremble:Q7NR08). Has FT PF05638:(IPR008514)Protein of unknown function FT (DUF796);This family consists of several bacterial proteins FT of unknown function. No signal peptide or TMH present." FT /db_xref="InterPro:IPR008514" FT /db_xref="InterPro:IPR017728" FT /db_xref="UniProtKB/TrEMBL:A1K517" FT /protein_id="CAL93922.1" FT /translation="MAFDAFLRIEGIPGESTDDKHQDWIEVLSFNHSMEQPASATASSV FT GGATAERVNHGSFEVTHLLDQASPKIYDACCTGKHIKEVTLELCRAGGDKVKYMEVKLE FT QVVISKVVPAGAANDQGFPQEKISFSYGRIKWTYTRQKRDDGTGGGNVSAGWDLTANKA FT VA" FT CDS 1423378..1423854 FT /transl_table=11 FT /locus_tag="azo1306" FT /product="hypothetical secreted protein" FT /function="Outer membrane protein and related FT peptidoglycan-associated (lipo)proteins" FT /note="Hypothetical secreted protein. Homology to CV3976 of FT Chromobacterium violaceum of 26% (trembl|Q7NR09(SRS)). No FT TMHs Signal Peptide Present. Has PF00691:OmpA FT family;(IPR006665 OmpA/MotB):The Pfam entry also includes FT MotB and related proteins which are not included in the FT Prosite family." FT /db_xref="GOA:A1K518" FT /db_xref="InterPro:IPR006665" FT /db_xref="UniProtKB/TrEMBL:A1K518" FT /protein_id="CAL93923.1" FT /translation="MALIGLSHRVRTRARGAAGALLVAVLLSACAGAPPQAEPAAEVEP FT LRPAPESPVVAPAGEPEPAVAGRHTFRFDTLSVALSESEKVRVVTLAEQVRGARAVVVR FT GSCDRNAVGNAREAAIARALAVRHVLVENGVPAAKIRTRYSTEDGTHAVVLRVN" FT CDS 1423911..1426628 FT /transl_table=11 FT /locus_tag="azo1307" FT /product="probable vgr related protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Probable vgr-related protein,41% identity (55% FT similarity) to TrEMBL;Q7NY43. TrEMBL;Q8XSF8 Has (IPR006533 FT Rhs_Vgr)PF04524:Protein of unknown function, DUF586;This FT family contains a conserved region in several bacterial FT proteins of unknown function. Coils2 program predicts FT presence of a coiled coil." FT /db_xref="InterPro:IPR006531" FT /db_xref="InterPro:IPR006533" FT /db_xref="InterPro:IPR017847" FT /db_xref="InterPro:IPR018769" FT /db_xref="UniProtKB/TrEMBL:A1K519" FT /protein_id="CAL93924.1" FT /translation="MTDSLRSAAADLLSVADAISFLPATRLVELRFAGGGPEGSPLIAL FT SAYGEEGLNMCHRITVRCVAVDARIELITMLGLRAAIGIRTADGRERIRCGVVTAGVAL FT GADGGFAAYEITVEPPLALLRHRWGSRVFQALTVPEIVRALVEEHRGRNPIFNAGLGLR FT FDLQRRYECRSYCVQYHESDLEFIERLLAEEGIGWRFDHEEDAAGAGPSTLLVLFDAAD FT SLPPAEPPSVRFHRGNASETEDSLTSWSAQRSVGAGRTTLTSFDYKPAATTTARAEGVE FT EDGGDATSLEQALEDFRPQTLHYAPTVDGLAAYAALRQQARDAERNTFEADGDARGLTA FT GAWFQLEGHPRHEHEPGEERRFVVTRLTFVARSNLPVHSSLIDAAGEGRAWAGAGKTPY FT QIRLTAVRRGQASAGIFPPRRDLRPTARGPQSAIVVGPHDEEVHTDEYGRIRIQFHWQR FT QEDHPDGGAAYDERSSCWVRVALPSAGIAWGHQFIPRVGQEVLVDFLDGDIDRPVVTGV FT LGNGCHPPVRFSGVGALPANKALSGIKSREHGGAGFNELVFDDTAGQLRARLSTEHAAT FT QLNLGCLVHPRENGQATVRGDGAELRTDGAAAVRGARGVLVSAHGRPRAAGSQLAREEL FT MELLEQARELARTLSDYAGSHQGVPAESSGADALLQAVRQWDGDRAEGADRERGDGLVC FT AAAPEGIVIATGATLISCAAEDHEVCASHQLRLTAGEGLVANAGAGIGLFAQSGDLRSI FT AHQGLHLTQAQQGDVVTEAARNVRVSAAEGEVLISAPVIRLVAQDGSFLRLGGGIALGT FT EGAVQVKAARHSLGGPATDSIDLPVFDRAGADQRFALLYPGAEGAEPQPAGGRRYEITL FT KDGRVVAGTADAEGRTDMLTSEAMQVAHIRVFDR" FT CDS 1426635..1428473 FT /transl_table=11 FT /locus_tag="azo1308" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to CV3969 FT of C.violaceum of 56% (tremble: Q7NR16). Has FT (IPR010272)PF05947:Bacterial protein of unknown function FT (DUF879);This family consists of several hypothetical FT bacterial proteins of unknown function. No signal peptide FT or TMH present." FT /db_xref="InterPro:IPR010272" FT /db_xref="UniProtKB/TrEMBL:A1K520" FT /protein_id="CAL93925.1" FT /translation="MFDELLRYYETELGYLRELSGEFARRYPKIAGRLQLEGDQCEDPH FT VERLIEAFAFLGARIHRRLDDDLPEITASLLDALYPHFLQPVPSASIVQFELDPARPEV FT AGRYRIERGQMLLSPPVDDLACRFRTCYPVELYPLTVASARVVFTAVSAHLAAQAPDAT FT AVLTLSLETQGGVDLGALQLDRLRFFLDGEPALTYLIHQLLLQHEAQPWVEDQGGRLQR FT LPRGALRPVGFARDEGLLAYDDRSFLGYRLLTEYFTLPEKFLFVDVTGLPALSGQRFRL FT HCPIRRYPGAERHTRLLESVEARHFRLGCTPVINLFPRAAEPVRVTHRRESYPIVVDAR FT RPLGYEVIAIERVHYVERDDAGTRATEVPPLYGLNGAAEADAARFRWHARRDGSTRAND FT RGTEVSLHLVDARFSAVRPATEVLSLALLCSNRDLPERLPFGGGDAGPHTDFTLPGQAV FT VKRVRLLRKPTSSLRNPHRKGFQWRLVSHLSLNYLSIVSQGKGALQDILALYNPLDRPA FT ARRHIEGIREVNSAPAVARLAGPDFISFVRGTGVDLVLDEEAFVGASAYLFASVLERFF FT ALYCAPNSFVQLRYRCLNDEENVVQWPPRSGEAIVI" FT CDS 1428437..1429453 FT /transl_table=11 FT /locus_tag="azo1309" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to CV3967 FT of C.violaceum of 45% (tremble:Q7NR18) Has FT (IPR010732)PF06996:Protein of unknown function FT (DUF1305);This family consists of several hypothetical FT bacterial proteins of around 300 residues in length. The FT function of this family is unknown although one member FT (Q93IT4) from Salmonella enterica is thought to be involved FT in virulence. No signal peptide or TMH reported present." FT /db_xref="InterPro:IPR010732" FT /db_xref="UniProtKB/TrEMBL:A1K521" FT /protein_id="CAL93926.1" FT /translation="MATPQRRSDRDLSAELAAEPHCFGFFQAVRLLELISEAAGHERPV FT RFRAALSLAFPPSELAAATVPAGAEGERPMGGELSVAFMGLTGPSGVLPHVYTEMLLER FT NHLRHDGAAGAFLDLFNHRALALFHEGWRKYRHWLAAERAGTDRFAEHLLDLCGLGPAA FT LASIGGGETPARLAFLRYAGLLAQRPLSAHALETVIAGVLGVTVRIESFSGRWMVLPEA FT ERSRLGTYACGLGSEACSGDRVWDAQGAVRLRVGPVRRQQFDTLLPGGAAARMLAGLIR FT YAVGHALACTVVVVLDRRDIPQPRLGADAPLSLGGNLWFEARAREDDADDLRYALLD" FT CDS complement(1429450..1430565) FT /transl_table=11 FT /locus_tag="azo1310" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to CV3963 FT of C.violaceum of 37% (tremble:Q7NR22). Has FT (IPR01065)PF06812:ImpA-related N-terminal;This family FT represents a conserved region located towards the FT N-terminal end of ImpA and related proteins. ImpA is an FT inner membrane protein, which has been suggested to be FT involved with proteins that are exported and associated FT with colony variations in Actinobacillus FT actinomycetemcomitans. Note that many family members are FT hypothetical proteins. No signal peptide present. No TMH FT present." FT /db_xref="InterPro:IPR010657" FT /db_xref="InterPro:IPR017740" FT /db_xref="UniProtKB/TrEMBL:A1K522" FT /protein_id="CAL93927.1" FT /translation="MDEAEFRAGLLAPISAANPAGEDLCYTPLFDDIRNARHADDDALG FT QGEWTHAVKAADWPRVVELCRTALCARSKDLQLAVWYVDALVRHQHWPALEFGLGFLSD FT LLDGFWAVVHPLPDGSDWGERTARLEWLGRQLADQVAALPLIADEVRSYSLHDYRTAIE FT RENRPDADSAAGAPAAAIDAERLRRAFRAADTAQLMQRRIQLAATLAAASRLQDCCDQH FT FGMDGPSFAALQAEIGACDALLSRHLPPTITPPQSSQASTPARLQGEPDRPPSSRADDL FT PSQPYSSDAPPLAPLPAGAPPDRDAAIRQLAEIGRFFRIHEPHSPVALLIERAVRWAGM FT PFEDWLQAVVKDAATLDHLRELLDLPPGARN" FT CDS complement(1430572..1430835) FT /transl_table=11 FT /locus_tag="azo1311" FT /product="conserved hypothetical protein" FT /function="uncharacterized conserved protein" FT /note="conserved hypothetical protein Has 2 PF05488 PAAR FT motif(IPR008727);This motif is found usually in pairs in a FT family of bacterial membrane proteins. It is also found as FT a triplet of tandem repeats comprising the entire length in FT a another family of hypothetical proteins." FT /note="Function unclear" FT /db_xref="InterPro:IPR008727" FT /db_xref="UniProtKB/TrEMBL:A1K523" FT /protein_id="CAL93928.1" FT /translation="MKRLIRLGDPTTHGGVVISASSSYEVLGRPVARVGDRVTCPMQGH FT GLAVIIEGDPDWLIDGRPVALEGHLTSCGATLIATVASVGRE" FT CDS 1431039..1432133 FT /transl_table=11 FT /locus_tag="azo1312" FT /product="tRNA (uracil-5-)-methyltransferase" FT /function="SAM-dependent methyltransferases related to tRNA FT (uracil-5-)-methyltransferase" FT /EC_number="2.1.1.35" FT /note="tRNA (Uracil-5-)-methyltransferase (EC 2.1.1.35) FT (tRNA(M-5-U54)- methyltransferase) (RUMT). Catalyzes the FT formation of 5-methyl-uridine at position 54 (M-5-U54) in FT all tRNA." FT /note="Family membership" FT /db_xref="GOA:A1K524" FT /db_xref="InterPro:IPR010280" FT /db_xref="InterPro:IPR011869" FT /db_xref="UniProtKB/Swiss-Prot:A1K524" FT /protein_id="CAL93929.1" FT /translation="MSLPRFDPAEYETQLAAKIARFKSDFAPLDLPEPEVFRSEPLHYR FT LRAEFRIWHSEGRLDYAMFDPADPKRPVLIDGFPAAAAPIAAAMPVLRERVMASEPLRR FT KLFQVEFLATLSGELMISLVYHRPLEADWEAAARELAAAMGVQLIGRSRKQKIVLERDW FT VLESFELDGRTLHYQQIEGSFSQPNGGVNRQMLVWARRQAEGSGADLLELYCGNGNFTV FT ALAPLFGKVLATEMSKSSVRAAHYNLAANAVDNVTMVRMASEEISDALAGGRAYRRMQG FT IDLAGYRFGTLFVDPPRSGLDEATVALARRFDRILYISCNPQTLHDNIAALRDTHGIAA FT AAAFDQFPYTHHLECGVLLQKTAA" FT CDS 1432168..1432506 FT /transl_table=11 FT /gene="phnA" FT /locus_tag="azo1313" FT /product="putative phosphonoacetate hydrolase protein" FT /function="uncharacterized Zn-ribbon-containing protein FT involved in phosphonate metabolism" FT /EC_number="3.11.1.2" FT /note="PhnA protein: Phosphonoacetate hydrolase is a novel FT carbon-phosphorus bond cleavage enzyme.The phnA gene is FT part of a large operon in Escherichia coli associated with FT alkylphosphonate uptake and carbon-phosphorus bond FT cleavage. PhnA is found in both gram positive 69% PhnA.PhnA FT protein Pfam:PF03831; PhnA; 1. TIGRFAMs:TIGR00686; phnA; FT 1." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K525" FT /db_xref="InterPro:IPR004624" FT /db_xref="InterPro:IPR013987" FT /db_xref="InterPro:IPR013988" FT /db_xref="UniProtKB/TrEMBL:A1K525" FT /protein_id="CAL93930.1" FT /translation="MSSLPKCPKCSSEYTYEDGENYVCPECAHEWPQAAAAGVEEARVV FT RDANGNVLQDGDTVVVIKDLKVKGVSSVVKVGTKVKNIRLVDGDHDIDCKIDGFGAMGL FT KSSFVKKA" FT CDS complement(1432522..1432893) FT /transl_table=11 FT /locus_tag="azo1314" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ebA3072 FT Azoarcus sp. EbN1 of 61% (gnl|keqq|eba:ebA3072(KEGG)). No FT domains predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K526" FT /protein_id="CAL93931.1" FT /translation="MQHDPIPAGTSERGLRVALIFALAAERLSTFYEHGQWLTEAQGAT FT LAAEWLARSRRQLPLEVRRALSAASDTLARQVQGSVSREAGLYIAHEMMEALDPRYESD FT IAKSLMEECERLLDSAGEG" FT CDS complement(1432952..1433749) FT /transl_table=11 FT /locus_tag="azo1315" FT /product="conserved hypothetical membrane protein" FT /function="ABC-type uncharacterized transport system FT permease component" FT /note="Conserved hypothetical membrane protein. Homology to FT blr8071 of B. japonicum of 56% (trembl|Q89BS7). No domains FT predicted signal peptide probable 6 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR005226" FT /db_xref="UniProtKB/TrEMBL:A1K527" FT /protein_id="CAL93932.1" FT /translation="MNVIELSPLDLALAALLVIALAAVSRWMRLAVEKQLLIAALRTTL FT QLLLIGLVLKALFENAHLYWVALMALGMVVIAGREVVARQKRRLAGWWGFGLGTLSMFV FT SSFSVTVLALLTVISNHPWYAPQYAIPLLGMVLGNTMSGISLGLDRLTQDAVQKRPMLE FT TRLALGEDWQSAIADSRRDAIRVGLIPIINAMAAAGVVSLPGMMTGQILSGTPPVEAVK FT YQILVMFLIAAGTGFGTMVAVSAAARRLFDDRHRLRLDRLRQD" FT CDS complement(1433746..1434351) FT /transl_table=11 FT /locus_tag="azo1316" FT /product="putative ATP binding protein" FT /function="ABC-type sulfate/molybdate transport systems FT ATPase component" FT /EC_number="3.6.3.-" FT /note="47% AAA_ATPase.IPR003439; ABC_transporter.IPR008995. FT Pfam:PF00005; ABC_tran; 1. SMART:SM00382; AAA; 1. FT non-secretory protein" FT /note="Function unclear" FT /db_xref="GOA:A1K528" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A1K528" FT /protein_id="CAL93933.1" FT /translation="MPSLRLDQLASRHVGPVSLEIAAGECVCLRGASGSGKSVLLRAIA FT DLDPHGGEAFLDDHACSAMPAPQWRRQVALVMAESQWWAAQVGEHFAHGLRPEWLERLG FT LAADAAQWEVARCSTGERQRLALLRTLMLQPAVLLLDEPTGNLDADSTRRVEALLRDYQ FT ADSGCAVLWVSHDEAQAARVAHRQFVLDGGQLREQAEQ" FT CDS 1434635..1435387 FT /transl_table=11 FT /locus_tag="azo1317" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to CCO1214 FT of Campylobacter coli of 38% FT (gi|57168023|ref|ZP_00367162.1|(NBCI ENTREZ)). Has PF07021, FT Methionine biosynthesis protein MetW;IPR010743; This family FT consists of several bacterial and one archaeal methionine FT biosynthesis MetW proteins. Biosynthesis of methionine from FT homoserine in Pseudomonas putida takes place in three FT steps. The first step is the acylation of homoserine to FT yield an acyl-L-homoserine. This reaction is catalysed by FT the products of the metXW genes and is equivalent to the FT first step in enterobacteria, gram-positive bacteria and FT fungi, except that in these microorganisms the reaction is FT catalysed by a single polypeptide (the product of the metA FT gene in Escherichia coli and the met5 gene product in FT Neurospora crassa). In Pseudomonas putida, as in FT gram-positive bacteria and certain fungi, the second and FT third steps are a direct sulfhydrylation that converts the FT O-acyl-L-homoserine into homocysteine and further FT methylation to yield methionine. The latter reaction can be FT mediated by either of the two methionine synthetases FT present in the cells. No signal peptide. No TMHs." FT /db_xref="UniProtKB/TrEMBL:A1K529" FT /protein_id="CAL93934.1" FT /translation="MKSYSQAFYADRHAKTVHSAHTILSIVLQRIPQVSSAVDLGCGVG FT TWLSVLQEKGVKDVQGLDGNWVDQNLLAIPRASFKQVDLANGDIRLPCRYDLAISLEVA FT EHLPETRARDFIASLTALSDFVLFSAAVPFQGGINHVNEQWQHYWAALFAERGYAVHDI FT VRARIWDDSLIPFWYRQNILLYSRHHHLPGAAEAGPAVALPAPMPLDVVHPEHYLAKAR FT AQDGVRRSFRVFGRSVRDYMWSKLGQTH" FT CDS complement(1435529..1436443) FT /transl_table=11 FT /locus_tag="azo1318" FT /product="conserved hypothetical membrane protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical membrane protein. Homology to FT RS04440 of Ralstonia solanacearum of 40% (trembl|Q8Y277) FT TMHMM2 reporting 2 TMH's present. Signal peptide Present. FT Has PF04280;Tim44-like domain(IPR007379):Tim44 is an FT essential component of the machinery that mediates the FT translocation of nuclear-encoded proteins across the FT mitochondrial inner membrane. Tim44 is thought to bind FT phospholipids of the mitochondrial inner membrane both by FT electrostatic interactions and by penetrating the polar FT head group region. This family includes the C-terminal FT region of Tim44 that has been shown to form a stable FT proteolytic fragment in yeast. This region is also found in FT a set of smaller bacterial proteins. The molecular function FT of the bacterial members of this family is unknown but FT transport seems likely." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K530" FT /db_xref="InterPro:IPR007379" FT /db_xref="UniProtKB/TrEMBL:A1K530" FT /protein_id="CAL93935.1" FT /translation="MKGISLFAAVLALGLALNAPQAEAAKRLGGGTSSGMQRQMSPAQT FT TPSAPPAQAPTAPAASSSAKAPAGTATPAAQPKRSWMGPIAGLAAGLGLAALASHLGFG FT EELASMMMIGLLVMAVLVVVGLIMRRRAAAQHQGGMQYAGASHGAPSARSYDVAMPQSA FT GNTPAPAAAVAEPAAGNIPADFDVQGFVRQAKVNFIRLQASHDAGNLDDLREFTTPEMF FT AELKTNILARGQSAQQTDVLEIDAEVVEVVEEGSRYIVSVLFRGLLREDRDAAPEQIHE FT VWHLVKPRDGSAGWKLAGIQQAQ" FT CDS complement(1436614..1437468) FT /transl_table=11 FT /locus_tag="azo1319" FT /product="putative methyltransferase" FT /function="SAM-dependent methyltransferases" FT /EC_number="2.1.1.-" FT /note="Hypothetical protein Rv1403c/MT1447/Mb1438c FT precursor. TREMBL:Q92U99_Putative methyl transferase, FT S-adenosyl-L-methionine (SAM)-29% identity, 42% similarity. FT InterPro: ubiE/COQ5 methyltransferase pimt: FT protein-L-isoaspartate O-methyltr Pfam: ubiE/COQ5 methyl FT transferase family, Dihydrodipicolinate synthetase family, FT TerD (Bacterial stress protein domains). HTH_1 predicted FT regulatory helix turn helix. TIGRFAM: moaC, met p-daseII" FT /note="Specificity unclear" FT /db_xref="GOA:A1K531" FT /db_xref="InterPro:IPR013216" FT /db_xref="UniProtKB/TrEMBL:A1K531" FT /protein_id="CAL93936.1" FT /translation="MNAPIEACASAPAATQPAPDLEAVKRRQQATWASGDFAVIGTTLQ FT IVGESLAEAVDLRAGEQVLDVAAGNGNATLAAARRFTAVTAIDYVPHLLDKAAARAKAE FT GLAVETKVADAEALPFEDGCFDVALSTFGSMFTPDHPRTAGELLRVVRHGGRIGLATWT FT PGGFLGDLFRVIGGHVPPPAGVRSPLRWGEESYLVELFGPQAAAIRCEHRMFNFRYRSA FT EHFIDIFRNYYGPTHKAFAALDADGQARLHADMKQLLEARNVGGADSLVVPAEYLEVVV FT TRH" FT CDS 1437635..1438639 FT /transl_table=11 FT /locus_tag="azo1320" FT /product="putative AraC-family transcriptional regulator" FT /function="AraC-type DNA-binding domain-containing FT proteins" FT /note="Putative AraC-family transcriptional regulator," FT /note="Family membership" FT /db_xref="GOA:A1K532" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR018060" FT /db_xref="InterPro:IPR018062" FT /db_xref="InterPro:IPR020449" FT /db_xref="UniProtKB/TrEMBL:A1K532" FT /protein_id="CAL93937.1" FT /translation="MSKDTLSDLLRAVRLRGAVFYYVSNRAQWAAEAPPARDIAAAVMP FT GAEHVMEFHLMARGCGWAAVDGLAPVRLAPGDIVVLPHGDAHVMSSAPGIAPQRISAEW FT VFATRQVPKPMPVAFHHGVHEPGATGPVDGAESVLVCGFLGCDLKPFNPLVAALPRLLH FT LPAARAGEWVAHVIDQAARESTEQRPGADAVLERLAEMMFVDTARRYLDSLPDDATGWL FT AGLRDRYVGRALALLHERPEQAWTMDDLGREVGLSRSALHERFLQYVGQPPMHYLANWR FT IQLGARLLRETNRTVASIAVEVGYESEAAFSRAFKRLVGQPPAAWRRTALTAA" FT CDS 1438850..1439548 FT /transl_table=11 FT /locus_tag="azo1321" FT /product="conserved hypothetical protein" FT /function="Phosphatidylserine/phosphatidylglycerophosphate/ FT cardiolipin synthases and related enzymes" FT /note="Conserved hypothetical protein. Homology to FT Psyc03001842 of Psychrobacter sp. 273-4 of 57% FT (gi|52853589|ref|ZP_00145853.2|(NBCI ENTREZ)). No domains FT predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K533" FT /protein_id="CAL93938.1" FT /translation="MAKFLNTSATNYFLEELIKNAKDRLILISPFLKLNDRMKELLADK FT NRLKIDVRIVYGKSELQPEEMNWLKELTYIRTSFCKNLHAKCYMNEELAIITSLNLYEF FT SQINNNEMGVLIRREEDGELYRETYDEAQRIIRISDEVRISLERVSADAKGEEEGKAEP FT EESGDKSGKLTTSKLAQKFGMKTGGVSGEACCCGTTGNAGWKALPDGQGEGGRRGVQDE FT FAFWAVFSLA" FT CDS 1439761..1440165 FT /transl_table=11 FT /locus_tag="azo1322" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K534" FT /inference="nucleotide motif:Gismo" FT /protein_id="CAL93939.1" FT /translation="MGAKEELLQNLSRLDASGGIQRIHRALTDAGLKYKGPSNSQTLLY FT YFRSRGHEIGVAAIRGSPALLSFPATFWRGRSGLAAALGRASSFHMQPEGFVSSSQYSA FT GQLRITTSSIETLLSIVDEIIIPEARAAGA" FT CDS 1440382..1441617 FT /transl_table=11 FT /locus_tag="azo1323" FT /product="probable protein kinase" FT /note="Probable protein kinase InterPro: Protein FT kinase,Protein kinase-like" FT /db_xref="GOA:A1K535" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR008271" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:A1K535" FT /protein_id="CAL93940.1" FT /translation="MIVVICTGSMAHSARFYWRRLGESRRLVNCVSSGRFPFLPRTLEM FT KKLWELPESLQRKLVEARLCKHGTLIGEMSSPHSSIYTFDLGANASPRYVVAKGIQVEE FT TMSDEERRKYFARALYEVNNAYAVFHHPLVHRFFDVDIILGVPFLLSRKRDATLRDVIA FT EGPVLLPEALSIAVQMAHSLSYCAQKGIVCHQDLKPENVFIDFINEHFSVPAEYPLACR FT VHLADFELANAYLVLRHPYGSRPYMAPEQYCNLHANTLPDFSRADVFAVGVILFEMLTG FT GVHPIGERTSLIWPRPAEGQSRKWLREDPWKQWLKSGAQTSTGDKSVDPETLLIIQDCL FT EVDSAMRPSKQALEVRLLERLRTVHKDTYDTLVLTLEYFDNISNESEELGWPYYAERLE FT SLNKAFSDRDPP" FT CDS complement(1441791..1442165) FT /transl_table=11 FT /locus_tag="azo1324" FT /product="conserved hypothetical GTP binding protein" FT /function="GTPases" FT /note="C-terminal part of GTP-binding protein hflX. FT TREMBL:Q7NU63: 66% identity; 83% similarity ( the protein FT of query matches only with C-terminal part (124 aminoacids) FT of putative GTP binding proteins in the database) FT InterPro:IPR006073; GTP1_OBG. PRINTS:PR00326; GTP1OBG FT Pfam:Sigma54_activat: Sigma-54 interaction domain Absence FT of transmembrane helices (TMHMM predicted)" FT /note="Function unclear" FT /db_xref="UniProtKB/TrEMBL:A1K536" FT /protein_id="CAL93941.1" FT /translation="MLEEIDAQDIPRIRVFNKIDHVGDAKAQAECEAALRARYPDCIVM FT SARRPDEVAKLRQTIVAFFQRDLVEAELLLPWSAQQLRKEIYANCEVLEERAEDKGAVF FT RLRGESEALERLRNRLLMVI" FT CDS complement(1442281..1443378) FT /transl_table=11 FT /locus_tag="azo1325" FT /product="hypothetical membrane protein" FT /function="unknown" FT /note="Region start changed from 1443402 to 1443378 (-24 FT bases), , Changed start codon from att to next atg" FT /db_xref="UniProtKB/TrEMBL:A1K537" FT /protein_id="CAL93942.1" FT /translation="MTTQTPTSPSRGADPNVGDELSVAAEPLENHGKAGDTPFAGEAEL FT KVLVAWLEQEPSDADGWHILNALTRRTLQRIDMAESTRCFTTEELCDWAQVTATSNLWK FT SVKTWWEARRRKIRHAMRYAGVEYEPLLDRRGGGGRGNKAVNSLRRIPLSETGSEDSLQ FT ETETSDDDTVTNARATPLAKETVYWGSTNSPVKLSGVLLRTLFSAGEIRIGSARHNILR FT ANLLGSSLFLLIFSLAVVVPMVIENRPIGTHHLALLFFVGIGAWMWWDKWRPVLHARED FT RITPLPDEWLPFVAAPAQLERKRTDSGEVLRLVRYVATCPVCGGSMHLASGAPEWPRRT FT VGRCADAPREHVFTFDPVKLTGHRL" FT CDS 1443478..1443669 FT /transl_table=11 FT /locus_tag="azo1326" FT /product="Hypothetical protein" FT /note="Hypothetical Protein. No domains, repeats, motifs or FT features could be predicted above threshold scores." FT /db_xref="UniProtKB/TrEMBL:A1K538" FT /protein_id="CAL93943.1" FT /translation="MINKDIVAEGARHFREHKNYKNPYELGSDAFNDFERGWVQALKRA FT DLANATPYLRSCSRHEEP" FT CDS complement(1443843..1445237) FT /transl_table=11 FT /gene="hflX2" FT /locus_tag="azo1327" FT /product="probable GTP-binding protein HflX" FT /function="GTPases" FT /EC_number="3.1.5.-" FT /note="GTP-binding protein hflX. trembl:Q7NU63:77% FT identity, 83% similarity The proteins contain GTP-binding FT motifs and are GTP1_OBG. PRINTS:PR00326; GTP1OBG FT Pfam:MMR_HSR1:GTPase of unknown function thdF: tRNA FT modification GTPase TrmE No signal peptide present (SignalP FT predicted). No transmembrane helices present (TMHMM FT predicted)" FT /note="Family membership" FT /db_xref="GOA:A1K539" FT /db_xref="InterPro:IPR006073" FT /db_xref="InterPro:IPR016496" FT /db_xref="UniProtKB/TrEMBL:A1K539" FT /protein_id="CAL93944.1" FT /translation="MASSGSISTYCRPTRARMQKDLADKPRYAIAASVQLPNVSDAEFE FT ASLAELRELAKTLGYQVVHTFVQKRGGFDTTGYLGVGKRQEIRDFVSAQAGFDAAPNAT FT VPRTGEIEALLVDHEISPSQARNLELETGCEVMDRTMVILEIFHRNARSRAAKAQVEIA FT RLGYMAPRLREAAKLAGPQGRQRSGVGGRGAGESHTELDRRKIRDRIAELQLEIVAMEA FT ERKTQRARRQGRQSLANVALVGYTNAGKSTLMRALTGSEVLVANKLFATLDTTVRTLYP FT ESVPRVLVSDTVGFIKNLPHGLVASFKSTLDEALDAALLLHVIDASDPGFERQLEVTDK FT VLEEIDAQDIPRIRVFNKIDHVGDAEAQAECEAALRAKYPDCIVMSARRPDEVAKLRQT FT IVAFFQRDLVEAELLLPWSAQQLRKEIYANCQVLEERAEDEGAVFRLRGERDVVERLRE FT RFLLVD" FT tRNA complement(1445319..1445408) FT /gene="tRNA-Ser" FT /locus_tag="azo_tRNA_0027" FT /product="transfer RNA-Ser" FT /anticodon=(pos:1445372..1445374,aa:Ser) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS 1445591..1446979 FT /transl_table=11 FT /locus_tag="azo1328" FT /product="conserved hypothetical protein" FT /function="predicted soluble lytic transglycosylase fused FT to an ABC-type amino acid-binding protein" FT /note="Conserved hypothetical protein. Fusion Protein of FT bacterial extracellular solute-binding protein and FT transglycosylase Homology to pp1036 of P. putida of 37% FT (trembl|Q88P17) InterPro: Bacterial extracellular FT solute-binding proteins family 3 (IPR001638); solute FT binding protein/glutamate receptor (IPR001311); SLT domain FT (IPR000189) Pfam: Bacterial extracellular solute-binding FT protein; Transglycosylase SLT domain signal peptide no TMHs FT recN: DNA repair protein RecN" FT /db_xref="GOA:A1K540" FT /db_xref="InterPro:IPR000189" FT /db_xref="InterPro:IPR001638" FT /db_xref="InterPro:IPR008258" FT /db_xref="InterPro:IPR023346" FT /db_xref="UniProtKB/TrEMBL:A1K540" FT /protein_id="CAL93945.1" FT /translation="MRLFFCLFFALLLSACGREAPTRIADFRTLGELRVATRLDAISYR FT EEGDGATSGFEHDLLVQLGQALEVPVRFVVYPDSVRALDAVIKGEAHLAAAGLARNDRL FT PLAWSAPLREVDFVLAGRSDGGDIGREADLAGRTVTVRRGSLAAEALEQIRRRVPSLRV FT NYAQRAEDSAMLEQLAAGQADLVATDRVHYALAAQIHPELNIAYDLPVKSHVAWALPRE FT QGGALGKAVAEFLDGAQGNGLIARSADRYFGYVRRLTDVDIETFLGRIRERLPQFRPHF FT HEAQARTGIDWRYLAALSYQESHWDPLATSRTGVRGIMMLTADTADRLGVADRLDPRQS FT ILGGARYLSMIREQLPDEIEEPDRSWMATAAYNLGMGHMNGARAIARTLGKDDASWWEM FT KSVLPLLSRQDYAARLKAGPARGGEAVIMTENIRNYHDILMRIEAPFDPRKAVPKLRLT FT AGDL" FT CDS complement(1446976..1448064) FT /transl_table=11 FT /gene="aapM" FT /locus_tag="azo1329" FT /product="putative amino acid permease" FT /function="ABC-type amino acid transport system permease FT component" FT /note="Putative amino-acid ABC transporter permease. FT Homology to aapM of R. leguminosarum of 38% FT (sprot|AAPM_RHILV) PROBABLY PART OF A FT BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM YDHWXYZ FOR AN FT AMINO ACID; PROBABLY RESPONSIBLE FOR THE TRANSLOCATION OF FT THE SUBSTRATE ACROSS THE MEMBRANE. Pfam: FT binding-protein-dependent transport system signal peptide FT probable 8 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K541" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR010065" FT /db_xref="UniProtKB/TrEMBL:A1K541" FT /protein_id="CAL93946.1" FT /translation="MKTPALSALAGLRGRCFDSPWSALATVLILAALLWLGQRVAGWAV FT IDAVWVADAARCEAATGACWGVIAEKHRAILFGRYPFDAQWRPLLATAILLVAIVATLR FT AAGSRPRPDGNRRWRRVALAWVVTIALFPVLMGGGVAGLAPVPTELWGGLPLTLMLAVG FT GIATAFPLAIVLALGRSGPLPAMRAVSSVYVELIRSVPLVPALFLASFLVPLLLPADWQ FT VDVLFRVQVAITLFAAAYLAEAIRGALLALPDGQRQAAAALGLGWWQTQRHILLPQALR FT NATPSIANSFINLFKDTSLVVVVSLYELTGALEIALAGDAEWRSYQLEGYVFIGAIYWT FT GCFALSRASRRLEQRDAARAGR" FT CDS complement(1448061..1449080) FT /transl_table=11 FT /gene="aapQ" FT /locus_tag="azo1330" FT /product="putative amino acid permease" FT /function="ABC-type amino acid transport system permease FT component" FT /note="Putative amino acid permease. Homology to aapQ of R. FT leguminosarum of 35% (sprot|AAPQ_RHILVast). PART OF A FT BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM FOR L-AMINO FT ACIDS. AFFECTS THE UPTAKE AS WELL AS EFFLUX OF THESE AMINO FT ACIDS. PROBABLY RESPONSIBLE FOR THE TRANSLOCATION OF THE FT SUBSTRATE ACROSS THE MEMBRANE. InterPro: FT Binding-protein-dependent transport systems inner membrane FT component (IPR000515) Pfam: Binding-protein -dependent FT transport system 1 HTH no signal peptide probable 4 TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K542" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR010065" FT /db_xref="UniProtKB/TrEMBL:A1K542" FT /protein_id="CAL93947.1" FT /translation="MEPGRPDVRPAAAVTRRPATPAGARRGLLLQLGLLALIASGLWLL FT AATAAGHMRERGIHSGFDFLLQSAGFWISEGVPAFDPAESYLKAFGVGLANTLRVALPA FT TLAALAIGFLVGLGRIAHNPLLRACCTAYVETLRNIPLLLQLLAWYFVLTAVLPPAAQA FT IELLPHVYLGKSGLALPWPGADGIELPERGGFSISGGAQLSPEYLALFIGLATYTASYI FT AESVRAGVQAVSAGQAQAAVALGLRRGQILRHITLPQALPAIVPPLANHALNVIKNSSL FT AVAIGYPDLVSIANTTLNQTGRAVECIAIVVAVYVLICALGIGLAHLLEHRWRRWTYA" FT CDS complement(1449038..1450072) FT /transl_table=11 FT /gene="aapJ" FT /locus_tag="azo1331" FT /product="putative amino acid-binding protein" FT /function="ABC-type amino acid transport/signal FT transduction systems periplasmic component/domain" FT /note="Putative amino acid ABC transporter periplasmic FT binding protein. Homology to aapJ of R. leguminosarum of FT 52% (sprot|AAPJ_RHILV). PART OF A BINDING-PROTEIN-DEPENDENT FT TRANSPORT SYSTEM FOR L-AMINO ACIDS AFFECTS THE UPTAKE AS FT WELL AS EFFLUX OF THESE AMINO ACIDS. InterPro: Bacterial FT extracellular solute-binding proteins family 3 (IPR001638); FT solute binding protein/glutamate receptor (IPR001311) Pfam: FT Bacterial extracellular solute-binding proteins signal FT peptide no TMHs TIGR00045: conserved hypothetical prote" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K543" FT /db_xref="InterPro:IPR001638" FT /db_xref="InterPro:IPR018313" FT /db_xref="UniProtKB/TrEMBL:A1K543" FT /protein_id="CAL93948.1" FT /translation="MKKSLRRIAPAVALGFAATLSATAAHAGATLDQIKRKGELACGVS FT SGVPGFSATDSRGNWSGLDVDVCRALAAAVLGDANKVKWVPLGSQQRFSALQAGEVDIL FT SRNTTWTLTRDASLGLAFTAITYYDGQGFLVPKSIKVTSAKQLRDAEICVQSGTTTEKN FT LADYFRRQGIRVKPVVFEKFDASLKAFFNGRCVAYTTDASSLAGIRAGEAPKPDDYLIL FT PETISKEPLGPIVRRGDDEWFTIVKWVVYALIEAEELGVTRDNADKQAAGGDPAVGRLL FT GKTEDLGKPLGLDAQWAYRAVRAVGNYGEVFERNLGAGSPLRLPRGQNALWSQGGLMYA FT PPLR" FT CDS complement(1450197..1451132) FT /transl_table=11 FT /gene="cbl 1" FT /locus_tag="azo1332" FT /product="putative HTH-type transcriptional regulator cbl" FT /function="Transcriptional regulator" FT /note="HTH-type transcriptional regulator cbl (Cys regulon FT transcriptional activator) Belongs to the LysR family of FT transcriptional regulators. THIS PROTEIN IS A POSITIVE FT REGULATOR OF GENE EXPRESSION FOR THE CYSTEINE REGULON. THE FT INDUCER FOR CYSB IS N-ACETYLSERINE (BY SIMILARITY). FT ribD_Cterm: riboflavin-specific deami 55% similarity to the FT HTH-type transcriptional regulator cbl, E. coli FT SWISSPROT:CBL_ECOLI IPR000847; HTH_LysR. IPR005119; FT LysR_subst. PF00126; HTH_1; 1. helix-turn-helix PF03466; FT LysR_substrate; 1. HTH reporting nucleic acid binding FT motif" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K544" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:A1K544" FT /protein_id="CAL93949.1" FT /translation="MNFQQLRIVRETVRRNFNLTEVANALYTAQSGVSKHIKDLEDELG FT VELFVRRGKRLLGLTEPGKELLPIVERILLDTQNIKRLGEQFAQKDKGHLAIATTHTQA FT RYALPPVVTRFKEEFPKVHLELHQCGPKEIVSLLRSGQVDIGIATEALGEEDDLVSFPF FT YQWQHTLIVPEDHPLTRVQPLTLEAVAEYPIITYHEGFTGRTRIDAAFARAGITPDIVM FT SALDADVIKAYVELGHGVGIIAAMAFHPQRDAGLKLLDSKGLFEMNTTWISLRRGHYLR FT GYALRFIECCSPALTESRVRDAVFPKVSTQ" FT CDS complement(1451135..1452220) FT /transl_table=11 FT /gene="cysA" FT /locus_tag="azo1333" FT /product="putative sulfate transport ATP-binding protein" FT /function="ABC-type sulfate/molybdate transport systems FT ATPase component" FT /EC_number="3.6.3.25" FT /note="Sulfate/thiosulfate import ATP-binding protein cysA FT (EC 3.6.3.25) (Sulfate-transporting ATPase). Part of the FT ABC transporter complex cysAWTP (TC 3.A.1.6.1) involved in FT sulfate/thiosulfate import. Responsible for energy coupling FT to the transport system (By similarity). InterPro: AAA FT ATPase superfamily ruvB: Holliday junction DNA helicase Ru" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K545" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005666" FT /db_xref="InterPro:IPR008995" FT /db_xref="InterPro:IPR014769" FT /db_xref="InterPro:IPR017871" FT /db_xref="InterPro:IPR024765" FT /db_xref="UniProtKB/TrEMBL:A1K545" FT /protein_id="CAL93950.1" FT /translation="MSIQVENIHKQFGSFTALNDVSLDFPSGELVALLGPSGCGKTTLL FT RVIAGLETADSGRVILEGEDASGTHVRERQVGFVFQHYALFRHMTVFENVAFGLRVKPR FT KERPNEAEIRKRVHRLLELVQLDWLADRFPAQLSGGQRQRIALARALAVEPRVLLLDEP FT FGALDAKVRKELRRWLRRLHDELHVTSIFVTHDQEEALEVADRVVLMNKGKVEQVGTPQ FT EVYEHPATPFVYGFLGAVNLFHGRVEGEHVRVGEAVLPHDGRDAEHGVDVVGFARPHEL FT DIVTDLAAPNGVDAIVARVLAFGASVRVELDAVEAEGDSGLPRHYEVVLTRERLTTLPL FT AEGQRVRLVPSQLRVFPREAA" FT CDS complement(1452232..1453119) FT /transl_table=11 FT /gene="cysW" FT /locus_tag="azo1334" FT /product="putative sulfate transport system permease FT protein" FT /function="ABC-type sulfate transport system permease FT component" FT /note="Sulfate transport system permease protein cysW. Part FT of the ABC transporter complex cysAWTP (TC 3.A.1.6.1) FT involved in sulfate/thiosulfate import. Probably FT responsible for the translocation of the substrate across FT the membrane. InterPro: Binding-protein-dependent transport FT systems inner membrane component uppS: undecaprenyl FT diphosphate synthase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K546" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR005667" FT /db_xref="InterPro:IPR011866" FT /db_xref="UniProtKB/TrEMBL:A1K546" FT /protein_id="CAL93951.1" FT /translation="MAAAAGVLHGRADARRYEDNSATREAPWVKWTILGLALSFFALFL FT LLPLIAVFAEALRKGWVTYLTSLSDSDALAAIKLTLITAAIAVPLNLVFGVAAAWAIAK FT FEFRGKHFLTTLIDLPFSVSPVVAGLIYVLLFGAHGWFGGWLAAHDVKIIFAVPGIVLA FT TVFVTFPFVARELIPLMEAQGREEEEAAVVLGASGFQTFWRVTLPNIKWGLLYGVILCN FT ARAFGEFGAVSVVSGHIRGQTNTMPLHVEILYNEYNFAAAFAVASLLALLALVTLGLKS FT FIEWKVGRTHTESE" FT CDS complement(1453119..1453973) FT /transl_table=11 FT /gene="cysT" FT /locus_tag="azo1335" FT /product="sulfate transport system permease protein FT probably" FT /function="ABC-type sulfate transport system permease FT component" FT /note="Probable sulfate transport system permease protein FT cysT. Part of the ABC transporter complex cysAWTP (TC FT 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably FT responsible for the translocation of the substrate across FT the membrane (By similarity). InterPro: FT Binding-protein-dependent transport systems inner membrane FT component gntP: gluconate transporter" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K547" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR005667" FT /db_xref="InterPro:IPR011865" FT /db_xref="UniProtKB/TrEMBL:A1K547" FT /protein_id="CAL93952.1" FT /translation="MSAASFLNPTRQTRVLPGFGLSLGYTLVYLSLIVLIPLAAVFLKT FT ASLGWAEFWAVVTSPRVVASYKLSFGASLLAAAINAVFGLMLAWALVRYTFPGKKLIDA FT LVDLPFALPTAVAGIALTALYAGNGWIGSKLAPLGIKVAFTPLGVLVALVFIGVPFVVR FT TVQPILEDLETELEEAAASLGAHRWQTFTKVILPILLPALLTGFALAFARAVGEYGSVI FT FIAGNIPMVSEITPLMIITKLEQYDYTGATAIAVVMLVISFALLLLINLLQAWSAKRTG FT RNR" FT CDS complement(1453973..1454983) FT /transl_table=11 FT /gene="cysP" FT /locus_tag="azo1336" FT /product="putative sulfate transport system FT substrate-binding protein" FT /function="ABC-type sulfate transport system periplasmic FT component" FT /note="CysP: sulfate/thiosulfate periplasmic binding FT protein. Sulfate-binding protein precursor (Sulfate FT starvation-induced protein 2) (SSI2). This protein FT specifically binds sulfate and is involved in its FT transmembrane transport. mazG: MazG family protein" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K548" FT /db_xref="InterPro:IPR005669" FT /db_xref="InterPro:IPR006059" FT /db_xref="UniProtKB/TrEMBL:A1K548" FT /protein_id="CAL93953.1" FT /translation="MKPALRTLLLSSVLAFGLGSASLASAQTTLLNASYDVTRELYKEI FT NPAFASWYKAKTGKDITINQSHGGSSKQALSVAAGLEADVVTMNQSTDIDILVERGKLV FT AADWRKRFPHDATPYTTYSVFLVHKGNPKKIKDWSDLAQPGLSVIVPNPKTSGNGRYTY FT LAAWGSVIAKGGSEADARNFVTKLFRNVPVLDGGGRGATTTFTQRELGDVLVTFENEAA FT QIARELGAGQFDVVYPSITIDASPPVAVVETVVAKRGTATEAKAYLDFLYTDEGQKIIA FT KHWFRPRSEALLKANADRFPPVKAFKVEELLGSWSEVQKKHFADGGIYDQIVVNR" FT CDS 1455298..1456512 FT /transl_table=11 FT /locus_tag="azo1337" FT /product="conserved hypothetical peptidoglycan-binding FT protein" FT /function="Membrane-bound lytic murein transglycosylase B" FT /note="Conserved hypothetical peptidoglycan binding FT protein. Homology to bb3579 of b. bronchiseptica of 69% FT (trembl|Q7WGL0) InterPro: Putative peptidoglycan binding FT domain 1 (IPR002477) Pfam: Putative peptidoglycan binding FT domain This domain is composed of three alpha helices. This FT domain is found at the N or C terminus of a variety of FT enzymes involved in bacterial cell wall degradation. This FT domain may have a general peptidoglycan binding function. FT signal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K549" FT /db_xref="InterPro:IPR002477" FT /db_xref="InterPro:IPR011970" FT /db_xref="InterPro:IPR023346" FT /db_xref="UniProtKB/TrEMBL:A1K549" FT /protein_id="CAL93954.1" FT /translation="MTTPRSKSRFPVSALLAVAPFALSLAAPAAAQDLACLAQLRAPAQ FT AYGVSAATFDRLTAGLQADPTVLPLLDAQPEFVTPIWDYMAALVDDERIADGRAMLEQW FT SAVLARVEAEYGVDAATVVAVWGVESNYGRNFGSRALLPSLATLACNGRRQSFFRQELF FT ATMKIVEDGHVAPERLNGSWAGAFGHTQFMPSTYLRLAVDFDGDGRRDLVDSIADALAS FT TANFLRQAGWQRGLAWGYEVGLPAGFDSSGAGRKNKRGIAEWAGRGVRRADGGALAQAG FT NAALLLPAGASGPAFLVTRNFDAIYSYNAAESYALAIAHLSDRLRGAGPFATPWPTDDP FT GLSRAERREVQTLLLARGHDIGNPDGMIGARTREALRVVQAEFGLPADGRAGRRVLDAL FT RQARP" FT CDS 1456606..1457373 FT /transl_table=11 FT /locus_tag="azo1338" FT /product="Short-chain dehydrogenase family protein" FT /function="Dehydrogenases with different specificities FT (related to short-chain alcohol dehydrogenases)" FT /note="The short-chain dehydrogenases/reductases family FT (SDR) is a very large family of enzymes, most of which are FT known to be NAD- or NADP-dependent FT oxidoreductases,TREMBL:Q8FWK3 (58% identity); TREMBL:Q9AHY1 FT (58% identity). Pfam (PF00106): Short chain dehydrogenase." FT /note="Family membership" FT /db_xref="GOA:A1K550" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020904" FT /db_xref="UniProtKB/TrEMBL:A1K550" FT /protein_id="CAL93955.1" FT /translation="MKIENSVFVVTGGGSGLGAATARMLVAGGGRVVLADVNAGAGEAV FT AAELGAHARFVSTDVTDEASAKAAFDCALTQFGGLNGLVNCAGVAPAEKVVGREAPHRL FT EAFARTVNINLVGSFNMMRLAADIMSKAAPNEEGERGVIVSTASVAAYDGQVGQAAYAA FT SKAGIVGLTLPVARELARFGIRVMTIAPGIMETPMLTGMPQEVQDSLGKMVPFPSRLGR FT PAEYAALVRSIIENPYLNGEVIRLDGAIRMAAK" FT CDS 1457532..1460015 FT /transl_table=11 FT /gene="ccoI" FT /locus_tag="azo1339" FT /product="putative cation-transporting ATPase" FT /function="Cation transport ATPase" FT /EC_number="3.6.3.-" FT /note="36% ATPase-IB1_Cu.IPR006416; FT ATPase-IB_hvy.IPR001757; ATPase_E1-E2.IPR005834; FT Dehal_like_hydro.IPR008250; E1-E2_ATPase_reg. IPR006121; FT HeavyMe_transpt.IPR000695; H_ATPase.IPR006191; Metal_bind. FT Pfam:PF00122; E1-E2_ATPase; 1.PF00403; HMA; 1.PF00702; FT Hydrolase; 1. TMHs:8" FT /note="Specificity unclear" FT /db_xref="GOA:A1K551" FT /db_xref="InterPro:IPR000150" FT /db_xref="InterPro:IPR001757" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006121" FT /db_xref="InterPro:IPR006403" FT /db_xref="InterPro:IPR006416" FT /db_xref="InterPro:IPR008250" FT /db_xref="InterPro:IPR018303" FT /db_xref="InterPro:IPR021993" FT /db_xref="InterPro:IPR023214" FT /db_xref="InterPro:IPR023299" FT /db_xref="InterPro:IPR023300" FT /db_xref="UniProtKB/TrEMBL:A1K551" FT /protein_id="CAL93956.1" FT /translation="MNSPDLPVADAATAASDSDCYHCGLPIPSDTHHYVRIDGANRRMC FT CIGCEAVARSIVDNGLEDYYRHRDAMPESRREAMPPELQELGLFDHPDFQKSFVRPVGE FT HEREASLILEGITCAACVWLNERHVARQPGVSAVDINYATRRARVRWDERQIKLSDILS FT AVAAIGYRAYPYDAERSEQIAHRERRSMLWRVFVAGFGMMQVMMYAVPVYIAREGEMTA FT DIEALMRWASLLLTLPVVLYSAAPFFRRAWRDLRLRRLGMDVPVALGVGSAFLASLWAT FT LTNGPEVYYDSVTMFVFFLLGGRYLEMLARQKAVRGVEELGKVIPAFAERLDSAGESSR FT VPVSELAVGDLVRVRPGEVIAADGVVEDGRSDANEALLTGESKPVSKTSGDPVTGGSIN FT ISSPLVFRVEQVGDATRLAAIRRLMERAAEEKPRVATQSDRVAGIFIVLLLVLAAATGI FT GWYLVEPQRALWVFVSVLVVACPCALSLATPTALTVATDVLARTGVLVTRGHAVETLAR FT VNHVLLDKTGTLTRGRMTLVEVVPLAGVAEQEVLRLAAALEAGSEHPIAAGLREAAPKS FT TSVATEVMVETGQGVGGVVDQQPLWVGRPDFVAGHAGVSLPSCLAEVEARGGSVVALGS FT ASEVLALFRLADVLRPEAPELVRRLADDGVEVSLLSGDAPTVVAATAAALGIEDAHGGM FT TPQGKQAYIVGLQQRPEAVVAMVGDGVNDAPVLAQAHVSVAMGGGTDLARNQADIVLLG FT EDLSALARGMVLARQTLRIIRQNLWWSFIYNFTSVPLAMAGLVTPWMAGIGMAGSSLLV FT VLNAMRLQRGRRNRY" FT CDS 1460020..1460229 FT /transl_table=11 FT /gene="ccoS" FT /locus_tag="azo1340" FT /product="conserved hypothetical cytochrome oxidase FT maturation protein" FT /function="uncharacterized protein, possibly involved in FT nitrogen" FT /note="Conserved hypothetical cytochrome oxidase maturation FT protein. Homology to cco of P.Putida of 42% FT (gnl|keqq|ppu:PP4262(KEGG)). Pfam: Cytochrome oxidase FT maturation protein cbb3-type. Genes encoding a cytochrome FT cbb3 oxidase were initially designated fixNOQP FT (ccoNOQP),the ccoNOQP operon is always found close to a FT second gene cluster, known as fixGHIS (ccoGHIS) whose FT expression is necessary for the assembly of a functional FT cbb3 oxidase. On the basis of their derived amino acid FT sequences each of the four proteins encoded by the ccoGHIS FT operon are thought to be membrane-bound. It has been FT suggested that they may function in concert as a FT multi-subunit complex,possibly playing a role in the uptake FT and metabolism of copper required for the assembly of the FT binuclear centre of cytochrome cbb3 oxidase. Interpro: FT IPR004714 Cytochrome oxidase maturation protein cbb3-type. FT No signal peptide. 1 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR004714" FT /db_xref="UniProtKB/TrEMBL:A1K552" FT /protein_id="CAL93957.1" FT /translation="METLYLLIPLSVVLVFVIGVVFWWSLRDGQYDDLEGPAYRLLLDD FT RDELPAKPADTDKPMPDSPDRRDV" FT CDS 1460596..1462020 FT /transl_table=11 FT /gene="ccoN" FT /locus_tag="azo1341" FT /product="probable cytochrome c oxidase, cbb3-type,subunit FT I" FT /function="Cbb3-type cytochrome oxidase subunit 1" FT /EC_number="1.9.3.1" FT /note="Probable cytochrome c oxidase, cbb3-type, subunit I. FT Homology to ccoN of R. capsulatus of 62% FT (sprot|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT FT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF FT OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF FT THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE FT ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL FT ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A FT HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c FT oxidase cbb3-type Pfam: cytochrome c and quinol oxidase FT polyppeptide no signal peptide 12 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K553" FT /db_xref="InterPro:IPR000883" FT /db_xref="InterPro:IPR004677" FT /db_xref="InterPro:IPR023615" FT /db_xref="InterPro:IPR023616" FT /db_xref="UniProtKB/TrEMBL:A1K553" FT /protein_id="CAL93958.1" FT /translation="MQSQATYNYKVVRQFAIMTVVWGIVGMLVGVIAAAQLVWPELNVH FT EWLGYGRLRPLHTNAVIFAFGGCALFATSYYVVQRTCHTRLFAPGLAAFTFWGWQLVIV FT LAAITLPLGFTSGKEYAELEWPIDLLIAVVWVSYAVVFFGTVAKRTVAHIYVANWFYGA FT FIITVALLHIVNSMAIPVSLTKSYSAYAGVQDAMVQWWYGHNAVGFFLTAGFLGMMYYF FT VPKQADRPVYSYRLSVVHFWALIFTYMWAGPHHLHYTALPDWTQSVGMIFSLILLAPSW FT GGMINGIMTLSGAWHKLRTDPILKFLITALSFYGMSTFEGPMMSVKTVNALSHYTDWTV FT GHVHSGALGWVAMISIGSVYFLLPRLYGKTEMYSVKLINAHFWIATIGVVLYIASMWIA FT GVMQGLMWRATNPDGTLTYSFVEGVKASYPFWSIRLLGGVLFLTGMLIMFYNMVKTIAG FT EKAYNAPVIAPAAAHA" FT CDS 1462036..1462671 FT /transl_table=11 FT /gene="ccoO" FT /locus_tag="azo1342" FT /product="probable cytochrome c oxidase, cbb3-type,subunit FT II" FT /function="Cbb3-type cytochrome oxidase cytochrome c FT subunit" FT /note="Probable cytochrome c oxidase, cbb3-type, subunit II FT Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). FT CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY FT CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. FT SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME FT COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. FT ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE FT TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN FT HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase FT cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme FT subunit no signal peptide probable 1 TMH" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K554" FT /db_xref="InterPro:IPR003468" FT /db_xref="InterPro:IPR009056" FT /db_xref="UniProtKB/TrEMBL:A1K554" FT /protein_id="CAL93959.1" FT /translation="MAQSKHAAIERSVFLMIVLTLLTVSVGGLVEIVPLFFQKSTTSPI FT DQKGNELAVKPYDPVRLVGRDIYIREGCYNCHSQMIRPFRAETERYGHYSVAGESIYDH FT PFQWGSKRTGPDLARVGGRYSDEWHRVHLLNPRDVVPESNMPGYAWLDRPAKVDNIQDK FT MRALNKVGLHKYSDDEIAAAPEKVKGITEIEAVVAYLQGLGLALQNVR" FT CDS 1462691..1462864 FT /transl_table=11 FT /gene="ccoQ" FT /locus_tag="azo1343" FT /product="Cbb3-type cytochrome oxidase, subuni" FT /note="Cbb3-type cytochrome oxidase, subunit ccoQ , 44% FT Identity to TrEMBL;Q8D9I3, Q7MKV5,Q9KS21. Has FT PF05545,Cbb3-type cytochrome oxidase component FixQ; FT IPR008621;This family consists of several Cbb3-type FT cytochrome oxidase components (FixQ/CcoQ). FixQ is found in FT nitrogen fixing bacteria. Since nitrogen fixation is an FT energy-consuming process, effective symbioses depend on FT operation of a respiratory chain with a high affinity for FT O2, closely coupled to ATP production. This requirement is FT fulfilled by a special three-subunit terminal oxidase FT (cytochrome terminal oxidase cbb3), which was first FT identified in Bradyrhizobium japonicum as the product of FT the fixNOQP operon." FT /db_xref="InterPro:IPR008621" FT /db_xref="UniProtKB/TrEMBL:A1K555" FT /protein_id="CAL93960.1" FT /translation="MDVNDLRTVITVMGFLCFLAICAWAYSGHAKAGFDEAARLPLTDE FT DPVVAGRQGKEG" FT CDS 1462868..1463761 FT /transl_table=11 FT /gene="ccoP" FT /locus_tag="azo1344" FT /product="probable cytochrome c oxidase, cbb3-type,subunit FT III" FT /function="Cytochrome c mono- and diheme variants" FT /note="Probable cytochrome C oxidase subunit III. Homology FT to ccoP of P. stutzeri of 46% (trembl|Q8KS19) CYTOCHROME C FT OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT FT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FT FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE FT CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN FT CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC FT CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: FT ccoP: cytochrome c oxidase cbb3-type Pfam: cytochrome c no FT signal peptide probable 2 TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K556" FT /db_xref="InterPro:IPR003088" FT /db_xref="InterPro:IPR004678" FT /db_xref="InterPro:IPR009056" FT /db_xref="UniProtKB/TrEMBL:A1K556" FT /protein_id="CAL93961.1" FT /translation="MADFVSGFWNVYVMGLVALSLLFCVFVLVSNTTKREAGPVELHGH FT VWDETLAEYNNPLPRWWMYLFWITLVFAVVYLAIYPGFGRTNDGRGALHQYENEMAKAE FT ERYAPIFNQYLDKDLKVVAADPEANAMGQRMFLTYCAQCHGAAAQGAKGFPNLTDDEWN FT WGGDPETIKTTITGGRMGVMPPFGPALGAEGVKDVANYVRSLSGLAHDSLRAQRGKDIF FT AQNCVACHGADGTGSTAVGAPNLTNKSWLYGSSEATIIETVTNGRTNQMPTFQAFLGDA FT KIHLLAAYVTSLSNKK" FT CDS 1463836..1465260 FT /transl_table=11 FT /gene="ccoG" FT /locus_tag="azo1345" FT /product="putative iron-sulfur 4Fe-4S ferredoxin FT transmembrane protein" FT /function="Polyferredoxin" FT /note="Putative iron-sulfur 4Fe-4S ferredoxin transmembrane FT protein. Homology to fixG of R. meliloti of 36% FT (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that FT mediate electron transfer in a range of metabolic FT reactions; they fall into several subgroups according to FT the nature of their iron-sulphur cluster(s). One FT group,originally found in bacteria, has been termed FT ""bacterial-type"", in which the active centre is a 4Fe-4S FT cluster. 4Fe-4S ferredoxins may in turn be subdivided into FT further groups, based on their sequence properties. Most FT contain at least one conserved domain, including four Cys FT residues that bind to a 4Fe-4S centre. InterPro: 4Fe-4S FT ferredoxin iron-sulfur binding domain (IPR001450) probable FT 5 TMHs . No signal peptide predicted." FT /note="Family membership" FT /db_xref="GOA:A1K557" FT /db_xref="InterPro:IPR001450" FT /db_xref="InterPro:IPR012285" FT /db_xref="InterPro:IPR013783" FT /db_xref="InterPro:IPR014116" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:A1K557" FT /protein_id="CAL93962.1" FT /translation="MSEPLPSPKTSVADEMEDSLYAVRKKVYTRAVSGTFATWRWALVW FT FTQLIFYGLPWLTWNDRQAVLFHLTERKFYIFGWVFWPQDVFFLAILLIISAYALFFFT FT AIAGRLWCGYACPQTVYTEIFMWIEQKIEGDHNKRAKLDKAPLGVRKIAIKAAKYGAWG FT AVALWTGFTFVSYFSPLREMLASVSSLSFGPWELFWILFYAGFTYLFAGVMREQVCKYM FT CPYARFQSVMFDADTLVITYDEERGEPRGTRKKGVDPKSVGKGDCIDCGICVQVCPTGI FT DIRKGLQYECIGCAACIDACDQVMEKMSYPKGLIRYSTENAVKKHWGSKEIIGHVLRPR FT TLIYGGVLALVSLAFLWGLATREPLRVDVLRDRTSLAREVEDGMIENVYRLQVMNMTES FT ARSFHFGVEGLDQARIGSAETSISVPPASTQSVTLRVLVPGGVGKSGANELFILVAPDD FT APQERLREKTTFLMPN" FT CDS 1465265..1465780 FT /transl_table=11 FT /gene="ccoH" FT /locus_tag="azo1346" FT /product="conserved hypothetical membrane protein." FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical membrane protein. Homology to FT ebA5136 Azoarcus sp. EbN1 of 51% FT (gnl|keqq|eba:ebA5136(KEGG)). Has PF05751, FixH;IPR008620; FT This family consists of several Rhizobium FixH like FT proteins. It has been suggested that suggested that the FT four proteins FixG, FixH, FixI, and FixS may participate in FT a membrane-bound complex coupling the FixI cation pump with FT a redox process catalysed by FixG. No signal peptide FT predicted. 1 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="InterPro:IPR008620" FT /db_xref="UniProtKB/TrEMBL:A1K558" FT /protein_id="CAL93963.1" FT /translation="MSFSVTQKKAAPWYRQGWPWFLIAIPATAIVAGVITLILAIRSWD FT GLVVDDYYREGKAFVQTIERTERAKQLGLSAQLNVSTDRVLIVLSSSVPSVTLPGTVRL FT TVSHPTKGGLDQEMVVTGRDGVFEVKISPLATGRWLFQIEDEPRAWRMNGAAYLPTETE FT IRINPTGS" FT CDS 1465806..1465955 FT /transl_table=11 FT /locus_tag="azo1347" FT /product="hypothetical membrane protein" FT /note="Hypothetical membrane protein. No homology to the FT data bank. No domain predicted. No signal peptide 1 TMH" FT /db_xref="InterPro:IPR021494" FT /db_xref="UniProtKB/TrEMBL:A1K559" FT /protein_id="CAL93964.1" FT /translation="MAWRELFGSDIGLLSLFTIGFVLVMGVYIYRFAVRHMAEDEQKAK FT LRHQ" FT CDS 1465986..1466222 FT /transl_table=11 FT /locus_tag="azo1348" FT /product="probable transmemebrane Protein" FT /note="Probable transmemebrane Protein, 38% Idneity to FT TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. FT TMHMM2 reporting 1 TMH present." FT /db_xref="UniProtKB/TrEMBL:A1K560" FT /protein_id="CAL93965.1" FT /translation="MLKWIQVLWPSFLVAALAEAAFFTVIDPQELYFQGEAVHFSPIST FT YSIGFIGFWLICAASSLTTLFFQRTSDEVNQRD" FT tRNA complement(1466272..1466348) FT /gene="tRNA-Arg" FT /locus_tag="azo_tRNA_0028" FT /product="transfer RNA-Arg" FT /anticodon=(pos:1466312..1466314,aa:Arg) FT /inference="nucleotide motif:Simple tRNAscan Autoannotator" FT CDS complement(1466484..1466927) FT /transl_table=11 FT /locus_tag="azo1349" FT /product="putative universal stress protein f" FT /function="Universal stress protein UspA and related FT nucleotide-binding proteins" FT /note="Putative universal stress protein F," FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K561" FT /db_xref="InterPro:IPR006015" FT /db_xref="InterPro:IPR006016" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:A1K561" FT /protein_id="CAL93966.1" FT /translation="MFKHILVPTDGSALSESTVARAVSFARDASARITFFYAQPDFPMP FT IYGEGALIDPTTPEQFAKAAAQEAERILNAAKAVADASGVLADTDTLVNEVPYEAIINA FT ADRHGCDLIFMASHGRRGLASLLLGSETQKVLTHSTIPVLVYR" FT CDS 1467151..1468884 FT /transl_table=11 FT /gene="phbC2" FT /locus_tag="azo1350" FT /product="probable poly-beta-hydroxybutyrate synthase" FT /function="Poly(3-hydroxyalkanoate) synthetase" FT /EC_number="2.3.1.-" FT /note="FUNCTION: Polymerizes d(-)-3-hydroxybutyryl-CoA to FT create PHB which consists of thousands of hydroxybutyrate FT molecules linked end to end. PHB serves as an intracellular FT energy reserve material when cells grow under conditions of FT nutrient limitation. Entry name :-PHBC_AZOCA Primary FT accession number:- O66392 Identity:-41% InterPro :- FT IPR000073; A/b_hydrolase. Pfam:- PF07167; PhaC_N; 1. Signal FT peptide probability: 0.000 Number of predicted TMHs: 0" FT /note="Family membership" FT /db_xref="GOA:A1K562" FT /db_xref="InterPro:IPR000073" FT /db_xref="InterPro:IPR010941" FT /db_xref="UniProtKB/TrEMBL:A1K562" FT /protein_id="CAL93967.1" FT /translation="MNKSERLDPGQTVKRSIKQLHEAVEGAFDPLGMAAPIIHAQLAWA FT AHPQELADRLLRLSSDLWRLQWHSWNRVLGLDSEDPVRPNPDDARFADPVWTESPTWDL FT TKEWYLALTHHVQDMLYDTPGLTGKERRRAAFWWRKWLNAVAPTNFFWTNPVAVRKAWE FT TKGESLVRGFGNFLDDVRAGEVRMTRPDDFEVGKNLATTPGAVVFRNDLLEVIHYQPTR FT PQVHRDPVVIVTPWINKFYILDLVPKKSLIRYLLDQGLDVFITSWKNPDASMRDVTFDD FT YVTRGVHAAVETARGLAGAEKVHAVGYCIGGTALSMYMAWANRHFPAEAVPVADWTVFT FT TLVDFQKPGDIEVFIDESSIRYLTGNMARTGYLEGKEMASAFRLLRSNSLIWHYVVHGW FT LYGETPASFDVLYWNMDATRMPYAMHSWYLRELYLHNRLIQKDALVVAGEPLDLAAISQ FT PLYAVAAEDDHIAPWGQTFRINNFVTGPKRYVLSSSGHILGIVNPVVQPPKRNYRAAEA FT HRSESAEAWLDRAERHEGSWWEDWMQWLKPRAGELVDARPVANAAFPALAPAPGTYVLE FT K" FT CDS complement(1468907..1469707) FT /transl_table=11 FT /gene="fnr" FT /locus_tag="azo1351" FT /product="probable fumarate and nitrate reduction FT regulatory protein" FT /function="cAMP-binding proteins - catabolite gene FT activator and regulatory subunit of cAMP-dependent protein FT kinases" FT /note="Fumarate and nitrate reduction regulatory protein. FT Global transcription factor that controls the expression of FT over 100 target genes in response to anoxia. It facilitates FT the adaptation to anaerobic growth conditions by regulating FT the expression of gene products that are involved in FT anaerobic energy metabolism. When the terminal electron FT acceptor O(2) is no longer available it represses the FT synthesis of enzymes involved in aerobic respiration and FT increases the synthesis of enzymes required for anaerobic FT respiration. Similar to SWISSPROT: sprot|FNR_ECOLI (39% FT Escherichia coli, fumarate and nitrate reduction regulatory FT protein Fnr) / sprot|ANR_PSEAE (40% Pseudomonas FT aeruginosa,transcriptional activator protein Anr) InterPro: FT IPR000595 cNMP_binding. IPR001808 HTH_Crp. Pfam: PF00027 FT cNMP_binding. PF00325 Crp. HTH reporting nucleic acid FT binding motif." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K563" FT /db_xref="InterPro:IPR000595" FT /db_xref="InterPro:IPR001808" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR012318" FT /db_xref="InterPro:IPR014710" FT /db_xref="InterPro:IPR018490" FT /db_xref="UniProtKB/TrEMBL:A1K563" FT /protein_id="CAL93968.1" FT /translation="MWLTWINAANLLRIRSKFIVQMKAVPITVAGLKTACSQCNLVELC FT LPFGMSENEIDRLDELVGARRKIKRQQHLYRAGDPFEAIYAIRTGSFKTDVLLEDGRDQ FT VTGFQMTGEILGLDGISSEVHSCNAIALEDSEVCVIAYGKLEELSREVEGLQHQFHKVM FT SREIVRDHGVMMLLGSMRAEERLAAFLLNMSQRFTARGFSAAEFHLRMTREEIGSYLGL FT KLETVSRAFSRFQEEGLVTVQQKHIRILDSGGLKKLIQHQPACR" FT CDS 1469756..1471147 FT /transl_table=11 FT /gene="hemN" FT /locus_tag="azo1352" FT /product="coproporphyrinogen oxidase" FT /function="Coproporphyrinogen III oxidase and related Fe-S FT oxidoreductases" FT /EC_number="1.3.3.3" FT /note="Oxygen-independent coproporphyrinogen III oxidase. FT ANAEROBIC TRANSFORMATION OF COPROPORPHYRINOGEN-III INTO FT PROTOPORPHYRINOGEN-IX. hemN: oxygen-independent FT coproporphyrinogen III oxidase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K564" FT /db_xref="InterPro:IPR004558" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR010723" FT /db_xref="InterPro:IPR023404" FT /db_xref="UniProtKB/TrEMBL:A1K564" FT /protein_id="CAL93969.1" FT /translation="MNAQPDLIFDPQLIRRFDVNGPRYTSYPTADRFVEAFDANALQDW FT LAKRAVGGVSRPLSLYFHIPFCNTICYYCACNKIITKDHGRSAKYLKYLEKEIEMQVAA FT LGGSRQVTQLHLGGGTPTFLSHEEMHQLMDAVRRFFNLAPNGEYSIEVDPRKVDFDTVE FT MLANLGFNRMSVGVQDFSDDVQRAVNRVQSVEETRLVIDAARATGFKSVSLDLIYGLPK FT QNVISFNRTLEQVLDISPDRISLYSYAHLPGLFKPQRRILQSDMPTPEAKLQILQLAIR FT RLTEAGYVYIGMDHFAKPDDELTVAQRQGRLHRNFQGYSTQAECDLLAFGVSAIGKVGA FT AYAQNVKTLDEYYDALDRDQLPVLRGVELTADDLLRRSVIQALMCHFELSMQSIEIAHL FT IDFRDYFAAELADLAEMQAAGLLEIDGDWITVLPAGRMLVRGIAMVFDRYLRADRERAR FT YSKVI" FT CDS 1471235..1471951 FT /transl_table=11 FT /locus_tag="azo1353" FT /product="conserved hypothetical membrane protein" FT /function="uncharacterized conserved protein" FT /note="Conserved hypothetical membrane protein. Homology to FT ebA5153 of Azoarcus sp. EbN1 of 79% FT (gnl|keqq|eba:ebA5153(KEGG)). Has PF02683;Cytochrome C FT biogenesis protein transmembrane region (IPR003834 FT Ctytoch_TM): This family consists of the transmembrane FT (i.e. non-catalytic) region of Cytochrome C biogenesis FT proteins also known as disulphide interchange proteins. FT These proteins posses a protein disulphide isomerase like FT domain that is not found within the aligned region of this FT family. No signal peptide. 5 TMHs" FT /note="Conserved hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A1K565" FT /protein_id="CAL93970.1" FT /translation="MPESGYLAVFLIGLLGGTHCVSMCGGIVGALSVQKMQGPHDAARQ FT WPLHLAYNLGRIGTYTGMGALLGALGSVGMIYSGVLPAQMALYVLANLMLVALGLYLTG FT FTSVLAPVERAGHAVWRRVQPLTRRFLPARSVSQALPLGALWGFLPCGLVYSVLTTALV FT TGSAARGAGIMLAFGLGTLPNLLLAGMLFKRFRDITRNGKVRFVAGLAVLGFGVFGLFH FT AQSLGGALWSGVVCAV" FT CDS complement(1471968..1472363) FT /transl_table=11 FT /gene="copY" FT /locus_tag="azo1354" FT /product="putative regulatory protein" FT /function="predicted transcriptional regulators" FT /note="Heavy metal dependent transcription regulator 2. FT TRANSCRIPTIONAL REGULATOR INVOLVED IN ACID TOLERANCE. BINDS FT COPPER (By similarity). It contains a n-terminal dna FT binding region and a c- terminal metal binding region (by FT similarity). 35% HTH_MerR.IPR009061; Putativ_DNA_bind. FT Pfam:PF00376; MerR; 1. TIGR00372: conserved hypothetical FT protei" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K566" FT /db_xref="InterPro:IPR000551" FT /db_xref="InterPro:IPR009061" FT /db_xref="InterPro:IPR015358" FT /db_xref="UniProtKB/TrEMBL:A1K566" FT /protein_id="CAL93971.1" FT /translation="MDHTYTIGQLAAQAEVGVETIRYYHRRGLLAEPERRGSYRAYQED FT DLERLKAIRRAQQLGFSLEEIDELLGLNEERDREKARRIAQGKIDDIEVRIRQLEEMRG FT ALRALVKCCRDTEAPAPCPILKSLAGK" FT CDS 1472442..1474877 FT /transl_table=11 FT /gene="copA" FT /locus_tag="azo1355" FT /product="putative Cu2+ transporting ATPase" FT /function="Cation transport ATPase" FT /EC_number="3.6.3.4" FT /note="CopA: copper transporting P-type ATPase FT protein,involved in the uptake and metabolism of copper. FT 44% ATPase-IB1_Cu.IPR006416; ATPase-IB_hvy.IPR001757; FT ATPase_E1-E2.IPR001756; Cu_ATPase.IPR005834; FT Dehal_like_hydro.IPR008250; E1-E2_ATPase_reg.IPR006121; FT HeavyMe_transpt.IPR006191; Metal_bind. Pfam:PF00122; FT E1-E2_ATPase; 1.PF00403; HMA; 1.PF00702; Hydrolase; 1. FT TIGR00003: copper-ion-binding protein. TMHs:8." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K567" FT /db_xref="InterPro:IPR001757" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006121" FT /db_xref="InterPro:IPR006122" FT /db_xref="InterPro:IPR006403" FT /db_xref="InterPro:IPR006404" FT /db_xref="InterPro:IPR006416" FT /db_xref="InterPro:IPR008250" FT /db_xref="InterPro:IPR017969" FT /db_xref="InterPro:IPR018303" FT /db_xref="InterPro:IPR023214" FT /db_xref="InterPro:IPR023299" FT /db_xref="InterPro:IPR023300" FT /db_xref="UniProtKB/TrEMBL:A1K567" FT /protein_id="CAL93972.1" FT /translation="MADAVLDQRRPEDSALHVVDLPVAGMTCAACATRIEKVLNRMDGV FT SASVNLAAEKAHVRLDGARIGAGEVVAAIRKAGFEVPDASLELEISGMTCVACAQRLEK FT VLGRLPGVSAAVNFATERATVRYTPGLSNADAIKAAVVRAGFEVAETGPAQREQIRARQ FT QAQWRHERIRFWIAAALTLPLAAQMPAMFGWVGEAGIHDVIPRGFQLLLATPVQFWIGA FT RFYHGAWSALRGRSANMDVLVALGTTMAYFYSLVVTALGRHDLHVYFEASTMIITLVLL FT GKLLEARAKARTTAALDALVRLQPRMARVERGGMIVEVPVERLQPGDTFLVRPGDAVPV FT DGVVESGASAVNESMLTGESLPIDKAGGDKVYAATVNGEGVLRCRATGVGGSTLLAGII FT RLVEQAQGSKAPVQRRADQVSAIFVPVVVTLAVVTFAGWWLVAGDFQQALVNAVAVLVI FT ACPCALGLATPTAIMVATGQGARAGMLVKNAAALELAEQIAVLALDKTGTLTEGRPAVT FT EIRPGAGVSRSELLRLAAAVEQASAHPVALAVVEAARAEGCVLPPASELQAVSGKGMEG FT VVEGRKLRVGSPDFLAEAGVAVAEADIAALAAGANTLVAIAGDGHWLGVIGVADPLRGD FT SADAVRRLRAKGVHVLMLTGDHPATAAAIAGRVGIDEWQAGVLPAGKAEAVSSLVAERN FT GKARVGMAGDGINDAPALAAADVSFAIGVGADVAVEAADITLVRNSLHGVADAIDLSRA FT TLSKIRQNLFFAFIYNVLGIPLAAAGMLNPVVAGAAMAMSSVSVVTNSLLLRRWKPGR" FT CDS 1474902..1475111 FT /transl_table=11 FT /gene="copZ" FT /locus_tag="azo1356" FT /product="conserved hypothetical copper chaperon" FT /function="Copper chaperone" FT /note="Conserved hypothetical copper chaperon. Homology to FT copZ of copZ Azoarcus sp. EbN1 of 66%. Pfam: FT Heavy-metal-associated domain. Proteins that transport FT heavy metals in micro-organisms and mammals share FT similarities in their sequences and structures. Tigrfam: FT TIGR00003: copper-ion-binding protein. No signal peptide. FT No TMHs." FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K568" FT /db_xref="InterPro:IPR001802" FT /db_xref="InterPro:IPR006121" FT /db_xref="InterPro:IPR017969" FT /db_xref="UniProtKB/TrEMBL:A1K568" FT /protein_id="CAL93973.1" FT /translation="MEEVTLKVEGMSCGGCVRNVTGVLKALPGVSEADVSLDAAQARVR FT FDPARVSVAELRQAVEGAGFDSPA" FT CDS complement(1475126..1477969) FT /transl_table=11 FT /locus_tag="azo1357" FT /product="EAL/GGDEF/PAS/PAC-domain containing signalling FT protein" FT /function="predicted signal transduction protein containing FT a membrane domain an EAL and a GGDEF domain" FT /note="EAL/GGDEF/PAS/PAC-domain containing signalling FT protein," FT /note="Conserved hypothetical protein" FT /db_xref="GOA:A1K569" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR000160" FT /db_xref="InterPro:IPR000700" FT /db_xref="InterPro:IPR001054" FT /db_xref="InterPro:IPR001610" FT /db_xref="InterPro:IPR001633" FT /db_xref="InterPro:IPR004010" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K569" FT /protein_id="CAL93974.1" FT /translation="MLLLILLMTATVGLLSTLQDRRDLEKRLVTREAETLASHEAHLRN FT QLAGLADYLEFQRARSEERARQIVREQVDIVFRMAEAIYEREHGRLSDAHIRQLIIEAI FT RPLRFLDGRGYYFIDTTDGHCVLLPIAPQLEGSSLWDNRDDTGHYVMRGLAEAANNPAG FT AGFSRYRWYSPDNPRQMQEKIAYVRRFEPFDWIIGAGEYLYQIEADLQAEALKRIGAIS FT FHPDGVIGVTTADGRILVEPNLLAQPSARHAGLPEQPAVPWTAAAREVIQRNGGGRLQF FT SLPGPDGRAQRRLGYAVEHAGWQWYLVASVGLDGLDAALEHERDEVRNTARHRLEFTLL FT LLAVASTVAVIVSLAFSSWIGRRFASYRGEIAQRNAALEAKNRELQLAARVFECGNEAM FT MVLDADHRFITVNSACAQLAGLDAAALRGRPAAQLLNDHDGAGWERIARELAEQGAWSG FT EVTVRREDGPTLPAQLSVSAVLNSAGGATHYVGALTDMSAHKQTEALLRHMAEYDALTD FT LPNRSLLHDRARAAIQGAARTDRLAALLFIDLDRFKNVNDSLGHSVGDALLRQAAKRLA FT SLLHGGDTIARPGGDEFVMLLAEITDRAVAANRAAQIIDAFSTPFRVEHYELSVTPSIG FT IAIAPDDGVDADTLLRNADAAMYHAKESGRNTYRFFTDEMSLRVRERLELENLLRQAMS FT RDEFEVFYQPQFGLSDHRILGCEALVRWRHPERGLIAPERFIPLAEDTGLIVAIGRRVL FT ETACHTAQGWRAAGLGDIPVAVNASPVQIHHGNFAETVAEVLAETGLPARLLEIELTES FT TLMADAAPVAATLAALQDMGVRLAIDDFGTGYSSLAYLKRFQLDKLKIDRSFINDLPGD FT PDDANITVAIIGIARSLGMSVIAEGVETAAQERFLVDQGCAEGQGYLFSPPVPVESMTA FT LLATARDAATGPADCER" FT CDS 1478241..1478768 FT /transl_table=11 FT /gene="ppa" FT /locus_tag="azo1358" FT /product="probable inorganic pyrophosphatase" FT /function="Inorganic pyrophosphatase" FT /EC_number="3.6.1.1" FT /note="Probable inorganic pyrophosphatase. Homology to ppa FT of E. coli of 66% (sprot|IPYR_ECOLI). CATALYTIC ACTIVITY FT Diphosphate + H(2)O = 2 phosphate. Pfam: Inorganic FT pyrophospatease no signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K570" FT /db_xref="InterPro:IPR008162" FT /db_xref="UniProtKB/TrEMBL:A1K570" FT /protein_id="CAL93975.1" FT /translation="MGFDLVKAGKDVPNDINVIIEISAQGDPIKFEVDKDSGAVFVDRF FT MGTSMRYPLNYGYVPHTIAGDGDPVDVLVVTPFPLQPGVVIRCRPVGVLKMEDDGGVDA FT KVVAVPVSKLTPLYDKVQTTEDLPELLMKQTVHFFEHYKDLEPGKWVKVLGWGTVDEAK FT QEILDGLAKAAK" FT CDS complement(1478841..1479977) FT /transl_table=11 FT /locus_tag="azo1359" FT /product="conserved hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Conserved hypothetical protein. Homology to BB3581 FT of B.bronchiseptica of 53% (tremble:Q7WGK8). Has FT PF04339:(IPR00743)Protein of unknown function, DUF482;This FT family contains several proteins of uncharacterised FT function. NO signal peptide or TMH present." FT /db_xref="InterPro:IPR007434" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:A1K571" FT /protein_id="CAL93976.1" FT /translation="MTTSNGFHLTNRLADLDEQEWDALTDGQVTLSYAYLDTLERTGCV FT GDGTGWIPRHAVLRRNQTLVAALPMYVKHHSYGEYVFDWAWANAYRQHGLDYYPKWLAA FT VPFTPVPGARLLGRNTADRRLLLADVVALAARSGLSSLHILFPDQDEGRWMQEAGLSLR FT QGVQFHWQNAGYPDFEAFLATLNHDKRKKIRQERRKAATHGLRLRWLDGYTANDADWAF FT FYRCYTTTYALHRSTPYLTDEFFTELARRSPASVRLLLAERDEGPVAGAFFLCDRHALY FT GRYWGATSALPFLHFELCYYQAIEYCIAHGLARFEGGAQGEHKLSRGLLPTPTRSAHWI FT ADPRFRDAVDRFLEREREGIGFYLDELAERSPFRKSAG" FT CDS 1480139..1481755 FT /transl_table=11 FT /gene="nadE" FT /locus_tag="azo1360" FT /product="NAD(+) synthase (glutamine-hydrolyzing)" FT /function="NAD synthase" FT /EC_number="6.3.5.1" FT /note="Probable glutamine- or nh3-dependent NAD(+) FT synthetase (EC 6.3.5.1) (NAD(+) synthase FT [glutamine-hydrolyzing]). CAN USE BOTH GLUTAMINE OR AMMONIA FT AS A NITROGEN SOURCE (BY SIMILARITY). InterPro: NAD+ FT synthase nadE: NAD+ synthetase" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K572" FT /db_xref="InterPro:IPR003010" FT /db_xref="InterPro:IPR003694" FT /db_xref="InterPro:IPR014445" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR022310" FT /db_xref="UniProtKB/TrEMBL:A1K572" FT /protein_id="CAL93977.1" FT /translation="MNTALSIAVAQLNFTVGDLVGNADRIIEAISAARERGAGLLITPE FT LALSGYPPEDLLLRPDFYRGCAREVRRIAGHCRDFCLVLGHPTERGGVYYNAASVIRDG FT EVIATYHKHLLPNYEVFDEERYFESGVAPCVFEHGGVRIGVNICADVWESGPAEVARAA FT GAEVLVSLNASPFHIDKQQLRYAVLRDRVRETRLPVLYCNMVGGQDELVFDGASFALDR FT DGTVAYQSEAFAACIDVLRFEQGRWSGGGHAAPKGTEADIYAALVCGVRDYLGKNGFPG FT AIIGLSGGIDSALTLAVAVDALGADRVHAVMMPSPYTAQMSLDDSREMVKRLGVRYDEI FT AIEPAMNVFADLLAPQFAGLAADTTEENLQSRIRGMILMALSNKTGAIVLTTGNKSEMA FT TGYATLYGDMAGGFAVLKDLYKTTVYRLAAWRNSVGEVIPQNIIDRPPSAELKPDQKDQ FT DSLPPYEVLDAIIQAYMEHDESPREIIARGLPEADVRRTVTMLKRNEYKRRQAPVGIRV FT TQRGFGRDWRYPITSRYQDEF" FT CDS 1481805..1482143 FT /transl_table=11 FT /gene="glnB" FT /locus_tag="azo1361" FT /product="PII-like signal transmitter protein GlnB" FT /function="Nitrogen regulatory protein PII" FT /note="PII-like signal transmitter proteins are involved in FT the regulation of ammonium assimilation and nitrogen FT fixation. The PII-like proteins differed from each other in FT details of N-sensing. They were covalently modified by FT uridylylation upon nitrogen limitation. Similar to FT trembl|Q9EZQ2 (100%) and to trembl|Q8XWX5 (82%). Pfam: FT Nitrogen regulatory protein P-II" FT /note="High confidence in function and specificity" FT /db_xref="GOA:Q9EZQ2" FT /db_xref="HSSP:1HWU" FT /db_xref="InterPro:IPR002187" FT /db_xref="InterPro:IPR002332" FT /db_xref="InterPro:IPR011322" FT /db_xref="InterPro:IPR015867" FT /db_xref="InterPro:IPR017918" FT /db_xref="UniProtKB/TrEMBL:Q9EZQ2" FT /protein_id="CAL93978.1" FT /translation="MKKIEAIIKPFKLDEVREALSEVGIAGLTVTEVKGFGRQKGHTEL FT YRGAEYVVDFLPKIKVEVVVADDMVEQTMDAVIKAAQTGKIGDGKIFVTPVEQVVRIRT FT GETNEAAI" FT CDS complement(1482173..1483225) FT /transl_table=11 FT /locus_tag="azo1362" FT /product="hypothetical protein" FT /function="uncharacterized protein conserved in bacteria" FT /note="Hypothetical protein. no homology of the entire FT protein with the data bank. Pfam: Smr domain InterPro: Smr FT domain This family includes the Smr (Small MutS Related) FT proteins, and the C-terminal region of the MutS2 protein. FT It has been suggested that this domain interacts with the FT MutS1 protein in the case of Smr proteins and with the FT N-terminal MutS related region of MutS2. no signal peptide FT no TMHs" FT /db_xref="InterPro:IPR002625" FT /db_xref="UniProtKB/TrEMBL:A1K574" FT /protein_id="CAL93979.1" FT /translation="MARRPKDSSSTAAEKGGARRDHPFQALASLRGKGRPTGRPAASTP FT AARAQRAEANAQDAGAEDDTALFRAAVRDAAPIRDGGRKEIEAPRPEPVVRPREVEPEP FT DHAVRPRRGLDPLAEAYADVTPLRDANRVALGPAPSRHGRATTDPGAAFTATGTPTFVL FT PPDLDEHADPAAVFRHIVAGAQPLDQRNRVELERPRPAPAPLKREADERSALDESLEAP FT LTFEDRLDMGDEAAFLRPGLPRRVLSDLRRGRWVLQGEIDLHGCTREQARDTLASFLGS FT ALQQGKRCVRVIHGKGLGSPGKVSILKQLSRGWLAQREEILAFCQAGPYDGGGGALLVL FT LRGPGATRRA" FT CDS complement(1483241..1484191) FT /transl_table=11 FT /gene="trxB2" FT /locus_tag="azo1363" FT /product="thioredoxin-disulfide reductase" FT /function="Thioredoxin reductase" FT /EC_number="1.8.1.9" FT /note="Thioredoxin-disulfide reductase(EC 1.8.1.9). FT Homology to trxB of E. coli of 71% (sprot|TRXB_ECOLI). FT Catalyse the reaction: thioredoxin + nadp(+) = thioredoxin FT disulfide + nadph Pfam: Pyridine nucleotide-disulphide FT oxidoreductase signal peptide no TMHs" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K575" FT /db_xref="InterPro:IPR000103" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR005982" FT /db_xref="InterPro:IPR008255" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K575" FT /protein_id="CAL93980.1" FT /translation="MTTKHARLLILGSGPAGYTAAVYAARANLKPVLVTGLAQGGQLMT FT TTEVDNWPADADGVQGPELMERFQKHAERFNTEMIFDHIHTVQLQQRPFRLIGDAGEYT FT CDALIIATGATAKYLGLPSEEKFAGRGVSACATCDGFFYRNQDVAVIGGGNTAVEEALY FT LANIAKKVTVVHRREKFRAEKILIDKLMEKVEAGKIELVLNATLDEVLGDNTGVTGMRV FT RNESGATQDIALQGVFIAIGHKPNTDIFKGQLEMDETGYLITQGGRNGNATQTNIAGVF FT AAGDVQDHIYRQAVTSAGSGCMAALDAERYLDALS" FT CDS 1484423..1485094 FT /transl_table=11 FT /gene="vfr" FT /locus_tag="azo1364" FT /product="probable cyclic AMP receptor protein" FT /function="cAMP-binding proteins - catabolite gene FT activator and regulatory subunit of cAMP-dependent protein FT kinases" FT /note="Probable cyclic amp receptor-like protein," FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K576" FT /db_xref="InterPro:IPR000595" FT /db_xref="InterPro:IPR001808" FT /db_xref="InterPro:IPR002373" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR012318" FT /db_xref="InterPro:IPR014710" FT /db_xref="InterPro:IPR018488" FT /db_xref="InterPro:IPR018490" FT /db_xref="UniProtKB/TrEMBL:A1K576" FT /protein_id="CAL93981.1" FT /translation="MSQPTAVSTIALKTFPLFQGLSDEVLGNVARVSMMRRIPRGQAVV FT RAGDRTDYVYFVLTGNLKVVVSDEDGREVILSILGQGELFGEMGMFGEQPRSASVIAVV FT PADLVMIAKQDFRQIMQENFEIAWRIMSNLAERLRNADRKIESLALMDVYGRVARLLID FT MSEDVNGKTMVVRKISKQDIAKMIGASREMVSRVMKDLGQEGLIEETPQGIILLDRLNE FT V" FT CDS 1485243..1487531 FT /transl_table=11 FT /gene="FtsK" FT /locus_tag="azo1365" FT /product="putative cell division protein" FT /function="DNA segregation ATPase FtsK/SpoIIIE and related FT proteins" FT /note="DNA translocase ftsK 2. InterPro: FtsK/SpoIIIE FT family" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K577" FT /db_xref="InterPro:IPR002543" FT /db_xref="InterPro:IPR018541" FT /db_xref="UniProtKB/TrEMBL:A1K577" FT /protein_id="CAL93982.1" FT /translation="MLPRSSRSQPLPEKISLLLQEARWLILGVMSLYVGLVLIGYNKAD FT PGWSHAAEVARVANPGGRFGAWLADLLLYLFGISAWWWVVFLGYSLMWGFRRLKNQLTL FT DRRSFFFVLVGFFSVLVTSSALEYLRFHSHGVAVPLSPGGLLGMEFGQLVQRYLGYTGG FT TLMLLALMASGLSLFTGVSWLAAVERVGLAIEQAVAGAQQAYYRWLDRKAGRQVAEKRE FT AVVETRRKKTEQAPAAPLRIEPAVTVVQKSERVEKERQQTLFADAVEGAIPPLSLLDPA FT SGDIEPPSAESLEFTSRLIETKLGDFGVEVKVLAAYPGPVITRYEIEPATGVKGSQVVN FT LAKDLARALSLVSVRVVETVPGKSCMALELPNPKRQTVRLSEIVGSKAYHDMASPLTVV FT LGKDIGGQPVVADLAKMPHLLVAGTTGSGKSVGINAMILSLLYKSEPERVRMIMVDPKM FT LELSIYEGIPHLLAPVVTDMKHAANALNWCVAEMEKRYKLMAAVGVRNLAGFNKAVLEA FT RKAEAPLTNPFAINPDNPEPLETLPYIVVVVDELADMMMVVGKKVEELIARLAQKARAA FT GIHLILATQRPSVDVITGLIKANVPTRIAFQVSSKIDSRTILDQMGAETLLGMGDMLYL FT APGTGLPVRVHGAFVADEEVHKVVDHLKRVGPPDYIDGILAAPEDDLEALAGAGGEDGD FT GEADPLYDQAVEVVLKTRRPSISLVQRHLRIGYNRSARLIEQMERAGLVSPMGSNGNRE FT VIVPAKEAE" FT CDS 1487528..1488205 FT /transl_table=11 FT /gene="lolA" FT /locus_tag="azo1366" FT /product="putative outer membrane lipoprotein carrier FT protein" FT /function="Outer membrane lipoprotein-sorting protein" FT /note="Putative outer-membrane lipoprotein carrier protein. FT Homology to lolA of E. coli of 25% (sprot|LOLA_ECOLI) FT Participates in the translocation of lipoproteins from the FT inner membrane to the outer membrane. Only forms a complex FT with a lipoprotein if the residue after the N-terminal Cys FT is not an aspartate (The Asp acts as a targeting signal to FT indicate that the lipoprotein should stay in the inner FT membrane) (By similarity). Pfam: outer membrane lipoprotein FT carrier protein LolA Tigrfam: lolA: outer membrane FT lipoprotein carrier singal peptide no TMHs" FT /note="Family membership" FT /db_xref="GOA:A1K578" FT /db_xref="InterPro:IPR004564" FT /db_xref="InterPro:IPR018323" FT /db_xref="UniProtKB/TrEMBL:A1K578" FT /protein_id="CAL93983.1" FT /translation="MKRVLGMNAGHWGALVVCAALVFGTRCAVAADGVDQLRQFVTATR FT SAEGSFEQVVTAKSGRKPQQSEGSFAFSRPGKFRWQYELPYQQLLVGDGEKLWSWDKDL FT NQVAVKRLGDALGATPAAILFGGSDLEQNFELSDGGSAEGLAWVEARPRKPESGFENLR FT LGLYAGQLRRMEMRDSFGQATVIVFTRLVANPALDPARFRFVPPAGADVIGDDVAPARA FT PRR" FT CDS 1488217..1489554 FT /transl_table=11 FT /locus_tag="azo1367" FT /product="conserved hypothetical protein" FT /function="uncharacterized ATPase related to the helicase FT subunit of the Holliday junction resolvase" FT /note="Hypothetical protein CBU1189. InterPro: AAA-protein FT (ATPases associated with various cellular activities) ruvB: FT Holliday junction DNA helicase R." FT /note="Specificity unclear" FT /db_xref="GOA:A1K579" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003959" FT /db_xref="InterPro:IPR021886" FT /db_xref="UniProtKB/TrEMBL:A1K579" FT /protein_id="CAL93984.1" FT /translation="MADLFDSVEPQRVPLAERMRPGTLDEVAGQAHLLGPGKPLRLAFA FT SGKPHSMILWGPPGVGKTTLARLMAKGFDAEFVALSAVFSGVKDIREAIVQAQAAKARG FT RHTILFVDEVHRFNKAQQDAFLPYVEQGLVTFIGATTENPSFEVNSALLSRAAVYVLEP FT LDTEAMQGLFERARSLACPDLVFEEAARERMIGFADGDARRLMNLIEQIQVAAETAGVA FT PVTADFVDEALSRDLRRFDKGGEAFYDQISALHKSVRGSNPDAALYWLCRMLDGGADAH FT YLGRRLVRMAVEDIGLADPRALEIALNACETYERLGSPEGELALAEATVFLACAAKSNA FT VYKAYNAARQFIAKDGSRPVPLHLRNAPTRLMKELGYGQTYRYAHDEPDAYAAGESYLP FT EGMAPPGWYQPTPRGLEARIADKLAHLRELDRQAGAREGTAKGERG" FT CDS complement(1489593..1489856) FT /transl_table=11 FT /locus_tag="azo1368" FT /product="conserved hypothetical protein" FT /note="Conserved hypothetical protein. Homology to ebA7035 FT of Azoarcus sp. EbN1 of 79% (gnl|keqq|eba:ebA7035(KEGG)). FT No domains predicted. No TMHs. No signal peptide." FT /db_xref="UniProtKB/TrEMBL:A1K580" FT /protein_id="CAL93985.1" FT /translation="MLSIRDCLDYCDLTEDEVSLIAEHEGIPDVAAAQVACGLVQTPEG FT VLVLTNYMRDLIERATERGDTEKAERAKSLCARFMEDHPLPH" FT CDS 1490125..1491417 FT /transl_table=11 FT /locus_tag="azo1369" FT /product="SerS protein" FT /function="Seryl-tRNA synthetase" FT /EC_number="6.1.1.11" FT /note="Seryl-tRNA synthetase (EC 6.1.1.11) (Serine--tRNA FT ligase) (SerRS)." FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K581" FT /db_xref="InterPro:IPR002314" FT /db_xref="InterPro:IPR002317" FT /db_xref="InterPro:IPR006195" FT /db_xref="InterPro:IPR010978" FT /db_xref="InterPro:IPR015866" FT /db_xref="UniProtKB/Swiss-Prot:A1K581" FT /protein_id="CAL93986.1" FT /translation="MLDIQLLRGQLSQVAERLALRGVTLDSGAFTALEDERKQLQTRTQ FT ELQAKRNALSKQIGILKGKGEDASAVMAEVGQLGDELKACEQALPVVLEKLNAFLAGLP FT NLPQEGVPVGEDETGNVEVRRWGTPRSFDFEVKDHVDLGAALGLDFDTGAKLSGSRFTF FT MRGQIARLHRALAQFMLDTQTLEHGYTECYAPYIVNREVLVGTGQLPKFKEDMFWVLRG FT GDEEGGEQYLISTSEIPLTNTVREQILAADALPIKLTAHSPCFRSEAGSAGRDTRGMIR FT QHQFDKVEMVQIVHPDASNAALEEMVGHAEAILQKLELPYRVITLCTGDMGFSAAKTYD FT LEVWLPAQNTYREISSCSNCEAFQARRMQARFKTAQGKNELVHTLNGSGLAVGRTLVAV FT LENYQQADGSIVVPKALVPYMGGLEVLRPAS" FT CDS 1491592..1493208 FT /transl_table=11 FT /locus_tag="azo1370" FT /product="putative aerotaxis receptor protein" FT /function="Methyl-accepting chemotaxis protein" FT /note="Aerotaxis receptor protein," FT /note="Specificity unclear" FT /db_xref="GOA:A1K582" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR003660" FT /db_xref="InterPro:IPR004089" FT /db_xref="InterPro:IPR013656" FT /db_xref="UniProtKB/TrEMBL:A1K582" FT /protein_id="CAL93987.1" FT /translation="MIDNKSATTREHAFPRGKLVVLKYDMDFKITYANEACAEMVGSTR FT EALIGSSIKEIAHPDVPQELLADVRGTTSSGRPWLGLSKLKHRDGGVAWSTALTIPVRQ FT NGRNVGFMSLRSEAPRERVQAEEALYEAMRRKQARYRNLDMPVRRALSSAAMLCALGGL FT GSSLALLLVFAGLALDAGAWAYALIAAGGLGLAGMLALVATLWRRSITESATMLKAFER FT IAEGDLTSTLPVGRSDEMGRLMESLMYMQGRLKVMLDEIRLAAALTDKENAALRAEVQS FT LKDAADAQRDRILSVSAASEQNSAAVAEVAGGAKASAQAANEALALVAEGRAHLNQTVG FT AARRTVDAVEGANRAMRALGDSIQSVATISAEIREISDQTNLLALNAAIEAARAGEVGR FT GFAVVADEVRKLAERTAHCTGNIASMVGEIRRVSDEVAGDMDKAAGLVGEASGSAGDSL FT GIMGRIEQGSGRVAGLAGHIADASAEHSTASEQIAQDMELISGLVERSAAGIDAVDRAA FT DGVQCNVGNLKQLVGFFRVVA" FT CDS complement(1493285..1495105) FT /transl_table=11 FT /gene="lpdA" FT /locus_tag="azo1371" FT /product="dihydrolipoamide dehydrogenase" FT /function="Pyruvate/2-oxoglutarate dehydrogenase complex FT dihydrolipoamide dehydrogenase (E3) component and related FT enzymes" FT /EC_number="1.8.1.4" FT /note="Dihydrolipoamide dehydrogenase. Homology to lpdA of FT N. meningitides of 70% (trembl|Q59099). THE BRANCHED-CHAIN FT ALPHA-KETO DEHYDROGENASE COMPLEX CATALYZES THE OVERALL FT CONVERSION OF ALPHA-KETO ACIDS TO ACYL-COA AND CO(2). IT FT CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: FT BRANCHED-CHAIN ALPHA-KETO ACID DECARBOXYLASE (E1) LIPOAMIDE FT ACYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3) (BY FT SIMILARITY). InterPro: FAD-dependent pyridine FT nucleotide-disulphide oxidoreductase (IPR001327); Pyridine FT nucleotide-disulphide oxidoreductase, classI (IPR001100); FT biotin/Lipoyl attachment (IPR000089); Pyridine FT nucleotide-disulphide oxidoreductase dimersiation domain FT (IPR004099); NAD binding site (IPR000205); 2-oxo acid FT dehydrogenase acetyltransferase, classI (IPR003016) Pfam: FT Biotin-requiring enzyme; Pyridine nucleotide-disulphide FT oxidoreductase; Pyridine nucleotide oxidoreductase FT dimersation domain no TMHs no signal peptide" FT /note="High confidence in function and specificity" FT /db_xref="GOA:A1K583" FT /db_xref="InterPro:IPR000089" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR003016" FT /db_xref="InterPro:IPR004099" FT /db_xref="InterPro:IPR006258" FT /db_xref="InterPro:IPR011053" FT /db_xref="InterPro:IPR012999" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR016156" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:A1K583" FT /protein_id="CAL93988.1" FT /translation="MSLVEVKVPDIGDFDSVPVIELFVKVGDTIKVDDAICTLESDKAT FT MDVPSSAAGVVKEVLVKVGDKVGEGAVLLKVEAAGAAASPLQGEGRGGDGVKPASDVPH FT PPPSLPLEGGGAKAAPAAASHTGGADAEYDMVVLGAGPGGYSAAFRAADLGLKTAIIER FT YATLGGVCLNVGCIPSKALLHVAAVIEEAEHVETAGIKFAKPSVDVDALRKHKDGVIGK FT LTGGLAGMAKARKVDVIRGYGSFLDPHHLEVEETTGNGQDKTGAKKVVKFKNCIIAAGS FT AAVHLPFIPKDPRIVDSTGALELRQVPGKMLVIGGGIIGLEMATVYSTLGARIDVVEML FT DGLMQGPDRDAVKVWEKQNAARFDKVMLKTKTVAVEAKDDGLWVKFEGEGAPAEPVRYD FT MILQSAGRSPNGKKIGADKAGVIVGERGFIPVDVQMRTNVPHIFAIGDIVGQPMLAHKA FT VHEAHVAAEVAAGHKAAFDATVIPGVAYTHPEVAWVGYTEAQAKSEGKKVEVAKFPWAA FT SGRAIANGADYGFTKLIFDAETHRVIGGTIVGPSAGDMIGEVCLAIEMGADAVDIGKTI FT HPHPTLGETVGMAAEVAHGSCTDLPPMRKK" FT CDS complement(1495116..1496804) FT /transl_table=11 FT /gene="pdhB" FT /locus_tag="azo1372" FT /product="probable dihydrolipoamide acetyltransferase" FT /function="Pyruvate/2-oxoglutarate dehydrogenase complex FT dihydrolipoamide acyltransferase (E2) component and related FT enzymes" FT /EC_number="2.3.1.12" FT /note="Probable dihydrolipoamide acetyltransferase. FT Homology to pdhB of A. eutrophus of 62% (sprot|ODP2_ALCEU) FT THE PYRUVATE DEHYDROGENASE COMPLEX CATALYZES THE OVERALL FT CONVERSION OF PYRUVATE TO ACETYL-COA & CO(2). IT CONTAINS FT MULTIPLE COPIES OF THREE ENZYMATIC COMPONENTS: PYRUVATE FT DEHYDROGENASE (E1) DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2) FT & LIPOAMIDE DEHYDROGENASE (E3) (BY SIMILARITY). InterPro: FT 2-Oxo acid dehydrogenase acyltransferase catalytic domain FT (IPR001078); Type I antifreeze protein (IPR000104); FT Biotin/Lipoyl attachment (IPR000089); E3 binding domain FT (IPR004167); 2-Oxo acid dehydrogenase acyltransferase FT component lipoyl binding site (IPR003016) Pfam: FT Biotin-requiring enzyme; E3 binding domain; 2-oxo FT dehydrogenase acyltransferase Tigrfam: BCCP: acetyl-CoA FT carboxylase biotin carboxyl carrier protein no TMHs no FT signal peptide" FT