ID FQ311875; SV 1; circular; genomic DNA; STD; PRO; 3859257 BP. XX AC FQ311875; XX PR Project:PRJEA50353; XX DT 27-SEP-2010 (Rel. 106, Created) DT 20-JAN-2011 (Rel. 107, Last updated, Version 2) XX DE Arthrobacter arilaitensis RE117 chromosome, complete sequence. XX KW . XX OS Arthrobacter arilaitensis OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. XX RN [1] RP 1-3859257 RA Genoscope - CEA; RT ; RL Submitted (09-JUL-2010) to the INSDC. RL Genoscope - Centre National de Sequencage : BP 191 91006 EVRY cedex - RL FRANCE (E-mail : seqref@genoscope.cns.fr - Web : www.genoscope.cns.fr). XX RN [2] RX DOI; 10.1371/journal.pone.0015489. RX PUBMED; 21124797. RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B., RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F., RA Vallaeys T.; RT "The arthrobacter arilaitensis Re117 genome sequence reveals its genetic RT adaptation to the surface of cheese"; RL PLoS One 5(11):e15489-e15489(2010). XX DR GR; FQ311875_GR. DR SILVA-LSU; FQ311875. DR SILVA-SSU; FQ311875. DR StrainInfo; 382655; 1. XX FH Key Location/Qualifiers FH FT source 1..3859257 FT /organism="Arthrobacter arilaitensis" FT /strain="RE117" FT /mol_type="genomic DNA" FT /db_xref="taxon:256701" FT CDS 353..1789 FT /transl_table=11 FT /gene="dnaA" FT /locus_tag="AARI_00010" FT /product="chromosomal replication initiator protein DnaA" FT /function="3.1 DNA replication" FT /note="plays an important role in the initiation and FT regulation of chromosomal replication. Binds to the origin FT of replication" FT /db_xref="GOA:E1VRJ7" 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/TrEMBL:E1VRJ7" FT /protein_id="CBT74250.1" FT /translation="MSSDETNSIGSSWRQVIRKIEDDDRVKARYRAFVSLAKPQGLIGT FT TLLVAVPNDLTRDILQTQLREPLDEALREVFQDDIRCAVSVDLSLSDELEEDEQETKPA FT PPAAPAVVEAPGPRPQPAPQPTPPSNSQEFGRLNPKYIFDTFVIGSSNRFAHAAAVAVA FT EAPAKAYNPLFIYGDSGLGKTHLLHAIGHYARHLYKGIRVRYVNSEEFTNDFINSIRDD FT EGASFKQTYRNVDILLIDDIQFLANKDATQEEFFHTFNALHNHNKQVVITSDLPPKQLQ FT GFEDRMRSRFEWGLLTDIQPPELETRIAILRKKADAENLSAPGDVMEYIASRISTNIRE FT LEGALIRVTAFASLNNQPVDLALAETVLKDLISEDGAQEITPSTIIKQTAEYFGLSIDE FT LNSKSRTRTLVTARQIAMYLLRELTDMSLPKIGAELGGRDHTTVIHADRKIRELMAERR FT AIFNQVTELTNRIKQSQREH" FT CDS 2256..3383 FT /transl_table=11 FT /gene="dnaN" FT /locus_tag="AARI_00020" FT /product="DNA polymerase III subunit beta" FT /function="3.1 DNA replication" FT /EC_number="2.7.7.7" FT /note="DNA polymerase III is a complex, multichain enzyme FT responsible for most of the replicative synthesis in FT bacteria. The beta chain is required for initiation of FT replication once it is clamped onto DNA. DNA polymerase III FT contains a core (composed of alpha, epsilon and theta FT chains) that associates with a tau subunit. This core FT dimerizes to form the POLIII complex. PolIII associates FT with the gamma complex (composed of gamma, delta, delta, FT psi and chi chains) and with the beta chain to form the FT complete DNA polymerase III complex" FT /db_xref="GOA:E1VRJ8" 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:E1VRJ8" FT /protein_id="CBT74251.1" FT /translation="MKFSVEKDVLADAVSWTARSLAQRPPSPVLAGILITSHEGLVRLE FT GFDYEISSHIEIPADISEQGSILVSGKLLAEITRSLPNSTVTIETDGTKISLNCGRSRF FT HLATMPVDEYPTLPELPAIAGTIDGQAFSEAVSQVIVAASKDDTLPVLTGIKVEIENDL FT ITFLATDRYRLALRELNWSPNKSEISTSFLIKAKTLSEVAKTLSNSGELKLALGENGEM FT VGFESSNRRTTSLLINGEYPKIRSLFPSDTPIHATVRTSELMEAVRRVSVVAERNTPVR FT MAFTDGQLTLDAGTGEDAQAEEAIVAALRGEDIVVAFNPTFLSEGLNSFNTDFVRFSFT FT SAPKPAMLTGQKKLDEDDQDQYRYLVMPVRLPNSN" FT CDS 3442..4605 FT /transl_table=11 FT /gene="recF" FT /locus_tag="AARI_00030" FT /product="DNA replication and repair protein RecF" FT /function="3.1 DNA replication" FT /note="RecF is a recombinational DNA repair ATPase that FT maintains replication in the presence of DNA damage. When FT replication is prematurely disrupted by DNA damage, several FT recF pathway gene products play critical roles processing FT the arrested replication fork, allowing it to resume and FT complete its task." FT /db_xref="GOA:E1VRJ9" FT /db_xref="InterPro:IPR001238" FT /db_xref="InterPro:IPR003395" FT /db_xref="InterPro:IPR018078" FT /db_xref="UniProtKB/TrEMBL:E1VRJ9" FT /protein_id="CBT74252.1" FT /translation="MYISQLSLTGFRSYAQADVHLAPGINVLIGPNGVGKTNIVESIGY FT LANLSSHRVSNDAPLLNFESDRALIRGTVHRGPQTTTLEVEITSGKINRARINRANPVR FT AREILGMVRTVLFAPEDLALIKGDPSNRRKFLDELLVALRPIESGTKNDYDRIVKQRNA FT LLKSIRGKSKLSTSQENTLKAWDLQLTMTGARLIRGRLDVLALIRPYMQAAYADLADGA FT KDARAVYRSSLEGELDENSLPAEDLESLEQEEIQELLLTAIEANRSREVDRGISLFGPH FT RDDLTLILGPAPAKGYASHGETWSFALALRLAAYRVFGDDDPRPGSGPILILDDVFAEL FT DTTRRDRLAHIVAGAEQVLVTAAVVEDVPEALKGHFFQVSPGQVVDA" FT CDS 4598..5155 FT /transl_table=11 FT /locus_tag="AARI_00040" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF05258. This family FT contains several actinomycete proteins of unknown function" FT /db_xref="InterPro:IPR007922" FT /db_xref="UniProtKB/TrEMBL:E1VRK0" FT /protein_id="CBT74253.1" FT /translation="MHEPSERDEHRFDPEIDAAKALLNRMRKLAEERGETRVDAARMEK FT VRKRKASRRGFAAEKPESAEGAIRDPRAIGDVVSRLSKARGWNTQVAVGSVLGRWAEII FT GADNAKHCQPESFEDTVVVMRCDTTARAAQMRLMSHDILKKFDAELGPGIVTVLKVLGP FT NAPSWRHGMRSVAGRGPRDTYG" FT CDS 5438..7501 FT /transl_table=11 FT /gene="gyrB" FT /locus_tag="AARI_00050" FT /product="DNA gyrase subunit B" FT /function="3.1 DNA replication" FT /EC_number="5.99.1.3" FT /note="DNA gyrase negatively supercoils closed circular FT double-stranded DNA in an ATP-dependent manner and also FT catalyzes the interconversion of other topological isomers FT of double-stranded DNA rings. Made up of two chains. The A FT chain is responsible for DNA breakage and rejoining; the B FT chain catalyzes ATP hydrolysis" FT /db_xref="GOA:E1VRK2" FT /db_xref="InterPro:IPR001241" FT /db_xref="InterPro:IPR002288" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR006171" 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:E1VRK2" FT /protein_id="CBT74254.1" FT /translation="MSTENASPQEPAESQAAAESMTSKVEHTYGAQDITVLEGLEAVRK FT RPGMYIGSTGPRGLHHLVYEVVDNSVDEALAGYCDTINVTLQADGGVRCEDNGRGIPVD FT VHPTEGKPTVEVVMTILHAGGKFGGGGYAVSGGLHGVGISVVNALSEKVNTIVRRQGHA FT WRIGFGNGGHTTQQLTKGEETDRTGTSQTFYPDPEIFETVEFDFETLRARFQQMAFLNK FT GLRITLTDERPQDNAEPEAEVEEEIENQVVKPRTVDYLYKDGLLDYVKHLNAAKKIELV FT HDEVIAFESEDSKRGISLEIAMQWTNAYAESVHTYANTINTHEGGTHEEGFRAALTGLL FT NRYARDNKILREKDDNLTGEDAREGLTAVISVKLSEPQFEGQTKTKLGNSMARGFVQGV FT VNEELGDWFERNPNVARDIIRKAQLASQARMAARKARDNARRKSPMESFGMPGKLSDCS FT SKNPAECEVFIVEGDSAGGSAKRGRDPHTQAILPLRGKILNVERARLDRALGNAEVQAM FT ITAFGTGIGEEFDMAKLRYHKIVLMADADVDGQHITTLLLTLIFRFMRPLIEHGYVYLA FT APPLYRIKWSNAAHDYVFSDKERDDALLAGQASNKRLPKDNGIQRYKGLGEMDYSELWD FT TTMDPERRTLRQVTMDDAAAADEVFSVLMGEDVESRRNFIQQNAKDVRFLDI" FT CDS 7560..10187 FT /transl_table=11 FT /gene="gyrA" FT /locus_tag="AARI_00060" FT /product="DNA gyrase subunit A" FT /function="3.1 DNA replication" FT /EC_number="5.99.1.3" FT /note="DNA gyrase negatively supercoils closed circular FT double-stranded DNA in an ATP-dependent manner and also FT catalyzes the interconversion of other topological isomers FT of double-stranded DNA rings. Made up of two chains. The A FT chain is responsible for DNA breakage and rejoining; the B FT chain catalyzes ATP hydrolysis" FT /db_xref="GOA:E1VRK1" 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:E1VRK1" FT /protein_id="CBT74255.1" FT /translation="MSDEQTPENAPMDGEIIEPIHEGGRVDQIDLQTEMQRSYLDYAMA FT VIVGRALPDVRDGLKPVHRRVLYAMYDGGYRPERSYNKCARVVGEVMGQYHPHGDTAIY FT DALVRLIQDWVMRYPLALGQGNFGSPGNDGAAAQRYTETKMAPLAMEMVRDINENTVDF FT QDNYDGKNQEPTVLPARFPNLLVNGSSGIAVGMATNIPPHNLREVAEGVQWYLQNPEAS FT REELLAELMLRVKGPDFPSGAMILGTKGISDAYRTGRGSITMRAVVNVEEIQGRTCLVV FT TELPYMANPDNLAVKIAELVRDGKISGIADMRDETSGRTGQRLVIVLKRDAVAKVVLNN FT LYKHTELQSNFSANMLAIVDGVPRTLPLDGFIRHWVTHQIEVIVRRTEYRLKKAEEEAH FT ILRGLLKALDALDEVIALIRRSATTEAARDGLMELLDIDEDQARAILDMQLRRLAALER FT QKIQDRHAELDRMIAEFKAIIADPARQRQIVSEELQEIVAKHGDDRRTKVLMGYDGDMS FT VEDLIPEEEMVVTITRGGYVKRTRIDNYRSQARGGKGIKGANLRGDDVVEHFFVTSTHN FT WLLFFTNHGRVYRTKCYELAEAGRDAKGQHVANVMAFQPDEHIAQVLDLRTYQDAAYLM FT LATRNGLVKKTRLEDYDTNRTAGVIAINLREDDELVSAQLVSESDDVMLVSRKGQSVRF FT TATDTALRPMGRATSGVTGMKFREGDELLAADVVRDDSYVFTVTNEGYAKRTTVAEYRV FT QSRGGLGIKVAKLNEERGELVGALIVDETDEVLVVMGSGKVVRSAVSQVPSKGRDTMGV FT IFAKPDKKDHIIAVAKNSETELEENLEEDAVTLDAENTIDESSAAPETESGAENDDDTN FT GGNA" FT CDS 10184..10807 FT /transl_table=11 FT /locus_tag="AARI_00070" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR021949" FT /db_xref="UniProtKB/TrEMBL:E1VRK3" FT /protein_id="CBT74256.1" FT /translation="MSTPSTPRPSGSAPKSAAPRPTQVKRPAPTGTGARPANAGARPAA FT GQQRPAGARPAGQRPTGAPQRPTSQQRPANGQDRLVRPAPKAKVRKARLLVSKVEPFSV FT LKLAFLLSVAFGVITVVAAVGIWAVLDLTGTFDSFNQLMRDAIGADGNFDLRDSMSLGQ FT VASYATIIAVVNVVVISVVSMLGAVLYNIAASLVGGAGVTLTDD" FT tRNA 10930..11003 FT /locus_tag="AARI_36270" FT /product="transfer RNA-Ile" FT /anticodon=(pos:10964..10966,aa:Ile) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 11161..11236 FT /locus_tag="AARI_36280" FT /product="transfer RNA-Ala" FT /anticodon=(pos:11194..11196,aa:Ala) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 11329..11401 FT /locus_tag="AARI_36290" FT /product="transfer RNA-Ala" FT /anticodon=(pos:11362..11364,aa:Ala) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(11465..12640) FT /transl_table=11 FT /locus_tag="AARI_00080" FT /product="putative group 1 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00534: Glycosyl transferases group 1. FT Proteins containing this domain transfer UDP, ADP, GDP or FT CMP linked sugars to a variety of substrates, including FT glycogen, fructose-6-phosphate and lipopolysaccharides. The FT bacterial enzymes are involved in various biosynthetic FT processes that include exopolysaccharide biosynthesis, FT lipopolysaccharide core biosynthesis and the biosynthesis FT of the slime polysaccaride colanic acid" FT /db_xref="GOA:E1VRK4" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VRK4" FT /protein_id="CBT74257.1" FT /translation="MRVIHDVHPEDVKVAIVAESFLPHFNGVTNSILKTLDHLRQAGHE FT AVVITPNSSLAGELSGQGVPKVYQGFKIITVPSVPLASYPEVRVATASVWRLRKLLARE FT QVDVVHLASPFILGWQALRAAQELDLPTVALYQTEVPSYAARYKMPWLTQRLWEHVRAI FT HTAADRTLVPSTFSCRQLQSLGVQRLAICGRGVDTAQFTPRLRSEQFRRAVAPNDEVVI FT GYVGRLAAEKQVADLKALADLGNTRLVIVGSGPLEDELREILPNAHFTGFLSGERLAEV FT MASMDIFVHPGSSETFCQTIQEAMACGVPVVAVGRGGPLDLVDSSRTGWLYQPGNLEEL FT RSRVSDLAYDDAKRLAFASAALSSVQDRSWHSIGEQLLGHYEQVRTAKIRN" FT CDS 12719..13690 FT /transl_table=11 FT /locus_tag="AARI_00090" FT /product="putative sodium-dependent transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="identified by match to protein family PF01758. Bile FT acid:Na+ symporter (BASS) family (TC 2.A.28.y.z): these FT symporters exhibit broad specificity, taking up a variety FT of non bile organic compounds as well as taurocholate and FT other bile salts" FT /db_xref="GOA:E1VRK5" FT /db_xref="InterPro:IPR002657" FT /db_xref="UniProtKB/TrEMBL:E1VRK5" FT /protein_id="CBT74258.1" FT /translation="MHSEQPGPDAVASKAKKLDKDSRIAVLLFPVLILLGGLCGMLLPQ FT AFAGLAGWINPLLMVIMFCMGLTLALPDFALVFKNPLPVLGGVAAQFIVMPLVAWLVAA FT LLQLEPALAAGLILVGCAPGGTASNVVSYLARGNVALSVAMTSVSTLLAPLLTPVLALW FT LAGQYMPVDASSMAISVVQIVLIPVVLGIVLRMLFNRIVTKINAVLPWLSVLAITFVVT FT IIVAGSAQTILTAGLLVLVAVVLHNSLGLALGYGIGVLLRVPTASRRTIAIEVGMQNSG FT LAGGLAKQYFSPEAALLGAVFSVWHNLSGALVAAYWRRKDAE" FT CDS 13822..14691 FT /transl_table=11 FT /locus_tag="AARI_00100" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.973) with cleavage site probability 0.306 FT between position 22 and 23. 8 transmembrane helices FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="GOA:E1VRK6" FT /db_xref="InterPro:IPR000620" FT /db_xref="UniProtKB/TrEMBL:E1VRK6" FT /protein_id="CBT74259.1" FT /translation="MTILLALVGIIGISASGPIIAAFPGVPVLSMAFWRNGAAAAVLSA FT PALRKNPKAYLHMTSREWFFTGIAGVALALHFVCFMYSMRLTSVAAGTALVCIQGVWIA FT MFQVLRGTKYRTQVFLGMGVALLGAIVITGFDMGLGRDAIVGDLLALAGGILAAVYTLA FT GSVARRTLGTTTYASSCYAITAAVLLVLCFLTGTPIWGFDARGWIAIILLTLCAQIFGH FT TAMNHLLSVLGPLTVSTLILLEIPGAAILAALFLGQVVSIATYAGLAVILVGLALVIRG FT QAQPKTEV" FT CDS complement(14698..14904) FT /transl_table=11 FT /locus_tag="AARI_00110" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRK7" FT /protein_id="CBT74260.1" FT /translation="MSKKSKVGKVLAVGLIAGLVAVLVAVWKASKPIEDPWENEPVPAQ FT PHQPVQTREASVEEIREILEDDK" FT CDS 15075..15620 FT /transl_table=11 FT /gene="ppiA" FT /locus_tag="AARI_00120" FT /product="peptidylprolyl isomerase" FT /function="3.9 Protein folding" FT /EC_number="5.2.1.8" FT /note="identified by match to protein family PF00160: FT Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD. FT Peptidylprolyl isomerase is an enzyme that accelerates FT protein folding by catalyzing the cis-trans isomerization FT of proline imidic peptide bonds in oligopeptides" FT /db_xref="GOA:E1VRK8" FT /db_xref="InterPro:IPR002130" FT /db_xref="InterPro:IPR020892" FT /db_xref="InterPro:IPR024936" FT /db_xref="UniProtKB/TrEMBL:E1VRK8" FT /protein_id="CBT74261.1" FT /translation="MTANATHKATIHTTLGDIVVDLFGNHAPKTVKNFVGLSTGEQEWV FT HPESGDKKTNTPLYSGTIFHRIIADFMIQGGDPLGQGFGGPGYQFDDEIHPELNFNEPY FT KLAMANAGIRMGRGTNGSQFFITTVPTAWLQGKHTIFGEVVEPESRKIVDALNAVSTDG FT RDKPLEDVVINSVDIETL" FT CDS 15722..16579 FT /transl_table=11 FT /locus_tag="AARI_00130" FT /product="rhomboid family protein" FT /function="3.10 Protein degradation" FT /note="identified by match to protein family PF01694. This FT group of proteins contain serine peptidases belonging to FT the MEROPS peptidase family S54 (Rhomboid, clan S-). They FT are integral membrane proteins related to the Drosophila FT melanogaster (Fruit fly) rhomboid protein. 7 transmembrane FT helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VRK9" FT /db_xref="InterPro:IPR002610" FT /db_xref="InterPro:IPR022764" FT /db_xref="UniProtKB/TrEMBL:E1VRK9" FT /protein_id="CBT74262.1" FT /translation="MSYGQVSPEGQAAPTCFRHPQTISFVSCNRCGRPVCPQCQVSAPV FT GVQCVECVAQANKRLPQQKTQFGGRLRAGAPIVTYTFIGLNVLVYVLQWVIPGLTNQLV FT LAPALAAYEPWRLITSAFAHSTSSLLHLAMNMYGVYIFGTMLEPRMGRLRFTWLYLLSA FT FGGSLGILLLSAPLSATLGASGALAGLFLATFVVFRSNKQALRSMGIILALNVALGFFV FT QSISWQGHLGGAILGILAACCIVLIPRSNPQRARIQILLLTALSVALLTGIYVSTEAVK FT WPLG" FT CDS complement(17061..17678) FT /transl_table=11 FT /gene="lysE" FT /locus_tag="AARI_00140" FT /product="L-lysine exporter" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="L-lysine exporter (LysE) family, L-lysine exporter FT (TC 2.A.75.1.1). Identified by match to protein family FT PF01810. In Corynebacterium glutamicum, LysE appears to FT catalyze unidirectional efflux of L-lysine (and other basic FT amino acids such as L-arginine). The physiological function FT of the exporter is to excrete excess l-Lysine as a result FT of natural flux imbalances" FT /db_xref="GOA:E1VRL0" FT /db_xref="InterPro:IPR001123" FT /db_xref="UniProtKB/TrEMBL:E1VRL0" FT /protein_id="CBT74263.1" FT /translation="MFFGSLVFGFTTGLSLIVAIGSQNAFVLRQGIRKEHVLITALVCS FT LSDAILITAGASGMGALVERAPLLLVFARVGGFIFLLSYAIFAFRRAVKPEALKVSAIQ FT GRTAKISVIGTVLALTWLNPHVYIDTVLLLGSIATSQAEGAAYFAVGAIVASFVWFFAL FT AYAARFLAPFFAKPKAWQVLDVLVGLLMILFATTLILPIITD" FT CDS 17749..18633 FT /transl_table=11 FT /gene="lysG" FT /locus_tag="AARI_00150" FT /product="lysine export transcriptional regulatory protein FT LysG" FT /function="3.5.2 Transcription regulation" FT /note="probable transcriptional regulator of lysE. FT Identified by similarity to protein SP: P94632 FT (Corynebacterium glutamicum)" FT /db_xref="GOA:E1VRL1" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR017685" FT /db_xref="UniProtKB/TrEMBL:E1VRL1" FT /protein_id="CBT74264.1" FT /translation="MNLDVEHLETLLAVVDAGSFDDASIDLGVTASAVSQRIKALENRL FT GAILLVRSRPVVPTDQGTRVLRYARQMSLLSAEFSAEVASEQPIAVAVGVNADSLSTWF FT APVFAELAKYEDLSCEFVRTDENRGLELLRTGRVSAVVTNAVDTIQGCTSHKLGTMRYR FT AAAKSAFAQRYVPTGTAAELVHAPMVVYDREDPLQYDMLKQVAGAEARPAAQVHYVPDS FT MQFVAAIEAGMGWGMVPEPQLLKASDLRVLDEQWFIDVPLYFQRWSVDSKILGCIGDIL FT VTAARDHGLHLLA" FT CDS 18716..19033 FT /transl_table=11 FT /gene="sugE" FT /locus_tag="AARI_00160" FT /product="quaternary ammonium compound-resistance protein FT SugE" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="drug/metabolite transporter (DMT) superfamily, small FT multidrug resistance (SMR) family, quaternary ammonium FT compound (cetylpyridinium, cetyldimethyl ethylammonium, FT hexadecyltrimethyl ammonium) efflux pump (TC 2.A.7.1.4). FT Confers resistance to cetylpyridinium, cetyldimethylethyl FT ammonium and cetrimide cations" FT /db_xref="GOA:E1VRL2" FT /db_xref="InterPro:IPR000390" FT /db_xref="UniProtKB/TrEMBL:E1VRL2" FT /protein_id="CBT74265.1" FT /translation="MYWIVLIVSGLFEAVWAIALGMSDGLSKLVPSIVFFVALAISMGG FT LAYAMKEIPVGTAYAIWVGVGASLAVIYSMVTGQEAFSILKMVFILGLVGCVIGLKAVS FT D" FT CDS complement(19094..19351) FT /transl_table=11 FT /locus_tag="AARI_00170" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR009619" FT /db_xref="UniProtKB/TrEMBL:E1VRL3" FT /protein_id="CBT74266.1" FT /translation="MPESKPRRKKNSQPQESRQSAHAIDKPMPGWYKPVMFGLMLLSLV FT WIIVYYVSQTLYPIPNIGGWNIVVGFGIAMVGFFMTTGWK" FT CDS 19574..20350 FT /transl_table=11 FT /locus_tag="AARI_00180" FT /product="putative sortase" FT /function="1.6 Protein secretion" FT /note="identified by match to protein family PF04203. FT Sortase is a transpeptidase that attaches surface proteins FT by the threonine of an LPXTG motif to the cell wall" FT /db_xref="InterPro:IPR005754" FT /db_xref="InterPro:IPR023365" FT /db_xref="UniProtKB/TrEMBL:E1VRL4" FT /protein_id="CBT74267.1" FT /translation="MNRSATAPGRRLQRRQTSAGSRVVGFFGELMITLGILLMLYVVWE FT LWWTNIDSAQAQKEVTANLVEELGEVVVPEKTEQEEVEKDYGPALVTEVSAGETFGIMY FT FPRFGANGSHHPVTYGVEDRVIDNLGIGYYPTTQQPGEMGNFAVAAHRQTHGQVFWDID FT KLQEGDKIYLQTSEGYYTYTWYATEIVAPSNGDVLLPTPHQWGVEPTKSILTMTTCHPK FT YSTQQRMIAYSELTDWRPLDAGPPKEIRDMVIEATS" FT CDS 20359..20529 FT /transl_table=11 FT /locus_tag="AARI_00190" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRL5" FT /protein_id="CBT74268.1" FT /translation="MYAWIFRNLPGPLWLRIFEALILIAAIVLLLMMYVFPWLNQYISP FT FTDSTIGQSTP" FT CDS 20526..21170 FT /transl_table=11 FT /gene="trpG" FT /locus_tag="AARI_00200" FT /product="anthranilate synthase component II" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.1.3.27" FT /note="anthranilate synthase is the first enzyme in the FT branch pathway in tryptophane biosynthesis. It catalyzes FT the biosynthesis of anthranilate from chorismate and FT glutamine" FT /db_xref="GOA:E1VRL6" FT /db_xref="InterPro:IPR006221" FT /db_xref="InterPro:IPR017926" FT /db_xref="UniProtKB/TrEMBL:E1VRL6" FT /protein_id="CBT74269.1" FT /translation="MSSTKILVIDNYDSFVYTLVGYLQEMGAETTVYRNDDLSVEDARA FT MAAEYDGVLISPGPGEPAGAGVSIDLIKWCGEQRKPMLGVCLGHQALAEAYGGTVTHAE FT ELMHGKTSLVNHENHPVFNQVANPFTATRYHSLAAVRESIPAELEIIAETAGGVIMGLA FT HREAPLWGLQYHPESVLTEQGYQMLGNWLEFVGLEGAAKKAAALSPLFSGE" FT CDS complement(21263..21787) FT /transl_table=11 FT /locus_tag="AARI_00210" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VRL7" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VRL7" FT /protein_id="CBT74270.1" FT /translation="MTSANIIVRQPAEGDASTLADIQISAWRAAYRGVMTEEYLDAMDS FT ERYAEGWARNIANPKPGTSHLVAESGSQVVGFCILGPATGDSDTAFGQLYAINVHPQWW FT DKGAGSALFTAAEEKLVALGYDRAFLWVEANNKRAIDFYTKRGWLDDGGTLQDTRFDPP FT VSERRHSRELK" FT CDS 22056..22346 FT /transl_table=11 FT /locus_tag="AARI_00220" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRL8" FT /protein_id="CBT74271.1" FT /translation="MRAIETVHAEPRDSDDSPCYRVNFWEQPLPGYGWNLDAFVLVEVK FT DVSEALRWVEEHANGRPFELFAEMDSEPEKPFGAPRKATLVRLLGNNPNAG" FT CDS complement(22423..22902) FT /transl_table=11 FT /locus_tag="AARI_00230" FT /product="NUDIX domain-containing protein" FT /function="4.6 Miscellaneous" FT /note="identified by match to PF00293. Members of the Nudix FT hydrolase superfamily catalyze the hydrolysis of nucleoside FT diphosphates linked to other moieties. Substrates of nudix FT hydrolases include intact and oxidatively damaged FT nucleoside triphosphates, dinucleoside polyphosphates, FT nucleotide-sugars and dinucleotide enzymes. These FT substrates are metabolites or cell signaling molecules that FT require regulation during different stages of the cell FT cycle or during periods of stress. In general, the role of FT the nudix hydrolase is to sanitize the nucleotide pools and FT to maintain cell viability, thereby serving as surveillance FT and house- cleaning enzymes" FT /db_xref="GOA:E1VRL9" FT /db_xref="InterPro:IPR000086" FT /db_xref="InterPro:IPR015797" FT /db_xref="InterPro:IPR020084" FT /db_xref="UniProtKB/TrEMBL:E1VRL9" FT /protein_id="CBT74272.1" FT /translation="MPVSDYVAGLRQLIGPRLLVLPGVTAVIRDDNAHYLLALHVAGNR FT WGLIGGAVEPLEGPRDALKREVREEIGADIEIHSVLDSYGGTNLLNKYPNGDLVSYVTT FT VYLCQLLGDASAVEADEISDIAWFSRDQIRALERFEWIDPVLDDAQRFFDDEDAR" FT CDS 23100..23429 FT /transl_table=11 FT /locus_tag="AARI_00240" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRM0" FT /protein_id="CBT74273.1" FT /translation="MVKLFGKGRRGDDIIFELAAIASCAVHPKFLDDSVVSTASVDDDY FT LDFSEHLNCFVDTVEERFAADGRLQASFVWSEWTRHMSGLPQEFVPLRIAQVHFQRLMD FT RLAKF" FT gene complement(23799..24188) FT /pseudo FT /locus_tag="AARI_00250" FT /product="Tn554-related transposase C segment" FT /function="4.5 Transposon and IS" FT /note="three proteins encoded by transposon Tn554 are FT required for its transposition, TnpA, B and C" FT gene complement(24175..24375) FT /pseudo FT /locus_tag="AARI_00260" FT /product="Tn554-related transposase B segment" FT /function="4.5 Transposon and IS" FT /note="C-terminal segment of a Tn554-related transposase B. FT Three proteins encoded by transposon Tn554 are required for FT its transposition, TnpA, B and C" FT gene complement(24481..24609) FT /pseudo FT /locus_tag="AARI_00270" FT /product="Tn554-related transposase B segment" FT /function="4.5 Transposon and IS" FT /note="segment of a Tn554-related transposase B. Three FT proteins encoded by transposon Tn554 are required for its FT transposition, TnpA, B and C" FT gene complement(24734..25663) FT /pseudo FT /locus_tag="AARI_00280" FT /product="Tn554-related transposase B segment" FT /function="4.5 Transposon and IS" FT /note="segment of a Tn554-related transposase B. Three FT proteins encoded by transposon Tn554 are required for its FT transposition, TnpA, B and C" FT gene complement(25660..27009) FT /pseudo FT /locus_tag="AARI_00290" FT /product="Tn554-related transposase A (pseudogene)" FT /function="4.5 Transposon and IS" FT /note="related to Tn554 transposase A. Three proteins FT encoded by transposon Tn554 are required for its FT transposition, TnpA, B and C" FT gene complement(27064..27363) FT /pseudo FT /locus_tag="AARI_00300" FT /product="truncated MerR-family transcriptional regulator" FT /note="C-terminal section of a MerR-family transcriptional FT regulator" FT gene complement(27360..27812) FT /pseudo FT /locus_tag="AARI_00310" FT /product="truncated MerR-family transcriptional regulator" FT /note="N-terminal section of a MerR-family transcriptional FT regulator" FT CDS complement(27827..28318) FT /transl_table=11 FT /locus_tag="AARI_00320" FT /product="putative glyoxalase family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00903: glyoxalase/bleomycin FT resistance protein/dioxygenase superfamily" FT /db_xref="UniProtKB/TrEMBL:E1VRM1" FT /protein_id="CBT74274.1" FT /translation="MTEKNGPDIDRSIYPMPMFINLVVSDLTAGEAFYASAGFVTLATI FT PGPGGVPSLVHLRREKYQDILMTQGTAARGTVSASFAAGQIDLDEVADSIRGAGGNVTG FT PIDTPWFTTDVTFSDPDGNTVTLTAPRMVDQTAAQAWVNDQITGDFEAPESVVPNPSEN FT " FT CDS complement(28611..30524) FT /transl_table=11 FT /locus_tag="AARI_00330" FT /product="putative serine/threonine protein kinase" FT /function="4.6 Miscellaneous" FT /EC_number="2.7.11.1" FT /note="identified by match to protein domain PD000001. FT Match to PS00108 pattern. Protein kinases are a group of FT enzymes that possess a catalytic subunit which transfers FT the gamma phosphate from nucleotide triphosphates (often FT ATP) to one or more amino acid residues in a protein FT substrate side chain, resulting in a conformational change FT affecting protein function. They play a role in a FT mulititude of cellular processes, including division, FT proliferation, apoptosis, and differentiation" FT /db_xref="GOA:E1VRM2" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR005543" FT /db_xref="InterPro:IPR008271" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR017441" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:E1VRM2" FT /protein_id="CBT74275.1" FT /translation="MSDNEALPPGLPRLINDRYEIESLIGRGGMADVYLATDEVLSRKV FT AVKVLRPDTASNPMVVNRFRREARAVAGLSHPNIVSVYDTGELPATDFHRDRLPFMVME FT YVTGHTLKQVIASGDIDAAFAVHVTRGVCDALDHSHHKNVVHRDIKPANVMVTDAGHVK FT LMDFGIARAVDTSATMTQTAAVVGTAQYFSPEQARGEQVDFRSDIYSVGCLFYELMTQE FT PPFTGDSPVSVAYQHVGEIPSTLSDVKDGVDPIFDPIVSKVLSKERDDRFQTAGAFAAA FT LEDALNGIEFHDEQSAPSTYTLPIYGTHSETETSFIAQSAPHTSQHPVFAEEEAHGSER FT RNKSNRGLIILLTIIALLAVGIASFLVIRSIQTEAEKRAPVAVPKVLEMTEDDARAALR FT DATFQVRVEHEFSDDVEQDKATRTEPEEGAMASKDSTVTLFISDGSEQRTIPKDLANQS FT ETAARDALREAGLEVGEVSRKNSATIPTDWVIGTTPELGSKVKAGSEVDLILSTGMVTV FT PVVTEMSRKEAEEKLGAEDIGLEAQFDEVVTADYAEGTLFKQSPAARDDVPQGSLVKIS FT VAKAPEPEPEPTEESSPPESESPDSEESDDSTDESSPSGEDSPPSSGNGPPDRPGPPRE FT NG" FT CDS complement(30521..32326) FT /transl_table=11 FT /locus_tag="AARI_00340" FT /product="putative serine/threonine protein kinase" FT /function="4.6 Miscellaneous" FT /EC_number="2.7.11.1" FT /note="identified by match to protein domain PD000001. FT Match to PS00108 pattern. Protein kinases are a group of FT enzymes that possess a catalytic subunit which transfers FT the gamma phosphate from nucleotide triphosphates (often FT ATP) to one or more amino acid residues in a protein FT substrate side chain, resulting in a conformational change FT affecting protein function. They play a role in a FT mulititude of cellular processes, including division, FT proliferation, apoptosis, and differentiation" FT /db_xref="GOA:E1VRM3" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR005543" FT /db_xref="InterPro:IPR008271" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:E1VRM3" FT /protein_id="CBT74276.1" FT /translation="MRPVTGTTLGGRYKLTDRIAIGGMGEVWKARDQVLGRLVAIKILK FT EEYTDNESFLTRFRVEARHTALLNHPGIAGVFDYGEEQGSAYLVMELVPGPPLSTIIER FT ERKLEVDRTLSLIAQTARALAAAHEHGLVHRDVKPGNILVMPSGVVKITDFGIARLADQ FT VPLTATGQVMGTAQYLAPEQATGQVATGSSDIYALGVIGYECLAGRRPFTGESQIAIAL FT AQVNDAPPALPDTIPAPVRQLIMSMLAKNPADRPKDATALAKAADALRSGDTNTATLAV FT PGMLATGISDDATQVVNMDNDSTQVVPRADSAPTMTNAMPTVVEPARAASGFSGSSAAE FT GFDDEDADAQDPAMEPASKRSPWLIPLIVIIALAAVIALLAWLIPAMSSDKDNEPTASV FT TQSSELSESPSPTEETTEPSEETTEASETSESSSPTPSETVTYVEVSASLVGQDIDTVT FT AELEGKGLVVDSTPQETSEYEPREVISLNPTGSVEEGETISITYAMAPETVAVPSVTGM FT SFEAAQKRIQDAGLAVAKGEERNDPSVAGTVLEQDIAAESEVEPGTTVTLDISAGPEEV FT EESESPSETATESPEAAKPEQSEAP" FT CDS complement(32323..33786) FT /transl_table=11 FT /locus_tag="AARI_00350" FT /product="penicillin-binding protein" FT /function="1.1 Cell wall" FT /note="match to PF00905. The large number of penicillin FT binding proteins, which are represented in this group of FT sequences, are responsible for the final stages of FT peptidoglycan biosynthesis for cell wall formation. The FT proteins synthesise cross-linked peptidoglycan from lipid FT intermediates, and contain a penicillin-sensitive FT transpeptidase carboxy-terminal domain" FT /db_xref="GOA:E1VRM4" FT /db_xref="InterPro:IPR001460" FT /db_xref="InterPro:IPR012338" FT /db_xref="UniProtKB/TrEMBL:E1VRM4" FT /protein_id="CBT74277.1" FT /translation="MNHAIKRVWVALTTLFIICLGGLSYIQFFDAESLSENALNKRQLF FT REFDLPRGAILVDGKPIAESVPTDDGQFEFQRVYNDPNTYAHLTGYYSLANGTTQLESK FT LNDWLTGTSSDLLFDRLSAMFTGTRSEGASVELTIDGQLQKTAFDAIRDDLKATIIVTN FT PKTGDILAMASKPSYNTNLLAVHSTAKAAENLKEISNIDGLSPYLNPAITNPVTPGSSF FT KIISTVAALESGKFDMETPIDNPVSKNYPHTNTPLNNFSEGICARDTRAKLEFIFAQSC FT NTPFIEISQTVGKDAFTEVAERFGYGQQLSIPQNVVPSEFPSAEASEAQMAQMAIGEWE FT NKATPLQMNMVAMAIANDGVIMKPNLIDKVIAPDLRVIEDPKPEKFSTATTPEVAEQLT FT ELMEGPVLHGTAMNARVPGVDFRAKTGTSERPSEPGGPRMVNSWMTGFAPADDPQVAIT FT VNIQDVDYDTGHNTVGALMKTMLEAVFNK" FT CDS complement(33783..35180) FT /transl_table=11 FT /gene="ftsW" FT /locus_tag="AARI_00360" FT /product="cell division protein FtsW" FT /function="1.7 Cell division" FT /note="plays a role in the stabilization of the FtsZ ring FT during cell division" FT /db_xref="GOA:E1VRM5" FT /db_xref="InterPro:IPR001182" FT /db_xref="UniProtKB/TrEMBL:E1VRM5" FT /protein_id="CBT74278.1" FT /translation="MTEVQTAPVPRRNLELLLVLLALCVGGAAFYLVGSSTDGVDNTDF FT YVQISILSALALTVHVLLRIFAKYADPAILPITVALNSLGLAMIHRIDLAKGTSQSARQ FT LLWTAIAIVIACVVLWAIKDHRILRRFTYIALLASVFLLLLPMIPNLGVTINGARIWIR FT IGIFSMQPGELAKITLSIFFAGYLSSNRDLILMAGRKFGPLQLPRLRDMAPMVIAWLLS FT IGVLVIQRDLGSAILFFGLFIVMIYVATARISWVLIGALMVVVGGIVAGLTMGHVTRRF FT DVWLNAFDPEIYQATGGSMQIVEGLFGMADGGLFGTGLGAGSPYRVPLANSDMIIASFG FT EEIGLIGLTAIVLLYMLLISRGLRAALGSADTFGKLLAAGLSFTLGLQCIVIIGGVARL FT IPLTGLATPFMAAGGSSLLANWIIISLLLLISHNSRRPKTGVVGPTDEFASAQTTFTNS FT TKVVTKK" FT CDS complement(35177..36571) FT /transl_table=11 FT /locus_tag="AARI_00370" FT /product="protein phosphatase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00481: protein phosphatase 2C" FT /db_xref="GOA:E1VRM6" FT /db_xref="InterPro:IPR001932" FT /db_xref="InterPro:IPR015655" FT /db_xref="UniProtKB/TrEMBL:E1VRM6" FT /protein_id="CBT74279.1" FT /translation="MALKLKFAAKSDVGRVRKKNDDSAYAGAYLAVLADGMGGHVGGDV FT ASASTVLDLVHLDHDGTADPQNALPDEIQAANLVLNELVGANPKLSGMGTTVTSLLLSG FT DTLHMAHIGDSRAYRLKHGVFEQISKDHTFVQRLVDEGRIKPAEAEVHPHKNVLLRVLG FT DSDASPELDVDQFQAEPGERWMLCSDGLTDAVPVPVIEQIIRSTPDMDEAVNDLVAITL FT KNGAPDNVTVVMFEVVQDSVIEGEEPAEQEPAPDTGQLTIAAEGDVEASASLLRHEISQ FT RPHLLVGAAQLATQTGQIPVVTQHTGERRAAALLTHRSPAAGEVLDPLDTPTQQRRWLM FT PILLTFTAFLVIALGVWGYMWTQTQYFVGTVDGKVAIYKGVPQELGPISLSEVATVSKV FT PLEALPEYSRHRVESTISAENQQHAQMIIQELLVTAKQNCPVTVPGATDSDASTNLPAY FT CQEIMQ" FT CDS complement(36575..37054) FT /transl_table=11 FT /locus_tag="AARI_00380" FT /product="FHA domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00498. The forkhead-associated (FHA) FT domain is a phosphopeptide recognition domain found in many FT regulatory proteins" FT /db_xref="InterPro:IPR000253" FT /db_xref="InterPro:IPR008984" FT /db_xref="UniProtKB/TrEMBL:E1VRM7" FT /protein_id="CBT74280.1" FT /translation="MNDLVLSLFRLGFLVLIWLLVLSVVGSMRRDLAIGSRARTGKPSA FT RELKKNPELAEPEVPARKAATTLEVVEGPLTGSSIPLRGQPILFGRAQDATVVLDDDYA FT SGRHARLFPQGSRWFIEDLGSTNGTFVGDSQLSRAQAVEPGQRIRIGKTVMELKS" FT CDS complement(37051..37866) FT /transl_table=11 FT /locus_tag="AARI_00390" FT /product="FHA domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00498. The forkhead-associated (FHA) FT domain is a phosphopeptide recognition domain found in many FT regulatory proteins" FT /db_xref="InterPro:IPR000253" FT /db_xref="InterPro:IPR008984" FT /db_xref="InterPro:IPR022128" FT /db_xref="UniProtKB/TrEMBL:E1VRM8" FT /protein_id="CBT74281.1" FT /translation="MGFLDNVERGLEKVVTSFFRGTSTADLKPVELTTAIRNEMDRGIM FT PISEGRSLAANDFVVSLSSKDYNTAQGWGRGVVNEMAKVTAEHAVAQDYSVRGDVMIHF FT VSKGDFKPGEMEIASSVKESSARPVASAPAKRPATTPAAPVAAPKTTAQPRPTVRPIAE FT IPNKPMQKQAILEVAGQRFALNHHSIVLGRSASTDIPVDDSGVSRQHVRVETRGKTSFV FT VTDLGSTNGTYVDGKKISEETRIFDGSIITIGQTKIVFRLITANNGGRA" FT tRNA 38148..38234 FT /locus_tag="AARI_36300" FT /product="transfer RNA-Leu" FT /anticodon=(pos:38182..38184,aa:Leu) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(38316..38771) FT /transl_table=11 FT /locus_tag="AARI_00400" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="InterPro:IPR007553" FT /db_xref="UniProtKB/TrEMBL:E1VRM9" FT /protein_id="CBT74282.1" FT /translation="MIHRRILVSSCLAGIPCRYDGKAKTDPEILESVEHNEAIALCAEE FT LGNLPTPRPPAEIVGGDGQAVLDGLGAVIDINGEDVSNQFIDGAQKVVAVIQREGITEA FT ILQDRSPSCGCGRIYDGTHYGKLVEGDGVLAALLKRRGVTVSGSSAL" FT CDS 38850..39386 FT /transl_table=11 FT /locus_tag="AARI_00410" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRN0" FT /protein_id="CBT74283.1" FT /translation="MAVSNEEIELRGTVDLVNERKILRLEQESSDKLPSRGQVAVELLS FT AHEGHTIVVDPDGRRGHWLALDNLGMPQLPAEAGEQVLLTARVAGTWPETKIPQDLAGA FT LDEADDLEQMWAGLTPMARWEWVRWVGATKNPSTRERRVEVSISKLRDGKRRPCCFDLS FT SCTDPEVDKGGKLIQ" FT CDS complement(39375..39536) FT /transl_table=11 FT /locus_tag="AARI_00420" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRN1" FT /protein_id="CBT74284.1" FT /translation="MRKWPAKVTAVIALLVALGLVVISSGALSLITGPEAPSGSEIESA FT VHRLPLLD" FT CDS complement(39546..40595) FT /transl_table=11 FT /locus_tag="AARI_00430" FT /product="LacI-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domain PF00356. Numerous bacterial FT transcription regulatory proteins bind DNA via a helix- FT turn-helix (HTH) motif. These proteins are very diverse, FT but for convenience may be grouped into subfamilies on the FT basis of sequence similarity. One such family groups FT together a range of proteins, including ascG, ccpA, cytR, FT ebgR, fruR, galR, galS, lacI, malI, opnR, purF, rafR, rbtR FT and scrR. Within this family, the HTH motif is situated FT towards the N-terminus" FT /db_xref="GOA:E1VRN2" FT /db_xref="InterPro:IPR000843" FT /db_xref="InterPro:IPR001761" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VRN2" FT /protein_id="CBT74285.1" FT /translation="MNNGENSGNSRAPRRVTAAMVAEHAGVSTATVSLVANGKSAGRVS FT AVNEQRVREAIRELGYFVDSIGSSLAKGVSSLVVLVAPDISNPFFAKVIAGVRSVLASD FT YQLLLSVTDAGVSPSAIETRKIMGLRPAGLLVHAPSQDFLEEISSNLPLVALDAPGIDP FT RIPAVNMDVAQGAREVVAHFAAQGHTKAAYLDASTGTETLAVRREAFLAAAADYGIKVL FT PSSVASSMIDVTAASAAFTQRWTQWRDSGVTALGCATDNHAFGVLHASRHLGISIPQQL FT AVAGFDDLPYSATSNPSITSVQLNAQEGGRQAALKLRALLDGKTPDPLQSMLPSSLIVR FT GSTLNNKGN" FT CDS 40746..41717 FT /transl_table=11 FT /gene="iunH" FT /locus_tag="AARI_00440" FT /product="putative inosine/uridine-preferring nucleoside FT hydrolase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.2.2.1" FT /note="catalyzes the hydrolysis of all of the commonly FT occuring purine and pyrimidine nucleosides into ribose and FT the associated base, but has a preference for inosine and FT uridine as substrates" FT /db_xref="GOA:E1VRN3" FT /db_xref="InterPro:IPR001910" FT /db_xref="InterPro:IPR015910" FT /db_xref="InterPro:IPR023186" FT /db_xref="UniProtKB/TrEMBL:E1VRN3" FT /protein_id="CBT74286.1" FT /translation="MTQDNTAPRKIILDCDPGHDDAVAMILAHGNPKIELLAVTTVAGN FT QTLDKVTTNALVVGTIAGITGIPFAAGCARPLVREVETAGDVHGDSGMDGPAQPESTIE FT LDERHAVDVIIDLVMSHEPGEITLVPTGALTNIALAVRKEPRIVERVREVVLMGGGYHT FT GNWSAVAEFNIKIDPEAAHIVFNEAWPVVMVGLDLTHQALATADVVQRIEQIGTGPSQF FT VRELMDFFAQAYRDHQGFDAPPVHDPCAVAYVIDPDIVRTVKAPVSVELRGELTLGMTV FT TDFRAPASADCNTSVAVDLDHEGFWNLVVDALERIGEVTAGK" FT CDS 41805..42503 FT /transl_table=11 FT /locus_tag="AARI_00450" FT /product="putative carboxymethylenebutenolidase" FT /function="4.2 Detoxification" FT /EC_number="3.1.1.45" FT /note="identified by match to PF01738: dienelactone FT hydrolase family. Carboxymethylenebutenolidases play a FT crucial role in chlorocatechol degradation via the modified FT ortho cleavage pathway" FT /db_xref="GOA:E1VRN4" FT /db_xref="InterPro:IPR002925" FT /db_xref="UniProtKB/TrEMBL:E1VRN4" FT /protein_id="CBT74287.1" FT /translation="MTDKTPHQNVTFPSSGPQAHGYLAVPESGKGPGVIVIQEWWGLAD FT HIRDVADRLAALGFVALAPDLYGGSITHDGEEAVQMMSQLPEAKGAQLLSGAVDYLLAS FT DHVTSEKLGTIGFCMGGGFVLQLAAQQGEKIAAAVPFYGVGQGVPNDFSGVRAAIQGHY FT ANFDQMYPPQQAKAQEEQIRQESGAEVQYFYYDADHAFHNDENPAGNYDSEQAAVAWQR FT AVDFLQAKVA" FT CDS 42559..42990 FT /transl_table=11 FT /locus_tag="AARI_00460" FT /product="universal stress family domain-containing FT protein" FT /function="4.1 Adaptation to atypical conditions" FT /note="identified by match to PF00582: universal stress FT protein family. The universal stress protein UspA is a FT small cytoplasmic bacterial protein whose expression is FT enhanced when the cell is exposed to stress agents. UspA FT enhances the rate of cell survival during prolonged FT exposure to such conditions, and may provide a general FT stress endurance activity" FT /db_xref="GOA:E1VRN5" FT /db_xref="InterPro:IPR006015" FT /db_xref="InterPro:IPR006016" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VRN5" FT /protein_id="CBT74288.1" FT /translation="MSETIIVGVDGSETAQRAARRAAELAVKLDADLVVITAHASDNTE FT VVSIGSDTWILDDAEQARKLAQRVANDVKNAVPGVKITAAAGRGKPGDVLISDAEDRKA FT SMIVVGNVGMKGLGRVLGSVASSIAHSAPCDVLVVKTDK" FT CDS 43078..43794 FT /transl_table=11 FT /locus_tag="AARI_00470" FT /product="possible lysR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="InterPro:IPR005119" FT /db_xref="UniProtKB/TrEMBL:E1VRN6" FT /protein_id="CBT74289.1" FT /translation="MQKLSIAYQTGVTPGKWIDRFVERYPAVDLKVWREDEGQILDLLA FT TGEADAVFVRYRGESPKDATRHVIPLYEELEVVCAGKDHDVEYFEESVPLETVESFPQL FT DLADYPLSTGGIPVAMEVVASGAQVLRTQQSIARLFARKDVVVRFIEDGSPTQVGIAWP FT SVAEDTTLLEEFIGIVRGRTASSSRQTSVRNQEQKAKRINEQKKAKAKAQAKAKQQDKS FT SSKRPQGAKAKPRKHR" FT CDS 43837..44625 FT /transl_table=11 FT /locus_tag="AARI_00480" FT /product="enoyl-CoA hydratase/isomerase family protein" FT /function="2.4 Metabolism of lipids" FT /note="match to protein family PF00378. This family FT contains a diverse set of enzymes including: Enoyl-CoA FT hydratase, Napthoate synthase, Carnitate racemase, 3- FT hydoxybutyryl-CoA dehydratase, Dodecanoyl-CoA delta- FT isomerase" FT /db_xref="GOA:E1VRN7" FT /db_xref="InterPro:IPR001753" FT /db_xref="InterPro:IPR014748" FT /db_xref="InterPro:IPR018376" FT /db_xref="UniProtKB/TrEMBL:E1VRN7" FT /protein_id="CBT74290.1" FT /translation="MKQFDTLSLSTQGSALIVTVNQPKSLNALAKEVVNDLEAFLDWFQ FT GTGFAYRGVILTGAGEKSFVAGANIVQLREMDPEAALAYGRQMHAVTERLEKLQVPVIA FT AVNGFALGGGCELALACDFIYASESASFGQPEVNLGLVPGFGGMVRLPRRVGNAMAREL FT IFTGRRIKAAEALRIGLANRVVPAGELIDQAVAAIEEVAKVAPTAVANAKNALMDMDGL FT NTHDALLVEADSFQQAFKTADSVEGRAAFVEKRAPQFPGN" FT CDS 44640..45305 FT /transl_table=11 FT /locus_tag="AARI_00490" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRN8" FT /protein_id="CBT74291.1" FT /translation="MHYGARQDQYLQFYEPQHITAAGAVMIIHGGYWREKYTAELGVPL FT AEDLAARGIPAYNLEYRRGPGSAAQMLADARLALGLIKEEGPITLIGHSAGAQLACVLA FT AHDERVSQVISQAGVLDLESAQHLKLSDGAVDQMLAGASLSAYSPVELWPMRARVVIFH FT GRDDADVPLRIARSAAQKAAALGQEHSFALFAGDHYTWIDPRSSQWAACVRALSPLHY" FT CDS 45315..46214 FT /transl_table=11 FT /locus_tag="AARI_00500" FT /product="putative fructokinase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="2.7.1.4" FT /note="fructokinase catalyzes the conversion of fructose to FT fructose-6-phosphate, which is an entry point into FT glycolysis via conversion into glucose-6-phosphate" FT /db_xref="GOA:E1VRN9" FT /db_xref="InterPro:IPR002173" FT /db_xref="InterPro:IPR011611" FT /db_xref="UniProtKB/TrEMBL:E1VRN9" FT /protein_id="CBT74292.1" FT /translation="MNPTVIGEALVDVLASGIAPAQEFVGGSPLNVAVALSRLGYPGTL FT ISRWGADDKGRKIEEYLKDNNVAYLGGADDEATVIAHGILDPAGGAAFAFNAYWQMPTI FT GPELAQDAELVHTGSIATLFSPEELLPLLSAARTHATISYDPNLRPSLVTNHAQTVAEV FT ERFVGQADVVRVSGIDLKWLYPMRSVRDSARAWLDMGPAIVVSTAGSQGSWGVVRAGDA FT EFTSPSVEVTDTVGAGDTFTAALLCWLAEHQMIGAGNREKLNQLKISELSQALEFAAMA FT AAVTVQRAGANPPHREEL" FT CDS 46215..47009 FT /transl_table=11 FT /locus_tag="AARI_00510" FT /product="haloacid dehalogenase-like hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF08282: haloacid FT dehalogenase-like hydrolase. The Haloacid Dehydrogenase FT (HAD) superfamily includes phosphatases, phosphonatases, P- FT type ATPases, beta-phosphoglucomutases, FT phosphomannomutases, and dehalogenases, which are involved FT in a variety of cellular processes ranging from amino acid FT biosynthesis to detoxification" FT /db_xref="GOA:E1VRP0" FT /db_xref="InterPro:IPR000150" FT /db_xref="InterPro:IPR006379" FT /db_xref="InterPro:IPR013200" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:E1VRP0" FT /protein_id="CBT74293.1" FT /translation="MIKLIASDLDGTIVSQNGTISERTKRAFIEARDSGIQIVFVTGRP FT FRWLTPVIESFGGLGKVICSNGAVLYDLEQDEVIWSRTLSAATARRATEIILELEPQAS FT FAAETTKGLHLGDGFADRHHKSGVQAVLDLASDSIDSEGIVKFLARSNTMPIDQFYASV FT QPQLADLVEVTHSAFDVSLLEMSRVDIHKATTLHEYCQRLGITADEVMAFGDMPNDIEM FT LEYAGHGYAMASGHPAALASARFRAPALAEDGVAQIIEKLLK" FT CDS 47006..47737 FT /transl_table=11 FT /gene="glpQ" FT /locus_tag="AARI_00520" FT /product="putative glycerophosphodiester phosphodiesterase" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.4.46" FT /note="glycerophosphoryl diester phosphodiesterases display FT broad specificity for glycerophosphodiesters; FT glycerophosphocholine, glycerophosphoethanolamine, FT glycerophosphoglycerol, and bis(glycerophosphoglycerol)" FT /db_xref="GOA:E1VRP1" FT /db_xref="InterPro:IPR004129" FT /db_xref="InterPro:IPR017946" FT /db_xref="UniProtKB/TrEMBL:E1VRP1" FT /protein_id="CBT74294.1" FT /translation="MTYAFSHRGVRTWNEENTLIAFQRAVDLGITHLESDVHASADGTV FT YLFHDETLDRVTDASGNFNDCTDEQLAQIRAGGQPLCTLDALLDAFPQATLNLDVKDEQ FT VIGPLAALIERRKAHGAIALAAFSTARSAAVSHLLSAPIRRSPGQRELVLIWLCAHLLG FT WVPKRMLASYWAVQVPLKQGPLPVATRRFIKAVHRAGAQVHVWVIDDEPTMRLLMDRKA FT DAIMSDDAALLVQVLGSPAAG" FT CDS complement(47734..48711) FT /transl_table=11 FT /locus_tag="AARI_00530" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRP2" FT /protein_id="CBT74295.1" FT /translation="MAQWIDVWNSDDWREATAEWIDAACEAYGIQRTAGPDFWPANLHQ FT IQAVVQTDAADLIFSANAPGLTSEAATTVTAGTLLPDRVVMPVAIDRMAGYMLSPDYGH FT TLADLGDTVENWELAMASLGSFQVALMGREEEFFDSGVTVVDPQFLPEQYEQALTMHVS FT LDSAHPLHVDGSSADKMASHIDTLKKAAATLHSGPVPLSLEHGNFDLSQVVVPAEPDDH FT GRILNLASAHWAHPFSSLNTPLAAMCEAWGCQTSDERVMKVLFAYLDQFAAYGSPDELY FT DLINPACLVAPLSQHETWLRLLLDVSDERLQENAPTVLDTLDLS" FT CDS 48804..51986 FT /transl_table=11 FT /locus_tag="AARI_00540" FT /product="glycosyl hydrolase, family 65" FT /function="2.1.4 Substrate-specific entries to carbohydrate FT metabolic pathway" FT /note="match to PF03632, PF03633 and PF03636. This family FT includes a maltose phosphorylase (EC 2.4.1.8), which FT catalyzes the conversion of maltose and inorganic phosphate FT into beta-D-glucose-1-phosphate and glucose" FT /db_xref="GOA:E1VRP3" FT /db_xref="InterPro:IPR005194" FT /db_xref="InterPro:IPR005195" FT /db_xref="InterPro:IPR005196" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006402" FT /db_xref="InterPro:IPR008928" FT /db_xref="InterPro:IPR010976" FT /db_xref="InterPro:IPR011013" FT /db_xref="InterPro:IPR012341" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:E1VRP3" FT /protein_id="CBT74296.1" FT /translation="MNAFRPEYRHRDYKAVLFDLDGVITPTALLHRKAWEELFTAYFSE FT HPGVSAYTSEDYYNLLDGRPRYEAVAAILASRGISLPRGSESDPAGTNSICALGNMKND FT KFTQVLHRDGIDPYAGSLAYLQQVLGAGLNVAVVSSSRNARTVLKAAGLEEHFPLVIGG FT QEAAARGLAGKPAPDTFLAAAADLGWRPEECVVIEDATSGVAAARAGGFGVVGVAREDN FT AAALLEAGADFVVEDLSELVSEQAVKAWEEDPWSIARTGHRESSGAEDTVFSLGNGFLG FT SRAAQLGLGDQSGGTFINGLHEVWQIRHAESAFGLAETGQTMISAPDFRTLRVFINDEA FT LEVGRTEMLRDDLRLDFLDGTLNAHTLWRTAEGHRIEVKSRSMISFTDRHLAVQDIHVR FT LLDAPAQVLIQSSVIGYRSTRTVASPEETDAGGPVDPRKSEEASANPLNPAGTFAEDAR FT LGISYEVSGSGMSVAAMVEHQVAITGGAQADLSISRKAADERADEVISTRLGAGQGVRV FT SKFVVYHSSRRHPAQEMLLRSERVLKHLVPLGIDEHFRTQRRFLADYWERSDVQVDCDD FT PALQRKIRWNLFQLAQAAGRADGLGISAKGVSGNGYSGHYFWDTEIYVMPFLTYTNQQW FT ARNTLRARVSMLPASTRRARTMNEAGLLFPWRTINGEEASAYYPAGTAQYHINADVVYS FT LNRYLSVMEDDEFLLAGGAEILVGTARMWASLGFWRGEPGDERFHIHGVTGPDEYTAVV FT NDNLYTNVMARFNLRRSAQLLTEMAQERPRDYALLADKYALEEEEILLWLKAAHCMHIP FT YSESVGIHPQDEHFLNREVWDLENTAADKRPLLLHYHPLVIYRFQVIKQADAVLALWLR FT SSDFTAEQKLADFNYYDPLTTGDSTLSATVQSILAAEVGYRDLALEYFEHALNVDLDNL FT HGNTADGVHVASTGGVWSALIYGFAGLRDDDDRLCFDPRLPEKWRSLSFSLGWRGMRIA FT VELRARSIEFTLQGDFSRPIWVRGEQIDLQPGQALVVPLPDQGPALEGRPSLDHVLSLQ FT RVAGVEVPKKAW" FT CDS complement(52080..53486) FT /transl_table=11 FT /locus_tag="AARI_00550" FT /product="putative MFS superfamily sugar transporter" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="major facilitator superfamily, sugar porter family FT (TC 2.A.1.1.z)" FT /db_xref="GOA:E1VRP4" FT /db_xref="InterPro:IPR003663" FT /db_xref="InterPro:IPR005828" FT /db_xref="InterPro:IPR005829" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VRP4" FT /protein_id="CBT74297.1" FT /translation="MTATTSDGKLSARLIFIALGAALGGFVFGYDSSIVNGTVDAVEHE FT FGLNAVTIGFTVSCALLGAAVGAWVAGVVSERVGRVRTMLIASMLLLISALGCGLCFGV FT ADLILWRIVGGIGVGFASVIAPAYIAEVSPAAHRGRLGTMQQMAIVLGIFVAFLVSALL FT VFVMGSADAIGLFGLAAWRWMYLSLIVPAVVYGLLVLRLPESPRYLVERGRYVEAATVL FT TRDIGMQAGTETEAKIEEIRATVHIERRQVLKDLLGRFGFHPLVWTGILLSVFQQFVGI FT NVIFYYSTTLWKSVGFAESDSFTISLITSITNVVATIVAVLLIDVIGRKLLLTIGSAIM FT TVSLGMMAVAFAQSVTTNGAVELPGSWGIVALVAANLFVVGFGATWGPAVWVLLGEMFP FT NSIRALALGVAAAAQWIANFIVSTSFPALAEAGLALAYGIYAFFALLSLVFVIFLVKET FT KGRKLEEMTL" FT CDS complement(53700..54983) FT /transl_table=11 FT /locus_tag="AARI_00560" FT /product="putative uracil/xanthine permease" FT /function="1.2.6 Transport/binding of nucleosides, FT nucleotides, purines and pyrimidines" FT /note="nucleobase:cation symporter-2 (NCS2) Family (TC 2.A. FT 40.y.z). Identified by match to protein family PF00860" FT /db_xref="GOA:E1VRP5" FT /db_xref="InterPro:IPR006043" FT /db_xref="UniProtKB/TrEMBL:E1VRP5" FT /protein_id="CBT74298.1" FT /translation="MSWSIHGNGRTITPGEVVAPDERLHWPQTVSIGAQHILAMFGASI FT LVPTITGFPVTTTLLFTGLATVIFLLMTRNKVPSYLGSSFAMIAPVLSTTQSHSMSGAL FT GGIVMTGALLFVVGLIVQKTGTGWIHALMPPVVMGTIVALIGLNLASATLVPMTEFPLT FT TFLTVIFTVVATVAFKGLLGRLSILMGLLCGYLVALAQGQVSFKAVAAAEWIGLPEFHT FT PTFHFDTALMFLPAVFVLIAENIGHVRTVGVMTNRDLSKFNGRALMADGAASVLAGFGG FT GSATTTYAENIGVMAASRVYSTAAYWVAAIVAMALAFLPKFGALIGTIPVGVIGGLGIV FT LYGMIGIVGARLWIEAKVDFGNPINLMTAGTGLIIAIAVTKEIAFGQFQLGGIALGSIA FT TLVVFHVMSLVAKARGNDLADSQKPAKQ" FT CDS complement(55011..56435) FT /transl_table=11 FT /gene="thiD" FT /locus_tag="AARI_00570" FT /product="phosphomethylpyrimidine kinase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.4.7" FT /note="involved in thiamin biosynthesis. Catalyzes the FT phosphorylation of HMP-P to HMP-PP" FT /db_xref="GOA:E1VRP6" FT /db_xref="InterPro:IPR004305" FT /db_xref="InterPro:IPR004399" FT /db_xref="InterPro:IPR013749" FT /db_xref="InterPro:IPR016084" FT /db_xref="UniProtKB/TrEMBL:E1VRP6" FT /protein_id="CBT74299.1" FT /translation="MNILSIAGSDPSGGAGIQADLKAIAANGGYGMCVITALTAQNTHG FT VSGVQAISGDFVLTQLEAVSTDIRIDAIKIGMLANAEVIRAVTSWLETVDAPVVLDPVM FT VATSGDRLLDDESALDSLLDRATVITPNLLELASLLREPVAPSWDEALRQAQRLAAKHD FT TLVLAKGGHLAGADCPDALVSAGGVQLELHGARHATRNTHGTGCTLSSTLATRFAATGD FT WIAALEQSKSYLSKAIAAADQLQVGSGHGPVNHFIDFFGTADPMGDWWQKIQPIREEID FT QLDFITRLSEGTLDREDFHYYIAQDALYLLRYAKVLSLASSMAPDLGAQRFWSRGANGI FT LDGELQLHGSYLDEFADTPSAITLNYTNHLAASQESYGELIAAILPCYWLYQDIGKRLA FT AANHAEHPYRQWLETYASEEFDSATEQAIEMVRQAFEQADPQLRARMEAAFIRSAEHER FT SFFAQAHENRVDFSTA" FT CDS complement(56432..57073) FT /transl_table=11 FT /gene="thiE" FT /locus_tag="AARI_00580" FT /product="thiamine-phosphate diphosphorylase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.5.1.3" FT /note="catalyses the following reaction: 2-methyl-4-amino- FT 5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2- FT phosphono-oxyethyl)thiazole <=> diphosphate + thiamine FT phosphate" FT /db_xref="GOA:E1VRP7" FT /db_xref="InterPro:IPR003733" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR022998" FT /db_xref="UniProtKB/TrEMBL:E1VRP7" FT /protein_id="CBT74300.1" FT /translation="MHNYGAYLVANTASCTPRSTLEVIEGAVAGGIGWIQLRAKDESAR FT EFFELACAAAKLTEGKAQLLINDRIDVYLAARAAGAAVNGIHIGQKDVPVQLARQIIGE FT GIIGLSASSDEQLAQANKVASVIDYLGVGAIRATPTKKDHPAPLGLDGFARAAALAKLP FT CVAIGAITQDDAAAIRAGGGAGLAVVRAICNAEDPQLASAQLVAAWEASK" FT CDS complement(57066..57860) FT /transl_table=11 FT /gene="thiM" FT /locus_tag="AARI_00590" FT /product="hydroxyethylthiazole kinase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.1.50" FT /note="catalyses the following reaction : ATP + 4-methyl-5- FT (2-hydroxyethyl)thiazole <=> ADP + 4-methyl-5-(2- FT phosphonooxyethyl)thiazole" FT /db_xref="GOA:E1VRP8" FT /db_xref="InterPro:IPR000417" FT /db_xref="UniProtKB/TrEMBL:E1VRP8" FT /protein_id="CBT74301.1" FT /translation="MALHAVAQKYRQQSPLVFCLTNTVVSNFTANVLLASGASPAMTDL FT PGEAGPFAQAASAVLVNLGTPSTEQLTAMEEAVQSASAAGTPWVLDPVAVGALPVRTEF FT ARRIVRQRPTLIRGNASEILALAGRQSASRGVDALDEVSAALAAGRELATEHDCVVAIS FT GQADAIIDATRTVLVHTNGIGLTRMTGGGCALGAVCAGMVAVHDDPFEATIAAHGFYGL FT AAEKALAGSSGPGSFAVAFLDALSAADPGELKTLKYEELNHA" FT CDS complement(57979..58347) FT /transl_table=11 FT /locus_tag="AARI_00600" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="GOA:E1VRP9" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VRP9" FT /protein_id="CBT74302.1" FT /translation="MSTQISVDLQAATPPYEQIRSQIASLISLGDLPSGSKLPTVRALA FT TDLGVAAGTVARAYKELEAEELITSRRRAGTVVNERPQTVDTREDLLAAVDRLWALAAA FT QKVDAATLKALVARRERK" FT CDS complement(58344..59882) FT /transl_table=11 FT /locus_tag="AARI_00610" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="12 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VRQ1" FT /protein_id="CBT74303.1" FT /translation="MISMNQFSASAISIAFVAAIICVWLRSVAHRRGTPAIDRARSHSF FT WCALIAFFASTSWDLSETWRVSMTEPNSGSALAEALTPGIWVLLVYLIGLFTWPKELQP FT VRTASLEARSLTTPFPKALGAFVGLLLLIAVGSLWPASKVEGLVGVPASEFTTFDFDGI FT YSYTSEGPYDGRLPGTQMLPVFIVALAGIIVAAAVITVVILKRPALAGISAEDNQALRT FT VWLNRLMRNIGIVLLAFTVSVVNYSQANSPDGQYEFVSYGALAVALTLLFWGPRSTFSA FT QSTTRERTAFSRLRDQLFTLQYVTAALTLLSVAIGWSFLPLDDELQMPTNERTTWILMI FT FAGAALSYAVLNALYLSYVSTVARQASAAPKYHAPLPLWSYIAAGLLFATSTYFLLDPP FT LDYLWGFVPPGKTMVAGLILLLLATHLGFVWFSRRAIIPWAVSSAEEIWYRKVLELRSM FT RVNTSAVVAMLLIGYGFPAGLGLFALLIFVVPAVIFLERPGSAFVREHQPAATS" FT CDS 59963..61396 FT /transl_table=11 FT /locus_tag="AARI_00620" FT /product="aldehyde dehydrogenase family protein" FT /function="2 Intermediary metabolism" FT /EC_number="1.2.1.-" FT /note="identified by match to protein family PF00171" FT /db_xref="GOA:E1VRQ0" FT /db_xref="InterPro:IPR012394" 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:E1VRQ0" FT /protein_id="CBT74304.1" FT /translation="MGLFTSTPLPEPVGDSAPPVDEHPSRIATVLSHLRRSADTRITHP FT RRFRRQQLKALEKMLEEHLEDFVQALAEDLGKSATEAKFSEIDVVRAEIDFAQRHLVEW FT MDSTSVKVPLALQPAMAKVEPRPLGVMLIIGAWNYPVQLVLAPLVAAIAAGNAAVIKPS FT ELAPATSGALAKFLPVYLDERVYAVVEGGVDTSTELLAARWDHIFYTGGERVAKIVAAA FT AAKHLTPTTLELGGKSPAVVENDSLASAKRLAYAKFMNAGQTCVAPDYVLSVGDSSELI FT RRLGQAITSFYGKEPLTHPDFGRIVSRKHFERLLSMFEQGEVVFGGEYDEDTLRIAPSI FT MRNVDLEGSLMTEEIFGPILPVIEVETFEEALEFIARRPSPLAAYLMSESPRLQSIFSD FT RVRAGSIVHNAPLAQMIVPTLPFGGVGPSGMGAYHGKHGFDRLSQMRSELNKTTVVDTL FT SAIYPPYSWAKRKIIDRLL" FT CDS 61476..62924 FT /transl_table=11 FT /gene="lysP" FT /locus_tag="AARI_00630" FT /product="lysine-specific permease" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="amino acid-polyamine-organocation (APC) superfamily, FT amino acid transporter (AAT) family, lysine:H+ symporter FT (TC 2.A.3.1.2). Identified by similarity to protein FT SP:P25737 (Escherichia coli)" FT /db_xref="GOA:E1VRQ2" FT /db_xref="InterPro:IPR002293" FT /db_xref="InterPro:IPR004840" FT /db_xref="InterPro:IPR004841" FT /db_xref="UniProtKB/TrEMBL:E1VRQ2" FT /protein_id="CBT74305.1" FT /translation="MTEPAPSQDGLKRGLKARHMQMIAIGGSIGTGLFVASGGTIAQAG FT PGGSLVAYALIGMMVLLLMQSLGEMSARLPVAGSFQTYASVFVNRHFGFAIGWNYWFNW FT AITVAAELVAAGIIMSYWFPDTPGWIWAGLFLILLTGLNALSAKAFGEGEYWLAAIKVI FT TVVVFLICGVAMIFGILGDSTPGFSNWTDGEAPFVGGWLSIVSVFMIAGFSFQGTELIG FT VAAGEAENPKRDIPRAIKAIFWRIMLFYIGAIFVIGMLIPYLDPSLLSSEASDITTSPF FT TLVFERAGVAFAAALMNAVILSAILSAGNSGLYASSRMLYSMALDGKAPKIFARLNKRG FT VPMPAMLLTASVGLFGFLTAIVGQGSAYTWLLNVSGLSGFIAWIGIAVCHYKFRKAYIA FT SGQDLANLPYKAPLFPLGPVLAFVILIVVIIGQNYQAIVDGNLLQMASSYIGLPIFLLL FT WLGHWLATRKQPAVAIDPWTAKLN" FT CDS complement(62921..64519) FT /transl_table=11 FT /gene="pgm" FT /locus_tag="AARI_00640" FT /product="phosphoglucomutase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="5.4.2.2" FT /note="catalyzes the interconversion of alpha-D-glucose 1- FT phosphate to alpha-D-glucose 6-phosphate" FT /db_xref="GOA:E1VRQ3" FT /db_xref="InterPro:IPR005843" FT /db_xref="InterPro:IPR005844" FT /db_xref="InterPro:IPR005845" FT /db_xref="InterPro:IPR005846" FT /db_xref="InterPro:IPR005852" FT /db_xref="InterPro:IPR016055" FT /db_xref="InterPro:IPR016066" FT /db_xref="UniProtKB/TrEMBL:E1VRQ3" FT /protein_id="CBT74306.1" FT /translation="MAHLRAGEPATVSDLINLQEVLDAYSSITPSASNPGQAVIFGTSG FT HRGSSLNGTFNEAHIAAITQAVVDYRNGAGITGPMYVGKDSHALSEPAYRTALEVLAGN FT GVTVLAEDGLTPTPAVSHAILVHNAEGGEQADGLIITPSHNPPADGGIKYNPPHGGPAE FT SEITGPIAARANELLANGQIKRGEPSARPFDFRELYITDLAAVIDFKAIAASGISIGAD FT PLGGASVHYWGEIGRRYGLNLEVVNESVDPRFGFMTLDKDGKIRMDCSSAHAMASLVAN FT REKYDIATGNDADADRHGIVTPDAGLMNPNHFLAVAIDYLLTHREHWPADAQLGKTLVS FT SVLIDKVVASHGRTLREVPVGFKYFVEPLSSGMVAFCGEESAGASFLDFSGKAFSTDKD FT GLMLALLASEIRAVTGKSPSQLHAQLVQRHGASFYDRFDAPADREQKALLSKLDASMVA FT ATELAGDTITAKVTEAAGFAIGGLKVSSEHAWFAARPSGTEDIYKIYAESTKSPEHLQQ FT VLAEARVIVDAALAG" FT gene 64576..64914 FT /pseudo FT /locus_tag="AARI_00650" FT /product="truncated protein" FT /note="C-terminal section of an uncharacterized protein" FT CDS complement(64978..66435) FT /transl_table=11 FT /locus_tag="AARI_00660" FT /product="dipeptide/tripeptide permease" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="proton-dependent oligopeptide transporter (POT) FT family (TC 2.A.17), di- or tripeptide:H+ symporter (TC 2.A. FT 17.1.1). Identified by match to protein family PF00854" FT /db_xref="GOA:E1VRQ4" FT /db_xref="InterPro:IPR000109" FT /db_xref="InterPro:IPR005279" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR018456" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VRQ4" FT /protein_id="CBT74307.1" FT /translation="MSTATTSTQASGKTFFGHPGALASLFSVEMWERFSFYGMQGLLAY FT YMYYSVTDGGLGMDQALALSLVGAYGGAVYLSTILGAWLSDRLYGSERVLFFSAIAIMI FT GHIGLALLPGYTGLVIGLIFVAVGSGGLKANAVALVGSLYSKDDPRIDAGFSLFYMGVN FT IGGLLGPLLTGWLQVAYGFHIGFAAAAVGMGIGLGIYAVGRKNLPESGRIPSNPLPAAE FT RKRYVVIFAAVIVLIVAAFVSKIVTPENLASTIAYVVIAASIIYFALILRSKKVDATER FT KQVWAFIPFYIGSAAFWALFQQQFTFIAAYSDQRLDRHLGSWEMPPSWVTSINPVFIII FT FAGIFAALWTKLGKRQPRTSMKFGLALVVVGAAFLLFIPLESFVKTPLLALVGILLLCT FT FAELLLSPVGQAIATKLAPASFGTQMIALFFLSVSLGTTLSGVLAGYYTEGNEIPYFIA FT MGGTAVVLGVAMMAATPALKKLMGPIL" FT CDS complement(66488..67834) FT /transl_table=11 FT /locus_tag="AARI_00670" FT /product="putative amidase" FT /function="4.6 Miscellaneous" FT /EC_number="3.5.1.-" FT /db_xref="GOA:E1VRQ5" FT /db_xref="InterPro:IPR000120" FT /db_xref="InterPro:IPR020556" FT /db_xref="InterPro:IPR023631" FT /db_xref="UniProtKB/TrEMBL:E1VRQ5" FT /protein_id="CBT74308.1" FT /translation="MFPSSTLKLRDELARGERSSREVTEHCLARIEEQADLGAFVHVAE FT NAMEAAAAADAAHARGEIGRLHGLPTAFKDLNEVAGMPTTYGTAAMPTTVAERDHSLVA FT RLRSEGVVILGKTQVPEFGLSSYSENLVAAPSRNPLDPTRSSGGSSGGQAAAIAAGMIP FT LGPGSDGGGSVRIPAAACGLVGLKPSLGRIPSDVLDGYNDPMGAPKLAVSGPLAHDALD FT AALLLDAMRGKDHYLPLLQGSYPERLSDLKIGYSTHSPFEPVYEISLAPEARDAFTQGL FT ERLGQRHRVEPADLHYAEDYPETFAAVWTNGLKHVPVSDDSLLGELARDFRGRAADRSL FT EQSLQAGSRLKQIAADFVRQWSAFDVVATPAMASIPPSIGHYTQSTADVDYMLQCQYAP FT YTSMVNVASVAAITIPVGHSKEGLPMSIQLISPRSDEGLLLALAAQIQL" FT CDS 67902..68228 FT /transl_table=11 FT /locus_tag="AARI_00680" FT /product="rhodanese domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein domain PF00581. FT Rhodanese has an internal duplication. This HMM represents FT a single copy of this duplicated domain. The domain is FT found as a single copy in other proteins, including FT phosphatases and ubiquitin C-terminal hydrolases" FT /db_xref="InterPro:IPR001763" FT /db_xref="UniProtKB/TrEMBL:E1VRQ6" FT /protein_id="CBT74309.1" FT /translation="MSDFETVSVNDVPKDAFILDVREDFEWEAGRAAGATHVVLGTLPE FT RVGELDPDVDTYVICRTGGRSAQAAAWLTGMGYTAFNIAGGSDAWLEAGLPMEAENGQE FT PTVR" FT CDS 68225..69148 FT /transl_table=11 FT /locus_tag="AARI_00690" FT /product="prephenate dehydratase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.1.51" FT /note="catalyzes the decarboxylation of prephenate into FT phenylpyruvate. Involved in phenylalanine biosynthesis" FT /db_xref="GOA:E1VRQ7" FT /db_xref="InterPro:IPR001086" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR018528" FT /db_xref="UniProtKB/TrEMBL:E1VRQ7" FT /protein_id="CBT74310.1" FT /translation="MSYAYLGPAGTFTESALLQVPGAADAQRIPASSVNVALSMVREGS FT VEAAMVPIENSVEGGVSATLDAIAQGEALQIVAEILVPISFVLAVRPGIDSLEQIKRIS FT THGHAWAQCRLWAEANIPQAAFTPASSTAAGALALEEAEPPHDAAICSPLVAQERGLKV FT LARGVEDNQGAVTRFILVTRPGKIPAPTKVDKSTLILPLPEDRPGALMEILEQFTARGV FT NLSRIESRPTGQGLGQYFFSVDFEGHVADERVAAALSGLHRLSPELRFLGSYPAAEGVE FT PFVDAHNSDAAFSEARDWVKSLRERL" FT CDS complement(69219..70265) FT /transl_table=11 FT /locus_tag="AARI_00700" FT /product="conserved hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.999) with cleavage site probability 0.916 FT between position 19 and 20" FT /db_xref="GOA:E1VRQ8" FT /db_xref="InterPro:IPR001206" FT /db_xref="InterPro:IPR005218" FT /db_xref="InterPro:IPR017438" FT /db_xref="UniProtKB/TrEMBL:E1VRQ8" FT /protein_id="CBT74311.1" FT /translation="MQTNRVIVFSAVAAAAAAAATSWYSVRKLSHYSKPLVKQPEAAEQ FT AVATKVAIVINPSKSGAEEAKEAVERVCAEAGLEAPLIIETTKENAGQDAAREALDAQC FT DTILAAGGDGTIRAVAEVLEGTDASLGILPLGTGNLLARNVDIPLDDLHTAALVAVRGM FT VRRIDVGHMKLKLLDGEQADHAFLVIAGVGTDADLFDDTNEELKSKVGWLAYSEAGLRQ FT LPGQRKKVSFKLADDENWQTRKVRSVLFANCGKLQGLDFVPDAKIDDGVLDAVILSPRS FT AAGWTWILLKTAFRAKNKIPVMSFYQTAGVSLRCDEPMNTQIDGDPTGQVNELQVSVNP FT SALRLRTP" FT CDS 70304..71581 FT /transl_table=11 FT /gene="serS" FT /locus_tag="AARI_00710" FT /product="serine--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.11" FT /note="activates serine and transfers it to tRNA(Ser) as FT the first step in protein biosynthesis" FT /db_xref="GOA:E1VRQ9" 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/TrEMBL:E1VRQ9" FT /protein_id="CBT74312.1" FT /translation="MIDLKMLTENPDMYRASQRARGADESLIDQLLAADTARRETIATY FT ERLRAEQNAFSKKVGKAKGDERAALLAEVKELAASVKSAQAESDAAAAKCTALQRSIPN FT LIIDGIPAGGEDDFTVVKHVGTVRDFKAEGFEPLDHLQLAEKLDAIDMERGAKVSGSRF FT YFLKGIGARLEIAMMNMALDVAMEHEFIPMITPTLVRPETMQGTGFDVEHDDEIYKLER FT DNMYLVGTSEVALAGYHADEIMDLAEGSIRYAGWSSCYRREAGSAGKDTRGIIRVHQFN FT KLEMFVYTSVENAEAEHAKLLAMEEDMLGRMELPYRVIDTAAGDLGMSAARKFDCEAWV FT PTQDTFRELTSTSNCTTFQARRLNIREREIIDGKPGKTRSVATLNGTLATTRWIVAILE FT NHQNPDGSVNVPKALQPYLGGIEVLK" FT CDS 71706..72536 FT /transl_table=11 FT /locus_tag="AARI_00720" FT /product="haloacid dehalogenase-like hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF08282: haloacid FT dehalogenase-like hydrolase. The Haloacid Dehydrogenase FT (HAD) superfamily includes phosphatases, phosphonatases, P- FT type ATPases, beta-phosphoglucomutases, FT phosphomannomutases, and dehalogenases, which are involved FT in a variety of cellular processes ranging from amino acid FT biosynthesis to detoxification" FT /db_xref="GOA:E1VRR0" FT /db_xref="InterPro:IPR000150" FT /db_xref="InterPro:IPR001757" FT /db_xref="InterPro:IPR006379" FT /db_xref="InterPro:IPR013200" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:E1VRR0" FT /protein_id="CBT74313.1" FT /translation="MTVMTKIGNDDRLDKQKLMICLDVDGTIVNHQGQMSQRVRDAARA FT VVERGHEVVISTGRSLGAALPVMEELGIDHGYVVVSNGGVLAKVTGSDIEVIHREVFDP FT SAALKALWKQLPKAKYALENERGEFLSNESFGDASFGAETKVVDFDELLENKAVRVVVF FT STDNTAEEFGHAVQGLGLSGVTYSVGWTAWLDIAADGTTKASGLERLRAILKFDLADSL FT AVGDGRNDIEMLQWAGHGVAMGQAPDEVKDAADAVTEGVDDDGLAIVLEELLQD" FT CDS complement(72555..73157) FT /transl_table=11 FT /locus_tag="AARI_00730" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRR1" FT /protein_id="CBT74314.1" FT /translation="MFVVALSPRPRSVTDVAAASEQLWDQLSEVDTHAPFTAVSGQLLL FT GVPKDPEAAVDALMRVTRLNFCNIGLGIGSLYEPVPAEADLVEGKAMRRALGALEAASH FT RGERVPICVSSGTDEMDAELEGLLRMLGHWIRTRTEAEWSVVDLLTPGVRGQQKAVAEI FT LGITPQAVSAAIVRSGYNDELGARAAISRLLEFTDQL" FT gene complement(73477..73677) FT /pseudo FT /locus_tag="AARI_00740" FT /product="truncated protein" FT /note="C-terminal section of a protein" FT gene complement(73677..74117) FT /pseudo FT /locus_tag="AARI_00750" FT /product="truncated protein" FT /note="N-terminal section of a protein" FT CDS complement(74302..74961) FT /transl_table=11 FT /gene="pcp" FT /locus_tag="AARI_00760" FT /product="pyroglutamyl-peptidase I" FT /function="3.10 Protein degradation" FT /EC_number="3.4.19.3" FT /note="selectively removes pyroglutamate (pGlu) from the N- FT terminus of proteins and peptides. The enzyme appears to FT play an important role in the activation and inactivation FT of many N-terminal pyroglutamyl-terminating peptides" FT /db_xref="GOA:E1VRR2" FT /db_xref="InterPro:IPR000816" FT /db_xref="InterPro:IPR016125" FT /db_xref="UniProtKB/TrEMBL:E1VRR2" FT /protein_id="CBT74315.1" FT /translation="MHILVTGFEPFGKDSFNASQEAVSQLPGQISNHRITTAILPVSFK FT RSAQELDHLLAEHRPDALICVGEAGGRDAITPEARGANLDDARIQDNDGDQPRAAAIDP FT RGPDFLEASLNPAAAVKMMLNEGFKAELSTDAGRFVCNHVAYLAYRQPVPSLFIHVPAL FT RPHGVEATVGAETDPGARKRSKLEVGQLPRALEAAIRGACSIQEETSAENTGDVHQ" FT CDS 75044..76252 FT /transl_table=11 FT /locus_tag="AARI_00770" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="InterPro:IPR003798" FT /db_xref="UniProtKB/TrEMBL:E1VRR3" FT /protein_id="CBT74316.1" FT /translation="MVIAVLVLVILNILATVCIALLLIRRTAGSDEAQISEAVRSANAE FT LRQELGIQRTELRQSMGEVRTDIDSKLTAMAESNANRHLQVQALLQQEMDKLRSGNEAK FT LEKMRETVDEKLQGTLEKRLGESFELVSKRLEMVQQGLGEMQSLAQDVGGLKRVLTNVK FT SRGSWGEVQLSRQLEDILTAEQYEQNATVVPGSRESVEFAVILPGREAGTIYLPIDSKL FT PQEDYERLLDAQESGEKTAIDAAAKALDRAIIEQAKLISSKYIAPPYSTDFAIMYLPTE FT GLFAEVVRSPGLASKLQTEHRVLVTGPTTLMSLLNSLQMGFRTLAIEKRSSEVWQVLSA FT AKEEFRKYGDVWDKLGKQLSAAQNTVSAAGTRTRVLEKTLRDVQTSEVSAQEDVLTGLL FT PES" FT CDS 76314..76655 FT /transl_table=11 FT /locus_tag="AARI_00780" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR005545" FT /db_xref="InterPro:IPR011008" FT /db_xref="UniProtKB/TrEMBL:E1VRR4" FT /protein_id="CBT74317.1" FT /translation="MSKYLISFPSPAMKFPESDLEAVAHAAHEVLREAKAAGGWIFGGG FT IDESIAAVMVESDGTLREGTYRQTAHIEGGYAVLELASYEQAVAWAAKFAAACRCAQEV FT RVFQDDPEN" FT CDS complement(76714..77193) FT /transl_table=11 FT /gene="ppa" FT /locus_tag="AARI_00790" FT /product="inorganic diphosphatase" FT /function="2.6 Metabolism of phosphate" FT /EC_number="3.6.1.1" FT /note="responsible for the hydrolysis of pyrophosphate FT (PPi) which is formed principally as the product of the FT many biosynthetic reactions that utilize ATP" FT /db_xref="GOA:E1VRR5" FT /db_xref="InterPro:IPR008162" FT /db_xref="UniProtKB/TrEMBL:E1VRR5" FT /protein_id="CBT74318.1" FT /translation="MSHDVTIEIPTGSRVKYEIDHETHRLRLDRVLFTSMQYPTHYGYF FT DDTLGEDGDPLDAMVYIPGVDLIPGVVVEARPIGVFNMTDDGGGDAKLLCVPADKRFDH FT IKELEDIDEWLIKEIEHFFTRYKDLEPGKWVKAEGWEGREAAEAELARSIERFKA" FT CDS 77291..78655 FT /transl_table=11 FT /locus_tag="AARI_00800" FT /product="putative serine-type D-Ala-D-Ala FT carboxypeptidase" FT /function="1.1 Cell wall" FT /EC_number="3.4.16.4" FT /note="identified by match to protein family PF02113. Is FT involved in the metabolism of cell components; it is FT synthesised with a leader peptide to target it to the cell FT membrane. Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D- FT Ala. Also transpeptidation of peptidyl-alanyl moieties that FT are N-acyl substituents of D-alanine" FT /db_xref="GOA:E1VRR6" FT /db_xref="InterPro:IPR000667" FT /db_xref="InterPro:IPR012338" FT /db_xref="UniProtKB/TrEMBL:E1VRR6" FT /protein_id="CBT74319.1" FT /translation="MNTAARRAITLGVAIVAMVAVIVAMLLAPRFFTGEPEASYIPASA FT QLAEASPVAVQDLDPNAAQPDPAVLTASLDAILADKSDKTSFNAQVVDVATGNVLYDRN FT SEINGTPASSLKVVTAIAALDALGGDTQLSTSVLLDGGTLVLRGGGDVLLGDRESDPTH FT PKGYAGLATLAKQAADELDKRGIEEVELWLDDSLFGDARNNPAWDKSLFTSNNIGEVYP FT IAHYAGRAGESTSTAYQSDAAQQVRKVFAKALAERVKVTEGGRGPYAGGQQITEVKSAP FT LRDVIKHMLLVSDNYIAETMGRLVALNRQMPAEQAGAAVAAVAQEHGASDLALFDTSGL FT AAKNKISPASLTAVLRSAATSKKPELREVVYSLPVAGYNGTLMNRLGGSETLGLVRAKT FT GSLTGVATLTGMTMTEDGRLLAFSIFANQPNGTLAPHKPTIDSAVTAIRGCGCRV" FT CDS 78674..79600 FT /transl_table=11 FT /locus_tag="AARI_00810" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR018766" FT /db_xref="UniProtKB/TrEMBL:E1VRR7" FT /protein_id="CBT74320.1" FT /translation="MNQFVDWKLAAKAAKTLMPAGPKIQSQDAARIVEELRIAAGEGLV FT EAEKVSKLSSSAPSQTLVVDRAGWAKAVSQNFSAMLPAARQEVPGAVPLIAGAELGAVL FT SVLGTRVLGQFDPFVGPRLLLNAPTITQIRGELNVNARDFYLWIATHEQTHRLQFEHAP FT WIPEVMKQTLAEAFEPLAGNTSSMRDLGERLKSMKSEVSELTSIMSVLEGHAMVVMNDV FT TSIRSIKTIRRRFEARGENRSALAILLGKVLGLDAKALQYKRGAKFVRHIVDEIGYEGF FT NEIFTDREMFPSADELDHPERWRARTR" FT CDS 79597..80523 FT /transl_table=11 FT /gene="tilS" FT /locus_tag="AARI_00820" FT /product="putative tRNA(Ile)-lysidine synthase" FT /function="3.6 RNA modification" FT /EC_number="6.3.4.-" FT /note="ligates lysine onto the cytidine present at position FT 34 of the AUA codon-specific tRNA(Ile) that contains the FT anticodon CAU, in an ATP-dependent manner. Cytidine is FT converted to lysidine, thus changing the amino acid FT specificity of the tRNA from methionine to isoleucine" FT /db_xref="GOA:E1VRR8" FT /db_xref="InterPro:IPR011063" FT /db_xref="InterPro:IPR012094" FT /db_xref="InterPro:IPR012795" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VRR8" FT /protein_id="CBT74321.1" FT /translation="MTHALHVARAAISASSAPGLNLIGISGGADSLALAIAAATLPGRF FT GAVIVDHSLQAGSAQAAQRAGQQCRELGLNPVLISEVETSPDEASARDARYQAFDQALA FT QFDADTLMLAHTRDDQAEQVLLGLVRGSGTRSLAGMPAQRGAYRRPLLELSRAQTEEIC FT RHAGIEYWDDPSNADTGYKRNLIRHRILPFLEQELGTHLRQALARTANLAAADAQALDH FT WAQKAKDEHGLQLPELRKLPVAVSSRVLRLGAMEAGAKNVGHERTAALCALAGIGQPMS FT KSAGPVQLDGAISAHRRRSVIVFTTTG" FT CDS 80588..81139 FT /transl_table=11 FT /gene="hpt" FT /locus_tag="AARI_00830" FT /product="hypoxanthine phosphoribosyltransferase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.4.2.8" FT /note="catalyses the formation of IMP and diphosphate from FT hypoxanthine and 5-phospho-alpha-D-ribose 1-diphosphate. FT Guanine and 6-mercaptopurine can replace hypoxanthine. This FT enzyme is essential for salvaging exogenous purine bases" FT /db_xref="GOA:E1VRR9" FT /db_xref="InterPro:IPR000836" FT /db_xref="InterPro:IPR005904" FT /db_xref="UniProtKB/TrEMBL:E1VRR9" FT /protein_id="CBT74322.1" FT /translation="MDSNAVKADLTHVLYTKEEIQARVEELAAQIDKDYEGRDILVVGV FT LKGAVMIMADLVRALDSHLTMDWMAVSSYGSGTQSSGVVRILKDLDSDLMGKHVLIVED FT IIDSGLTLSWLKSNLESRGPASVEICALLRKPEAAKVEIDVKYVGMDIPNEFVVGYGLD FT YAEKYRNLDCVATLAPHIYQ" FT CDS 81247..83172 FT /transl_table=11 FT /gene="ftsH" FT /locus_tag="AARI_00840" FT /product="putative cell division protein FtsH" FT /function="3.10 Protein degradation" FT /EC_number="3.4.24.-" FT /note="FtsH is a membrane-anchored ATP-dependent protease FT that degrades misfolded or misassembled membrane proteins FT as well as a subset of cytoplasmic regulatory proteins. 2 FT transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VRS0" FT /db_xref="InterPro:IPR000642" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003959" FT /db_xref="InterPro:IPR003960" FT /db_xref="InterPro:IPR005936" FT /db_xref="UniProtKB/TrEMBL:E1VRS0" FT /protein_id="CBT74323.1" FT /translation="MKTKKLFNSWIIWVLVGVVAVVLFLPMVFGNNSAKVDTSVGLHQL FT TSGNVTEAKMFDGDQRVDLKLRDALKVDGVDKGTSVSFYYSTARAEQVVDEINKANLGK FT FTDQPVESNWLLSMLGVIIPFLLIAGIFWFILARSQGGGSKVMQFGKSKAKLITKDMPQ FT VTFKDVAGADEAVEELHEIKEFLQEPAKFQAVGAKIPKGVLLYGPPGTGKTLLAKAVAG FT EAQVPFYSISGSDFVEMFVGVGASRVRDLFEQAKTNSPAIIFVDEIDAVGRHRGAGIGG FT GNDEREQTLNQLLVEMDGFDATTNVILIAATNRPDVLDPALLRPGRFDRQIPVEAPDLK FT GREQILQVHVKGKPMDATVDLNAVAKKTPGYTGADLANVLNEAALLTARSNANLIDDRA FT LDEAIDRVMAGPQKRTRLMDEHERKVTAYHEGGHALVAAAMNQTAPVTKITILPRGRAL FT GYTMVVPESDKYSVTRNELLDQMAYAMGGRVAEEIVFHDPSTGASNDIEKATSTARKMV FT TQYGMSEKVGAVRLAGSAAEQGMGTASRDFSDEMAHLVDQEVRELIEQAHNDAYQALTA FT NRHVLDRLALALLERETLNQKEIAEIFSDLVKREKREVWLSNEARPVHTEGPILSPKER FT AASSTD" FT CDS 83182..83760 FT /transl_table=11 FT /gene="folE" FT /locus_tag="AARI_00850" FT /product="GTP cyclohydrolase I" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="3.5.4.16" FT /note="catalyzes the biosynthesis of formic acid and FT dihydroneopterin triphosphate from GTP : GTP + H2O <=> FT formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- FT trihydroxypropyl)- dihydropteridine triphosphate" FT /db_xref="GOA:E1VRS1" FT /db_xref="InterPro:IPR001474" FT /db_xref="InterPro:IPR018234" FT /db_xref="InterPro:IPR020602" FT /db_xref="UniProtKB/TrEMBL:E1VRS1" FT /protein_id="CBT74324.1" FT /translation="MSELQEIDQPRIAAAVREILEAIGEDPDRDGLVDTPKRVAKAYAE FT FFAGLHQDAADHLATTFDIEHDEMVLVKDIPFYSTCEHHLVPFYGSAHIGYIPGKGGKV FT TGLSKLARLVEVYARRPQVQERLTTQIVDALVEHLSPSGAIVVVECEHMCMSMRGVRKP FT GAKTVTSAVRGQLRETATRAEAMSLILGK" FT CDS 83769..84671 FT /transl_table=11 FT /gene="folP" FT /locus_tag="AARI_00860" FT /product="dihydropteroate synthase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.5.1.15" FT /note="catalyzes the condensation of 6-hydroxymethyl-7,8- FT dihydropteridine pyrophosphate to para-aminobenzoic acid to FT form 7,8-dihydropteroate. This is the second step in the FT three steps pathway leading from 6-hydroxymethyl-7,8- FT dihydropterin to 7,8-dihydrofolate. It is the target of FT sulfonamides which are substrates analog that compete with FT para-aminobenzoic acid" FT /db_xref="GOA:E1VRS3" FT /db_xref="InterPro:IPR000489" FT /db_xref="InterPro:IPR006390" FT /db_xref="InterPro:IPR011005" FT /db_xref="UniProtKB/TrEMBL:E1VRS3" FT /protein_id="CBT74325.1" FT /translation="MSLGAIPGTGPNTSPLPVIRKSSKKTLADLPTGRTLVMGILNVTE FT DSFSDGGKYLSTDAAIDQGLKLLYSGADIIDVGGESTRPGARDVDPALESERILPVIET FT LAKAGAVISVDTMHVSTARAAIEAGAHIINDVSGLTYEEGMPELIAETGVPYVLMHRRG FT TAQNMVSEANYADVVAEVVQELRQLRDEFVAKGVAPEQIIIDPGLGFAKDAQHNWALLA FT NLSAIEELGHRVLIGTSRKRFLGELLAEGSKSREPLARDAATAATTALGARDKVWAVRV FT HDVVGSRDAIEVVQAYGSH" FT CDS 84658..85491 FT /transl_table=11 FT /gene="folBK" FT /locus_tag="AARI_00870" FT /product="bifunctional dihydroneopterin FT aldolase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine FT diphosphokinase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="4.1.2.25" FT /EC_number="2.7.6.3" FT /note="EC 4.1.2.25 catalyzes the following reaction: 2- FT amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7, 8- FT dihydropteridine <=> 2-amino-4-hydroxy-6-hydroxymethyl-7, FT 8- dihydropteridine + glycolaldehyde. EC 2.7.6.3 catalyses FT the following reaction: ATP + 2-amino-4-hydroxy-6- FT hydroxymethyl-7,8-dihydropteridine <=> AMP + (2-amino-4- FT hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate" FT /db_xref="GOA:E1VRS2" FT /db_xref="InterPro:IPR000550" FT /db_xref="InterPro:IPR006156" FT /db_xref="InterPro:IPR006157" FT /db_xref="UniProtKB/TrEMBL:E1VRS2" FT /protein_id="CBT74326.1" FT /translation="MDRISVCGISATGYHGVFDHEKRDGQKFIIDVVLHVDISRAAASD FT NVLDTVHYGEVSELVVQQIQSGPWDLIEKLGSEIAEAILAAYPSVYTIDVVVHKPQAPI FT PVPFTDVTISLTRHQKQHTAIIALGANLGDPQATLAAAVQELGADVELLKVSPLAITKP FT VGGPPEQPDYTNQVVQVRTGLSPHELLDLCQSIEAKHHRTREVRWEARTLDLDLIAYDH FT LRMDDERLTLPHPRAAIRGFVLAPWSWMDPDAVLDGQLVSRLAAEAADTKDIIRL" FT CDS 85488..85949 FT /transl_table=11 FT /locus_tag="AARI_00880" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.991) with cleavage site probability 0.734 FT between position 31 and 32. 3 transmembrane helices FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="InterPro:IPR021517" FT /db_xref="UniProtKB/TrEMBL:E1VRS4" FT /protein_id="CBT74327.1" FT /translation="MTKLKLRWLLWCAVLGALAGWIALRLLTAAGKYAPVLDYSALYSL FT GAVCAVILFLGIRVKRSSQGKSDFEPIAAARTLVLAQASAYAGAVIAGWHVPAIITLWL FT ANGLTPTLTRGLVLTGAGILMVVIGYIVQHLCKLPPEDTDGNSDSVVTE" FT CDS 85975..86415 FT /transl_table=11 FT /locus_tag="AARI_00890" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR005182" FT /db_xref="UniProtKB/TrEMBL:E1VRS5" FT /protein_id="CBT74328.1" FT /translation="MKVKLTTWAITWSLVLLASLVPLLMAVLDLIHPLWVTLIPVVLVL FT ALALLRLRIIRRQVRALGYLEREEDFIVRSGVLWRKQVVIPYGRMQYVEVNSGPLERRY FT GLCRLTLNTAGSAATAHVFGLPEAEGQALRERLVAAGEEKML" FT CDS 86412..87809 FT /transl_table=11 FT /locus_tag="AARI_00900" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR005182" FT /db_xref="UniProtKB/TrEMBL:E1VRS6" FT /protein_id="CBT74329.1" FT /translation="MSQPEEAAAAETGESWQRVHPASPFVHGWLAVVGLAYIYWQNTDD FT LSWSERFTGDRLVWTVAGASIALLVVLIFYFLSWYFTRYKLTGTHVYVNAGMLFRSQKQ FT ARIDKVQGIDIAQPLVARLLGLAELRFDVADSSESVLKLAFLRKAEAHQLRVVILERAH FT GAEPAAVQEPASEIAAAPSAAVGLAPAVQPPLMAKVPAGRLLASLFLQLPVIIGMLACL FT AMLIMWISGVDGIVAGLIPAVLTFGSWFYKQLNQGWNFTASASDTGMRISYGLADTRQH FT SIPAGRVQAISVTAPFFWRMLGWYKVEVNVLGTKSDDMDNLQVLPVGDFEAVTRIMGIL FT LPQLGIENQREVLATAVSTGYEHGFIGSPQRAKPLSPGAWKHQGFLATDTTVISRYGWL FT ARQASFVPHNRVQGMSWVQGPWEQRRKLAGVRLHCAGGSVIGYLHQLDADVAAGFTRAQ FT AQRLVER" FT CDS 87812..88678 FT /transl_table=11 FT /locus_tag="AARI_00910" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VRS7" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR018931" FT /db_xref="InterPro:IPR019665" FT /db_xref="UniProtKB/TrEMBL:E1VRS7" FT /protein_id="CBT74330.1" FT /translation="MDAPRLGIGIISAGKVGTVLGAALAASGHRITGIHAVSEDSRDRA FT DALLPEVELLDPPEILRRSELVIFAVPDDVLGELVAGLAEAGHIAPGQLIAHTAGRYGT FT SILQPAMDAGAFGLAIHPAMTFTGMSMDLQRLTDCVFAVTADEAILPVAQALVVEMRGE FT PVVIAEANRVSYHAALAHAANHLNTITAQSADILRRIGVEDPSNTLRALMYASLDNALR FT SGAGALTGPVARGDSGTVTAHLQALSHDPAETNNSYRSLSRATALRAAARGLISQRTLE FT ELLRVLE" FT CDS 88683..89549 FT /transl_table=11 FT /gene="panC" FT /locus_tag="AARI_00920" FT /product="pantoate--beta-alanine ligase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="6.3.2.1" FT /note="catalyzes the formation of pantothenate from FT pantoate and beta-alanine" FT /db_xref="GOA:E1VRS8" FT /db_xref="InterPro:IPR003721" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VRS8" FT /protein_id="CBT74331.1" FT /translation="MKTPKIAKTRAELKAAIAEANPGSLGFVPTMGALHSGHGSLFKAA FT REENEVVVISVFVNELQFNDATDYANYPRQLEADVQLAAEAGVDIVFAPEAEEIYHAGL FT PLVRLNSGALGDMYEGASRPGHFDGMLAVVAKLLHLADPRQGQYRAYFGQKDAQQLALI FT RRMVADLDYPVQLRSVPIVRSEKGLALSSRNALLSEEEKEAALVLHRSIQLIAGRAARN FT EPLYVEDAIGMCQMAPLVELDYFVVVNPDTLQELAFNCQDTPFTGEGLILVAAKVGKVR FT LIDNQPI" FT CDS complement(89546..90499) FT /transl_table=11 FT /locus_tag="AARI_00930" FT /product="2-nitropropane dioxygenase-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF03060: 2- FT nitropropane dioxygenase" FT /db_xref="GOA:E1VRS9" FT /db_xref="InterPro:IPR001295" FT /db_xref="InterPro:IPR004136" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:E1VRS9" FT /protein_id="CBT74332.1" FT /translation="MSDLQRLLGYREPIFNASMAGAAGGALAAAVSQAGGVGMIGSPAA FT PKTEWIEQQVQHVASLSTPWGVGFMAWALEADLYPLEAFLDFGPSLVTLSFGDVSRAAA FT LAHEAGVLTAMQVGNAADLERAMADDIDIIIARGGEGGGHGRNEAGTLPLLQLATAQQQ FT KPVIAAGGIGTARGVAAVLAAGASAAWVGTRFLAASEATGHKNVKDAIQQAGLDDTTYT FT RAFDVAQQLPWAPEFGGRALRNEFSDTHADLSTWAPDEQLRLEMQEARAEARTSMAPVY FT AGEAVQFIDSVQSAAEVMAELAGFRKVLADAASRFA" FT rRNA 90954..92472 FT /locus_tag="AARI_36310" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 93107..96229 FT /locus_tag="AARI_36320" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 96386..96501 FT /locus_tag="AARI_36330" FT /inference="ab initio prediction:rRNAScan:1.0" FT CDS 96904..96996 FT /transl_table=11 FT /locus_tag="AARI_00940" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRT0" FT /protein_id="CBT74333.1" FT /translation="MKRDIKEVFPVCAPRAEHSASKANVQGIDA" FT CDS 97559..97759 FT /transl_table=11 FT /locus_tag="AARI_00950" FT /product="helix-turn-helix domain-containing protein" FT /function="3.5.2 Transcription regulation" FT /note="match to PF01381: helix-turn-helix. This is large FT family of DNA binding helix-turn helix proteins that FT include a bacterial plasmid copy control protein, bacterial FT methylases, various bacteriophage transcription control FT proteins and a vegetative specific protein from FT Dictyostelium discoideum (Slime mould)" FT /db_xref="GOA:E1VRT1" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VRT1" FT /protein_id="CBT74334.1" FT /translation="MNSVSELGAELQRARKQNGLTQEQLADLAGISERTLRSIERGAGN FT PSIDAVLSVADVLGLRIVVAK" FT CDS 97756..98952 FT /transl_table=11 FT /locus_tag="AARI_00960" FT /product="HipA-like protein" FT /function="1.1 Cell wall" FT /note="identified by match to PF07804 (HipA-like C- FT terminal domain) and PF07805 (HipA-like N-terminal domain). FT The HipA protein is known to be involved in high- frequency FT persistence to the lethal effects of inhibition of either FT DNA or peptidoglycan synthesis. When expressed alone, it is FT toxic to bacterial cells but it is usually tightly FT associated with HipB and the HipA-HipB complex may be FT involved in autoregulation of the hip operon. The hip FT proteins may be involved in cell division control and may FT interact with cell division genes or their products" FT /db_xref="InterPro:IPR012893" FT /db_xref="InterPro:IPR012894" FT /db_xref="InterPro:IPR017508" FT /db_xref="UniProtKB/TrEMBL:E1VRT2" FT /protein_id="CBT74335.1" FT /translation="MTPSLQELRLVAQADVYCNDNLAGYLTRQDDGSIAFTYDLHYLHD FT GGSAIATSLPVARDAYVGPGGALPSFFSGLLPEGHRLTVLKDATKTSLSDELTLLMAVG FT SDTPGNVRVIPSGSKLEQTPVVAEFSTTEDLDFSVLSRTLDRHSIPGVQDKISATMLTT FT PVEFKNSAYLLKLDPRDHPHLVLNEALHLKAARALKLPVAKNQLVMDSKKNPGLLVERF FT DRMAVEPEGQPQRLPLEDAMQVLNLPPASKYAVSTEQVIQALAQHCQAPVLARRNLYIQ FT FAFAWLTGNGDLHGKNVSILANEQGQFGVAPIYDIPCTLVYGDDTMALTVAGKTKNLKR FT KHWAELSGELGLADRAAQSANQLALKAALTADLDELPFEGSPLRGAQRELRFRRMELE" FT CDS complement(98974..99417) FT /transl_table=11 FT /locus_tag="AARI_00970" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR011235" FT /db_xref="UniProtKB/TrEMBL:E1VRT3" FT /protein_id="CBT74336.1" FT /translation="MTYTALDRYCLITGQTHGEVIPEEQQSDYQAGIVEIDELLWRIRT FT ARTTPTKSGGFVAIWHRDETGATAPYASNAELHGALVFIEQSGRFGVFRFTQQHLEQLG FT VYASATAPGKRGFRVYPSWVTGLHGQAKKSQDAQRPAFSVLVD" FT rRNA 100378..101896 FT /locus_tag="AARI_36340" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 102531..105653 FT /locus_tag="AARI_36350" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 105810..105925 FT /locus_tag="AARI_36360" FT /inference="ab initio prediction:rRNAScan:1.0" FT CDS 106102..108075 FT /transl_table=11 FT /locus_tag="AARI_00980" FT /product="putative metalloproteinase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.24.-" FT /note="identified by match to PF05649 and PF01431" FT /db_xref="GOA:E1VRT4" FT /db_xref="InterPro:IPR000718" FT /db_xref="InterPro:IPR008753" FT /db_xref="InterPro:IPR018497" FT /db_xref="InterPro:IPR024079" FT /db_xref="UniProtKB/TrEMBL:E1VRT4" FT /protein_id="CBT74337.1" FT /translation="MTTETTSPLTYRDDSIRPQDDLYRHSNGKWFETATIPGDQGIYGS FT FMELRDQAEAAVHEIITEAVQKLDSGVEVDPATKRIAQLYSSFMNEAVIEERGADPVGV FT FLNTISDIQNSEHLLEVSGFFQRKGISGFMDIGAMNDAGNPERNLLTFLQGGLGLPDES FT YYREEQFADTVADYQEHLGRLLSLGGIADAQTAAEMVVELEKALASHHWDRVKVRDAQA FT RYNLISGEELIELFPGVKTWLAGAGIEQNYYSEVVVWQPSYLQGLAELVNAQPLDAWKN FT WLRVQVLRSFAPFLSSDFVNENFSFYSAKLGGVEQLKDRWKRGVAFTEGAVGEDIGQLY FT VAKNFPAEAKDAMDALVQRLIEAYRNSINELSWMGPETIEKALDKLSKFRPKIGYPNQW FT IDYSAIETDELDVIANLASANEFEFARELKKIDDGVDRELWFMFPQTVNAYYHPLLNEI FT AFPAAILRPPFFDVNRDIASNFGGIGAVIGHEIGHGFDDQGSQFDGTGQLTNWWTDDDR FT AAFEKLTGKLVDQYNALSPTEAPEHNVNGALTLGENIGDLGGLGIAYKAYKLELAARSI FT EEDEVIDGITGDQRFFYSWAECWRTLIRPETAVVRVTTDPHAPGEFRCNQVPKNLDAFH FT QAFGTKPGDGMWLDPADRVEIW" FT CDS 108213..109727 FT /transl_table=11 FT /gene="lysS" FT /locus_tag="AARI_00990" FT /product="lysine-tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.6" FT /db_xref="GOA:E1VRT5" FT /db_xref="InterPro:IPR002313" FT /db_xref="InterPro:IPR004364" FT /db_xref="InterPro:IPR004365" FT /db_xref="InterPro:IPR006195" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR018149" FT /db_xref="InterPro:IPR018150" FT /db_xref="UniProtKB/TrEMBL:E1VRT5" FT /protein_id="CBT74338.1" FT /translation="MTSENNSAQAIDPNDQRQVRTDKRNQLLAKGEEAYPVGVARTHSL FT QAIRDKYEHLEAGEETEDVVGVVGRIVFMRNTGKLCFATLQEGGKKGEGVRLQVMLSLA FT NVGEERLAQWKSLVDLGDHVFVTGKVISSRRGELSIMADAWEMASKALRPLPVLHADLN FT EETRVRQRYADLIVRNEAREMVYKRAAIIRAVRNTLEGHDYVEVETPMLQLVHGGASAR FT PFKTHLNAFDQEMTMRIALELYLKRAVVGGVDRVFEIGRIFRNEGVDSTHSPEFTMLEC FT YEAYADQYVMAQRMQQMILNAADAIGAGRTIETANGTINLDGEWRWLSVYPGLSEAVGV FT EITPDTDASVLREIAQKHEVKIDPAWGAQKLVIELFGEIVEPTLIDPTFVCDYPPLAQP FT LARPHRSKPGVIEAWDLIIGGMERGTAFSELIDPVIQRERLTEQSLLAAGGDPEAMQLD FT EDFLRALEYGAPPMGGIGLGIDRLVMLFSNAGIRETILFPLLKPEA" FT CDS 109729..109896 FT /transl_table=11 FT /locus_tag="AARI_01000" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRT6" FT /protein_id="CBT74339.1" FT /translation="MPYIEAIVPTIGLALLFWYVMKAITNADRKERQAEAEADALIQNH FT PDSNNPVIEN" FT CDS 110035..110355 FT /transl_table=11 FT /locus_tag="AARI_01010" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR024412" FT /db_xref="UniProtKB/TrEMBL:E1VRT7" FT /protein_id="CBT74340.1" FT /translation="MARQVQIALIDDIDGSEATESIAFSVAGQHFEIDLNDEHAAQFHA FT AIEPYIEAARSSKQTAASEAPAIRAWAKENNIKVNARGRLNAEVVDAYNAAMRKGGRNR FT AK" FT CDS 110617..113139 FT /transl_table=11 FT /gene="clpC" FT /locus_tag="AARI_01020" FT /product="ATP-dependent Clp protease ATP-binding subunit" FT /function="3.9 Protein folding" FT /note="ATP-dependent Clp proteases act as chaperones to FT target the proteases to substrates" FT /db_xref="GOA:E1VRT8" FT /db_xref="InterPro:IPR001270" FT /db_xref="InterPro:IPR001943" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003959" FT /db_xref="InterPro:IPR004176" FT /db_xref="InterPro:IPR013093" FT /db_xref="InterPro:IPR018368" FT /db_xref="InterPro:IPR019489" FT /db_xref="InterPro:IPR023150" FT /db_xref="UniProtKB/TrEMBL:E1VRT8" FT /protein_id="CBT74341.1" FT /translation="MPKMFERFTDRARRVVVLAQEEARMLNHNYIGTEHLLLGLIHEGD FT GVAAKALESLNISLGAVREQVQEIIGKGQQAPSGHIPFTPRAKKVLELSLREALQLGHN FT YIGTEHILLGLIREGEGVAAQVLVKLGADLGRVRQQVIQLLSGYQGGKETASAGVSSGG FT QQEGTPAGSAVLDQFGRNLTAAAREGKLDPVIGREHEMERVMQVLSRRTKNNPVLIGEP FT GVGKTAVVEGLAQSIVRGDVPETIKDKQLYTLDLGSLVAGSRYRGDFEERLKKVLKEIR FT TRGDIILFIDEIHTLVGAGAAEGAIDAASILKPMLARGELQTIGATTLDEYRKNIEKDA FT ALERRFQPIQVKEPSVELTTQILRGLRDRYEAHHRVTITDGALQAAATLAHRYISDRFL FT PDKAVDLIDEAGARLRIQRMTAPPALKEMDEEIATVRLEKEAAIDAQDFEGAASLRDKE FT SKLIEARNEKEKSWRNGDMDEVSEVTEELIAEVLANSTGIPVVKLTEEESSRLLNMEDE FT LHKRVIGQDSAIKAISQAIRRTRAGLKDPNRPGGSFIFAGPTGVGKTELAKALAEFLFG FT EEEALITLDMSEYSEKHTVSRLFGAPPGYVGYEEGGQLTEKVRRRPFSVVLFDEVEKAH FT ADLFNSLLQILEDGRLTDSQGRVVDFKNTIIIMTTNLGTRDISKGVMTGFQSAADTKTG FT YERMQAKVQEELRQHFRPEFLNRVDDTVVFPQLNQDEIEEIVDLFVARLAKRLKDRDMT FT IELTQAARSLLAQRGYDPAMGARPLRRTIQRDIEDQLSERILFGQIVAGQKITVDVEGE FT GELQKFVFHAEGGTGQLEGEPAPAALES" FT CDS 113231..113698 FT /transl_table=11 FT /locus_tag="AARI_01030" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VRT9" FT /protein_id="CBT74342.1" FT /translation="MKMRSAGQQVIAVSILAAMAYWALYLFLSPRLPDQLVRHVGTEGI FT GYSPMWLVVLIIGAAAALSIAIGIITYRDFTSLGHWNPGPKAIVVCFLAAGFGILGLGS FT AMILTVIGQEAAQLGALPIGMGLLALVTVFALSAVLLARTLPRAEQEALDR" FT CDS complement(113730..114176) FT /transl_table=11 FT /locus_tag="AARI_01040" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR014922" FT /db_xref="UniProtKB/TrEMBL:E1VRU0" FT /protein_id="CBT74343.1" FT /translation="MSDSEQDGFSAAEKAAMKERAKEVRAPKKRMTKAEKAQQARKEVE FT EKIASFEGNDKVLAEKLHRIITATAPELEPKTWYGMPAYALDGKILCFMQDAKKFGTRY FT LTFGFNDGAQLDEGTFWPTAFAITALDEQLEEKVSALVAKAVGR" FT CDS complement(114189..114596) FT /transl_table=11 FT /locus_tag="AARI_01050" FT /product="putative glyoxalase family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00903: glyoxalase/bleomycin FT resistance protein/dioxygenase superfamily" FT /db_xref="UniProtKB/TrEMBL:E1VRU1" FT /protein_id="CBT74344.1" FT /translation="MANISINFVPLSVLDVDQALLFYRDGLGFTVVSDVANGDFRWVSL FT VGSDGSGTNLVLSTPGAGRSEADAQALAELVAKGAIGPLVLSTTDLDGLFESLSASGAE FT VLQEPMDQPWGPRDCAFRDPSGNMVRINQAA" FT CDS complement(114644..115042) FT /transl_table=11 FT /locus_tag="AARI_01060" FT /product="AraC-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein domain PF00165: FT bacterial regulatory helix-turn-helix proteins, AraC FT family" FT /db_xref="GOA:E1VRU2" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR018060" FT /db_xref="UniProtKB/TrEMBL:E1VRU2" FT /protein_id="CBT74345.1" FT /translation="MNSETLKTLAHLRRAKDLMDRHYAEPLDVPAMAQRAAMSPAHFSR FT EFKRAYGETPHSYLLTRRIERAMHLLRAGATVTDACMQVGWTSLGSFSSRFTEVVGETP FT SSYRDRDHSATEAVPACLAKLLLRPERF" FT CDS complement(115046..116230) FT /transl_table=11 FT /locus_tag="AARI_01070" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VRU3" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VRU3" FT /protein_id="CBT74346.1" FT /translation="MLAILLSAVGIAPLLNYGLNATSDLVIRDLGITESQFGLLATVCF FT GCAALGNAAFGKFSDKQPDTRLLLLIFGTTAVALGLAAIPAGFVLLLIASGLAGFAQSF FT PNGVTNRILVQRVPSAQRITWTGIKQSGVQVSQLVGSLGFPLLAAVIGWHGASLVGAAL FT AAILAILALRIVSATPMLAAPAPRSPQPDKSRPAPAAAPSTRFVIIALSSYGFINGVGV FT QATNVYLALFAVRELDFSLVAGGLTAAVAGIIGVSARIGWGKMMSRGVSAPRLLLLLAL FT LAMVGALSFLGAQQMHSPALLWLAVGLHGASALGVSVVLMAALLRAIPAKNLGSASGIV FT SAGQFGGFTVGPAAMGLLVGSAGGFTAGWITVTGIYLCSTFLGIFLVVRAKKRA" FT CDS 116394..116903 FT /transl_table=11 FT /locus_tag="AARI_01080" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VRU4" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VRU4" FT /protein_id="CBT74347.1" FT /translation="MNSYTVRPAKTSDVHAIRNLVRPLAEERILLDKEAVTYYESIQEF FT LVAEDAEGNVVGCGGLHVIWEDIAEIRTLATSGELRGKGVGHVLLSGLLKRAKDVGVSR FT VFCLTFEVAFFERQGFKVMADQSAVDPAVYQELLLSRDEGVAEFLDLARVKPNTLGNTR FT MIITLN" FT CDS complement(116909..117709) FT /transl_table=11 FT /locus_tag="AARI_01090" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR009597" FT /db_xref="UniProtKB/TrEMBL:E1VRU5" FT /protein_id="CBT74348.1" FT /translation="MNSSVDPAGAARQVAKNPWFERAARLGYAANGVLHATLGILAAVI FT ATGGKAEADQSGAMRTLADQPFGMVLLWVCAIGALLLGLWSLAQAFLPENKVRERIKHA FT ATSVSFLAVGFTFGRFAVGKPSDSGKTATSFSGEMMKSGLGRTLLIAIGIGLLVMAGYY FT IYKGVTRRFLKDLSGSRHSEVSRAIKTSGMIGYPAKGVVLGTLGVLFIVATVQGDPKEA FT NGIDGALKTIQDQPFGPVALIAIGVGLVCYAIYLVFRARYDQMD" FT CDS complement(117774..118682) FT /transl_table=11 FT /gene="mutY" FT /locus_tag="AARI_01100" FT /product="putative A/G-specific DNA glycosylase" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.2.2.-" FT /note="identified by match to protein domain PF00730. This FT domain is found in a diverse range of structurally related FT DNA repair proteins that include: endonuclease III, and DNA FT glycosylase MutY, an A/G-specific adenine glycosylase. Both FT of these enzymes have a C terminal iron-sulphur cluster FT loop (FCL)" FT /db_xref="GOA:E1VRU6" FT /db_xref="InterPro:IPR000445" FT /db_xref="InterPro:IPR003265" FT /db_xref="InterPro:IPR003583" FT /db_xref="InterPro:IPR003651" FT /db_xref="InterPro:IPR004035" FT /db_xref="InterPro:IPR004036" FT /db_xref="InterPro:IPR011257" FT /db_xref="InterPro:IPR023170" FT /db_xref="UniProtKB/TrEMBL:E1VRU6" FT /protein_id="CBT74349.1" FT /translation="MQQIHNSINRWYSRNARDLPWRRPGVSGWEVMVSEFMLQQTPVVR FT VLPVYEEWMRRWPRPQDLAAEPLSEALKAWGRLGYPRRAQRLHAAAVEITTEYNGEVPR FT TEAELLSLPGIGDYTAAAIACFAFGERTVVVDTNIRRVHARLFGGMALPEPTPRASEFA FT RAREVQPEEHQIANMWNISVMELGALVCTARSPKCEQCPVFEQCAWIAAGQPAPHYTPK FT GQSWKGTDRQIRGAIMAILREHEQAVPERSFLNDLAQESHAKYLALEKLGSPLEQRERA FT LAGLLKDGLAVADEDGIRLPS" FT CDS 118805..119422 FT /transl_table=11 FT /locus_tag="AARI_01110" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VRU7" FT /protein_id="CBT74350.1" FT /translation="MSNTSGGKPGARVYRRRRITVAVIALVLLGVLIWGIVALVGLFTP FT DAQKTAGNESRTEQTQPASSPSSEQKDDEASAAMCKDDEIEITATTDAKHYASDKNPTL FT ILGIENVSKRECDLNVGSRQQEFLVSSGADRIFSTIDCLDQAEDVNLTFKPGQKENSRF FT TWNRERSAPGCKAVSVQPRPGTYKFTAAIGDFVSEPVSFVLE" FT CDS complement(119428..120501) FT /transl_table=11 FT /gene="disA" FT /locus_tag="AARI_01120" FT /product="DNA integrity scanning protein DisA" FT /function="3.3 DNA recombination, and repair" FT /note="participates in a DNA-damage check-point that is FT active prior to asymmetric division when DNA is damaged" FT /db_xref="GOA:E1VRU8" FT /db_xref="InterPro:IPR003390" FT /db_xref="InterPro:IPR003583" FT /db_xref="InterPro:IPR010994" FT /db_xref="InterPro:IPR018906" FT /db_xref="InterPro:IPR023763" FT /db_xref="UniProtKB/TrEMBL:E1VRU8" FT /protein_id="CBT74351.1" FT /translation="MKAHPTPGFLAVLAQIAPGTELAQGLERIQRGRTGALIVLGHDKV FT VESISSGGFRINTEYTPTRIRELAKMDGAIILDGTGRQILQAGVQLMPDAQIETQESGT FT RHRTAERVAAQTGFPTISVSQSMQTITLYADGERHVLEPAERLLARGNQAIATLERYRH FT RLDQVTSTLSAAEIEDVATAREVLAVLQRTEMLRRTSEEISRYVLELGIDGRLLAAQHA FT ELLSGIQVDNQLLLRDYSDAEGQELDIEQALEKLHEVSDAQLIDIDGLIKILFPHSMVG FT QDDQLTPKGYRLLSQIRTVPKLVGDRLVASFDNLQLLMAASTSQLMEIEGVGEQRARSI FT REGLARMAESSLLDRYI" FT CDS complement(120536..121930) FT /transl_table=11 FT /gene="radA" FT /locus_tag="AARI_01130" FT /product="DNA repair protein RadA" FT /function="3.3 DNA recombination, and repair" FT /note="may play a role in the repair of endogenous FT alkylation damage" FT /db_xref="GOA:E1VRU9" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR004504" FT /db_xref="InterPro:IPR014774" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/TrEMBL:E1VRU9" FT /protein_id="CBT74352.1" FT /translation="MAKTSTRSKSSASFKCSECGWTTIKWVGRCGECQAWGTVEEVGVV FT SARTIAAAKIAHPAKPIAQIDGSEAAFRPSGVSELDRVLGGGLVPAAAILLAGEPGVGK FT STLLLDVAAKAAQTGLRVLYLTGEESAAQVKSRAERINAIADTLYLAAETDLSLALGQI FT QEIDPQLLILDSVQTFSSAEIDGAAGGVSQVREVAASIINAAKTRAMSTIMVGHVTKEG FT SVAGPRLLEHLVDVVCQFDGEKHSRLRILRALKNRYGATDEVGCFDLNEDGIESLTDPS FT KLFVTRTRNPVPGTCITVTLEGRRPLVAEVQTLLSRSNAPAARRATSGLDAARAQMVVA FT VLQARAHMDLSSMDSYIATVGGVKIAEPASDLACALALASSMNEFPLPQDFVAFGEVGL FT AGEVRQVPEISRRITEAQRLGFSFAMAPATPEPLKNIPEGIRVFQVENIAQALDIAFNQ FT RQKPTG" FT CDS complement(121966..123108) FT /transl_table=11 FT /locus_tag="AARI_01140" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR010343" FT /db_xref="UniProtKB/TrEMBL:E1VRV0" FT /protein_id="CBT74353.1" FT /translation="MATTRKAKRMPAHVFGFLSQRNRAGLIRARSSLPRILRMTLGAIG FT AFWIAESIWGHSQPIFAATSALVSLGFGASTTVRKTAEVALGCTLGVALGDILMHWFGQ FT GIWQAALVMSLSLVVARYLDSGAIFSTQLGMQSALVVLLPISVDGPFARSIDALTGSLL FT ALLVIVFWPTDPRRSPVSALSDLFKELSEALLECAWAIRDDDRRAAFHALIKTRGTQKH FT LDMLPAAFRASKEIAMISPTGRRHRHELNRLSKRFNHYDWAARNSRVFARRLASVLSNS FT ALTPEGAQTLAPLMRELSEAVNTMAHSVRETTVAGQRKYEKSAQLQLEGVAAQLDPRAL FT GVEGLQGEGLVLLLRPMVVDLLEAAGREHQEAIDVLPKLS" FT CDS 123321..124436 FT /transl_table=11 FT /gene="pstS" FT /locus_tag="AARI_01150" FT /product="phosphate ABC transporter, substrate-binding FT protein PstS" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT phosphate uptake transporter (PhoT) family, phosphate FT transporter (TC 3.A.1.7.2). ABCISSE: ABC transporter, FT binding protein (BP), MOI-family, phosphate import. Part of FT the ABC transporter complex PstSACB involved in phosphate FT import. The complex is composed of two ATP- binding FT proteins (PstB), two transmembrane proteins (PstC and PstA) FT and a solute-binding protein (PstS)" FT /db_xref="GOA:E1VRV1" FT /db_xref="InterPro:IPR005673" FT /db_xref="InterPro:IPR024370" FT /db_xref="UniProtKB/TrEMBL:E1VRV1" FT /protein_id="CBT74354.1" FT /translation="MKLNRIGSAAAVLSVAALALTACGSDSPTAAAGSEGAETSAASGV FT TGTLTGIGASSQNSAMEAWSTGFKAANPDANVQYSPDGSGAGREAFLAGGAQFAGSDAY FT LKEDEAAKAKEVCGPEGAFNIPAYVSPIAIAFNLEGVEEINMDAATIAKVFKKEITKWN FT DEAIAKQNPDVELPDTAITVVHRNDESGTTENFVEYLKAAAADVWTYDVSGDWPSDIQS FT ENAKGTSGVVSTTTSTDGAITYADFSAVGNLSTVNVKVGEDYTKISAEAAAKALETATP FT VEGAAENDLALDLERDTSESGTYPIVLVSYHIFCSSYKDQATADLVKAFGNYVISEDGQ FT KTAQASAGNAPISAAIAEKAKKSIDGITVAE" FT CDS 124556..125491 FT /transl_table=11 FT /gene="pstC" FT /locus_tag="AARI_01160" FT /product="phosphate ABC transporter, inner membrane subunit FT PstC" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT phosphate uptake transporter (PhoT) family, phosphate FT transporter (TC 3.A.1.7.2). ABCISSE: ABC transporter, FT permease (IM), MOI-family, phosphate import. Part of the FT ABC transporter complex pstSACB involved in phosphate FT import. The complex is composed of two ATP-binding proteins FT (pstB), two transmembrane proteins (pstC and pstA) and a FT solute-binding protein (pstS)" FT /db_xref="GOA:E1VRV2" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR011864" FT /db_xref="UniProtKB/TrEMBL:E1VRV2" FT /protein_id="CBT74355.1" FT /translation="MTANALTSKSSTSGRAGDKIFSGAALGAGVLILITLFAVAVFLLI FT QALPTFFADPAEISGGEGFFAYIWPIVIGTVIAAAIALLIATPIGIGVALFISHFAPRK FT VAGPLGYLIDLLAAIPSVIYGAWGYMVLAPALVPGYEWLAKNLGFIPIFEGPASQTGKT FT MLTAGIVLAVMVLPIITSLSREIFLQTPKLHEEAALALGATRWEMITTAVIPFARPGII FT SAVMLGLGRALGETMAVALVLSTGNLIPSLIKTGNQTIAAEIALNFPEAFGLRLAELIA FT AGLVLFLITLVVNMIARGIIARHKEFSGAN" FT CDS 125491..126630 FT /transl_table=11 FT /gene="pstA" FT /locus_tag="AARI_01170" FT /product="phosphate ABC transporter, inner membrane subunit FT PstA" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT phosphate uptake transporter (PhoT) family, phosphate FT transporter (TC 3.A.1.7.2). ABCISSE: ABC transporter, FT permease (IM), MOI-family, phosphate import. Part of the FT ABC transporter complex pstSACB involved in phosphate FT import. The complex is composed of two ATP-binding proteins FT (pstB), two transmembrane proteins (pstC and pstA) and a FT solute-binding protein (pstS)" FT /db_xref="GOA:E1VRV3" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR005672" FT /db_xref="UniProtKB/TrEMBL:E1VRV3" FT /protein_id="CBT74356.1" FT /translation="MSTMTTNQSNMAGRPTPPVRKRNSLAKGKLPKWAIWAIAAGAIII FT GAAASTLTGFNVASFAIYSALIFLVAASVITSAVEGKRRGKNAMWTYLIYAAFIVAVIP FT LVSVLYTVLEKGMPGMNAHFLFNSMNGVTGAVDNESVANGAPVVGGAYHAVVGTLLITL FT WATLISVPVGMLTAVYLVEYGQGKALSKAITFFVDVMTGIPSIVAGLFAAAFFGMILGP FT NARMGIVAAVALSVLMIPTVVRSTEEMLKIVPNELREASFALGVRRWRTILKVVIPTAI FT SGIASGVTLAIARVIGETAPILVTAGIASQINMNVFANWMSTLPTFIYYQILTPTSPTN FT IDPSVQRAWAAALLLIFMVMALNLLARLVASIFAPKKGR" FT CDS 126677..127456 FT /transl_table=11 FT /gene="pstB" FT /locus_tag="AARI_01180" FT /product="phosphate ABC transporter, ATP-binding subunit FT PstB" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.27" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT phosphate uptake transporter (PhoT) family, phosphate FT transporter (TC 3.A.1.7.2). ABCISSE: ABC transporter, ATP- FT binding protein (ABC), MOI-family, phosphate import. Part FT of the ABC transporter complex pstSACB involved in FT phosphate import. The complex is composed of two ATP- FT binding proteins (pstB), two transmembrane proteins (pstC FT and pstA) and a solute-binding protein (pstS)" FT /db_xref="GOA:E1VRV4" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005670" FT /db_xref="InterPro:IPR015850" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VRV4" FT /protein_id="CBT74357.1" FT /translation="MAKRIDVNDLNVYYSKFLAVEGVSINIEPKSVTAFIGPSGCGKST FT FLRTLNRMHEVIPGGRVEGQVLLDGDDLYGAGVDPVTVRSQIGMVFQRPNPFPTMSIKD FT NVLAGVKLNGQKISKSDADSLVEKSLRGANLWNEVKDRLDKPGSGLSGGQQQRLCIART FT IAVKPDVILMDEPCSALDPISTLAIEDLINELKNDYTVVIVTHNMQQAARVSDRTAFFN FT IAGTGKPGKLIEFNDTAAIFSNPEQKATEDYVSGRFG" FT CDS 127466..127585 FT /transl_table=11 FT /locus_tag="AARI_01190" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRV5" FT /protein_id="CBT74358.1" FT /translation="MPPLLELAVDGPEGGSSGDPGGDHRQRRTDYGAPLHFNY" FT CDS 127667..128134 FT /transl_table=11 FT /locus_tag="AARI_01200" FT /product="hypothetical membrane protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VRV6" FT /protein_id="CBT74359.1" FT /translation="MTTATQSKWERTRFGGSPALLIVLSVLGGLILSAAIAWLIWQFGP FT DAVVQRKALAAVVAGLVMLPATFALCWVIMLDRDTLAGAVKDPDSSIEGKWYDKAAFGA FT FHDLIAVCGLGAMALFLLPIDVDPAMVLCGVVMFAAVDTTVRYLLIKKVEG" FT CDS 128134..128625 FT /transl_table=11 FT /locus_tag="AARI_01210" FT /product="hypothetical membrane protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VRV7" FT /protein_id="CBT74360.1" FT /translation="MGNRGIEPRTLALGRSRFGGGKALMITLVLGSGLLATVVLSTLIS FT LLVDFDEGFWPAWINLAFTFWLVASAIAWFVFVDRSALPKPAVNPEQTVEQNWRTRAQA FT GVYRDLVIFLGLGCVAASLCSLLADQPLSVPVALVFAGVVWIALLDYMIRYQLIKRAES FT " FT CDS 128625..128822 FT /transl_table=11 FT /locus_tag="AARI_01220" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domain PF01381: helix-turn-helix" FT /db_xref="GOA:E1VRV8" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VRV8" FT /protein_id="CBT74361.1" FT /translation="MQNNLSEYRKEHGFSQQALADLLGVSRQTIISLEKGRYDPSLPLA FT FKLSAVFGCKIEDLFIPGED" FT CDS complement(128819..129847) FT /transl_table=11 FT /locus_tag="AARI_01230" FT /product="putative phosphate transporter" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="inorganic phosphate transporter (PiT) family (TC 2. FT A.20.y.z). Identified by match to protein family PF01384" FT /db_xref="GOA:E1VRV9" FT /db_xref="InterPro:IPR001204" FT /db_xref="UniProtKB/TrEMBL:E1VRV9" FT /protein_id="CBT74362.1" FT /translation="MAILSVLTGIAIVLTLGYGVLNGFRDASTAVAASIRTRALRPAVA FT VSVAALFAFLGTLATTGLSVALVDKLNFNVPDGVVGLKLLICGLLTAGAWGLYCWWRGL FT PVSSTHALFSGLVGASGASAFMGDMSMSGAWGLLLGSVLLPLLVTPVIAYILSYLLVIP FT ATWLMRHNTSQSVNNGSRAGQAIAACAVALGLGLQDGQRTGAMIALVLITGHAMDPGPM FT TWAIQLAAGAALSLGVLLGGWRITYTLSRRLVNFDPLRGMIAQGVAATMLFLGSLVLHL FT PLSTTQAVTSGIVGAGNNQAFESVVWRNVSKVLVHWVLTPAICVAGGAILTLAVHPLLG FT NA" FT CDS complement(129852..130481) FT /transl_table=11 FT /locus_tag="AARI_01240" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRW0" FT /protein_id="CBT74363.1" FT /translation="MVRRKVKFQIFPSTSRGIELLCGLTTTIRTSVANVSEMIGSPDTR FT ADQLRDLASAEAEASDLVHAVLTHLRTSYISPLPREDMYTLSRLLHETMEHLRGTGELI FT MNVGSTPLSERSSEQLELISQLAELASDSVQRLHNLDDLEDNWLQMLQFSKRAARTHLV FT WVNEISKFAKPGTIHRHQRVADHLMLTANTLRQFADHLGRVLVKES" FT CDS 130526..130645 FT /transl_table=11 FT /locus_tag="AARI_01250" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRW1" FT /protein_id="CBT74364.1" FT /translation="MEVNESYLKVPDRERLSAEGRSKRQNFGARGYQRPGTDT" FT CDS 130841..131086 FT /transl_table=11 FT /locus_tag="AARI_01260" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRW2" FT /protein_id="CBT74365.1" FT /translation="MSLTANAAPRSTAGTDVEIMVMVIGWPRPRKNPPISSAAPEAHKL FT SMNTGASAMAIVLSQNIAYTLTHNIAYRMYQHIADR" FT repeat_region 130993..131007 FT /rpt_type=DIRECT FT repeat_region 131008..131057 FT /rpt_type=INVERTED FT mobile_element 131008..132729 FT /mobile_element_type="insertion sequence:ISAar22" FT /rpt_family="IS481" FT CDS 131139..132584 FT /transl_table=11 FT /locus_tag="AARI_34370" FT /product="transposase of ISAar22, IS481 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRW3" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VRW3" FT /protein_id="CBT74366.1" FT /translation="MSNSLSASIRRQIIEFDPGLPDSLSISQFCKELGISRPSYYKVKE FT RFVAEGNKALNPHSRAPKTDRRIYSDQTKTTVLRIRKRLAKDGWDNGPLSIWFESLDTQ FT EFGELRPSVATIGRILAEAGATKRNPRKRPRKSWLRFARSHPMEMWQIDGLEYRLFDQD FT ATKAMIYQLIDDGSRFDVGTRCFEQMENAQDAMETLKAAFAEYGVPQQLLSDNGGAFNL FT SRQGLVNQTEIFLASVGCEAITGRFSHPQTQGKNERSHNTLTRFLDAHAPHNLAELSTL FT LEQYRNHYNHRRRHQALKVGHTYLTPAQAWEAGDHRGSDGVAIDIARIQAKAQSYLDKA FT LAVKADLVPEGVVDDGLQVLGRTKVENYTGSPSVLTDQRDDVIQIRRTNPQIYFRGRVF FT KVPAHLIGEYQLVLSKDAYTLYSTVDGEQSLSFPLPVRLHSSARLVPLWQVYGARIRDP FT KPAWTQKRIEYEDIYYSPDVAVS" FT gene complement(132634..133617) FT /pseudo FT /locus_tag="AARI_01270" FT /product="truncated MFS superfamily transporter" FT /note="N-terminal section of a MFS superfamily transporter. FT Insertion of ISAar22" FT repeat_region 132680..132729 FT /rpt_type=INVERTED FT repeat_region 132730..132744 FT /rpt_type=DIRECT FT CDS complement(133717..134382) FT /transl_table=11 FT /locus_tag="AARI_01280" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRW4" FT /protein_id="CBT74367.1" FT /translation="MRGARAGSRVAQDAGFRHHKPRPFAPAEFEPYEGGADPARVSEAA FT HLSAQAFVRRGIANNNPEVSRRLIAVAEDEGLEVLAQLWSEAPAHSLPGALWRLYAVRA FT ATMSKPEVHSARFMAGAHRAEVERVVAGVAEPPTAEEMKKMTGSILSGAFNGDFAHALE FT RTAAYCRVLALGMTEHADAADFSNSDRGTKLTQQARALDGTAADLEVCARLWRQDALD" FT tRNA 134543..134618 FT /locus_tag="AARI_36370" FT /product="transfer RNA-Lys" FT /anticodon=(pos:134576..134578,aa:Lys) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(134707..135297) FT /transl_table=11 FT /locus_tag="AARI_01290" FT /product="dienelactone hydrolase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF01738: dienelactone FT hydrolase family" FT /db_xref="GOA:E1VRW5" FT /db_xref="InterPro:IPR002925" FT /db_xref="UniProtKB/TrEMBL:E1VRW5" FT /protein_id="CBT74368.1" FT /translation="MATIVLFHHVQGLTPGVQAMAAELRAAGHTVHALDLYAGKLPKDF FT DAGMRMAGKLTEDKIQERVDKLFGKLPEELVYIGTSWGAALAQQCAQQRPGAIAAILLE FT SFVDLDADWSFGPWPENVPVQIHGMDQDPFFAKEGDLEAAQRFVEAEGGDIAQLFTYPG FT KQHLFTDSSLRSHDPEARALVMERMVKFLQPYV" FT CDS complement(135316..135567) FT /transl_table=11 FT /locus_tag="AARI_01300" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRW6" FT /protein_id="CBT74369.1" FT /translation="MSYPQRTVEVVKTGLVIDQSATLLWQDIKRAFIYETGSGQEALTC FT AEFMLVEGYSVEINSQMPGWDLAIEHLTQRIENLVDER" FT CDS complement(135643..137247) FT /transl_table=11 FT /locus_tag="AARI_01310" FT /product="putative drug resistance ATP-binding protein" FT /function="4.2 Detoxification" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT (putative) drug resistance ATPase-1 (Drug RA1) family (TC FT 3.A.1.120.z). ABCISSE: fused ATP-binding protein (ABC2), FT ART-family. Duplicated ATPase domains (PF00005)" FT /db_xref="GOA:E1VRW7" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:E1VRW7" FT /protein_id="CBT74370.1" FT /translation="MSLTPPITLNNLSFAWPSGERALANLDGTFPSGRTGLIGANGSGK FT STLLKLIAGQLHPTSGTAETSAPLSYLPQTLALEQDTTVAQLLGVHRVLAALEAIESGS FT VDPADLDAVGASWDAEARVRAELAPLGFDGLDLGRKVATLSGGEAMLLAVLGLRIADSP FT ITLLDEPTNNLDRPARELLYDLVRAWKGTLVVVSHDIELLELMEHTVELYGGKLSVFGG FT PYSAYREQLETEQQAAEQAARTAQASLKVEKRQRVEAETKLARAKRKGRATQLSGGMPK FT ILANHLRQKSEANAGKMRSNLDGKVDSAQARLDDADQRVRQAEHINIELPDPRLPSGKQ FT VAALGPADHQFIIQGPERVGLVGPNGSGKTTLLKQMLAGEAPGPGLGGQLFLDRVGYLP FT QRLDGLDGELSAMQNVASVAPAATANDVRKMLARLLLRGDSADRPLAVLSGGERFRVYL FT ATLLLAEPAAQLLILDEPTNNLDMDSVRQLSEALGTYKGALLVVSHDQHFLAQLDLDYL FT LEVGPRGTLAKTYPNPV" FT CDS complement(137461..138243) FT /transl_table=11 FT /locus_tag="AARI_01320" FT /product="putative CAAX amino terminal protease family FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF02517: CAAX FT amino terminal protease family. Members of this family are FT probably proteases (after a prenyl group is attached to the FT Cys residue in the C-terminal CAAX motif of a protein, the FT AAX tripeptide is removed by one of the CAAX prenyl FT proteases). The family contains the Q03530 CAAX prenyl FT protease. Signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.755) with cleavage site probability 0.459 FT between position 27 and 28. 5 transmembrane helices FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="GOA:E1VRW8" FT /db_xref="InterPro:IPR003675" FT /db_xref="UniProtKB/TrEMBL:E1VRW8" FT /protein_id="CBT74371.1" FT /translation="MSWKLLPASLLSGSAVLLFGVGNDPAGYGLLALSLLCAGFIDRRL FT ARHLGLIATGLVVISLVPLNADLSLGHMALMGGALAAAVLLPWLISRFALREQIIKFPV FT NTGRKWPLAAKLYLLGVVALGFFILPVYLISTGAYQNWPDASDPAIFWRLFLGVNSVGI FT WDELFFICTAFALLRQHFPDWQANILQAVIFSSFLWEIGYQSWGPLLTFPFALLQGYTF FT KLTKSLSYVVGVHLIFDLVLFLALVHAHNREWLPVFLY" FT CDS complement(138406..139107) FT /transl_table=11 FT /locus_tag="AARI_01330" FT /product="ubiquinone/menaquinone biosynthesis FT methyltransferase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.1.1.-" FT /note="converts dimethylmenaquinone (DMKH2) to menaquinone FT (MKH2) and converts 2-polyprenyl-6-methoxy-1,4-benzoquinol FT (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4- FT benzoquinol (DMQH2)" FT /db_xref="GOA:E1VRW9" FT /db_xref="InterPro:IPR004033" FT /db_xref="UniProtKB/TrEMBL:E1VRW9" FT /protein_id="CBT74372.1" FT /translation="MSSQNARAGLDKKADQVQEMFDKLAPRYDLLNTLMTGGIVNYWRK FT ITTEAIAPKPGERILDLAAGTGTSSVPLAEAGADVTACDMSHGMLDEGRKRYPQLNFVY FT GDGTDLPFEDNTFDAVTISYGLRNIADTEKALSEMRRVAKPGGRIVVAEFSTPTVAPIK FT TAYKQFLPRAIPALGYLVSPNPTAYAYLAESIAAWPDQDELGAKFVNVGWKNVEYRNLT FT GGIVAVHRAWK" FT CDS complement(139166..140137) FT /transl_table=11 FT /locus_tag="AARI_01340" FT /product="activator of Hsp90 ATPase 1-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VRX0" FT /db_xref="InterPro:IPR013538" FT /db_xref="InterPro:IPR023393" FT /db_xref="UniProtKB/TrEMBL:E1VRX0" FT /protein_id="CBT74373.1" FT /translation="MPVTSVVKDSEALSLTVHAEFPVKVSRLWDAYLDAGQLEKFWGPV FT EYPATFTRHDAAPGGRSNYHMTSPEGEEFHGYWIWNEVVEHKFFEVSDGFAHADGTPNT FT DLPSNRIVFTFDPTSGGTKLAITSTFDSAEDLEQVVAMGMIDGTRSAMSQIEQVLIDLR FT NYAEDFITDAQILSDTQVRITRLVRGSVAQVWKAHHDQRLMKRWMLGPDGWQLAECVTA FT QEPGETYRYWWEPLSADDGSGFGFTGTVLETLPQSYERTTEQMIGTEYPATVNELTLTS FT NQGGTLLTILITYPDAQTRDMVLSTGMTDGMEASYARLESIL" FT CDS complement(140149..140487) FT /transl_table=11 FT /locus_tag="AARI_01350" FT /product="putative ArsR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF01022. ArsR-family FT transcriptional regulators include several proteins that FT appear to dissociate from DNA in the presence of metal FT ions" FT /db_xref="GOA:E1VRX1" FT /db_xref="InterPro:IPR001845" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VRX1" FT /protein_id="CBT74374.1" FT /translation="MVVHELSEEQVNKVFRALADATRRDIVRRTLHAEVSITDLASSYD FT MSFAAVQKHVAALEAAGLVRKIARGRERIVRGQPDTIRHAQELLTSLEDIWRQRISRLD FT DFLADEAP" FT CDS 140708..141928 FT /transl_table=11 FT /locus_tag="AARI_01360" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="GOA:E1VRX2" FT /db_xref="InterPro:IPR001867" FT /db_xref="UniProtKB/TrEMBL:E1VRX2" FT /protein_id="CBT74375.1" FT /translation="MSGFAIDWPGASRRAQHAHELLGSSGAGVTDLPLRNDVRESWKRS FT LQNSADLRVPSVLSDDHLRLARERSELQRIWPVFEKLLVPAAADANLLVALADAGGTLL FT WVAGGNGAMSQAEHVGFMAGADWAEKSVGTSAPGMALATGTGSQVSGAEHLYEQAHRYS FT CSAVPIRDPRTGQVIGAIDLTGGSEAIATHSLPLLQAAVMAAETQLLLPGAGVVADPDY FT LDLGRSDGAHLGSAPISLRHAEILTLLAHYREGLSTAQLVEELFERPDAAAEGTVRAEI FT VRLRKVLAGPGGRALTSRPYRLQWDLHTTLGRLWHALEQGDLDTALPLYSPGLLARSQA FT PGIVALLYRTEAALREMVLDRGTAHQLLNLGRQLADPGLLRAALRELPAQSPARSLVVA FT EVQAIEN" FT CDS 142094..143617 FT /transl_table=11 FT /locus_tag="AARI_01370" FT /product="aldehyde dehydrogenase (NAD(+))" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.2.1.3" FT /note="catalyses the following reaction: an aldehyde + FT NAD(+) + H(2)O <=> an acid + NADH" FT /db_xref="GOA:E1VRX3" 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:E1VRX3" FT /protein_id="CBT74376.1" FT /translation="MAVYANPNTDGALVNFKERYENYIGGQWVAPTKGMYFENVTPVTG FT KVFCEVARSTAEDIETALDAAHAAAPAWGKTSPAERAVILNKIADRIEENLEMMAVAET FT WDNGKAIRECLNADLPLAVDHFRYFAGAIRAQEGSLSQLDDDTTAYHYHEPLGVVGQII FT PWNFPILMAVWKLAPALAAGNAIVLKPAEQTPVSILVLMELIGDLLPAGVLNVVNGFGV FT EAGKPLASNKRIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDIASKDD FT AFYDKAQEGFTLFALNQGEVCTCPSRALIQESIYEKFMGDVVARTKAIKQGHPLDTETM FT MGAQASNDQLEKILSYMDIGKSEGAKVLLGGGRADLGGELSGGFYVQPTIFEGTNDMRI FT FQEEIFGPVVAVTKFKDYDDAISIANDTLYGLGSGVWSRNGNVAYRAGRAIQAGRVWVN FT QYHAYPAHSAFGGYKSSGIGRENHLMMLDHYQQTKNLLVSYSEDKLGFF" FT CDS 143767..144798 FT /transl_table=11 FT /locus_tag="AARI_01380" FT /product="Zn-dependent alcohol dehydrogenase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.1.1.1" FT /note="catalyses the following reaction: an alcohol + FT NAD(+) <=> an aldehyde or ketone + NADH" FT /db_xref="GOA:E1VRX4" FT /db_xref="InterPro:IPR002085" FT /db_xref="InterPro:IPR002328" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR013149" FT /db_xref="InterPro:IPR013154" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VRX4" FT /protein_id="CBT74377.1" FT /translation="MSKMKAAIVEGFGEEFQVKDAEIPEPGPGQVLVKLIASGVCHTDL FT HAAEGDWPVKPKLPLIPGHEGVGIVEKLGEGVTEVALGDMIGNAWLASACGHCQYCRTG FT WETLCEAQSNGGYSVDGSFGQYMLVDSRYAAHIPEGSDPHEIAPVLCAGVTVYKGLKMT FT EVKPGQWVAISGIGGLGHIAVQYAVAMGMRVIAIDVADDKLALASKHGAEITVNAFAQD FT PAEIIQQKVGGTHGVLVTAVHPKAFGQAIGMTRRGGTIVFNGLPAGDFPAPIFDIVLKG FT LTIRGSIVGTRQDMIEALEFYAAGKIKPTFHTRPLEDINAVFDEMRHGKIDGRVVIDYA FT GRA" FT CDS 144967..145392 FT /transl_table=11 FT /locus_tag="AARI_01390" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR008497" FT /db_xref="UniProtKB/TrEMBL:E1VRX5" FT /protein_id="CBT74378.1" FT /translation="MSTVTETRAAIEGEEFSRVAFTSEALDLLRKLWGIHGPLMFHQSG FT GCCDGSSPMCYPAGEFRTGGSDIRLGVLSLDGADGTALGDIDFWMSKEQFEYWKHTKLT FT VDVVNGRGSGFSVEAPEGKRFLIRSEIIEFPAGPNPD" FT CDS 145402..145854 FT /transl_table=11 FT /gene="uveA" FT /locus_tag="AARI_01400" FT /product="pyrimidine dimer DNA glycosylase" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.2.2.-" FT /note="identified by similarity to protein SP:P94957 FT (Micrococcus luteus). It is a DNA excision repair enzyme. FT Also named UV endonuclease (cyclobutane pyrimidine dimer- FT DNA glycosylase/abasic lyase)" FT /db_xref="GOA:E1VRX7" FT /db_xref="UniProtKB/TrEMBL:E1VRX7" FT /protein_id="CBT74379.1" FT /translation="MRLWSLHPSLLDAKGLVACWRETLLAQKVLAGQTKGYTGHPQLLR FT FKEQPAPLVHMGGYLQGLWDEAAVRGYRFDAAKILHPAAAAQLEKIPVTQGQVHFEREH FT LLRKLSVRDPARIARLEPAGQVALHPLFVQVPGPVEAWEKDALASG" FT CDS complement(145875..146858) FT /transl_table=11 FT /gene="ddh" FT /locus_tag="AARI_01410" FT /product="diaminopimelate dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.4.1.16" FT /note="catalyses the following reaction: L-2-amino-6- FT oxoheptanedioate + NH(3) + NADPH <=> meso-2,6- FT diaminoheptanedioate + H(2)O + NADP(+). Involved in lysine FT biosynthesis" FT /db_xref="GOA:E1VRX6" FT /db_xref="InterPro:IPR010190" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VRX6" FT /protein_id="CBT74380.1" FT /translation="MTSKIRIGIAGYGNLGRGVQSAIAKNPDMELVGVYTRRDPGTLDL FT AQPAPRFAMDELEQHAGGIDVLILCGGSRSDLPEQGPKFAALFNTVDSFDTHARIPEYF FT QSVDAPAKAAGKTALISVGWDPGMFSINRVFGEALLPDGQTYTFWGRGLSQGHSDAIRR FT VPGVAAGVQYTIPSQEAIDRVRAGQRPSLSTREKHQRECFVVLEDGADAQAVREAIVGM FT EHYFDQYDTTVEFIDEQTLAAEHSNMPHGGFVIRSGNTSDEQKQVIEYSLALGSNPEFT FT SSVLVAYARAAYRMNQSGITGAQTVYDVAPGLLSPKSPAQLRAELL" FT CDS complement(146972..147130) FT /transl_table=11 FT /locus_tag="AARI_01420" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRX8" FT /protein_id="CBT74381.1" FT /translation="MCRQVQCKTCKKTTWAGCGQHVEATMRNVPNKDRCQGHEAEPKKG FT FFKRLFG" FT CDS complement(147158..147439) FT /transl_table=11 FT /locus_tag="AARI_01430" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR003735" FT /db_xref="UniProtKB/TrEMBL:E1VRX9" FT /protein_id="CBT74382.1" FT /translation="MMRTADEATRKRILNRLKRARGQLDAVINAVETDGSCKEVVTQLA FT AVSTALDRAGFAIVSSAMQYCIADPEKASEEEDGLSVEELEKLFLSLS" FT CDS complement(147436..147786) FT /transl_table=11 FT /gene="trx" FT /locus_tag="AARI_01440" FT /product="thioredoxin" FT /function="4.6 Miscellaneous" FT /note="serves as a general protein disulphide FT oxidoreductase. It interacts with a broad range of proteins FT by a redox mechanism based on reversible oxidation of 2 FT cysteine thiol groups to a disulphide, accompanied by the FT transfer of 2 electrons and 2 protons. The net result is FT the covalent interconversion of a disulphide and a dithiol" FT /db_xref="GOA:E1VRY0" 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:E1VRY0" FT /protein_id="CBT74383.1" FT /translation="MKPLELSAANFERFIGNNQMVLVDFWAPWCGPCKRFAPVFELAAE FT AHEGIAFAKVNTETQPELARTMQIASIPTLVAFKNGILVHSKPGALKAAALEPLLMKLQ FT KPVDPPSLPRRE" FT CDS complement(147786..148652) FT /transl_table=11 FT /locus_tag="AARI_01450" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="8 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VRY1" FT /db_xref="InterPro:IPR002781" FT /db_xref="UniProtKB/TrEMBL:E1VRY1" FT /protein_id="CBT74384.1" FT /translation="MEIGPLLILAVALAGVVGLTLGLFGGGGSILMVPLLSYVAGMPGK FT EAIATSLLVVGSTSAASLIPHARKGHVRWAQGLVFATTSMLGAFGGGLLAESIPAQLLM FT LGFALIMLASARGMIRGRKNPGGASLPVWLFAPVGLGIGAVTGLVGAGGGFLIVPALAL FT LAGLSMAQAVGTSLLVITLNSAAALAGQLNSVALHWPLAMSLAVTAILGSLLGARLSHR FT IAEHRLRKGFGYFVLAMGVFVLSQEVPAPGGLAIALIAVFAGLLMLLCRKVPALHARCP FT LAMKSGA" FT CDS complement(148656..149195) FT /transl_table=11 FT /locus_tag="AARI_01460" FT /product="rhodanese domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein domain PF00581. FT Rhodanese has an internal duplication. This HMM represents FT a single copy of this duplicated domain. The domain is FT found as a single copy in other proteins, including FT phosphatases and ubiquitin C-terminal hydrolases" FT /db_xref="InterPro:IPR001763" FT /db_xref="InterPro:IPR021309" FT /db_xref="UniProtKB/TrEMBL:E1VRY2" FT /protein_id="CBT74385.1" FT /translation="MTSALNTMDAAALKCLVDAPDADLALIDVRTAGEFETVHIPGSYN FT VPLEEFTANAAEVLAKIPGTPVLICHSGNRASKAQRALNEQQLGHSTVLIGGVTAYENA FT GGTMVRGVQRWALDRQMRMTAGSLVLAGLLGAKFISPKFAYLSAGIGGGLVFSAVRDSC FT PMISALGKMPWNKVAK" FT CDS complement(149227..150612) FT /transl_table=11 FT /locus_tag="AARI_01470" FT /product="metallo-beta-lactamase superfamily protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00753: metallo-beta- FT lactamase superfamily. Apart from the beta-lactamases, a FT number of other proteins contain this domain. These FT proteins include thiolesterases, members of the glyoxalase FT II family, that catalyse the hydrolysis of S-D-lactoyl- FT glutathione to form glutathione and D-lactic acid and a FT competence protein that is essential for natural FT transformation in Neisseria gonorrhoeae and could be a FT transporter involved in DNA uptake" FT /db_xref="GOA:E1VRY3" FT /db_xref="InterPro:IPR001279" FT /db_xref="InterPro:IPR001307" FT /db_xref="InterPro:IPR001763" FT /db_xref="UniProtKB/TrEMBL:E1VRY3" FT /protein_id="CBT74386.1" FT /translation="MLLERLYDEDLAQASYFIGCQAKGEALVVDARRDISDYLALAAKH FT GMRITAVAETHIHADYLSGTRELAAATGATSYVSGEGGKDWQYGFEAERLMDGDAIVLG FT NLRITARHTPGHTPEHLAYAVTDGAFSKTPGYLLSGDFIFAGDLGRPDLLDEAAGGVDT FT RFQGARDLYASLKKTLAELPDYIQIHPGHGSGSACGKALGAVPSTTLGYEREFAWWSTY FT LANDDQEGFIAELLNGQPDAHAYFGRMKRQNRLGPAVLGELEALEEVPAARIVEQIRSG FT ASAFVDTRGPTQIAEGTVAGALSIPGTAKTASFGAWAYDPEKDERDLIVLADSVEHAAQ FT IRAHLMRVGIDAVKGFTTSLEGLTLVKPKSITPAQLEGFDYAMLLDVRNKTEFAAGHIP FT GATQLSGGRVLWNQDQLPTSGAIVTYCQSGMRNAVAASALRDAGFEIIELQGSYLGWSV FT FAN" FT CDS complement(150733..151185) FT /transl_table=11 FT /locus_tag="AARI_01480" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRY4" FT /protein_id="CBT74387.1" FT /translation="MGIFASRKSIEQDFARMEQRLARAKPMATDKFNVKTQILTKGMRK FT NTPEAGLELGIGTVTAWLSAHETLRLLEGTISILEGWPDSPAEIFISAPASASADSDAG FT AAMAHLPADHLGILHPSSDGELQLLGSLDPLEQKQLHSWLRQFAQG" FT CDS complement(151223..151822) FT /transl_table=11 FT /locus_tag="AARI_01490" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00440: bacterial regulatory proteins, FT tetR family" FT /db_xref="GOA:E1VRY5" 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:E1VRY5" FT /protein_id="CBT74388.1" FT /translation="MQSEAAAKSTRTRSAGATRERILEATSRLFYTQGIRATSADKIIE FT EVGITKVTFYRHFRSKSDLVVAYLGELGEKEREWLQSVHDPSDPAASLGAIAEGIGASS FT CNPGFRGCAFINAAAEYSDPADPVREIIGTHRQWMLEKFADIASDAGVKDPLTAARQFM FT MLRDGAMVNGYLAESADLAQSLKSAFTSVLSAATGK" FT CDS 152015..152365 FT /transl_table=11 FT /locus_tag="AARI_01500" FT /product="OsmC-like protein" FT /function="4.1 Adaptation to atypical conditions" FT /note="identified by match to protein family PF02566: OsmC, FT OsmC-like protein. Osmotically inducible protein C (OsmC) FT is a stress-induced protein found in Escherichia coli. This FT family also contains an organic hydroperoxide FT detoxification protein that has a novel pattern of FT oxidative stress regulation" FT /db_xref="GOA:E1VRY6" FT /db_xref="InterPro:IPR003718" FT /db_xref="InterPro:IPR015946" FT /db_xref="InterPro:IPR019953" FT /db_xref="UniProtKB/TrEMBL:E1VRY6" FT /protein_id="CBT74389.1" FT /translation="MLDVTLETPTSMGGPGGATNPEQLFAAGWASCFHSALKLVAAKRR FT VKIADSTVTAEVSLRKTPEGGFGLEAALQVNFAAGLNKEMADELVDAAHAVCPYSNATR FT GNIPVTLTSVVA" FT gene 152362..152718 FT /pseudo FT /locus_tag="AARI_01510" FT /product="truncated protein" FT /note="N-terminal section of a protein" FT gene 152631..152927 FT /pseudo FT /locus_tag="AARI_01520" FT /product="truncated protein" FT /note="C-terminal section of a conserved protein" FT CDS complement(152924..153577) FT /transl_table=11 FT /locus_tag="AARI_01530" FT /product="GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF00392. This FT family of regulatory proteins consists of the N-terminal FT HTH region of GntR-like bacterial transcription factors. At FT the C-terminus there is usually an effector- FT binding/oligomerisation domain. The GntR-like proteins can FT be divided into six sub-families: MocR, YtrR, FadR, AraR, FT HutC and PlmA. Many of these proteins have been shown FT experimentally to be autoregulatory, enabling the FT prediction of operator sites and the discovery of cis/trans FT relationships" FT /db_xref="GOA:E1VRY7" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VRY7" FT /protein_id="CBT74390.1" FT /translation="MAARLGVVSVVQTIVKSLRARIFSGELAPGTPLGEVDVAAHYEVA FT RPTAKAALENLVASGLLTRNAHQSAKVTLLTSADARDIYRTRAIIEAEAVRLLASTGQV FT PEAARQANAEITALRDASPIDIVDPDVQFHSALVQALQSQRTSSIYDQLSDEIRLCMTH FT VQDATLLNTADIADEHERLLQCIEAGDAHGAAEVLAQHLANASARLAKHLDSLA" FT CDS 153708..156539 FT /transl_table=11 FT /locus_tag="AARI_01540" FT /product="FAD linked oxidase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF02913 and PF01565" FT /db_xref="GOA:E1VRY8" FT /db_xref="InterPro:IPR001450" 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:IPR016168" FT /db_xref="InterPro:IPR016171" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:E1VRY8" FT /protein_id="CBT74391.1" FT /translation="MALSTPALGETTVSSTILDLVGDQDRVKTRSIDRVAYASDASHYL FT YTPQAVVLAKDAAEVSALLTAAAAKGQPVTLRSGGTSLAGQASGDGLMIDVRRNFRGIT FT VLDKGARVRVQPGATVRQVNARLAVYGTKLGPDPASEAACTIGGVIANNSSGMACGTEF FT NTYRTLESMTFVLPSGTMIDTADPEADRKLAAAEPRLVATLDKLLKRVRSNPASVAKIE FT KHFALKNTMGYGINAFLDFDTPAELMAHLIIGSEGTLAFVAEAVFRTVPIRKLAVATLA FT VFDNLDLATRALPELVESGAATLELMDSTSLRVGQSLPGVPDAIMGFDVEQQAALLVEY FT HADTEEELAGLRSAGQSLLDASALRAPAILSPDAKNRQAAWKFRKGLYASVAGARVSGT FT TALLEDVVVPVETLAETCDSLQELFTEYGYEDSVIFGHAKDGNIHFMLTDRFEGDVALN FT RYNSFNDKMVQLILDKDGNLKAEHGTGRAMAPFVRAQYGDELYEVHLELKAACDPRLMM FT NPGVIIDEDHAAHIRNIKLNETIEVEADHCVECGYCEPVCPSKDLTLTPRQRIVVRRAI FT AKAEAEGNTALVAELERDYEYNGVQTCAVDGMCVTACPVGINTGLLVKRLRREDAHPVL FT EAGFKAAAKGWGGATRAGSLALSVADKFPTAVVRGATDLVRKVVSEDLMPRYDADLPGG FT GEARKPMAGNLGAVGTEPLAIYLPACVNSMFGPAGDGEGVAPAFTKLLHAAGVSVYVPE FT GIESTCCGTPWTSKGYEQGHEVMGQRVLEEIRAAMPGKNLPIISDASSCTEGYEHTLAE FT HGYEVVDLLAFTSQHLLDKLPEMQKISSVTLHPTCSSTQMGLNPDMQKIAEAVADTVNT FT PVNWGCCGFAGDRGMLHPELTESATAREAAEVRELDAQEHASCNRTCELGMTRATGKEY FT RHIVELLAEAAGK" FT CDS complement(156622..158082) FT /transl_table=11 FT /locus_tag="AARI_01550" FT /product="HNH endonuclease domain-containing protein" FT /function="3 Information pathways" FT /note="identified by match to SM00507" FT /db_xref="GOA:E1VRY9" FT /db_xref="InterPro:IPR003615" FT /db_xref="UniProtKB/TrEMBL:E1VRY9" FT /protein_id="CBT74392.1" FT /translation="MSEAKAHGSSLTPPAPHEDFDLHMQMVQDDLSAIEEHGSKTECAQ FT GIELLESFISTLRFKQAALGHQLEKEFVRDHEERGIHMDDQTRGAAASVALARRQSPHG FT MRNYLVNCRILFEDTPHLAAACARGEFTEAQAQAILTPLQALKPLRRTEFDQFFAQNPD FT MFESMGTNQIKETVHKFVLSYTSDQESIEQKTVEEQRKLSLKIDHQRGRIMINGEYPLL FT QGMCLKNYLDDESKALRKKGDKRSRAQIRADLLFSYMMIGEPSKMPIALHVGVIMTDRA FT LFAGEREPAYLEGYGFIPAQSVREWISGHQIPNDLTPEQIDAKPDQELIEQLEVRTELA FT RFYTAPGDQDLITMDSKARIFPEKLKKFIAVRDRHCRTPFCDGIVEEIDHVKQYARGGK FT TTVFNGDGRCAACNKAKEAVGWYEYIAFGNGHPIMVCPGSAMSYKSTAPPATGYAHKPF FT PQLRCDSKWMQKLKERLKPHDGPEDLAA" FT CDS 158392..159873 FT /transl_table=11 FT /locus_tag="AARI_01560" FT /product="putative amino acid transporter" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="amino acid-polyamine-organocation (APC) Superfamily FT (TC 2.A.3.y.z)" FT /db_xref="GOA:E1VRZ0" FT /db_xref="InterPro:IPR002293" FT /db_xref="InterPro:IPR004841" FT /db_xref="UniProtKB/TrEMBL:E1VRZ0" FT /protein_id="CBT74393.1" FT /translation="MNRKPSMSSSQATMLGAQLRRRKSIANMITESQTNAGAGQLRRTL FT GMWQLTMISVGATMGTGILVILGDTVPVAGPAIWISFVIAGITALLSAVSYAEMAGMVP FT VSGSSYSYSYATMGEGIAWICGWCLVLEYAVSVAAVAVGAGQYVNETLRTFGMELPQML FT AGGPAEGGVVNLPALIVIALATLLLVRGARESAIVNSIVVAIKAGILIFFSIVAFSAFD FT AGNFEPLLPMGAAGVTAAASSVFFSYIGFDAASTAGEEAKNPKRDLPRAIMLSMLIVTI FT SYVLVAVSAIGAREWNWFEGAQAPLVQIVGELTGRPVFVLIFAVAAVLAIASVVLTVLY FT GQTRILLAMSRDGLVPPVFGKVSARTGTPVAGTWITGILVAITAGFIPLGALADATSIG FT TLFAFALVGASVMYLRKTQPKAERTFRVPLYPITPILGILACLFLMSQLGWHTWAVFII FT WMIVGAAVYLGYGRRRSRLGQMTKQEYAATLADEK" FT CDS 160003..160272 FT /transl_table=11 FT /locus_tag="AARI_01570" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VRZ1" FT /protein_id="CBT74394.1" FT /translation="MSTTGRRDIHLSLTADQADDLISALEAHRGSFERLEKEAGHGFGL FT PAAYWTGRVQEVQELLDAVRRQEPGDDTGLQGEGGAGRELGQAD" FT CDS complement(160295..160765) FT /transl_table=11 FT /locus_tag="AARI_01580" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VRZ2" FT /protein_id="CBT74395.1" FT /translation="MNHSNLRSNATRRITELLNSHAARRHLSTYGWTEGMPVVITEPHE FT LVKDVMGFISTQGRAVLLVLCGGEPDNLQIWHVTVPSPIFPEVPALPAESTMGDLCRRN FT SESRLATFRVGYWAHSAAIHEIPFSIRTQSAPGAESSEHLDLSDSQSDKHQD" FT gene complement(161084..161662) FT /pseudo FT /locus_tag="AARI_01590" FT /product="truncated glycosyl hydrolase" FT /note="N-terminal section of a glycosyl hydrolase" FT CDS 161722..162171 FT /transl_table=11 FT /gene="gntK" FT /locus_tag="AARI_01600" FT /product="gluconokinase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="2.7.1.12" FT /note="gluconokinase catalyzes the phosphoryl transfer from FT ATP to gluconate. The resulting product, gluconate-6- FT phoshate, is an important precursor of gluconate FT metabolism" FT /db_xref="GOA:E1VRZ4" FT /db_xref="InterPro:IPR000623" FT /db_xref="InterPro:IPR006001" FT /db_xref="UniProtKB/TrEMBL:E1VRZ4" FT /protein_id="CBT74396.1" FT /translation="MGELLGGQIKAEFLDGDSMHPKANIDKMASEKPLDDADREPWLGE FT IGRLLAAAGEREPLIIACSALKRKYRDQIREQAPATVFIHLHGSLELLTERMGERAGHF FT MPVGLLKSQFETLEELEPDERGLVLDISASPQQLASQAASWLGNH" FT CDS 162264..162428 FT /transl_table=11 FT /locus_tag="AARI_01610" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VRZ3" FT /protein_id="CBT74397.1" FT /translation="MHSTFGQQHASVREARRSNSSEVQLEVPSSLKEDSLRNPLISAPC FT LGHSFCKTP" FT CDS 162697..164367 FT /transl_table=11 FT /locus_tag="AARI_01620" FT /product="thiamine pyrophosphate binding domain-containing FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein domain PF00205. FT Thiamine pyrophosphate binding domains are present in FT enzymes such as acetolactate synthase, pyruvate FT dehydrogenase (cytochrome), glyoxylate carboligase and FT phosphonopyruvate decarboxylase" FT /db_xref="GOA:E1VRZ5" FT /db_xref="InterPro:IPR011766" FT /db_xref="InterPro:IPR012000" FT /db_xref="InterPro:IPR012001" FT /db_xref="UniProtKB/TrEMBL:E1VRZ5" FT /protein_id="CBT74398.1" FT /translation="MSSVSAAISHALKPIAPQIFGLMGNGNAHFLDAAVRAGFDYTAVR FT HESAAVSAADAYFRISNKLAIASTTYGAGYTNTITALAEAAAARTPLLFITGDAPTTGL FT RGWDVDQAAIDAGVRAARYVVDRHTPGATAMEAAAHALRERLPVVLAIPYDLAAADSLE FT EQLPDFASLRSTPPAPQLNSTQLEQIAQKLNASERTHILYGRGAIDAATHVKDLAQKLD FT ATTSGTLLARDLLDYEFDLGITGGFSTEANARIIAQADTVLVLGASLNQFTMRFGDLIA FT ADATLIQVDLGSTATNPRVDYFATADSALAAADLLEAVDPAAGGWRSSLDLSNLRSRPA FT GDEQAADGQLDPRRVASELEQILPANRLLVQDGGHFIGWGPMYWSTTGARSVSCVGTAY FT QSIGLGIASMVGAAPAADGRTVVLAAGDGGFLMGLADLESIVRTVESGVIVIYNDSAYG FT AEIHQYGSIGLHEDPMLIPTVDFAGIANAMGATGIRLDTLEDLAGVRQWVQAGARGVCL FT VDARVSTHVRAPYMEEVLAANKKAAAASGLQSGKGAGKR" FT CDS 164390..165478 FT /transl_table=11 FT /locus_tag="AARI_01630" FT /product="hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1) with cleavage site probability 0.973 FT between position 26 and 27" FT /db_xref="UniProtKB/TrEMBL:E1VRZ6" FT /protein_id="CBT74399.1" FT /translation="MRKLLVGTASLGLGALLMFPAAAAFAVPSGTGDETGASSAQLSET FT SLRVATIQANLSGETPEQLPADLLRGSDRQAGQVADKISRANADVVVLTEMDATQEAVD FT AFNDQYLQNPDDGRADVEYEYSYLAVGSKGLQSGADLNADGVIGSAEDAWGQGAFAEQG FT SIVVLSKYPIAQDQVTGVSQLRWQEVAHDMMHHTDFSGVLAASIPVMSTGLWDIPIQYR FT GEPVHVLATQTQPDAQDQEFADARLADELKVINGYLAGEDYIRTDEGRQAEGVGEDRYV FT IAGALGLQEGAADRVEPFLAGLDRENALHDSGSYLVPSQAWQVLGQGRIQEHQPSISQP FT ISGTVPNLVEESTPLLWTDIQF" FT CDS complement(165475..166776) FT /transl_table=11 FT /locus_tag="AARI_01640" FT /product="putative FAD-linked oxidoreductase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family TIGR01679. FT This entry identifies a family of bacterial oxidoreductases FT with covalently linked FAD, closely related to two FT different eukaryotic oxidases, L- gulonolactone oxidase FT (EC:1.1.3.8) from rat and D- arabinono-1,4-lactone oxidase FT (EC:1.1.3.37) from Saccharomyces cerevisiae" FT /db_xref="GOA:E1VRZ7" FT /db_xref="InterPro:IPR006094" FT /db_xref="InterPro:IPR007173" FT /db_xref="InterPro:IPR010032" FT /db_xref="InterPro:IPR016166" FT /db_xref="InterPro:IPR016167" FT /db_xref="InterPro:IPR016168" FT /db_xref="InterPro:IPR023595" FT /db_xref="UniProtKB/TrEMBL:E1VRZ7" FT /protein_id="CBT74400.1" FT /translation="MSTFKNFARTVHAHPAAINRPRSVTELSQYLQQAAARHQPVRTVG FT AGHSFTPLVHTDGVLLNLDGFQGIEEVDAFTHEVLFRAGTRLWQVPALLKPFHLALENM FT GDIDRQSIAGAISTGTHGTGLKFTGLSAAVTGVQIMLADGSHVRASSQENPELFEASRL FT GLGALGVLTHVRMRCVPHFMIHAAESIEPIGQIAESFMDRARHEDHLEFFWFPGTSKAQ FT VKINTRLDGQSPAKKPNPVAQWLNDELLSNGALQLLSSVSAAVPGSTAKLNAVACAALS FT DRSSIAPWNEAFTSPRRVRFTEMEYALPLDAFAEAFTRVRGYFERNGVEVFFPIEVRTA FT AADSTWLGTATGRDSVYIAVHRYIRDQAPGYFAAMEEIFRSLGGRPHWGKEHSLQAAEL FT AQLFPKFSDFTRLRETLDPQGLFLNPYLRELLGA" FT CDS complement(166773..167963) FT /transl_table=11 FT /locus_tag="AARI_01650" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR001608" FT /db_xref="UniProtKB/TrEMBL:E1VRZ8" FT /protein_id="CBT74401.1" FT /translation="MKNAQAKRYNHALKSAGISEHPVALLDLDAFDSNLIALRERASGV FT PIRVASKSLRVRKALERALDEPGFRGVLCFTLAEALWLASHGLRDLVVAYPQTDAEAIS FT RWAASEQAREEVTLMVDTEEQLDLIDRIAPKHGPLKVALELDAAYYPSSNWRIGAARSP FT LTRPAQVAELAAEVHRRPNFILDGLMGYESQIASVPDGGFSPKALVSRKLRQRSAAELA FT QRRAETVELVRNLGDLRFVNAGGTGSVESTVQEPAVTEIAAGSGLFAPALFDSFRAFRP FT APALFLGFPVVRRPDEQTVTILGGGWVASGPSGKDRLPKIEHPKKLRLLALEGAGEVQT FT PLTGPAAHRIAIGERVWLRHAKAGEPAERVNKVAVYGQGKIIEQWPTYRGEGKAFL" FT CDS 168077..168841 FT /transl_table=11 FT /locus_tag="AARI_01660" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VRZ9" FT /protein_id="CBT74402.1" FT /translation="MKNDPISMTLLGKDGKPRSGVQDAIMKGIGVQRPLVLAYIKRLRK FT KHPEATTAQLAAIAERDYLRVVTGSGAAVGGTAAVPAVGTGAALGLSVAATLGFLEASA FT LYAQSLAELHGIAIDDPDRSRVLVMGIMMGEEGSSMISGLTSQVAGRGGGPIQGWARSF FT GVGKSKTVYSSVQRALQKKFLRKIIGTQAASTLGRLVPFGVGAAIGGVGNRYMAKRVIE FT NAGVAFAGIPTIAPSSLPLDDPRVIEAEIVED" FT rRNA 169443..170961 FT /locus_tag="AARI_36380" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 171595..174717 FT /locus_tag="AARI_36390" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 174874..174989 FT /locus_tag="AARI_36400" FT /inference="ab initio prediction:rRNAScan:1.0" FT CDS 175227..175784 FT /transl_table=11 FT /locus_tag="AARI_01670" FT /product="RibD domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF01872. This domain is FT found in the C-terminus of the bifunctional deaminase- FT reductase in combination with PF00383 as well as in FT isolation in some archaebacterial proteins" FT /db_xref="GOA:E1VS00" FT /db_xref="InterPro:IPR002734" FT /db_xref="InterPro:IPR024072" FT /db_xref="UniProtKB/TrEMBL:E1VS00" FT /protein_id="CBT74403.1" FT /translation="MEHLTFAINVTLDGCIDHRVGIADDETHEYFTGLMDEHGAMLWGR FT TTYEMMEEYWPLVASGEVEAPQALLDWALKLQDKSKYVVSAQRADFPWNNSHYLIGNLR FT TSVQELIERVPDGVLLGSGQLATALDQLGLIDEYRFLVHPIIAGHGPRLYDAGLPASRR FT LELGETMSLGNGVIAAHYRRAQ" FT CDS complement(175843..177330) FT /transl_table=11 FT /gene="mtlK" FT /locus_tag="AARI_01680" FT /product="putative mannitol 2-dehydrogenase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="1.1.1.67" FT /note="mannitol 2-dehydrogenase catalyzes the NAD- FT dependent reduction of mannitol to fructose" FT /db_xref="GOA:E1VS01" FT /db_xref="InterPro:IPR000669" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR013118" FT /db_xref="InterPro:IPR013131" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR023027" FT /db_xref="UniProtKB/TrEMBL:E1VS01" FT /protein_id="CBT74404.1" FT /translation="MKLNNRTLTQLDPQVGTPQYDRNKATAGIVHFGVGGFHRAHQAMY FT LNRLMNQGKALDWGIIGMGVMESDQRMRDVLSASDGLYTLVVKNPDGSREVEVIGSILG FT FLYAPDDLDAAIEQLADPAIRIVSLTVTEGGYNVHPVTGEFDLGNQAIAADLANPRAPR FT TTFGLISAGLRLRRERGIAPFTVMSCDNIQGNGEVAHQMFGAFATALDPEFGDWVQENV FT SFPNSMVDRITPVTTDADRADVAERYGIEDGWPVVCEDFEQWVLEDKFVAGRPPYEEAG FT VQLVDDVVPYELMKLRLLNATHQGLCYFGHLAGYRAVHDVARNALFADFLLSYMKNEAE FT PTLRELPGVDLDAYQHKLIERYSNEYVADTVARLCADSSDRIPKWLMPVVRENLAADRD FT VTLSAAIVASWARYAEGTDESGEAIAIVDRLAEEVHAAASNHSDDPLAFLRQRDLFGDV FT VDDERFTAPYLKTLESLHEHGSLATLAELIGQKATTR" FT CDS complement(177368..178693) FT /transl_table=11 FT /locus_tag="AARI_01690" FT /product="putative polyol transporter" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="major facilitator superfamily, polyol porter (PP) FT family (TC 2.A.1.18.z). Possible mannitol transporter" FT /db_xref="GOA:E1VS02" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VS02" FT /protein_id="CBT74405.1" FT /translation="MNSHPLPAPPSTSTSILDKLGLPRPLLWGFVGLMIFMIGDGVETN FT ILAPYLTGEHGFSIPLAGTLVTIYGVAVAIAAFLSASLSDLWGPRKVMFIGAGIWVVFE FT LLFLGVALHSSSMPLIFIAYGLRGFGYPFFAYGFLVWISATANAKRLAVAIGWFYVAFS FT SGLPTLGALTASASLEIFSLSYYQTLWVSLALVVIGAAIALIGVKEKTGRAALVSNPEE FT VFKTMSFGLRLLASNRKALLVMLTRTINSVPTYGMAVFFPALFVDRFGWSVGQFLILTT FT VIYAVNIPFNLFFGALGDKLGWSKVVVWFGAVLCAISMAALYLVPAWAVDHGYSFAYAL FT TLVIGAVFGIGLAGFVPLSAIAVSLAPEHPGAAMASYNLGIGAAVFAGPLLVALLYNVL FT GASGMVFLFAALYLVAAIMSHALRGTQPGFHGVQQPATIAAH" FT CDS 178833..179669 FT /transl_table=11 FT /locus_tag="AARI_01700" FT /product="DeoR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="DeoR-like transcription repressors occur in diverse FT bacteria as regulators of sugar and nucleoside metabolic FT systems. The effector molecules for deoR-like regulators FT are generally phosphorylated intermediates of the relevant FT metabolic pathway" FT /db_xref="GOA:E1VS03" FT /db_xref="InterPro:IPR001034" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014036" FT /db_xref="InterPro:IPR018356" FT /db_xref="UniProtKB/TrEMBL:E1VS03" FT /protein_id="CBT74406.1" FT /translation="MAYNESDVKNDAPDAVQGLPPETRREEITGHVNKSRSCRVEELAE FT IFGVSAMTIHRDLEQLAKEGRVERIRGGARAITARLAERDVRLRRHLNAEVKRQLAATA FT AQLIERNSVIALDDSTTIGALGSYLEEREPSTVITHSLALMGAVSAMAHIDMVGLGGQY FT YAETDSFLGSIVVEQAQRLMADAVFVSTTAIKNQALLHPDAEAARTKRSLLQMGRRKIL FT VMDSSKFESAGIYHVMDLAEIDDVVIDDQLDQRLMSELQGLGPRIHIVRTSAKEQP" FT CDS 179666..181054 FT /transl_table=11 FT /gene="xylB" FT /locus_tag="AARI_01710" FT /product="xylulokinase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="2.7.1.17" FT /note="catalyses the following reaction: ATP + D-xylulose FT <=> ADP + D-xylulose 5-phosphate. Involved in the FT catabolism of xylose" FT /db_xref="GOA:E1VS04" FT /db_xref="InterPro:IPR000577" FT /db_xref="InterPro:IPR006000" FT /db_xref="InterPro:IPR018483" FT /db_xref="InterPro:IPR018484" FT /db_xref="InterPro:IPR018485" FT /db_xref="UniProtKB/TrEMBL:E1VS04" FT /protein_id="CBT74407.1" FT /translation="MKPTYVLGIDSSTQSCKALLVDAQSGEVVAEQRSSHLPGTQIDPQ FT HWVTALETATTGLLEQASAVSIAGQQHGMVALDEHGQPVREAMLWNDTSSAQQAKELTE FT ELGGAQACAEKIGSVPVASLTVTKLRWLRDHEPENASRTTQVLLPHDYLTWHLGGRKEA FT VTDHGDASGTGYYDPAARRFLPDLAADALGHSVQLPRLAQANEQVGRTSTGAVIGAGTG FT DNMAAALGLDLQPGDVCISIGTSGVASAVVEDSVHDGSGMVTGFVAANGKFLPLACTLN FT GAPVLDFGARMLGVGKQEFSDLALAAEPGSGGVVLLPYLGGERTPNRPEATGLLQGLRG FT TTTREQIARAYVEGLLCSMKDAVAALEASTKVATKRILLIGGGAQAEAVRVIAPQIFGV FT AVDVPRTAEYVALGAARQAAWALGGQEQPPVWDIAESTRYQARPRPEIYAGYAKLRDAT FT EGWN" FT CDS 181081..181950 FT /transl_table=11 FT /gene="glpQ" FT /locus_tag="AARI_01720" FT /product="putative glycerophosphodiester phosphodiesterase" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.4.46" FT /note="glycerophosphoryl diester phosphodiesterases display FT broad specificity for glycerophosphodiesters; FT glycerophosphocholine, glycerophosphoethanolamine, FT glycerophosphoglycerol, and bis(glycerophosphoglycerol)" FT /db_xref="GOA:E1VS05" FT /db_xref="InterPro:IPR004129" FT /db_xref="InterPro:IPR017946" FT /db_xref="UniProtKB/TrEMBL:E1VS05" FT /protein_id="CBT74408.1" FT /translation="MDTLFFAHRGSSHKYSENTRAAYLQAIDEGADGIECDVHLSKDGL FT VVCHHDPTVDRTSDSTGLVAEYTLAELKAMDFTGVVPSVLPAGYGAENEQLLSLDELFE FT LIEAHGKSVGLAIEIKHPSPYGHLLEKTVLQVLAAHGFDPQTGTAGSRGQISVTLMSFE FT PNSLRYLARTVNTSLLCQLMTEIHPERVQQLIDSGDLVRAGVYEVLYRSVAEGIELINA FT GGAGIIGCGVAWTRANEHLVRRWLEQGLKARVWTIDRPADAQFLVGLGVGELTSNRPAE FT LRKELEQG" FT CDS 181956..182639 FT /transl_table=11 FT /locus_tag="AARI_01730" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VS06" FT /db_xref="InterPro:IPR002318" FT /db_xref="InterPro:IPR012947" FT /db_xref="InterPro:IPR018163" FT /db_xref="UniProtKB/TrEMBL:E1VS06" FT /protein_id="CBT74409.1" FT /translation="MNDHAIEQDNLYLQDTYVFTTRATVIATGSSEDGQWIALSPNIFH FT PRGGGQPEDSGTVDGQPVAVQRDEAGLVVLYGADTKAVGEEVTAEIDAALRLSHAALHT FT AGHVLGFAGEDRGWQHKGHSHFPGQSRLDFDPASVDLPLGDEHERAAAREWIQARVNEL FT IAGGGEIATTTDEQGIRTVSIAGVNAEPCGGTHVKHPNQLRQVEIGEAKVKRGVYKVRY FT DAHVG" FT CDS 182662..183351 FT /transl_table=11 FT /locus_tag="AARI_01740" FT /product="AzlC family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF03591" FT /db_xref="InterPro:IPR011606" FT /db_xref="UniProtKB/TrEMBL:E1VS07" FT /protein_id="CBT74410.1" FT /translation="MGLSIAFATGLYGISFGALSIAAGLNLWQTVALSALMFTGGSQFA FT FIGVISGAGAPSAAFSAASLLGIRNAVYGMQIKQTLRPLGRHVPWMAQVTIDESTAVSL FT GQSDPAEKRRGFFTAGVGVYVLWNLFTLVGALLGERMGDPAAWGLDGAAVAAFIGLLWP FT RLKSVEPIMIAIAAAILTALAVPVTSPGLPILLTAGCAAIYAVATGRRAPAATEHGDLE FT SVEEERA" FT CDS 183348..183665 FT /transl_table=11 FT /locus_tag="AARI_01750" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR008407" FT /db_xref="UniProtKB/TrEMBL:E1VS08" FT /protein_id="CBT74411.1" FT /translation="MSELSWWILAACLTAYALKLCGYFVPRKVLDSPTMSNVAATLTIA FT LLASLVTVNAFTSGQELVIDARIGALAAAILALSFKAPYLVVVVTGALAAILLRATGLA FT A" FT CDS 183718..184038 FT /transl_table=11 FT /locus_tag="AARI_01760" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR002767" FT /db_xref="InterPro:IPR016198" FT /db_xref="UniProtKB/TrEMBL:E1VS09" FT /protein_id="CBT74412.1" FT /translation="MIVAFSVAPSNDNPNGSVHDAVAEAVKVVRDSGLPNRTSSMFTEI FT EGEWDEVMEVVKQASMAAGRFGSRVSLVLKADIRPGYEGELDGKLQRLEKAIEDSEERA FT SS" FT CDS 184035..184724 FT /transl_table=11 FT /locus_tag="AARI_01770" FT /product="putative O-methyltransferase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /EC_number="2.1.1.-" FT /note="match to PF01596. This family includes catechol o- FT methyltransferase, caffeoyl-CoA O-methyltransferase and a FT family of bacterial O-methyltransferases that may be FT involved in antibiotic production" FT /db_xref="GOA:E1VS10" FT /db_xref="InterPro:IPR002935" FT /db_xref="UniProtKB/TrEMBL:E1VS10" FT /protein_id="CBT74413.1" FT /translation="MIHHSADHHAAAVDEYLEQRLGLRIDALEAGREHAHNAGLPRIEV FT SPAQGKFLQLLVEITGARRVLEIGTLGGYSTSWLAKGVGESGTVISCEFEPLHASIARE FT NLQRAGLSERVEIKLGAAQGSMESLISRKSAPFDLIFIDADKRNNVRYLELAMDLARPG FT TVVVLDNVVRSGAILDAVADHGTQEADVRGVQDSLQWLRDDPRVSATALQTVGAKGWDG FT FALARVL" FT CDS complement(184729..185082) FT /transl_table=11 FT /locus_tag="AARI_01780" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VS11" FT /protein_id="CBT74414.1" FT /translation="MTGGLVGSLTLTISLSSTFWVILLGCVLLAAGFSILARFERFWGP FT AEPDHYYYIIPMLVGPVVAGLVRNTDFALWVGPPIGVLCGLGVYFLIMKSPPFKPEESE FT ELEIELHDHHRIR" FT CDS 185251..185766 FT /transl_table=11 FT /locus_tag="AARI_01790" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VS12" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VS12" FT /protein_id="CBT74415.1" FT /translation="MPQMNDYRIRLAAEEDVRPALQMKLQAWREAYATLRDESFFAHHE FT GQLDGQVAWWERGLASGAQFFIAEDRDGRIIGLAGGTPAIEEDQDAGVGIEVGMLYVLA FT EYYGTGLGKHLFDVVIGEQDALVWVMQGNDRARSFFAKQGFTHDGTSEALVGSWQGLIE FT ERMVRARG" FT CDS 185783..186586 FT /transl_table=11 FT /locus_tag="AARI_01800" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR001045" FT /db_xref="UniProtKB/TrEMBL:E1VS13" FT /protein_id="CBT74416.1" FT /translation="MLGEFPIDTGTAIIEADAYGASRYILKVNGVPSSHVDLEDPNYLD FT FEYMRWMEPVFTIGMPAEQFDGRARKLRVLHLGGGGCSMARWVAANYENARQVVVELDA FT KLAELVRVHFEIPRAPLVRLRVGDAAQVLPTLSDASRDVIIRDVFAGSTTPRELTTVAY FT AREAQRVLDAGGVYLMNCGDTADLAGAKAEAATLLEVFEHVAMIADPPMLKGRRYGNIV FT FLASDEPLKLGPAFERSLRTAPLPAQLVAGDAVRRFAVGATAITD" FT CDS complement(186583..187092) FT /transl_table=11 FT /locus_tag="AARI_01810" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR018656" FT /db_xref="UniProtKB/TrEMBL:E1VS14" FT /protein_id="CBT74417.1" FT /translation="MNQQLNTTGQWIQVAAGLKNPSMRRLLGAVLSGEGTGEAPGKSER FT KDLERWASIGLLRQEPSGWVLNDELLEQTLASAAAAKADRTGIRRYFDGHRLHTLPAKP FT ADRHEVLVYLRNAVIDAKEELREEQINERLRVFHPDVALLRRYMVDHSLLLRAADGSGY FT RKGSEN" FT CDS complement(187183..188634) FT /transl_table=11 FT /locus_tag="AARI_01820" FT /product="putative purine transporter" FT /function="1.2.6 Transport/binding of nucleosides, FT nucleotides, purines and pyrimidines" FT /note="major facilitator superfamily, AzgA family purine FT transporter (TC 2.A.1.40.z)" FT /db_xref="GOA:E1VS15" FT /db_xref="InterPro:IPR006043" FT /db_xref="UniProtKB/TrEMBL:E1VS15" FT /protein_id="CBT74418.1" FT /translation="MSSSTKTASGTTMGARIDRYFKISERRSTFSTEVRGGIATFFAMS FT YIVVLNPLVLSGADSSGGELGIQRVAAVTAFVAGILTIIMGIWARHPFAMATGLGVNAF FT VAITVATNPELTWADVMGLVLIAGVVMFGLVLTGFRTAVFNAVPAGLKTAIVVGIGMFI FT ALIGLVNAGFVQRLPDAANTTVPVGLGFDGELLGWPILVFIVGLLLTMTLVVRKTKGAI FT LIGIVVSAVLANILESVFHIGEFESRSWSLVVPSMPDWTLPDLSLIGQVSIFGAFSKIG FT VTAASLLAFVILLSIFFDAMGTMVGLASEAGSMDENGQIPDVDKVLLVDAAGAIVGGGT FT SSSSAQIFVESGAGIGEGARTGLASVVTGLLMIVAMFLSPLIYLVPFEAVAPALVVVGF FT MMITQVSKIDWNDWGIALPAFLTFTLMPFTYSIANGIGAGFISYVFIRATQGRAKEIHP FT LMWVVSAAFVLFFGIGLIEMWVGVK" FT CDS 188804..189781 FT /transl_table=11 FT /locus_tag="AARI_01830" FT /product="universal stress family domain-containing FT protein" FT /function="4.1 Adaptation to atypical conditions" FT /note="identified by match to PF00582: universal stress FT protein family. The universal stress protein UspA is a FT small cytoplasmic bacterial protein whose expression is FT enhanced when the cell is exposed to stress agents. UspA FT enhances the rate of cell survival during prolonged FT exposure to such conditions, and may provide a general FT stress endurance activity" FT /db_xref="GOA:E1VS16" FT /db_xref="InterPro:IPR006015" FT /db_xref="InterPro:IPR006016" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VS16" FT /protein_id="CBT74419.1" FT /translation="MSDEAPVAAEKIEGIVVGVDGSQQSKCALRWAEREAVRRGSVLNI FT VSAYTIPVFAASSMDAGYSTLDDDLIRGGAEDIVRQARADLEGSTATIRTYIESGDPSG FT VLLDLSQDAELVVVGTRGRGGFVGRLLGSVSSALPAHSKCPTVVVPLAMAKEQEDAGAA FT VASDRNCIVVGVDGSDRARSAVLAAADAAMAGSLTLRLICAVPPMGAALAWMPATVDQE FT AVLEDVRYQMSVGTKWLASHYPDLKMETDVVSGPPVEVLIRESEHAVLTVTGSRGRGGF FT TGMLLGSTSQGVLHHSKGPVMVVPDSEDPRLEDRKDFDTRAQEQ" FT CDS complement(189859..191556) FT /transl_table=11 FT /locus_tag="AARI_01840" FT /product="hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="Signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.432 FT between position 29 and 30" FT /db_xref="InterPro:IPR000064" FT /db_xref="UniProtKB/TrEMBL:E1VS17" FT /protein_id="CBT74420.1" FT /translation="MATRHTLGVAASTLALAVSCLAGALPASASTSASFPASVAIAAAP FT SSSALPSEAEVQEAKKDKASTNAMIARIEASLASSRAELQRVETEAAQAQESLLTAGEE FT RDLRTAAAEKAVEQLDYAKTYLEQSRQDLGAIASDIYRNGAGTSTLSLLLDDDQEGDLF FT YKAATIDALSEQKVQSVNTATEAEGLVSAWQEYADAAQSAAEEAAANYDAAAATANSTL FT STYEAAIEPEQQLRDELIGHLATLKQKEEAEVRKAVEKREAQEQEEALKEAIAEEETTK FT VPEPTEDSVQPLSVEKPQELEQTEPETESVKPKPEKVEAEAAEPKPAPSVEPTKSAEPK FT PTKTAEPKPTKSAEPKPTKTAEPKPTKTAEPEPTKTAEPKPTKTAEPKPTKTAEPKPTK FT SAEPKPTKTAEPKPEPKPKVTPKATPKPTPKPEPKPEIAPQSSNYSAAISWALNTAADP FT SKYYVYGANGPDAFDCSSFSQRAFGKSGINLPRTSSQQFASAPQYVSLSNLRVGDLVFS FT SSNGGSSFYHVAIYIGNGQVVHARNPSVGISVTPLSYVNNLYPKAARY" FT CDS complement(192227..192598) FT /transl_table=11 FT /locus_tag="AARI_01850" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PS00142 pattern: neutral zinc FT metallopeptidases, zinc-binding region signature" FT /db_xref="InterPro:IPR010428" FT /db_xref="UniProtKB/TrEMBL:E1VS18" FT /protein_id="CBT74421.1" FT /translation="MLFEMGDDEFQALVEQAIEAIPKAAFAMMDNVIFFIEDEYTPLPG FT EPKNPEILGLYEGIALTERDLDWGAGALPDRITIFKNPTLRACETREDVVREIGITVMH FT EVAHHFGIDDAKLHDLGWS" FT tRNA 192736..192811 FT /locus_tag="AARI_36410" FT /product="transfer RNA-Glu" FT /anticodon=(pos:192770..192772,aa:Glu) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 192863..192936 FT /locus_tag="AARI_36420" FT /product="transfer RNA-Asp" FT /anticodon=(pos:192897..192899,aa:Asp) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 192986..193058 FT /locus_tag="AARI_36430" FT /product="transfer RNA-Phe" FT /anticodon=(pos:193019..193021,aa:Phe) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 193120..193193 FT /locus_tag="AARI_36440" FT /product="transfer RNA-Asp" FT /anticodon=(pos:193154..193156,aa:Asp) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(193247..194101) FT /transl_table=11 FT /locus_tag="AARI_01860" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VS19" FT /protein_id="CBT74422.1" FT /translation="MTPKMTGPAAELTAATAHLRVYEPLDTFEDWAQSIILRTPQRTAE FT QWDAFENERLWSRTLRNVSDPYPHNEPEFFRSAKILDYQGTEHTRYCPGQLQARSLLAA FT EQAEEAMRAEVFDLLVPPVARQANSQRVDTDRLANDLTHLHTRTSSWGIPLGWFALFRE FT DDEHDVVPNGEHLKTVRIYASYEQAIDRLAWAVQALATHAPQSQLFEELGNLGSWLEAF FT DSRSLIELDYGLLAEIVWPDDSASDLMHGIQALEDEDMTSAAAAYRRLSNRWIGPRQLG FT RAN" FT CDS complement(194104..194904) FT /transl_table=11 FT /gene="xthA" FT /locus_tag="AARI_01870" FT /product="exodeoxyribonuclease III" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.1.11.2" FT /note="removes the damaged DNA at cytosines and guanines by FT cleaving on the 3 -side of the apurinic/apyrimidinic sites" FT /db_xref="GOA:E1VS20" FT /db_xref="InterPro:IPR000097" FT /db_xref="InterPro:IPR004808" FT /db_xref="InterPro:IPR005135" FT /db_xref="UniProtKB/TrEMBL:E1VS20" FT /protein_id="CBT74423.1" FT /translation="MKIATWNVNSLRARADRVEDWLRRTDVDVLAIQETKCKDDNFPWE FT LFENNDYEVAHFGVNQWNGVAIASRVGLENVERTFPGQPEFGKGGKNPIQEPRAIAATC FT GGVRIWSLYVPNGRALDDEHMGYKLNWLDVLKKESAGWLEENPQAQIALMGDWNIAPKN FT EDVWDIDFFVENNLTHVSAPERAAFAAFEDLGFTDVVRPHTEGEYTYWDYTQLRFPKGE FT GMRIDFSLTSPALTARVIGASIDREERKGKGASDHAPVIVELAD" FT CDS 195010..196062 FT /transl_table=11 FT /locus_tag="AARI_01880" FT /product="putative enoyl-CoA hydratase" FT /function="2.4 Metabolism of lipids" FT /EC_number="4.2.1.17" FT /note="enoyl-CoA hydratase catalyzes the hydratation of 2- FT trans-enoyl-CoA into 3-hydroxyacyl-CoA" FT /db_xref="GOA:E1VS22" FT /db_xref="InterPro:IPR001753" FT /db_xref="UniProtKB/TrEMBL:E1VS22" FT /protein_id="CBT74424.1" FT /translation="MPEILTERRGLLGLITLNRPKALNALNADMCRTILDALLEWKDDP FT NIAQVAVMGAGERGLCAGGDIVAIHRDILDRSGASADFWRIEYQLNVMIDEYPKPYIAL FT MDGIVLGGGIGISAHGSHRIVTETSRCGMPEVGIGFFPDVGGTHLLARAPHAAGRLAAL FT TGIKFGAADTISLGLADSYVPRDRLESLLADLETRPVVDVLANYAEIPEPGFLQEEWVQ FT AFEEPSTPAVLLALEQYGTAPARDAQQALKAACPSSVRLVEELMRLAGADLRTDLQREY FT RAAVNRLDDPDLAEGIRAAVIDKDRNPQWTDAIPSMSHEQRTQRHLAPLPGAELNFALL FT GKDLEEKSRS" FT CDS 196059..196955 FT /transl_table=11 FT /gene="mmsB" FT /locus_tag="AARI_01890" FT /product="3-hydroxyisobutyrate dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.1.1.31" FT /note="catalyzes the NAD-dependent, reversible oxidation of FT 3-hydroxbutyrate to methylmalonate. Involved in the FT catabolism of valine" FT /db_xref="GOA:E1VS21" FT /db_xref="InterPro:IPR006115" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR011548" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR015815" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VS21" FT /protein_id="CBT74425.1" FT /translation="MSAKPVIGFLGMGHMGLPMAINLHKAGYVLKGFDVVPAAVQAAQD FT AGIQTVATGAEAAVDVDIVLTMFPSGKHVLDAYREYLLESAKPNTLFLECSTIDVSQAR FT EAAALAVEAGHRSADAPVSGGVVGAEAGTLTFMLGAQGEDLEEITSVLDHMGKRIVHCG FT GYGAGQAAKVCNNMLLGISMIGAAEAFVLGERLGLEHQALYDVISSASGQCWAVTTNCP FT VPGPVPASPANRDYQPGFAAALMAKDLGLASSALEHTDTDAQLGSLAAALYRKFSEEGN FT SGTDFSGIINAIRDGSL" FT CDS complement(196950..197453) FT /transl_table=11 FT /locus_tag="AARI_01900" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VS23" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR023187" FT /db_xref="UniProtKB/TrEMBL:E1VS23" FT /protein_id="CBT74426.1" FT /translation="MTSPLPRDPIAQAREQWISHGWTAEADSMAAITAVMRTASIYLQR FT ADAILKPHGLTFARFEVLALLGFSKRGSLPMSRASQLLQVHATSLTNSVDRLEATGLVR FT RIAHPTDGRTRLLELTAAGQQVLSAARDDLNEKLFAQSNLSGTDATELFEILARLRKAS FT GDFL" FT CDS 197710..197913 FT /transl_table=11 FT /locus_tag="AARI_01910" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VS24" FT /protein_id="CBT74427.1" FT /translation="MKMSFNGWYSAIVIAAGLGFAAIALTAYATGQNFLIFVGMGIFMA FT ICMTMTSIQAQRQHKLRKASGK" FT CDS 197910..198350 FT /transl_table=11 FT /locus_tag="AARI_01920" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VS25" FT /protein_id="CBT74428.1" FT /translation="MSDDKQMSPEEQLAALGIAQRSMQHASEFGARLLGTYVIILGLLF FT GALAALLQVYSPEANFVGFMVITALFVVGVVAMSLAYARLYRSLPRGYSKKYLRGFILS FT LVLYAVAVALIAAGPMGWGMTVLIGLVVAAPLCLTGIAMVRK" FT CDS 198347..198646 FT /transl_table=11 FT /locus_tag="AARI_01930" FT /product="putative ArsR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF01022: bacterial regulatory FT protein, ArsR family. ArsR-family transcriptional FT regulators include several proteins that appear to FT dissociate from DNA in the presence of metal ions" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VS26" FT /protein_id="CBT74429.1" FT /translation="MSAHARERLNDDFSNPVRLSLMGSLHAVDEADFKSLKEAIGISDS FT VLSRHLSALEAAGYVHIKKGYVGKRPRTWAKLTSSGHQAFAQHVQALKEITGLV" FT CDS complement(198650..199474) FT /transl_table=11 FT /gene="nadE" FT /locus_tag="AARI_01940" FT /product="NAD(+) synthase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="6.3.1.5" FT /note="catalyses the final step in de novo nicotinamide FT adenine dinucleotide (NAD+) biosynthesis, an amide transfer FT from either ammonia or glutamine to nicotinic acid adenine FT dinucleotide" FT /db_xref="GOA:E1VS27" FT /db_xref="InterPro:IPR003694" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR022310" FT /db_xref="InterPro:IPR022926" FT /db_xref="UniProtKB/TrEMBL:E1VS27" FT /protein_id="CBT74430.1" FT /translation="MRELQAKIIEELGVRPEIDAAEEIRRRIDFLKDYLAATGAKGFVL FT GISGGIDSTLAGRLAQLAVEEVREAGGNARFVAARLPHGKQRDAADAQAAMDFVAADEQ FT FEINIEKPVAAFDEALADAGHKALSDFNRGNVKARARMIMQYALAGDRGMLVLGTDHAA FT ESVTGFFTKFGDGGADLLPLAGLNKRQNQALLRELRAPQQLWAKEPTADLLDGQPLRAD FT EDELGLTYPQIDDYLEGREIDPAAAEAIERRFTGSRHKRTVPATYWDKWWRS" FT CDS complement(199568..200005) FT /transl_table=11 FT /locus_tag="AARI_01950" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VS28" FT /protein_id="CBT74431.1" FT /translation="MNAKRPLGYWLKLVDSLIDEQFAATLEEHGVTRRQWQVLNLLEQQ FT PATEAQLGAGLSPFFASPDEPQSLKEHLAELVESGWIAAENGEYSITDRGHTSLLKLSE FT LVEKIRTQFGQDLDGSEYDAVVETLEKIARNLGWEPEQDQQ" FT CDS 200045..200602 FT /transl_table=11 FT /gene="pyrE" FT /locus_tag="AARI_01960" FT /product="orotate phosphoribosyltransferase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.4.2.10" FT /note="catalyses the formation of orotidine-5-phosphate FT from orotate and PRPP. Involved in pyrimidine biosynthesis" FT /db_xref="GOA:E1VS29" FT /db_xref="InterPro:IPR000836" FT /db_xref="InterPro:IPR004467" FT /db_xref="InterPro:IPR023031" FT /db_xref="UniProtKB/TrEMBL:E1VS29" FT /protein_id="CBT74432.1" FT /translation="MSETSARERLKELIQELAIVRGKVTLSSGKEADYYIDLRRVTLHQ FT EASGLVGEVMLDLLDEAKLEFSNVGGLTMGADPVGTAIMHTARAKQRAVDAFVVRKAQK FT SYGMGRQVEGPSIEGKDVIVLEDTSTTGGSALTAVEGVRKAGGNVIAVAVIVDRDTGAK FT ERIESEAGVPYLFAYGKDELGL" FT CDS complement(200672..201742) FT /transl_table=11 FT /locus_tag="AARI_01970" FT /product="LacI-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domain PF00356. Numerous bacterial FT transcription regulatory proteins bind DNA via a helix- FT turn-helix (HTH) motif. These proteins are very diverse, FT but for convenience may be grouped into subfamilies on the FT basis of sequence similarity. One such family groups FT together a range of proteins, including ascG, ccpA, cytR, FT ebgR, fruR, galR, galS, lacI, malI, opnR, purF, rafR, rbtR FT and scrR. Within this family, the HTH motif is situated FT towards the N-terminus" FT /db_xref="GOA:E1VS30" FT /db_xref="InterPro:IPR000843" FT /db_xref="InterPro:IPR001761" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VS30" FT /protein_id="CBT74433.1" FT /translation="MTPETSNPEMAQTLQGRKPVETSTGRATINDVARVAKVSVSTVSK FT VVNGRYGVAPATIAKVHQVINELGYETSLVASSLRSTRTNIIGILVAEFEPFSLELLNG FT ISATLRGTQYDLMAYAGNLSPEGHAGWERRSLSRLGGTLIDGAIIVTPTVEIPHSSVPV FT ISIDPHTGADMPISIDVDNYGGAYTATSHLLELGHRRIAHIRGREDLQSAHLREQGYRQ FT ALEDAGVEIEEQLVHHGDYQHEAAVLAAHDLLDLPHPPTAIFAANDLSALAALQVAGEH FT GLRIPEDLSIIGFDDIPAAAQSTPPLSTVRQPLHEMGAHAVKMLLGLLAGEEVESPGEF FT PAVLVPRKTTAAPDRG" FT CDS 201959..203263 FT /transl_table=11 FT /gene="bxlE" FT /locus_tag="AARI_01980" FT /product="putative xylobiose ABC transporter, FT substrate-binding protein BxlE" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family, xylobiose FT porter (TC 3.A.1.1.21). ABCISSE: ABC transporter, binding FT protein (BP), OSP-family (oligosaccharides or polyols)" FT /db_xref="GOA:E1VS31" FT /db_xref="InterPro:IPR006059" FT /db_xref="UniProtKB/TrEMBL:E1VS31" FT /protein_id="CBT74434.1" FT /translation="MLSETRGAQILALAATTALLATGCAAGAGGGEGEKPADGKTTITW FT WHNSNNGDGKAYYGKVAADFEAAHEGVDVEVNAMQHEDMLTKLDAAFQSGDAPDVYMER FT GGGELAAHVAAGLTKDLTEAASEEIAFLGENAGGWQLEGKTYALPFSLGGAGFWYNKAL FT FKEAGIDKAPQTFSELIDATEKLKKAGIDPISVGAGDKWPAAHYWYYAAVRECSQQTMA FT DSIANLDFSDQCFTKAGEDVDKLIKAEPFNPGFLSTPAQSGPTSASGLLATGKVAMELA FT GHWEPGVMQGLTEDGKGMGDDTGWFPFPEIEGGQGDPAAQLGGGDAWAVSEGAPDAAVD FT FVKYMLSDEVQRGFAELDMGLPTNPAAKGAISDPALASLMDVRDKAPYFQLYFDTAFGA FT SIGGAMNDEIALLFAGQSDAQKIVDASQDAADLEK" FT CDS 203272..204312 FT /transl_table=11 FT /gene="bxlF" FT /locus_tag="AARI_01990" FT /product="putative xylobiose ABC transporter, inner FT membrane subunit BxlF" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family, xylobiose FT porter (TC 3.A.1.1.21). ABCISSE: ABC transporter, permease FT (IM), OSP-family (oligosaccharides or polyols)" FT /db_xref="GOA:E1VS32" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VS32" FT /protein_id="CBT74435.1" FT /translation="MAQEVTYAADASARGTSELPERERAKADARQPQKGAKRPRKPADK FT RKNLEIFFFVSPALLLIAVFMLVPIIQAVRFSVYNWKGFGPLVDFVGLKNYVRVLGNEV FT FTDALVHNLIIIGGSIALQLPIGLGIALLLNRKMKIQSLLRTIIFVPYVLSEAIAGVVW FT FQLLQPQYGVIDTIMNKLGIDGPAQGWLGTPELALWTVLAVLTWKYLGLAVILFLAGLQ FT GVPSELYEAAEIDGASWWQIQRKITIPLLGPTLRTWGFLSMIGSLQLFDMVWILTGGGP FT ANATTTMATFLVSEGTKRQNFGIAAAASVILFVVALVLAISYQQFILKRDTQPDDERPK FT QKKVKA" FT CDS 204309..205196 FT /transl_table=11 FT /gene="bxlG" FT /locus_tag="AARI_02000" FT /product="putative xylobiose ABC transporter, inner FT membrane subunit BxlG" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family, xylobiose FT porter (TC 3.A.1.1.21). ABCISSE: ABC transporter, permease FT (IM), OSP-family (oligosaccharides or polyols)" FT /db_xref="GOA:E1VS33" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VS33" FT /protein_id="CBT74436.1" FT /translation="MSASLATRPQHTPAQAKRAKKRNGSQGRNVLVYAIALAVVAITLG FT PVLYGVLGGFRTNAQLAENPAGLPAPWVLDNYAGVLKNPDFWQYALNSTMIAVITTVVV FT VVFGIMAAYPLARYQFRLREPIFMVFVLGLLFPATVAIVPLFILISRDLNMGNTWWGVA FT LPQAAFALPMTVVILRPFLMALPQELEEAAQLDGASRIGFFWKILLPLSGPGMVTVGVL FT AFVGSWNAYLLPLLLLQGDMRTLPLGVADYSSEHSADTAGVFAFTALAMIPALIFFLAM FT QKRIVNGLQGAVKG" FT CDS 205244..207574 FT /transl_table=11 FT /gene="bxlA" FT /locus_tag="AARI_02010" FT /product="xylan 1,4-beta-xylosidase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="3.2.1.37" FT /note="hydrolysis of 1,4-beta-D-xylans, to remove FT successive D-xylose residues from the non-reducing termini. FT Also hydrolyzes xylobiose. Identified by similarity to FT protein SP: Q76BU6 (Streptomyces thermoviolaceus), involved FT in degradation of xylans" FT /db_xref="GOA:E1VS34" FT /db_xref="InterPro:IPR001764" FT /db_xref="InterPro:IPR002772" FT /db_xref="InterPro:IPR017853" FT /db_xref="UniProtKB/TrEMBL:E1VS34" FT /protein_id="CBT74437.1" FT /translation="MKTVEQTWHDTSLPAEQRIAALMEEMTLEEKAGQLGSFWIRPEDE FT NQDGESNVAPMADTFAGGPSFETAIKDGLGHITRAFGTVPLTPAEGRERLVELQEQVIA FT ANRLGIPAIAHEECLTGFTTLGATCYPASIAWGATFNPDLIGSMAQRIGADMLKMGVHQ FT GLSPVLDVTRDYRWGRVEETMGEDPHLVGELAVAYVRGLQDSGVHATLKHFAGYAASQA FT GRNHAPVSMGPRALEDTVFPPFERAVREAGVKSVMNSYADVDGEAPAGSHRLLTEVLRG FT RWGFNGTVVADYWSVSFLHSMHEVAEDEDAAGLLSLEAGMDVELPETTAFANLARAVRS FT GALDQEVLDTAVRRVLAQKLQMGLLDPDWNPRKAWLGEDVELDSADNRAHARKMAEESI FT ILLRNEQILPLRNPARLAVIGPSASQPRTHLGCYSFTNHVYSRFAEQQDYGVPMVSILE FT ALKQEPALAGSQIEYARGVDFTDLDDSGIDEAVEAARNAEVAVVTVGDLAGLFGRGTSG FT EGCDVVDLSLPGRQGELVEAVLATGTPTVLVMVTGRPYSLGKFADRTAAIIQCFMPGVE FT GGPALAGVLTGDVNPSGKLPVQIPNHVGGQPGTYLASKLAWHTEGVTNLDPRPLYPFGY FT GSSYTGFEISELELSEKEIATDGTIQISATVANTGARGGAEVVQLYLGDAVSQVVRPRR FT WLAGFAKVQLEAGESKRVAFTVHADRTSFTGLSGKRIVEPGKFTALVGSSSEDLAARED FT FWITGKVREVAEGRVMDTPVSMS" FT CDS complement(207578..209086) FT /transl_table=11 FT /locus_tag="AARI_02020" FT /product="putative ABC transporter, ATPase and permease FT components" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily (TC 3. FT A.1.y.z), DRI-family. Inverted organization, in which the FT permease component (IM) is C-terminal with respect to the FT ABC domain (ABC-IM)" FT /db_xref="GOA:E1VS35" FT /db_xref="InterPro:IPR000412" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR013525" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VS35" FT /protein_id="CBT74438.1" FT /translation="MNKSTCVDVQRLDVRRGKSLVLDQVDFQLSPGRIIGLLGPSGSGK FT STLLRSIVGNQITSDGAVTVLGKPAGHKSLRNRVGYMTQSASIYEDLSTRQNIAYFAKI FT LRQPSAEVDRVLHTTDLAGQAGHLGRDLSGGQRNRVSLAIALLGSPEIVILDEPTVGLD FT PVLRADLWKMFSQLAATGSCLVVSSHVMDEAMRCDEILLLREGKLLGQMTPAALMESTG FT AENPEDAFVSLIAAGGTKQVPNAACARAEASGNVRRRRAMNRTLATAGRVLAQVMHDPR FT TIALMLLVPSLLIGLIAWIFTETDAFSRIGPAMIALFPFVVMFLVTSIATLRERRSGTL FT ERLLSMPMAKGEFIFGYTLAFTLVAIVQTVIAVSFAIWVCGLHIEGQLWLLFAVAALDA FT LLGISLGLMASAFAHTEFQVVQFMPALVIPQFLLAGIILPREQLPGALQAIGDWLPLSP FT AIDALSDAAAGTTDSATAINMLLIAAWIAAALLIGSLTLRRRTA" FT CDS complement(209122..209760) FT /transl_table=11 FT /locus_tag="AARI_02030" FT /product="possible transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="GOA:E1VS36" 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:E1VS36" FT /protein_id="CBT74439.1" FT /translation="MNEKAPAEVPSARKRGRPKGSTAGAAKTMILKAASKEFAHVGYEA FT ASLRSVARRAGVDPALVHHYFKDKSDLFVQSMHIPINPGRIIAEAASAPLDQMGEALTR FT ALLDTWRKPAFRTAATAMVRGLISSSRATNMLRPFLHEQIFSRLGSRLPQEQAEQRVAL FT VASQIIGLIVSRYIIDLEPLVSMEDQQVIELVAPTIQRYLTGELPALNH" FT CDS complement(209840..210622) FT /transl_table=11 FT /gene="nagD" FT /locus_tag="AARI_02040" FT /product="protein NagD homolog" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="in E. coli, NagD is shown to be a nucleotide FT phosphatase. Its exact function has not been established, FT but it play a role in cell wall construction or disassembly FT (N-acetyl-glucosamine metabolism) or involved in NDP / NMP FT hydrolysis" FT /db_xref="GOA:E1VS37" FT /db_xref="InterPro:IPR006357" FT /db_xref="InterPro:IPR023214" FT /db_xref="InterPro:IPR023215" FT /db_xref="UniProtKB/TrEMBL:E1VS37" FT /protein_id="CBT74440.1" FT /translation="MDGVLVHENQAIKGAAELLNYWRENNLRFLVLTNNSIYTPRDLRA FT RLLASGLDVPEENIWTSAMATAEFLARQRPGGRTFVIGEAGLTTALHDAGFIMTDQNPD FT YVVLGETRTYSFEAITKAIRLIEGGAKFIATNPDATGPSTEGIMPATGAIAALITRATN FT RDPYVVGKPNPMMFRSALNRIDAHSETTAMIGDRMDTDIVAGMEAGLLTALVYTGITAR FT EDMDAFPFRPDLQFPSVANLHAELAKGAAAAETPAAKK" FT CDS 210821..211477 FT /transl_table=11 FT /locus_tag="AARI_02050" FT /product="putative RNA methyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.-" FT /note="identified by match to protein family PF00588: SpoU FT rRNA Methylase family. Possible role in rRNA modification" FT /db_xref="GOA:E1VS38" FT /db_xref="InterPro:IPR001537" FT /db_xref="UniProtKB/TrEMBL:E1VS38" FT /protein_id="CBT74441.1" FT /translation="MNEQTDEPVNDPSMQHVIGVGPWEGELPTDEKYDPRLLAEGDRRN FT VADKYRYWTMDAIIADLDERRHDFHIAIENWQHDMNIGTVVRSANAFLAKEVHIIGRRR FT WNRRGAMVTDRYQHVRHHATVEEFVAWAQEAGLTILGIDIFPDSVPLETYDLPKNCVLV FT FGQEGPGLSPEVHAAAKDTLSIEQFGSTRSINAASAAGIAMHAWVRRHVFGQKVG" FT CDS 211589..212998 FT /transl_table=11 FT /locus_tag="AARI_02060" FT /product="putative membrane-bound M23 family peptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.24.-" FT /note="identified by match to protein family PF01551. FT Members of this family are zinc metallopeptidases with a FT range of specificities. Peptidase family M23 are also FT endopeptidases. 1 transmembrane helice predicted by TMHMM2. FT 0" FT /db_xref="GOA:E1VS39" FT /db_xref="InterPro:IPR011055" FT /db_xref="InterPro:IPR016047" FT /db_xref="UniProtKB/TrEMBL:E1VS39" FT /protein_id="CBT74442.1" FT /translation="MKRRHQVNRDLLLPGLPRRRKPLVIWSTSVIAALGLTATLSIPIM FT AQVGDSRQGDIPVGIDAVADPSMFNGPVYVSADAPLNAFGGSGKELAIDGRPVGMIDGA FT DEESESTSEDNESTALLAGMVGELGKLPGDLQLMHPVKTRRISSPYGWRSNPTGPGNQI FT HIGQDYPISCGSPVYASEAGTVTVSAWAGHSGMRVTIDHGSNVQTGYSHNSKLIAKVGQ FT RVEQGELIALAGTTGNSTGCHVHFEVIIDGRWHDPRNYLPTIAGQRQAMINSQRLTVNA FT GTAPKGNGSRAPERTSSGPDPDVIVPKDDTPVIPKPKPTPSDSQRPSPTESETPRGSQS FT PDGSKSPDGSKSPDGSKSPDGSKSPDGSKSPDGSQSPDGSKSPDASKSPDENESTTSES FT PEGSQEDDTVTPTVPESTPEPAPEPAPVPTPDSSKSSSSGSETSKDSSSSAPAPSTTTK FT LVAPSGSATTE" FT CDS 213195..214217 FT /transl_table=11 FT /gene="fba" FT /locus_tag="AARI_02070" FT /product="fructose-bisphosphate aldolase" FT /function="2.1.2 Main glycolytic pathways" FT /EC_number="4.1.2.13" FT /note="catalyzes the formation of glycerone phosphate and FT glyceraldehyde 3-phosphate from fructose 1,6-bisphosphate" FT /db_xref="GOA:E1VS40" FT /db_xref="InterPro:IPR000771" FT /db_xref="InterPro:IPR006411" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:E1VS40" FT /protein_id="CBT74443.1" FT /translation="MPIATPDKYNAMIDAAKAGGYAFPAVNVTSSQTLNAAIRGFAEAE FT SDGIIQVSTGGAAYWSGASVKDMVIGSLGFAAFARQVAKNYGVNIALHTDHCPADKLDG FT FVLPLLAASEAEVAAGRDPFFNSHMWDGSAETLEENLRVAAELLPRTAAAKQILEVEIG FT AVGGEEDGVENAINDKLYSTVEDALATIDALGAGEKGRYITALTFGNVHGVYKPGNVKL FT RPEILKDIQAQVGAKIGKENPFDLVFHGGSGSSEQEIADAVAYGVIKMNIDTDTQYAFT FT RPVAGHMLANYDGVLKIDGEVGNKKTYDPRVWGAKAEESMAARIVEAAQQLGSAGKSLK FT " FT CDS 214220..214636 FT /transl_table=11 FT /locus_tag="AARI_02080" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR014487" FT /db_xref="UniProtKB/TrEMBL:E1VS41" FT /protein_id="CBT74444.1" FT /translation="MVGENLLGIPETLLPEETEVLARYEAGDEATDLAAKFPASSLVWA FT LLANEAHSEGRIVESYAFARVGYHRGLDSLRKAGWRGQGPVPWRHEPNRGFLRSLYALG FT RAAAAIGETEEVDRIGKFLNDSDASAKAEIEAGN" FT CDS 214921..215589 FT /transl_table=11 FT /locus_tag="AARI_02090" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VS42" FT /protein_id="CBT74445.1" FT /translation="MLSFWMGLGSNLIGMTVLVYFVYFRRHFRRDLVLAYIALSMGIFA FT VTLLLSGSGAGMGLGLGLFGILSIIRLRSDTLTQEEVAYYFISLAIGLVNGLHPEPAWL FT APAATAALVLVMFLADHPRFAPRTERQTVTLERAYPKKAELQAALEELLDAKVLRTVVV FT ELDMVRDLTIVDVRFRTHAVAGQASAKASSSESFSGTYELAKTPAAPAAQNGAKQETWS FT " FT CDS 215589..216407 FT /transl_table=11 FT /locus_tag="AARI_02100" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR018966" FT /db_xref="UniProtKB/TrEMBL:E1VS43" FT /protein_id="CBT74446.1" FT /translation="MTALSAIRCATGTPNARAALEAAVAARAPISLEDVISEAALQTRV FT DKKFLLTPGEFTALSQKLGDKFKIMQIDGLRTFRYESVYFDTEDLDQYRAHRQGRRRRY FT KVRSRTYADTGLSMFEIKTKGLRGSTVKHRVEQDLDTASELTEANLEFLESVLRSEYGQ FT EVPALQPVLDSAYTRATFVNPIDGERLTCDIELEYANGHGQIDGPDLIVVETKSADGRG FT ASDQALAELGIREVSMSKYCIGIALLNPQLPANRWSRLLQRSFVPDPTLR" FT CDS complement(216424..217092) FT /transl_table=11 FT /locus_tag="AARI_02110" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VS44" 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:E1VS44" FT /protein_id="CBT74447.1" FT /translation="MSQILIIEDEPRISSFVAKGLRAAGLTSSIAETGQDGFNLAIEGD FT HELIILDLGLPDEDGFSVLRRLRVAQIDTPVIILTARGSVEDTVAGLQNGADDYMAKPF FT HFDELLARVRLRLRTEDNAPEVSSLTHENLHMDLLRRRVTVNEREVDLSAREFALAEAF FT LRNPGQVLSREQLLSRVWGYDFDPGSNVVDVYVRYLRNKLGSERFETVRGFGYRLASER FT " FT CDS complement(217089..218483) FT /transl_table=11 FT /locus_tag="AARI_02120" FT /product="signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VS45" 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:E1VS45" FT /protein_id="CBT74448.1" FT /translation="MMLLVGLALVAAGTASFAVQRHELNDRLDESLIRTVKEFEVLTET FT GVDPRTMDRFKHAEDLLYIAMQRTLPSPKQGMLSLVADKVRWTAPDIVQTRLEDDPEFI FT EWAKSVQGTNHIRLGTVETEITTYRAVVVPVSLPADHEHSAFVLAYDYSAEAIANDRNF FT MIYSAVGGSVMLVAALAAWLVVGRMLEPIRRLQTTAQQISETDVSQRIEVSGNDEFAEL FT TVTVNEMLDRLDGALSAQRQLLDDVGHELRTPVTIINGHLELMDPNDPEDVAQSRDIAV FT DELRRMSLLINDLVTLAKSNRTDFLQVKPVEVGKLLDDILDKARGLGARQWRVDYRTEA FT TVALDPIRTTQAMLQLCANAVKFSAEDSRIGLGNEIIRDAHGGTTLRWWVSDAGVGIQA FT EDLERIFERFGRGQNSVRSSGSGLGLNIVQAIAETHGGRVWVNSEYGKGSTFYIDMPLS FT TGSKEA" FT CDS complement(218530..218994) FT /transl_table=11 FT /locus_tag="AARI_02130" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.998) with cleavage site probability 0.527 FT between position 29 and 30" FT /db_xref="UniProtKB/TrEMBL:E1VS46" FT /protein_id="CBT74449.1" FT /translation="MGKEALRRALATIAVIAVVVVGAFGISKALEGPADQDLGEGFIFE FT EVAPSPTSGIPKGPTPSPSESATKSQTPSSSPSKSAKPEVSEKPKTSATPSPKPKPKPK FT PKPVAPAPPKKTVVPLPPSGNQHYDDDDDDDDDDDDDDYGDDDDDDGDDD" FT CDS complement(219066..219515) FT /transl_table=11 FT /locus_tag="AARI_02140" FT /product="AsnC/Lrp-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01037" FT /db_xref="GOA:E1VS47" FT /db_xref="InterPro:IPR000485" FT /db_xref="InterPro:IPR011008" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR019887" FT /db_xref="InterPro:IPR019888" FT /db_xref="UniProtKB/TrEMBL:E1VS47" FT /protein_id="CBT74450.1" FT /translation="MPNPVRVDETDLSILAELSKDARIANNVLAAKVGLAPSTCLGRVK FT ALSKAGVITGYHAAINEELLGVAVNAMISVIVSSTARDRLLSSAHQLRELAEVKEVFVL FT GGSPDLLVRVATRSIGDLRTFVAAHLGSNRAFSSTQTVIIFEHLA" FT CDS 219681..220961 FT /transl_table=11 FT /gene="kynU" FT /locus_tag="AARI_02150" FT /product="kynureninase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="3.7.1.3" FT /note="identified by match to protein family PTHR14084. FT Kynureninase catalyzes the hydrolytic cleavage of L- FT kynurenine to anthranilic acid and L-alanine. Kynurinine is FT a Trp breakdown product and a precursor for NAD. This FT reaction is a key step in the catabolism of L-tryptophan by FT Pseudomonas fluorescens and some other bacteria" FT /db_xref="GOA:E1VS48" FT /db_xref="InterPro:IPR000192" FT /db_xref="InterPro:IPR010111" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:E1VS48" FT /protein_id="CBT74451.1" FT /translation="MSTELTRESLARLDAADPLSAFGERFNLPEGVIYLDGNSLGALPK FT GAAERAAQVVTEEWGQGLIRSWNTAGWFEMPLKLGDKLGQLLGAKPNETAITDTTTLNL FT FKALASALRTQKADSPQRRVILTERDNFPTDIYIAEGLADLVNSLSQETGVAYEVKLID FT GEASLRAALDETVAVVALSHVNYRTGSMWDMDETTAAIHGSGALVVWDLAHAAGAVPID FT LNAADADYAVGCTYKYLNGGPGSPAFIWVNARHHERFWQPLSGWWSHKSPFEMAGSYTP FT ANDIRRFMCGTQPVTSLAMIEVGLDIALEADMDKVRANSLELVDLFIELVETRCAGYGL FT ELVTPREHAARGSHVSFRHEHGYEIIAALIDQGVIGDYREPEVLRFGITPLYLTRTDIW FT DAVEKLREILHTNAWQREEYAVRNAVT" FT CDS 221085..222467 FT /transl_table=11 FT /locus_tag="AARI_02160" FT /product="putative amino acid transporter" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="amino acid-polyamine-organocation (APC) superfamily, FT amino acid transporter (AAT) family (TC 2.A.3.1.z)" FT /db_xref="GOA:E1VS49" FT /db_xref="InterPro:IPR002293" FT /db_xref="InterPro:IPR004840" FT /db_xref="InterPro:IPR004841" FT /db_xref="UniProtKB/TrEMBL:E1VS49" FT /protein_id="CBT74452.1" FT /translation="MGKQPVRATEVGSGFKKSLTPGQMSMIALGSAIGTGLFAGSKLAI FT AMAGPSVIISYLIGGAVALLVMGALAEMTVKQPVAGSFGVYAERYLGRFAGYLTKYLYW FT SALIFAVGTEVSAVGEYMQYWFPEIPGLLWILVFSAALLGVNFSSVKIFGTTEYWFSAI FT KVFAVIAFIIIALWLVFHDPRDEFGFHNYAADGGFFSNGVFGMWSAVIVAIFSYMGIEA FT ISIAAAEAKNPKTAVRKAFKVSFLRLLLFYVFTMALILAIAPTSELVSGGSPFVTVMSQ FT MGIPLADSVLNFVLIVAALSATNAQLYAATRMLHSLADAGHAPRLAHRTNSAGAPVHAV FT WMSAGGIAVAALVYALVPEGGFGIMMSLATFGALATWFMILVTHVSFRKKVRSEQTTLE FT FKLPGYPGASILGAVLLAGLLVTSFFVPEFKYTLIFGVPFVIVMSVLYKLVFAGKSQRA FT QK" FT CDS 222573..223196 FT /transl_table=11 FT /gene="tdk" FT /locus_tag="AARI_02170" FT /product="thymidine kinase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.7.1.21" FT /note="catalyzes the formation of thymidine 5-phosphate FT from thymidine" FT /db_xref="GOA:E1VS50" FT /db_xref="InterPro:IPR001267" FT /db_xref="UniProtKB/TrEMBL:E1VS50" FT /protein_id="CBT74453.1" FT /translation="MAKLYFRYGAMNSGKSTSLLQAAFNYEERGQRILLAKPGVDTKGE FT NSIVSRLGIQREVDFTVGPQENVREKFAAHSSGDDPDALLPHVDAPPVACLLVDEAQFL FT SGEQVDDLLRIAVMDDVPVLAYGIRTDFRTRAFPGSARLMELAHSLEELKTICRCGRKA FT MFNTRRVGQCVVFDGDQVAIDGDDVWYESLCATCYLQASGGKLS" FT CDS complement(223193..223726) FT /transl_table=11 FT /locus_tag="AARI_02180" FT /product="TetR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00440: bacterial regulatory FT proteins, tetR family" FT /db_xref="GOA:E1VS51" 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:IPR023772" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:E1VS51" FT /protein_id="CBT74454.1" FT /translation="MALTQLTVVDTAVGILQQFGLADLSMRRLAKELDVQVGALYWHVK FT NKQELLAQVAAKLLNTPALAVQAEDFDDPADAILHLARKLYLALLPIQDSPEVVEVASA FT MQATELQPVLALRSLLESAGLSAEHAIHGQQLLLNHVLGSVAFRQNLVQLDVDAPLADG FT FDWGLQRAVAGLVG" FT CDS complement(223760..225028) FT /transl_table=11 FT /locus_tag="AARI_02190" FT /product="putative xylitol oxidase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="1.1.3.41" FT /note="xylitol oxidase catalyzes the following reaction: FT xylitol + O(2) <=> xylose + H(2)O(2)" FT /db_xref="GOA:E1VS52" FT /db_xref="InterPro:IPR006094" FT /db_xref="InterPro:IPR007173" FT /db_xref="InterPro:IPR016166" FT /db_xref="InterPro:IPR016168" FT /db_xref="UniProtKB/TrEMBL:E1VS52" FT /protein_id="CBT74455.1" FT /translation="MEPEAKELNWAGNLSYQARELLYPTSIEQLAEQVRASDKARALGS FT RHSFNDIADTQATLICLSKMPETIEIDAQAMSVRVSAGTTYGALAETLQAAGFALHNLA FT SLPHISVAGAVSTGTHGSGQAHGNLATAVRGVELVLADGSLHAVRRGDAQFNGYVVSLG FT ALGVLTHLTLDIVPSFEVQQTVFEQLSWDKVLGGFDALQASAYSISLFTDWSGQNVGQT FT WLKRCVGDGLGDDIAQGKFGGFPATAAMHPLPESDGAICSEQLGAPGPWSDRLAHFRMD FT FTPSAGDELQTEYLVPREYAVQAIEAIRGLSATITPLLLVSEVRTIAADELWLSGNYGR FT DGIALHFTWKPQQEEVEALLPRIEEALAPFAARPHWGKLFAATSAQLHELYPKFNDFIG FT LAQRLDPAGKFRNDFLNRTVFGA" FT CDS complement(225038..226465) FT /transl_table=11 FT /gene="xylB" FT /locus_tag="AARI_02200" FT /product="xylulokinase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="2.7.1.17" FT /note="catalyses the following reaction: ATP + D-xylulose FT <=> ADP + D-xylulose 5-phosphate. Involved in the FT catabolism of xylose" FT /db_xref="GOA:E1VS53" FT /db_xref="InterPro:IPR000577" FT /db_xref="InterPro:IPR006000" FT /db_xref="InterPro:IPR018483" FT /db_xref="InterPro:IPR018484" FT /db_xref="InterPro:IPR018485" FT /db_xref="UniProtKB/TrEMBL:E1VS53" FT /protein_id="CBT74456.1" FT /translation="MTLVAGIDSSTQSCKVVIRDAATGALVRSGRASHPEGTEVDPQFW FT FSALQEAIAQAGGLDDVAAISVGGQQHGMVVLDESGAVIRPALLWNDTRSAAAATDIIA FT DAGNGDAEAGAVYWAQRTGTLPVSSITLAKLRWLKDNEPENAAKVAAICLPHDWLSWRL FT AGYGPGSGAEGLAALATDRSDASGTGYYRATENAYDLEALEQHLGHIPILPAVAGPLDS FT IGTTPAGASIGPGAGDNAAAGLGVGAKVGDVVMSLGTSGTVFAVADTPSADASGLVAGF FT ADATGNYLPLVCTLNATRIFDATASLMQVDLEEFNDLAMSANPGSDGLTLLPYFDGERT FT PNLPKATGSLHGITRANYTAANLARSAVEAVICSLADGLRALEAQGVEAQRIILVGGGA FT QSRALQQIAAQVLGLPITVPAPGEYVADGAARQAAGVLAGAFPDWTRDTTQVPAAESTP FT QVLERYRALVKSQWLDK" FT CDS complement(226506..227693) FT /transl_table=11 FT /gene="xylA" FT /locus_tag="AARI_02210" FT /product="xylose isomerase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="5.3.1.5" FT /note="catalyzes the interconversion of D-xylose to D- FT xylulose. It can also isomerize D-ribose to D-ribulose and FT D-glucose to D-fructose" FT /db_xref="GOA:E1VS55" FT /db_xref="InterPro:IPR001998" FT /db_xref="InterPro:IPR012307" FT /db_xref="InterPro:IPR013022" FT /db_xref="InterPro:IPR013453" FT /db_xref="UniProtKB/TrEMBL:E1VS55" FT /protein_id="CBT74457.1" FT /translation="MTLQPTSADRFTFGLWTVGWTGADPFGVATRKNLDPVEAVHKLAE FT LGAYGITFHDNDLIPFDATASQREQILADFRAALKETGLKVPMVTTNLFSHPVFKDGGF FT TSNDRSIRRFALSKVLHNIDLAAQMGAETFVMWGGREGAEYDGSKDLAAALNRMREGVD FT TAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAFIEQLEHGDIVGLNPETGHEQ FT MAGLNFTHGIAQALWAGKLFHIDLNGQRGIKYDQDLVFGHGDLTSAFFTVDLLENGFPT FT GGPKYDGPRHFDYKPSRTDGYDGVWDSAKANMSMYLMLKERAQAFRADPEVQEAMKLSG FT VFELGESTLDEGETAAQLMNDAASFADFDANAAAQRNFAFIRLNQLAIEHLLNAR" FT CDS 227825..229060 FT /transl_table=11 FT /gene="xylR" FT /locus_tag="AARI_02220" FT /product="putative xylose operon repressor" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00480: ROK family" FT /db_xref="InterPro:IPR000600" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VS54" FT /protein_id="CBT74458.1" FT /translation="MRQAASTARAATSSAPGNVGDVRKANLARVLSVIAASGNDQRLSR FT ADIAGLSQLTKASVSSLVADLLAAGLVIEIGVHRDGERGRPAVGLILNPARVVMGMEVN FT VDYIAAGLVDLSGKLLAHEIQPHADHRSAAKEVLAALGELSRRLQDAAAAQGLMILGGG FT LAVPGLVDDESFTVLQAPNLGWVEQDLDVAALLPEPKTRFRLFNEANASALAQQQLMDA FT QERDFLFVSGEVGIGGGLIIDAELFVGPQGHAGELGHVVIAPDGKKCSCGGRGCLETIA FT GQDAILAAANLGAVADGASRQQRISQLYQALETGTEPAVSAVAEAGKSLGIAVASALRL FT YNVSTVVFGGHFAALEQWLRPAMEASLKAHAPSIAGQARLLCSPLGQTGALVGAARSVV FT GDLLEAPHQLVG" FT CDS complement(229057..229854) FT /transl_table=11 FT /locus_tag="AARI_02230" FT /product="putative MerR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00376. Members of the FT family include the mercuric resistance operon regulatory FT protein merR; Bacillus subtilis bltR and bmrR; Bacillus FT glnR; Streptomyces coelicolor hspR; Bradyrhizobium FT japonicum nolA; Escherichia coli superoxide response FT regulator soxR; and Streptomyces lividans transcriptional FT activator tipA" FT /db_xref="GOA:E1VS56" FT /db_xref="InterPro:IPR000551" FT /db_xref="InterPro:IPR009061" FT /db_xref="InterPro:IPR010499" FT /db_xref="InterPro:IPR011256" FT /db_xref="UniProtKB/TrEMBL:E1VS56" FT /protein_id="CBT74459.1" FT /translation="MLSIGMFAQIGQVTHRMLRHWDTAGLLRPAQVDPSSGYRSYDPSQ FT LQRLHQIVALRDLGFGLEEISLILDRGATARKIAELLHIRQAQVAAEHQLATQRLADVQ FT RRLQLISKENLMSHIEIIHKPLPAVRLAAGRFTVAEQPEIAGRIGPLFDRIAQSLQGQS FT LATPIAQYNGTEDGVEVIAGYATSAQSLADVEIIVLPAVPEAICGVHLGSMDSIHESWQ FT AVHEEVLARGLLPTGPCREVYVRALSEDQADWVTELQQPVGTP" FT CDS 230117..231406 FT /transl_table=11 FT /gene="purA" FT /locus_tag="AARI_02240" FT /product="adenylosuccinate synthetase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="6.3.4.4" FT /note="catalyzes the first step in the conversion of IMP to FT AMP in de novo purine nucleotide metabolism" FT /db_xref="GOA:E1VS57" FT /db_xref="InterPro:IPR001114" FT /db_xref="InterPro:IPR018220" FT /db_xref="UniProtKB/TrEMBL:E1VS57" FT /protein_id="CBT74460.1" FT /translation="MPAIVIVGAQWGDEGKGKATDLLGGKVDYVVKPNGGNNAGHTVVV FT GGEKYELKLLPAGILSPNATPIIGNGCVVNLEALFEEIDGLESRGADTSKLRVSANAHL FT VAPYHQTMDKVTERFLGKRAIGTTGRGIGPAYMDKVGRLGIRVQDVFDESILRQKVEGA FT LRQKNELLVKIYNRRSVEVEEIVSYFLSYAERLRPLVIDSTYELNKALDEGKVVLMEGG FT QATFLDVDHGTYPFVTSSNPTAGGASVGSGIGPTRITRSIGIIKAYTTRVGAGPFPTEL FT FDDMGLYLQKTGGEFGVNTGRPRRCGWYDAVLARHASRVNGFTDYFVTKLDVLTNIEQI FT PVCVAYDVDGVRHDEMPMTQTDFHHAKPIFEYFPGWTEDISGAQTMEDLPENARNYILA FT LEKISGTRISAIGVGPDRDQTIVRHDLIQN" FT gene complement(231117..231824) FT /pseudo FT /locus_tag="AARI_02250" FT /product="truncated sodium/solute symporter" FT /note="N terminal section of the truncated protein: FT Solute:Sodium Symporter (SSS) family (2.A.21.y.z). Members FT of the SSS family catalyze solute:Na+ symport. The solutes FT transported may be sugars, amino acids, organo cations such FT as choline, nucleosides, inositols, vitamins, urea or FT anions, depending on the system" FT CDS 232196..233851 FT /transl_table=11 FT /locus_tag="AARI_02260" FT /product="putative acetolactate synthase large subunit" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.2.1.6" FT /note="PRK08199: acetolactate synthase 2 catalytic subunit" FT /db_xref="GOA:E1VS58" FT /db_xref="InterPro:IPR011766" FT /db_xref="InterPro:IPR012000" FT /db_xref="InterPro:IPR012001" FT /db_xref="UniProtKB/TrEMBL:E1VS58" FT /protein_id="CBT74461.1" FT /translation="MSENGQGLTKKSAGHVIVDTLAAHGVERAYVVPGESYLDVLDGLH FT NSPIETVVCRHEGGATYMAEAEGKMHQRPGIAMVTRGPGAANAHVGLHTAWQDSTPLVL FT FVGLIPFEHREKEAFQEFDPKAWFGTGAKRVMILDHADRASEVVAEAMFAAMSGRPGPV FT VVGLPEDIIRNEVPAEVHPEIPVATGGMTVTDWKALNAALQEADKPLFIFGGNDWSHEG FT AADFTRWLEEHDLPAAAEWRCEGTVPFNSPSYVGPIGYGRPKPTYDLLEETDLLIFVGT FT VPGDVITDGFNVRQNWDKKNFLVTIDPSLRGRSGPVSHQIVAKPDVFVRDLLLMDMPVK FT DSWKEWTSRMRAEQEKFAELPPAQPSDGQAKMATMMANLVNSLPEDALVTFGAGEHTNW FT AHRYFPTNGYASMLSARNGSMGYSIPSAVAASLNYPQRRVVTIAGDGEFLMNGQELATA FT AQYGATPLVIVMDNQQYGTIRTHQERQYPERVSGTQLANPDFALMAQSFGGFGVRVEKD FT ADVPAALENALKAIDEDKKFALIHLVVEQGVKAY" FT repeat_region complement(234138..234140) FT /rpt_type=DIRECT FT repeat_region complement(234141..234178) FT /rpt_type=INVERTED FT mobile_element complement(234141..235739) FT /mobile_element_type="insertion sequence:ISAar44" FT /rpt_family="IS3 group IS3" FT CDS complement(234175..235116) FT /transl_table=11 FT /locus_tag="AARI_34380" FT /product="transposase of ISAar44, IS3 family, IS3 group, FT orfB" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VS59" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VS59" FT /protein_id="CBT74462.1" FT /translation="MNRRQNAARAGRALRATAPRPAPANKLTAQEETTILATLNSERFV FT DQAPEQIHATLLSEGTYLCSVSSMYRLLRRAKQVAERRRQARHPARKVPELVADQPGEV FT FTWDITKLAGPTKGVYFDAYVMIDIYSRYIIGCQVHTRESGELARDFIAGVFAKAQVPK FT VVHADRGTSMTSKPVAALLADLDVLKSHSRPKVSNDNPFSEAWFKTLKYLPTFPQRFGS FT LVDARAFMDRFVQSYNGHHRHSGIGFHTPADVHFGMTGHVDDQRLAALQRAWDEHPERF FT GRRRLPKKLQMPEAAWINEPVKRLEGQEMQAG" FT CDS complement(235215..235652) FT /transl_table=11 FT /locus_tag="AARI_34390" FT /product="transposase of ISAar44, IS3 family, IS3 group, FT orfA" FT /function="4.5 Transposon and IS" FT /db_xref="UniProtKB/TrEMBL:E1VS60" FT /protein_id="CBT74463.1" FT /translation="MSIDSIHPTPGNMPENGTMDSIDSRPEQPRRRSISPAQKLAYLDG FT YEQAIQTGEGRGYLRANALYSSQIVEWRRLRDAGVLGDSTSNSFPARSSSRLSKEQAEI FT ARLKKQLAANEQKLATTQTALEIMGKAHALLEQISKSADSK" FT repeat_region complement(235702..235739) FT /rpt_type=INVERTED FT repeat_region complement(235740..235742) FT /rpt_type=DIRECT FT gene 236080..236580 FT /pseudo FT /locus_tag="AARI_02270" FT /product="truncated reverse transcriptase/maturase" FT /note="N-terminal section of a protein similar to SP:Q6DKY2 FT (Bacillus stearothermophilus), a heat-stable reverse FT transcriptase (possible group II intron associated FT protein). Disrupted by insertion of ISAar37, IS3 family" FT repeat_region 236534..236536 FT /rpt_type=DIRECT FT mobile_element 236537..237845 FT /mobile_element_type="insertion sequence:ISAar37" FT /rpt_family="IS3 group IS3" FT repeat_region 236537..236561 FT /rpt_type=INVERTED FT CDS 236585..236878 FT /transl_table=11 FT /locus_tag="AARI_34400" FT /product="transposase of ISAar37, IS3 family, IS3 group, FT orfA" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VS61" FT /db_xref="InterPro:IPR002514" FT /db_xref="InterPro:IPR009057" FT /db_xref="UniProtKB/TrEMBL:E1VS61" FT /protein_id="CBT74464.1" FT /translation="MSKRQKFTPEFRAEAVELVLSSGKSLVEVSESLGINEGTLGNWVR FT AYRTEHPETETEERGPVEWAQHEKLRRELAEVKRENEFLKDVSAYFASKGKK" FT CDS 236773..237795 FT /transl_table=11 FT /locus_tag="AARI_34410" FT /product="transposase of ISAar37, IS3 family, IS3 group, FT orfB" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VS62" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VS62" FT /protein_id="CBT74465.1" FT /translation="MGPAREAAPGIGGGETGERIFKRCQRLFRLEGQEISAIFRFIMEH FT SAKYPVNWMCQQLEVSRASYYRWLNPSTELSEAKALRAMRTVLVLTEYEASNGVAGAGQ FT LVDLIRNNHKQYVPKSTVLSIMNEHGLKAKRVSAFKVTTVHDQQARTAHIKNHMVDKLG FT RRDFRSSRPGTKLVGDITYLRTGEGWLYLATVIDLYSRQIVGWSMGANMQTQLVIDAMQ FT LAMSRGFISAGTVFHSDRGTQYTSDAFQAWCSENGVRQSMGRTGVCWDNAVAESAFSTI FT KNEMYHHRAFTSRVAARTAVMEFIEIWYNRKRPHTTNGGLSPQMLLDWYWEQNSLALAA FT " FT gene 237821..238729 FT /pseudo FT /locus_tag="AARI_02280" FT /product="truncated reverse transcriptase/maturase" FT /note="C-terminal section of a protein similar to SP:Q6DKY2 FT (Bacillus stearothermophilus), a heat-stable reverse FT transcriptase (possible group II intron associated FT protein). Disrupted by insertion of ISAar37, IS3 family" FT repeat_region 237821..237845 FT /rpt_type=INVERTED FT repeat_region 237846..237848 FT /rpt_type=DIRECT FT CDS 238986..239363 FT /transl_table=11 FT /locus_tag="AARI_02290" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VS63" FT /protein_id="CBT74466.1" FT /translation="MAQMSEELIEQWADATAEIYNESLTGINLSRLPDAMAQYVDLFSQ FT SEDLTFNADATPTDYFDNHPFLAVTAVLNNPEAMEVLDSDAQDALDAMADFTEAWYKFD FT LENEPELGISEADVDDVDEDW" FT CDS 239478..239909 FT /transl_table=11 FT /locus_tag="AARI_02300" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR019587" FT /db_xref="InterPro:IPR023393" FT /db_xref="UniProtKB/TrEMBL:E1VS64" FT /protein_id="CBT74467.1" FT /translation="MSQFSVFESTVVIHLPVHRVWELLTDWAATPLWIHGIGSMHSDDP FT ELKVGTNLTYRVAGHERLYRVHELIENRLLILHTSENPDGLSYRYDLKDDAGQTEVVLQ FT VAIINPDLSVEQCEALAQNIRESEGDKLDQLRFYAEQAP" FT gene complement(239880..240506) FT /pseudo FT /locus_tag="AARI_02310" FT /product="truncated polysaccharide deacetylase" FT /note="C-terminal section of a polysaccharide deacetylase" FT CDS complement(240509..241813) FT /transl_table=11 FT /gene="tetV" FT /locus_tag="AARI_02320" FT /product="tetracycline-resistance determinant TetV" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (MFS), drug:H+ FT antiporter-3 (12 spanner) (DHA3) family, tetracycline FT resistance determinant TetV (TC 2.A.1.21.3). Identified by FT similarity to protein SP:O31137 (Mycobacterium smegmatis). FT Probable drug antiporter which uses the proton motive force FT for the active efflux of tetracycline" FT /db_xref="InterPro:IPR010290" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VS65" FT /protein_id="CBT74468.1" FT /translation="MSALKTTALRLIKPFAIRDYALLASALVLSTFAAGMWTVAMVYQV FT RRLDGGPVELSMVATANAVGLLCFVLFGGIMADRHSCRRIVVLVEVFSLALMSTTAILA FT INGVLELWHLMVAGFLVGAGAAFFYPAYSALLPKMLPADQLLAANGLEGTIRPVVHTAL FT GPMTAGFLVAALSPAHAIIGLSLVHLLALLMLRRIPKREAYNRPGAADGQPQPGIFRQL FT REGIGYTVRTRWLLWTLLFSVISVFTFIGPFEVLLPFIVSDNLHGDAKLFSFALAFFGA FT GAAVGSLLIASAKFPRRYLSLMTACWCLGTLPLAIVGYVDEAWMLFAILLAFGITDAVG FT MVIWGTLLQRRVPSNLLGRISSLDFFVSLALMPLSMAVAGPLTQVMSLQAIFIIAGIAS FT PLFGIIAWRAGKFAQDEIAHPLRDEPALQEVKRAE" FT repeat_region 242113..242120 FT /rpt_type=DIRECT FT mobile_element 242121..243569 FT /mobile_element_type="insertion sequence:ISAar23" FT /rpt_family="ISL3" FT repeat_region 242121..242143 FT /rpt_type=INVERTED FT CDS 242256..243563 FT /transl_table=11 FT /locus_tag="AARI_34420" FT /product="transposase of ISAar23, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VS66" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VS66" FT /protein_id="CBT74469.1" FT /translation="MHHSIYTPANLTTFTNLDGLGLTAIGQRLTPKKAEILCQVTNPDP FT WCQTCGTPGNPRDTVTRRLAHEPFGWRPTVLVIKHRRYRCNHCQRVWREDLSQAVAPRQ FT KISRTGLRWALAGLVTQHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFNGVKV FT LGVDEHVWRHTKSGDKYVTVIVDLTPVKAGTGTARLLDMIPGRSKAVFKTWLAERGEAW FT KNNVEVVAMDGFTGFKSAAAEELPQAVEVLDPFHVVKLGSEALDQARQRVQREQYGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKQRVEDLFNVAKHEPVQLVWSVYQRMVDAYRQKKP FT EIGKWAMEQLINEIGTKVPKGLPELKKLGGTLRRRKPDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFTNLTHYIARSLLETGGFRSRLHPES" FT repeat_region 243547..243569 FT /rpt_type=INVERTED FT repeat_region 243570..243577 FT /rpt_type=DIRECT FT CDS complement(243730..245412) FT /transl_table=11 FT /gene="ptsI" FT /locus_tag="AARI_02330" FT /product="phosphoenolpyruvate--protein phosphotransferase" FT /function="1.2.4 Transport/binding of carbohydrates" FT /EC_number="2.7.3.9" FT /note="phosphotransferase system enzyme I (EI) Family (TC FT 8.A.7.y.z). Enzyme I of the phosphoenolpyruvate-dependent FT sugar phosphotransferase system (PTS), a major carbohydrate FT transport system in bacteria. The PTS catalyzes the FT phosphorylation of incoming sugar substrates concomitant FT with their translocation across the cell membrane" FT /db_xref="GOA:E1VS67" FT /db_xref="InterPro:IPR000121" FT /db_xref="InterPro:IPR006318" FT /db_xref="InterPro:IPR008279" FT /db_xref="InterPro:IPR008731" FT /db_xref="InterPro:IPR015813" FT /db_xref="InterPro:IPR023151" FT /db_xref="InterPro:IPR024692" FT /db_xref="UniProtKB/TrEMBL:E1VS67" FT /protein_id="CBT74470.1" FT /translation="MSKKFTGVGVSAGRVIGHVRRMPEPILPPADGAPLPQGMSAEEES FT QRLAEASKAVATGLKERAALATGDAQAVLKATALMASDRTLIKSATKLVTGGTCAESAI FT WEAADAVATQLAALGGYMAERAGDVLDVRARIVAELRGVPAPGIPDSDQPFILAAVDLA FT PADTATLDPAKVLALVTSDGGPQSHTAIIARSLGLPAIVAAPETTELANGDYVFVDGID FT GLVITDPTEAEEHLASTYANREVLPDFSGTGELADGYRVPLLSNVGSGEDAQLAAAAGA FT EGVGLLRTEFCFLGKEKEPTHQEQVSAYGAVFAAFPGQKVVVRTLDAGADKPLPFLTDS FT SEPNPALGVRGYRTDLSSPGVLERQLKAIAQATSEHEADVWVMAPMISTPAEAEDFAQM FT AKAAGFATAGTMIEVPSAAILAGQILQRCDFVSIGTNDLTQYTMAADRQLGTLAELNDP FT WQPAVLHMVAATTAGAQSADGKPVGVCGEAAADPALAVVLVGLGVTTLSMNKRALAPVS FT AVLRTVDLAKAQRLAKLALDAPSAELARSAVRAELGELDRFGL" FT gene complement(245409..247265) FT /pseudo FT /locus_tag="AARI_02340" FT /product="truncated fructose-specific phosphotransferase FT system IIABC components" FT /note="C-terminal section of a fructose-specific FT phosphotransferase system IIABC components" FT CDS complement(247409..248386) FT /transl_table=11 FT /gene="fruK" FT /locus_tag="AARI_02350" FT /product="1-phosphofructokinase" FT /function="2.1.4 Substrate-specific entries to carbohydrate FT metabolic pathway" FT /EC_number="2.7.1.56" FT /note="catalyzes the phosphorylation of fructose-1- FT phosphate to fructose-1,6-biphosphate. Involved in the FT catabolism of fructose" FT /db_xref="GOA:E1VS68" FT /db_xref="InterPro:IPR002173" FT /db_xref="InterPro:IPR011611" FT /db_xref="InterPro:IPR017583" FT /db_xref="UniProtKB/TrEMBL:E1VS68" FT /protein_id="CBT74471.1" FT /translation="MIVTLTCNPALDKTIELAAALQPGAVQRAAGSHLQAAGKGVNVAR FT VILAAGQRTLAVLPGAGNDPLIVALAADQLPYRALEINAPLRTNTTLTSPDGSTTKINE FT AGPELDAATLEQLSELVRDSCAGADWLVMAGSLPPGVPANYYALLTASLREQLGAKCPK FT IAVDTSGEPLRQLFAHGEIHIPDLVKPNAEELAELLGEDLGEAQLEADPGLAARASSKL FT LRRPGAAVLTTLGAHGAVLATAEGCWHGWPQPITPRSTVGAGDSSLAGYLLADTAGHLP FT AFKLRQAIAYGTAAASLPGSGIPTPTDLRIDAVSVIELTPRQGS" FT CDS complement(248383..249159) FT /transl_table=11 FT /locus_tag="AARI_02360" FT /product="DeoR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="DeoR-like transcription repressors occur in diverse FT bacteria as regulators of sugar and nucleoside metabolic FT systems. The effector molecules for deoR-like regulators FT are generally phosphorylated intermediates of the relevant FT metabolic pathway" FT /db_xref="GOA:E1VS69" FT /db_xref="InterPro:IPR001034" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014036" FT /db_xref="InterPro:IPR018356" FT /db_xref="UniProtKB/TrEMBL:E1VS69" FT /protein_id="CBT74472.1" FT /translation="MFAEERHRLIVEQLEADGKVTVAQLAQRFDITRETVRRDLAQLES FT ENCLRRVHGGAVATSEASTREESYVVRTTIHSDAKARIAQRALGLLPVSDASVIIDAGT FT TTEILAERMVKANAGSGLVVITHALPIASALIHCPDIALELIGGRVRGLTGATSGARTA FT QEYSQYRADIAFIGTNGLHAGFGLSTPDPLEAAVKRALVASARRVVLLADSSKFDQETL FT VRFASLEAIDTLVTDQQPGTELAAALDAADVEVVVA" FT CDS complement(249527..250525) FT /transl_table=11 FT /locus_tag="AARI_02370" FT /product="putative CAAX amino terminal protease family FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF02517: CAAX FT amino terminal protease family. Members of this family are FT probably proteases (after a prenyl group is attached to the FT Cys residue in the C-terminal CAAX motif of a protein, the FT AAX tripeptide is removed by one of the CAAX prenyl FT proteases). The family contains the Q03530 CAAX prenyl FT protease. 8 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VS70" FT /db_xref="InterPro:IPR003675" FT /db_xref="UniProtKB/TrEMBL:E1VS70" FT /protein_id="CBT74473.1" FT /translation="MPNAASNWLLQIDEPISASRVPSAAEYHRVYAGEKRRIPRGILAI FT ALLLVGFAGFAQLSLLGARHIDTEILGRAGFTPLQQAAGALSLALLIPYCMLLQRLLYG FT IPFSSLHSVAGIFRYGIFARSLLAFGPALLLVIAAGFLAAPADQVPWTAADLVAYFVIG FT MLLTPLAAAGEEYGFRGFMFRIVGGWARGARSGALISIIVPTVLFSLMHGSLDPYTLTS FT YLVLFGSLAIATWRTGGLETAIALHIVYNVTALVLGTTLHVDLGGALNSREEISGSIAN FT LVPSVVLILITATIWWITRKSGPARTPAHVRPSPRSNSPKEPATPAENATD" FT CDS complement(250547..251188) FT /transl_table=11 FT /locus_tag="AARI_02380" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VS71" FT /protein_id="CBT74474.1" FT /translation="MKFKRWLNHRVRAGSGEPVKRLRWWQIFSRSLRTIALPSPDGTAS FT TYTVDVRHGGDMTDGVIRARLYVNGSLHSYSKMPARFPVPGGHIEVAANGFGLKRCHYM FT PAGGSELQLAPDPASAEGRRARLHHRLPGLSRFIGIISTALVLAGLCITVPQIIESISQ FT IPPIADSIGTFTSPVQLPLQGNLFIGFGAVLGSTERALRMRSSWIDELAS" FT CDS 251279..251899 FT /transl_table=11 FT /locus_tag="AARI_02390" FT /product="putative TetR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00440: bacterial regulatory FT proteins, tetR family" FT /db_xref="GOA:E1VS72" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR015893" FT /db_xref="UniProtKB/TrEMBL:E1VS72" FT /protein_id="CBT74475.1" FT /translation="MVSQPDASREVGTREKILIAAATMLGENPTARLSVRAVAARAEVS FT TGSLRHFFPTQRALVDTVIAGIYDVDIPDDPINDRALMPAERLTACLRLLLAQFGAGDR FT AREQWGFLYEAYVASAPSEDETRTYLALERMGRHRVERWLGALIEEGAIPAGQIEQRAR FT FLATVISGLMTERALPSEAVRVEAEAETLRLAVHAVTTTWNAA" FT gene complement(252131..252400) FT /pseudo FT /locus_tag="AARI_02400" FT /product="truncated TraG-family protein" FT /note="fragment of protein that may be involved in FT bacterial conjugation" FT CDS 253139..253318 FT /transl_table=11 FT /locus_tag="AARI_02410" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VS73" FT /protein_id="CBT74476.1" FT /translation="MNLEVIAADFSDEEVLGVAVGALVLADQRTDPMRLVVESLKSVSQ FT LVGPARFNDISCET" FT repeat_region complement(253752..253759) FT /rpt_type=DIRECT FT mobile_element complement(253760..255208) FT /mobile_element_type="insertion sequence:ISAar23" FT /rpt_family="ISL3" FT repeat_region complement(253760..253782) FT /rpt_type=INVERTED FT CDS complement(253766..255073) FT /transl_table=11 FT /locus_tag="AARI_34430" FT /product="transposase of ISAar23, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VS66" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VS66" FT /protein_id="CBT74477.1" FT /translation="MHHSIYTPANLTTFTNLDGLGLTAIGQRLTPKKAEILCQVTNPDP FT WCQTCGTPGNPRDTVTRRLAHEPFGWRPTVLVIKHRRYRCNHCQRVWREDLSQAVAPRQ FT KISRTGLRWALAGLVTQHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFNGVKV FT LGVDEHVWRHTKSGDKYVTVIVDLTPVKAGTGTARLLDMIPGRSKAVFKTWLAERGEAW FT KNNVEVVAMDGFTGFKSAAAEELPQAVEVLDPFHVVKLGSEALDQARQRVQREQYGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKQRVEDLFNVAKHEPVQLVWSVYQRMVDAYRQKKP FT EIGKWAMEQLINEIGTKVPKGLPELKKLGGTLRRRKPDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFTNLTHYIARSLLETGGFRSRLHPES" FT repeat_region complement(255186..255208) FT /rpt_type=INVERTED FT CDS complement(255193..255729) FT /transl_table=11 FT /locus_tag="AARI_02420" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VS75" FT /protein_id="CBT74478.1" FT /translation="MIVPATLHVSWSAVVRGSSDPVTQPDGSTNGHFIVVTENDEFIDA FT TALQFDDIADRRGVSGFMPLVGRLEGLWSSITSMDPNVRTVVPEPGFQIGRGDSYAIYK FT LHASEAGSQVVKDYIELNASNNLLGWQRSLADIFAWMLGNHILVGERSNEVSQIDDPAF FT SHAVKNWLGKPALQN" FT repeat_region complement(255209..255216) FT /rpt_type=DIRECT FT CDS 256982..257416 FT /transl_table=11 FT /locus_tag="AARI_02430" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VS76" FT /protein_id="CBT74479.1" FT /translation="MQKPTQTTTKDSRETVTVPAIVERDMYGEGYDWMESLAGTGWYEV FT PGWGRDGWDLGSWPYIIFAAAKTTDETGKLFGYTTYVEGDVTARWYRSCEARNLAISKE FT AFWYWASGQSDGPEALEGMNPQEFKQIDGLCEPYIPNFGN" FT CDS complement(257496..257723) FT /transl_table=11 FT /locus_tag="AARI_02440" FT /product="hypothetical membrane protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VS77" FT /protein_id="CBT74480.1" FT /translation="MDANRRTLWSVALGMSLIALVCSGIALYSMGVIMDENNLDSWPAP FT ALWVVAIVGVVGLLISLPGWFATKQTKKAS" FT CDS complement(258309..258803) FT /transl_table=11 FT /locus_tag="AARI_02450" FT /product="CoA-binding domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VS78" FT /db_xref="InterPro:IPR003781" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VS78" FT /protein_id="CBT74481.1" FT /translation="MSAAETTWEAPGAAQRLEILRQTKTIAIVGASNKPSRASYFVATY FT LLSSSKYKVYFINPVLDEILGQPVYKSLADLPETPDLVEVFRKHDDLPTVLDEALAVGA FT KTLWLQLGSWHEEVAHRAEAAGMNVVMDRCVKIEHARFHGGLRLAGFNTGVISSKRQVL FT A" FT CDS complement(258803..260176) FT /transl_table=11 FT /locus_tag="AARI_02460" FT /product="O-acetylhomoserine aminocarboxypropyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.5.1.49" FT /note="catalyses several reactions, including the formation FT of L-homocysteine from O-acetyl-L-homoserine and H2S, and FT the formation of L-methionine from O-acetyl-L- homoserine FT and methanethiol" FT /db_xref="GOA:E1VS79" 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:E1VS79" FT /protein_id="CBT74482.1" FT /translation="MADHKFGFRTRALHAGGTPDAEHGARAVPIYQSTSFVFKDADDAA FT NLFALQKYGNIYSRIGNPTVAAFEERMASLEGGIGAVATGSGMAAEFVTFAALAQAGDH FT IVASSKLYGGTITQLDVSLRRFGIDTTFVSSNDPADFEAAIQENTKAVYTEIVANPSGD FT IADLKGLAEVAHRHNLPLVVDSTLTPPYILRPIEHGADIVIHSATKFIGGHGTTLGGVV FT IESGKFNWGNGKFPTMTEPVASYGNVSWWDNFGEYGFLTKLRSEQLRDFGPSLPAQSAF FT QLLQGLETLPQRMDNHLSNAKQVAAWLEADERVTYVNYAGLESHPQYAQAKELLPMGVG FT SVFSFGVKGGREAGSKFIEALQLASHLANIGDARTLVLHPASTTHQQLSADQLVSAGVP FT EDLIRLSVGLEDLEDILWDLDQALTASQEAVAGATEEFAAPTYDGAACAIPAASKGAN" FT CDS 260498..261058 FT /transl_table=11 FT /locus_tag="AARI_02470" FT /product="phosphoglycerate mutase family protein" FT /function="2 Intermediary metabolism" FT /note="identified by match to protein domain PF00300" FT /db_xref="GOA:E1VS80" FT /db_xref="InterPro:IPR001345" FT /db_xref="InterPro:IPR013078" FT /db_xref="UniProtKB/TrEMBL:E1VS80" FT /protein_id="CBT74483.1" FT /translation="METSLALVRHGQTDWNLAGRLQGRTDIPLNETGREQARAVGRALA FT GQGWSLILGSPLERAQETATLMAEQLGAATGDAVPELIERGFGPLEGRIMAEVSEEETA FT AAKDQLEPRADILSRAIPALLELAKAHAGTKIMIVSHGATMRNIRDALAGTKEARGVEN FT GEVLDIDSHRLQQLADELDLVAL" FT CDS 261179..261676 FT /transl_table=11 FT /locus_tag="AARI_02480" FT /product="RNA polymerase sigma factor" FT /function="3.5.1 Transcription initiation" FT /note="match to protein family TIGR02937. Sigma-70 family" FT /db_xref="GOA:E1VS81" FT /db_xref="InterPro:IPR007627" 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:E1VS81" FT /protein_id="CBT74484.1" FT /translation="MQAPFERIVQEYGLNVLRVCRALLDEHRAQDAWSETFLAALKAYP FT NLPEDANVAAWLVRIAHNKAIDELRKHKPESLVEIDLEGTLDSGPGPGAQLENLQLWHE FT VNQLPPKQRQVIAYRYLGGLSYAGIAGIISGSEAAARRAGADGIKNLRARLGESELWRE FT QP" FT CDS 261673..262299 FT /transl_table=11 FT /gene="ogt" FT /locus_tag="AARI_02490" FT /product="methylated-DNA--[protein]-cysteine FT S-methyltransferase" FT /function="3.3 DNA recombination, and repair" FT /EC_number="2.1.1.63" FT /note="involved in the repair of alkylated DNA" FT /db_xref="GOA:E1VS82" FT /db_xref="InterPro:IPR001497" FT /db_xref="InterPro:IPR008332" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014048" FT /db_xref="UniProtKB/TrEMBL:E1VS82" FT /protein_id="CBT74485.1" FT /translation="MNKSKAQEPGTEDSAVLASLGQKLAAQAHEQALVDVAYRIVDSPL FT GSLLLASTQNGLARVAFESEDHDRILELLSEKLGSRILRDAKRLDAAARQLDEYFSGQR FT QGFELALDLTLSTDFRRQVQLQLGQIAYGQTCSYAQMAQQIGKPKAVRAVGSACATNPI FT PIVLPCHRVLRTDGSLGGYLGGLEAKSELLKLENPHFAEQGATLF" FT CDS complement(262397..264577) FT /transl_table=11 FT /locus_tag="AARI_02500" FT /product="peroxidase/catalase" FT /function="4.2 Detoxification" FT /EC_number="1.11.1.6" FT /note="haem-containing catalase-peroxidases are FT bifunctional antioxidant enzymes that exhibit both catalase FT and broad-spectrum peroxidase activities, depending on the FT steady-state concentration of hydrogen peroxide" FT /db_xref="GOA:E1VS83" FT /db_xref="InterPro:IPR000763" FT /db_xref="InterPro:IPR002016" FT /db_xref="InterPro:IPR010255" FT /db_xref="InterPro:IPR019793" FT /db_xref="InterPro:IPR019794" FT /db_xref="UniProtKB/TrEMBL:E1VS83" FT /protein_id="CBT74486.1" FT /translation="MSETTAGQCPVVGQGRIHPTQGNANTEWWPNKLNLKILAKNQQVS FT NPLDEDFDYIEAFNALDMEALKADLIENMTTRQDWWPADFNHYGPLYIRMAWHSAGTYR FT SHDGRGGGGAGQQRFAPLNAWPDNVGLDKARRLLWPVKKKYGQSISWADLMILAGNVAM FT EHMGLKTFGFAGGRKDVWEADDDVYWGPEKVWLDNERYSGERDLEAPLAAVQMGLIYVN FT PEGPDGNPDPLASAIDVRETFRRMGMDDYETVALIAGGHTFGKTHGANNVDRIGADPEA FT APLEEQGLGWKNGYGEGNAENNTASGLEVTWTYHPTRWDNEFFHILFAYEWELFESAAG FT AKQWRPVNGGGAGLVQPAHDTLEHREPRMLTSDLALRFDPIYGPISKNFKENPDEFAEA FT YARAWFKLTHRDMGPKSRYFGPEVPAEDLAWQDPLPAAPQVTLGVQEIAALKALINDSG FT LTVQQLVSTAWKAASSFRSSDKRGGANGGRIRLEPQVSWTVNQPEQLKPVIAKLEEIVD FT TFNATSEIKASFADVVVLAGNVGVEQAAAAAGQPIEVPFTPGRVDATQEQTDVEQFAWL FT EPVSDGLRNYDSGFIKMPSEYLLIDKANLLGLSAPELTVLVGGLRVLGNNWDGSNLGVF FT TENPGALTNDFFANLLEPGIGWTASEDEQTYHSKDGRWVGSRVDLVFGANSELRAVAEV FT YASDDAKTKFVKDFAQAWAKVMDSDRFELRRK" FT CDS complement(264680..265108) FT /transl_table=11 FT /gene="fur" FT /locus_tag="AARI_02510" FT /product="ferric uptake regulation protein" FT /function="3.5.2 Transcription regulation" FT /note="acts as a global negative controlling element, FT employing Fe(2+) as a cofactor to bind the operator of the FT repressed genes. Match to protein family PF01475" FT /db_xref="GOA:E1VS84" FT /db_xref="InterPro:IPR002481" FT /db_xref="UniProtKB/TrEMBL:E1VS84" FT /protein_id="CBT74487.1" FT /translation="MTSEAGIEQVLKAASMRVTQPRVAVLAAVAAHPHADTETIISAVH FT GDHPHVSHQAVYDSLKLFTKLGVIRQIQPQGHIARYETRVGDNHHHVVCRQCGNLADVD FT CAVGEAPCLHASDHHGFIIDEAEVIYWGICPQCQVVNA" FT CDS 266135..267661 FT /transl_table=11 FT /locus_tag="AARI_02520" FT /product="possible betaine/carnitine/choline transporter" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="betaine/carnitine/choline fransporter (BCCT) family FT (TC 2.A.15.y.z)" FT /db_xref="GOA:E1VS86" FT /db_xref="InterPro:IPR000060" FT /db_xref="InterPro:IPR018093" FT /db_xref="UniProtKB/TrEMBL:E1VS86" FT /protein_id="CBT74488.1" FT /translation="MMFATGMGIGLVFYGVGEPLYFYMSPPPGTVEGSTDAALSTAMGT FT TLFHWTLFPWAMYAIVGLGMAYGSFRLGRPQLFSAMFTPIFGERAVHGWGGRIINVLAI FT IATLFGSACSLGLGALQIGGGIQATGMMEKVGSGVLVVIIAILTAMFVASAVSGIERGI FT QWLSNTNMVLALILALIVFIGGPTLFILNDIPNAVGAFIGDLPEMASRTAASGDGAMSD FT WLSSWTVFYWAWWISWSPFVGLFIARISRGRTIRQFVTGVLLVPSTVTLIWFAIFGGGA FT IGIQERAERAGETGQKLANMVDGAPDINFDLVLFDLLGSLPVANWVAVLLMVVTVLLIA FT IFFVTGADSASIVMGALSERGAENPSKKSVIFWGVATGAVAAVMLLAGGDHPAEALNGL FT KNITIVSALPFVIVMLLLCVAIWKDLSKDPLILRGKVAREVLEHSVVQGVERHEGSGFS FT LLTTEIPMVVADEKSGEAKIFATEATVDPASGSKPDAADGDSKATEPKNS" FT CDS complement(267727..269688) FT /transl_table=11 FT /gene="acsA" FT /locus_tag="AARI_02530" FT /product="acetate--CoA ligase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="6.2.1.1" FT /note="catalyzes the formation of acetyl-CoA from acetate FT and CoA" FT /db_xref="GOA:E1VS85" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR011904" FT /db_xref="InterPro:IPR020845" FT /db_xref="InterPro:IPR024597" FT /db_xref="UniProtKB/TrEMBL:E1VS85" FT /protein_id="CBT74489.1" FT /translation="MTTELAHTSAAASEAARQEFWDEAANLLDWDTPWHTTSQILPADP FT AAQRGPQISWYLGGKLNAAVNCADRHVAAGHGDKVALYFEGEPGDRVAVTYKNLQERIS FT QAANALESLGVVKGDRVVIYLPVLIETIVITLACARIGAIHSLVFGGFSAEALKFRVED FT TKAKVLVTTDGQFRRGTSVPVKDNADAAVAGENEIEKVLVIRRTGDEIPWTEGRDVWWH FT DVVDTQSTQHQAQAFDSETPLFIMYTSGTTGQPKGLVHTTGGYLTQAAASYNLLFANPD FT ESQRADDVHWCTADLAWVTAHTYEIYGPLANGVTQVIYEGVPNAPHPGRHFEVIERYKV FT TSYYTAPTLVRSLMGWFPEGLPAKYDLSSIKIGGTVGEAVNPEAWKWFREQIGRDSAAG FT LPMVDTWWQSESGATILSPLPTDDHFKPGCAARALPGISVDIVDAEGRSVAPNQQGNIV FT ITQTGPSMARTVWGNPQRYYTSYWEQYVQQGWFLAGDGARFDEDGDIYILGRTDDVINI FT SGHRLSTIEIESALVTHPGVIEAGVCPTADAKTGHAATAFVVPLDASLICEHPDEQLGA FT RQAEFIAQLRSTVATQIGPIAKPREVVLVPDVPKTRSGKIMRRLLTQLFEGSKLGDTTS FT LQNEPCIPQINEVCRARD" FT CDS complement(269753..270580) FT /transl_table=11 FT /gene="ssuC" FT /locus_tag="AARI_02540" FT /product="putative aliphatic sulfonates ABC transporter, FT inner membrane subunit SsuC" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT taurine uptake transporter (TauT) family (TC3.A.1.17). FT ABCISSE: ABC transporter, permease (IM), OTCN-family FT (osmoprotectants, taurine, cyanate and nitrate), aliphatic FT sulfonates import. Part of the ABC transporter complex FT ssuABC involved in aliphatic sulfonates import. Is also FT involved in taurine transport" FT /db_xref="GOA:E1VS87" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VS87" FT /protein_id="CBT74490.1" FT /translation="MSTPTVPQTRKAQPAGRQKSEIAATILRAPKWLLASVLPILTLAV FT WQYVTVTEIVAPWTLPTPGSVAAAAVELFQDGELGPHIGISTQRVLLGFFFGSLLGLAF FT GALVGLSKLADAFLGLSISALRAVPSLAWVPLLVLWMKYGEDSKVTLVIIGAFFPVFTT FT VALALRHVDAQLVEAARSFGLKGLKLLRTVQLPAVVPAIFSGLRLALAQAWLFLVAAEL FT LGASMGLGFLLTDSQNNGRLDRLIMTIVLLAIFGKITDALLSVAERWAIKRWT" FT CDS complement(270587..271609) FT /transl_table=11 FT /gene="ssuA" FT /locus_tag="AARI_02550" FT /product="putative aliphatic sulfonates ABC transporter, FT substrate-binding protein SsuA" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT taurine uptake transporter (TauT) family (TC 3.A.1.17.z). FT ABCISSE: ABC transporter, permease (IM), OTCN-family FT (osmoprotectants, taurine, cyanate and nitrate), aliphatic FT sulfonates import. Part of the ABC transporter complex FT ssuABC involved in aliphatic sulfonates import" FT /db_xref="GOA:E1VS88" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR010067" FT /db_xref="InterPro:IPR015168" FT /db_xref="UniProtKB/TrEMBL:E1VS88" FT /protein_id="CBT74491.1" FT /translation="MLSNRFTRRTALSAAALLLGTSALAGCAGENATAANADKTLSIDF FT ATYNPLSLVLKEKGWLDEAAKESGVSVEWIQSAGSNKANEALRADAIDVGSTAGSAALL FT ARSNGSPIKTIALYSQPEWAALVIGKDSKISSVKDLKGKTVAATKGTDPYFFLLQSLEE FT AGLSEDDIKLQNLQHADGRTALANGSVDAWSGLDPIMAAAEEDGASLVYRNLDFNTYGA FT LNAREDFIEESPELAQLVVDSYEKARAWATENPEETAEILADVAGLGPEVATTVIEERS FT NLDVPAAPSEKYTSVLLNIGPTLVASGDVSKQESVDEALATLVDDQFATQADATKISGE FT " FT CDS complement(271695..272516) FT /transl_table=11 FT /gene="ssuB" FT /locus_tag="AARI_02560" FT /product="putative aliphatic sulfonates ABC transporter, FT ATP-binding subunit SsuB" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT taurine uptake transporter (TauT) family (TC 3.A.1.17.z). FT ABCISSE: ABC transporter, ATP-binding protein (ABC), OTCN- FT family (osmoprotectants, taurine, cyanate and nitrate), FT aliphatic sulfonates import. Part of the ABC transporter FT complex ssuABC involved in aliphatic sulfonates import" FT /db_xref="GOA:E1VS89" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VS89" FT /protein_id="CBT74492.1" FT /translation="MALTYAAPPTGTSAASSGALDVSFTDVSRTFTTKKESRTVLAAIN FT LQITAGQVVAILGASGCGKSTLLRSVSGLDHPSTGSIRTGNHDVNGINDLCAVAFQEPR FT LLPWRSVRENIALGLAPGTEKSAGETLIDELIELTGLSHAAHLRPREISGGMAQRVSLA FT RALARRPGVLLLDEPFGALDALTRLKMQDLLLSIHKSFPTTVLMVTHDVDEALTLADRV FT IVLGRAGTTGAASVIEDLSLHAAQPRRHTDSQFAAHRAHLLRLLGVDPTNH" FT CDS 272997..274328 FT /transl_table=11 FT /locus_tag="AARI_02570" FT /product="putative acyl-CoA dehydrogenase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.3.99.-" FT /note="possibly involved in the metabolism of lipids. Match FT to PF08028. Acyl-CoA dehydrogenases catalyze the FT alpha,beta-dehydrogenation of acyl-CoA thioesters to the FT corresponding trans 2,3-enoyl CoA-products with FT concommitant reduction of enzyme-bound FAD" FT /db_xref="GOA:E1VS90" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR009075" FT /db_xref="InterPro:IPR009100" FT /db_xref="InterPro:IPR013107" FT /db_xref="InterPro:IPR013786" FT /db_xref="UniProtKB/TrEMBL:E1VS90" FT /protein_id="CBT74493.1" FT /translation="MPIGHSPNADGLDFNQLSDPSQATALELDNFEEQLPTRQLLKITP FT GPSADEQYDRLAGIFRPVFSQIAANAKDRDLNRVLPFEQVGLLNRERFGALRLPVADGG FT YGARLSDVFRLLIELSEADSHVGQLWRAHIAFVENVLALDDEALRTKWIARIAAGQIIG FT NAYTERGGNALGTLNTAASLVDGRWVVDGEKYYCTGTIFADWTTVAVSHPELAGRQIAV FT VSTQRSGVKILDDWDGFGQGLTGTGTTEFRQVPVDCFMPQQTNDSEAAIFQLVLMAVQA FT GIARAALNDLRRAVQSRTRIFTTGTGVPVYQEPQVLQLVGEVSAESFAADSVVIGAVLE FT VEAALGDPGLNDEERYAVCELAANRAQTVVQPLAIGVTSKIFDGLGASSTRSGCNLDRH FT WRNARTIATHNPAIYKARIVGDYEINGVQPQRLSVTGEDSTHRA" FT CDS 274382..275785 FT /transl_table=11 FT /locus_tag="AARI_02580" FT /product="putative luciferase-like monooxygenase" FT /function="2.4 Metabolism of lipids" FT /note="possibly involved in the metabolism of lipids. FT Identified by match to PF00296. Bacterial luciferase is a FT flavin monooxygenase that catalyses the oxidation of long- FT chain aldehydes and releases energy in the form of visible FT light, and which uses flavin as a substrate rather than a FT cofactor. There are structural similarities between FT bacterial luciferase and nonfluorescent flavoproteins FT (LuxF, FP390), alkanesulfonate monooxygenase (SsuD), and FT coenzyme F420-dependent terahydromethanopterin reductase, FT which make up clearly related families with somewhat FT different folds" FT /db_xref="GOA:E1VS91" FT /db_xref="InterPro:IPR011251" FT /db_xref="InterPro:IPR016215" FT /db_xref="UniProtKB/TrEMBL:E1VS91" FT /protein_id="CBT74494.1" FT /translation="MSENKREILFNAFDMNCVVHQSPGLWRHPDDKASTYNTLGYWTHL FT AKVLEKGKFHGLFLADVLGTYDVYKGTNVTPLSSGAQAPVNDPMMLVSAMAAVTENLGF FT GVTAGTAYEHPYAFARRLATLDHLTNGRVGWNVVTGYLPSAARNMGQEDQMEHDERYNH FT ADEYLEVVYKLLEGSWEDDAVQNDKETGIYTDPGKVHPINHEGKYFKVPGIAITEPSTQ FT RTPVIYQAGASKRGTEFAASNAEAIFVNCPTRDLLKEAVAKIRDAAEAAGRGRYDIKVF FT AMQTIITGETSELAQAKFEDYASYVDIEGSLALLSGWTGIDMSVYGPDDVIGDDVKSNA FT IQSSVETFKKASGDTGKPWTIRQLAEWIGVGGFGPVSVGSGAEVAEKLIDWVEHTDVDG FT FNLAYAVTPGTFEDVVEYVVPELQARGVYKTDYAEGSLRNKLFGEGDRVKDTHRAAKYK FT VANRLAPQA" FT CDS complement(275862..277685) FT /transl_table=11 FT /gene="ggt" FT /locus_tag="AARI_02590" FT /product="gamma-glutamyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.3.2.2" FT /note="catalyzes the transfer of the gamma-glutamyl moiety FT of glutathione to an acceptor that may be an amino acid, a FT peptide or water (forming glutamate)" FT /db_xref="GOA:E1VS92" FT /db_xref="InterPro:IPR000101" FT /db_xref="UniProtKB/TrEMBL:E1VS92" FT /protein_id="CBT74495.1" FT /translation="MSRARLRSVACAAVIALGLGAFSALPASAEPRHTQKDSTAIGTGG FT AVSSVDPEATAAGIEVLRKGGNAVDAAVATAAALGVTEPYSAGIGGGGYFLYYDAKSGK FT VSTIDGRETAPAGISHDAFIDPATGDPYNFTPELVTSGVAVGVPGTLATWQRALDNWGS FT QNLKQVLRPATQIASRGFVVDETFREQTLDNKERFNAFDSTSQLFLPGGDAPQVGTIFK FT NPDLAATYRMLAKQDLDGFYEGPLATEIAQSVQAPPTSDDTTLPVPAGTLSTADLAGYE FT VVEQAPTTVNYRGYEVFGMAPSSSGGTTIGESLNILSEFNLSAMDEPDALHLYFEATAL FT AYADRGKFVGDPAFVQVPTQALTDKLFGADRACAIDPQQAAVKPVAPGDVENYDGRCPA FT DTGEPVAEQDTENISTTHLSVVDRWGNMVSYTLTIEQTGGSGMVVPGRGFLLNNELTDF FT STVYDPADPNRIDPGKRPRSSMTPTIVLQDGKPVLAIGSPGGSTIITTVLQTLVNRIDL FT GMDISQAIAAPRASQRNTAAVTAEPEFIDAHGAALEAFGHKLTAAGDSFTPQAEIGAVE FT AVEIAADGTLTAAAEPSRRGGGSAMVLEPID" FT CDS complement(277900..278763) FT /transl_table=11 FT /locus_tag="AARI_02600" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VS93" FT /db_xref="InterPro:IPR008030" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VS93" FT /protein_id="CBT74496.1" FT /translation="MKIAVTGATGQLGNLVVDALLARGAKAADLVAIGRSAQKLEPLAG FT KGLETRVADYNVEQALISALKGVDKLLLISASEVGQRVAQHENVINAAKKVDVQLIAYT FT SIANALTGGMKLAEEHIATERLLAGSGIDYVLLRNGWYIENYTDQLMGYLNSGMVLGAA FT GEGKISAAARADYADAAAAVLLSEEEQSGKIYELGSDKPFTLTQLAGAVGAAAGQDVAY FT QQMDPEQLEKIYADAGVPAAFAHILVDTDLRVREGALEVNSGDLAKLIGRTPASLGKVI FT KENLDK" FT CDS 279257..280276 FT /transl_table=11 FT /gene="metN" FT /locus_tag="AARI_02610" FT /product="methionine ABC transporter, ATP-binding subunit FT MetN" FT /function="1.2.5 Transport/binding of amino-acids" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT methionine uptake transporter (MUT) family (TC 3.A.1.24.z). FT ABCISSE: ABC transporter, ATP-binding protein (ABC), FT DLM-family. Part of the ABC transporter complex MetNIQ FT involved in methionine import. The complex is composed of FT two ATP-binding proteins (MetN), two transmembrane proteins FT (MetI) and a solute-binding protein (MetQ)" FT /db_xref="GOA:E1VS94" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VS94" FT /protein_id="CBT74497.1" FT /translation="MIEIKDLHKHYDTAQGRIEVLKGIDLSVPEGSITAVVGPSGAGKS FT TLSHCISLLEKPSSGQILIDGKDLGALSGRALRAERRAIGTIFQNSALLSRLSVAENVA FT LPLRNLGVVHHEMQQRVAQLLDRVGLLEKADAYPGQLSGGQRQRVGIARALALRPRLLL FT SDEATSGLDPESTHQVLGLLDSLRSDLGLSIILITHEMDVVRHVADEVAQLASGRIAEH FT GALHELVASPGSATGEKLLPLRSEELPAGFDYAVTVAYRKDRVDPGWISRLGIEHGIAV FT ALLGGAVEAHHEGTLGRVRLGVQGATPQDLLRLLDGWGLQADPGSLARNNHELVEANA" FT CDS 280273..280968 FT /transl_table=11 FT /gene="metI" FT /locus_tag="AARI_02620" FT /product="methionine ABC transporter, inner membrane FT subunit MetI" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT methionine uptake transporter (MUT) family (TC 3.A.1.24.z). FT ABCISSE: ABC transporter, permease (IM), DLM- family. Part FT of the ABC transporter complex MetNIQ involved in FT methionine import. The complex is composed of two FT ATP-binding proteins (MetN), two transmembrane proteins FT (MetI) and a solute-binding protein (MetQ)" FT /db_xref="GOA:E1VS95" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VS95" FT /protein_id="CBT74498.1" FT /translation="MRIPFESAAVGTDTPWQQLPALMLPAYGQTWAMVGIVMALVISLG FT GLMGIALYNTDRQGLFPRARLHAVLSWIANMGRSLPFLVLMAAIIPFTKWVTGTTIGIA FT AAAVPMTIAGIPFFARLVQNALNDLPRHNLAVGLVTGGSAAQIIGTTQIREALPALASA FT ITLNTISMIEYSAIAGTIGAGGIGYLAVTYGYQRFDMNVMLATIVVLILTVQIVQFLGD FT RIARALARP" FT CDS 280998..281909 FT /transl_table=11 FT /gene="metQ" FT /locus_tag="AARI_02630" FT /product="methionine ABC transporter, substrate-binding FT protein MetQ" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT methionine uptake transporter (MUT) family (TC 3.A.1.24.z). FT ABCISSE: ABC transporter, lipoprotein (LPP), DLM-family. FT Part of the ABC transporter complex metNIQ involved in FT methionine import. The complex is composed of two FT ATP-binding proteins (MetN), two transmembrane proteins FT (MetI) and a solute-binding protein (MetQ)" FT /db_xref="InterPro:IPR004872" FT /db_xref="UniProtKB/TrEMBL:E1VS96" FT /protein_id="CBT74499.1" FT /translation="MTTPHTGHDHGFTLRKNRNALPWTIAALAAVAALILGVLLGQQRS FT APAAASAAGNQTKFTVHFEPAMAGEEKILDFVAQQIAPDYGIEIEKVGLQDPIQANQAV FT ASGQFDATIFEHQWYMKQSAEAAGVELEPTVELFQWGFGLYSNHYDSVEDIPRGASLLL FT PNDVANQGQALWLLQREGLLGLDPDIEPRTAKIPDVIDNPRGFELKEADLLAMPRMLDD FT VGVAIGYVSQFDAGKVDREQGILFPEPPKTFASRLVMGAEYAKSADAQKLVEAFSDPRL FT QEYLATTEDPLVQGVLTPVSGS" FT CDS 282353..284050 FT /transl_table=11 FT /locus_tag="AARI_02640" FT /product="putative dipeptide/oligopeptide ABC transporter, FT substrate-binding protein" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5). ABCISSE: ABC transporter, binding protein (BP), FT OPN-family (oligopeptides and nickel), oligopeptides FT import" FT /db_xref="GOA:E1VS97" FT /db_xref="InterPro:IPR000914" FT /db_xref="UniProtKB/TrEMBL:E1VS97" FT /protein_id="CBT74500.1" FT /translation="MAERAANLGVILGSPTERTFEIMRTAHFGLKTTAILAVLGLSLTA FT CGGNATKTGAAQAAADPETPVEGGTFTFAEVTPINNWQTQAARFYEKANVLNSVLDRLT FT YYDVEAGKLVGWIASEFEANEDQTEFTFTIRDGVTFSDGSTLDAEAVKLNLDALGKGIK FT SAQIAPNVDFAAYKSAEVVGDNKVKVTLKRPDANFLRSTSSVTAGLVSPKTLELDNAAQ FT SSISKIVGSGPFVFESEKPDEEVVFSSRDDYAWAPETAPNQGDAYLDTLVIKYLPEVAS FT RAGAAQSGQVDLVRGLQPVDEQVLASSGGKVYAAEGVDLTTNHAAVRIGSGKLEDVKVR FT QALQVAIDRQAIKDTVLSDSYVISGSILNHKAPGFVDLSAELAYNPEKAKQLLDEAGWK FT PGADGIREKDGKKLEVTVSTSNNSVVIKPAFELIEQQWREIGVQLINRAADNTFLTNAL FT VDDKVEFYGTRQFAYGGLGPVYAPANNNQTLRADPELNKLFTKEQSATTDEEHLKLVEE FT EQRALVLDKALTLVLWDEVQVYGANSSANVEFTSGTAPIFQGAWKSEG" FT CDS 284062..285018 FT /transl_table=11 FT /locus_tag="AARI_02650" FT /product="dipeptide/oligopeptide ABC transporter, inner FT membrane subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, permease (IM), OPN- FT family (oligopeptides and nickel), oligopeptides import" FT /db_xref="GOA:E1VS98" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VS98" FT /protein_id="CBT74501.1" FT /translation="MGTYIVKRLGQALLVIWLAYTAVFIAVQSLPNDPVTIFLSTDSAA FT DPATIAQMKAYYGYDQPLFVQYFSQLLGLLRGDLGYSLSNGSEVATRIGEVAGSTLILA FT GSAFVLSVVFALIIASAASLARGGKLRKALLNLPPLMVSIPVFWLGLLLLQLLAVQLGV FT MSLFPDGSFMSLAVPIFVLAVHLSAPIAQVLIKSVQEVNRQPFIEVLRAKGASEAWIFY FT RHTLKNAAPAALSIAGITIGALLAGSVITETVFSRAGLGQLILQSVTAQDIPLVQGLVL FT LTAVVFTAVNLLVDLIHPQLDPRIVTSTSGATRSLVA" FT CDS 285033..285920 FT /transl_table=11 FT /locus_tag="AARI_02660" FT /product="dipeptide/oligopeptide ABC transporter, inner FT membrane subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, permease (IM), OPN- FT family (oligopeptides and nickel), oligopeptides import" FT /db_xref="GOA:E1VS99" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VS99" FT /protein_id="CBT74502.1" FT /translation="MSLITEHVGSVASDVQPMASTKPATKIGNPAARWFAAWWVLIPLA FT VFVAWAFLPSLFTGHDPITGVPADKLLAPSADHLFGTDHLGRDIYSRVVYGTRQTLLTA FT GLACLVGSVVGSILGLLAGTAGRFADTVAMRFVDIVLAVPAFLIALILVTATEPGPLSL FT GLGVGIASIAAFARLVRTEVLRVRSRDFVQAALMSGGKYFTVLRRHIIPHIVGPVLSLL FT AVDLGAAILAISGLGFLGFGSPPPTPEWGLLISEGRQYLSVAWWLTTLPGLVIVSAVML FT TAVLGRAINKAFRF" FT CDS 285949..287571 FT /transl_table=11 FT /locus_tag="AARI_02670" FT /product="dipeptide/oligopeptide ABC transporter, FT ATP-binding subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, fused ATP-binding FT protein (ABC2), OPN-family (oligopeptides and nickel), FT oligopeptides import" FT /db_xref="GOA:E1VSA0" 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:E1VSA0" FT /protein_id="CBT74503.1" FT /translation="MNATSNASSAVIRIEDLTVQYAQGTVAADSINLEIPAGQIVAIVG FT ESGSGKSTLTKTLIGLLPQGTEVQGSVRFGGTEVTNLSLSDWRAIRGAGIGLVPQDPGA FT SLDPVKTIGSQIIEVFRLHPSRSVPKAQWRSKAIELMQSVGIDRAESRLDQFPHELSGG FT LKQRVLIAIAFALNPQLLIADEPTSALDVTVQRTVLEVFVSLARKKGTTVLFVTHDLAV FT ATDIADRVLVMNSGRVLEDRSVPALVAQSTEPYTKALLDQAYAHQDRQQPSTSDDIAIT FT VEGLGKVFGKGSNEHQVLSGVSFEVQRGTTFSLVGESGSGKSTTAKIIMGMHPATEGSV FT RVNGREVANISGKQRYDLWRDAQLVYQNPDSALDPRQSIGSIIAEPMVNYRLGDSAWRA FT QRVAQLMEQVNLPEQLAGRRPAELSGGQRQRVAIARALASGAKILVLDEALSALDVLTQ FT EQILELLDQLQREEQLTYLFISHDLHVVERISHRVGVMCRGQIVESGTVDEIYSNPQHE FT YTRTLLAANPGKVLRELADTRTV" FT CDS 287610..288851 FT /transl_table=11 FT /locus_tag="AARI_02680" FT /product="putative acyl-CoA dehydrogenase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.3.99.-" FT /note="possibly involved in the metabolism of lipids. Match FT to PF08028. Acyl-CoA dehydrogenases catalyze the FT alpha,beta-dehydrogenation of acyl-CoA thioesters to the FT corresponding trans 2,3-enoyl CoA-products with FT concommitant reduction of enzyme-bound FAD" FT /db_xref="GOA:E1VSA1" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR006092" FT /db_xref="InterPro:IPR009075" FT /db_xref="InterPro:IPR009100" FT /db_xref="InterPro:IPR013107" FT /db_xref="InterPro:IPR013786" FT /db_xref="UniProtKB/TrEMBL:E1VSA1" FT /protein_id="CBT74504.1" FT /translation="MSTEALATFRPSAQQHTEAAYQELLAHFSQVFARIAQGATEREQQ FT RILPFEQVQWLKDAGFTTLRVPASHGGSPVSHEHLFRLLIELAAADSNVAHLLRSHFSF FT VETIALQPQEFQDRWFPRVLAGEIFGNAATERGGNALGSTNTKLVKTDAGWVLRGEKYY FT TTGSIFADWVVVMATTDGVEGRQYAVVERHAKGVKILDDWDGFGQPLTGTGTAIFTDVA FT VDEQNIIQRKVASTLEPAFFQLCLLSVLVGIGKAARNEAARIVATRTRTFNTGSGALFK FT DDPQIQELVGRLASNVFAAESIVVSAARDLDAALDESLGLNAEEAFLRAELAVQQAHVA FT APKLVLDATSELFDVTGASAVSTSKSLDRFWRNARTVATHNPVAFKARSVGDYFINGTI FT PTGLHSIGEAKGAK" FT CDS 288854..290272 FT /transl_table=11 FT /locus_tag="AARI_02690" FT /product="putative luciferase-like monooxygenase" FT /function="2.4 Metabolism of lipids" FT /note="possibly involved in the metabolism of lipids. FT Identified by match to PF00296. Bacterial luciferase is a FT flavin monooxygenase that catalyses the oxidation of long- FT chain aldehydes and releases energy in the form of visible FT light, and which uses flavin as a substrate rather than a FT cofactor. There are structural similarities between FT bacterial luciferase and nonfluorescent flavoproteins FT (LuxF, FP390), alkanesulfonate monooxygenase (SsuD), and FT coenzyme F420-dependent terahydromethanopterin reductase, FT which make up clearly related families with somewhat FT different folds" FT /db_xref="GOA:E1VSA2" FT /db_xref="InterPro:IPR011251" FT /db_xref="InterPro:IPR016215" FT /db_xref="UniProtKB/TrEMBL:E1VSA2" FT /protein_id="CBT74505.1" FT /translation="MGTFESRPRFLLSAFLMNTSSHILGGMWRHPEAQQHKFNELELWV FT DLAKKLEDAKFDNLFFADVVGLYGDHEGGWASHVRKGMQVPSHDPMVLLSALAATTKDI FT GLAMTSSVIQAHPFQFARQLSTLDHLSRGRVAWNIVTSVLENSHRNFGGASLVAHDDRY FT AWAEEYVEAAYKLWEGSWEDDALLADKESGIYADPARVNKINHRGELYSIDGPHLALPS FT AQRTPFLFQAGSSPRGSQFAATHAEATFLFAPHPQYVAKKNAQLTSNLQAAGRTREDIK FT VFAGLSFVVGSTEAEAKALEAEYDQYLDPHAIIAHIGGGIGVDLGGLDLDTPLGNVKTE FT GAQGVLEAALASTPGRNPTLRDLAHYRAKAQQIVGTPEQIVDELERWQDAGIDGLNIMN FT HILPGSYDNFIEGVLPELHKRGLAQREYVPGSLRQKFFGRGDKLPQNHPAAQYRGVFSE FT LSAANTEVSLQEQV" FT gene 290379..290633 FT /pseudo FT /locus_tag="AARI_02700" FT /product="truncated CoA-binding domain protein" FT /note="N-terminal section of a CoA-binding domain protein" FT CDS 291018..294218 FT /transl_table=11 FT /locus_tag="AARI_02710" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.987) with cleavage site probability 0.986 FT between position 61 and 62. 1 transmembrane helice FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="GOA:E1VSA3" FT /db_xref="InterPro:IPR001899" FT /db_xref="InterPro:IPR002035" FT /db_xref="InterPro:IPR008454" FT /db_xref="InterPro:IPR019931" FT /db_xref="UniProtKB/TrEMBL:E1VSA3" FT /protein_id="CBT74506.1" FT /translation="MFGKPDGDGFVRSRDAQNRQSRTLHRDGTWKNRTLRAVGGLSLSA FT ALVASMSFSGVVPSFAAGTNQTDETVTATAEPSASLQTSPSDEETSSAKSLDEVSEPTA FT ESELAESSRDGSSSDIEAASDAPEAVDEDVAERQADVAVSPLSLDANGNSVVKTPTRTS FT TIIKVTKGDVRTAETTIASNFSTGARFQLYYVRWNGSIGDAVTEPWGTCQIEAGDNGIC FT YFSVPNTNNGGANRTKFYIRELAPAAGSLAAQNYNVLSKFNTGANGSTESTYQYRTKTL FT TSNSTISMPADHDGALRTADASSGTWANSIKNPTLPVTCELGIKVALVFDLSGSVKNAG FT AADTLGNAGKGFVDALSGTNSSVALFSFGNTSPRAGTPNFPELRNIDSGTNSTRIKNDI FT QDYINSFSGEGYTSNGTNWDAGLWATAQNAKQYDLVVVLTDGNPTFSGIESTVGPGTST FT YFRELEAAVFSANAVKAQGARIINVGIGEGLNADNNLAATSGPVKYSPGASLNTADYLN FT VGWEALKPLLEDFAKSISCQAGVTVTKKVKDLGGTTKVASGWTIDAATQTGNASLTPET FT SQQTNTDGEVKFDLGFSKPDGKETVQIAETQQNGYKLSSVICTINDRTVQVSQSEKFTL FT ALTVGDKANCVITNEMKPSTPTVVKTSNPVSGTEIQPGEEIEYKLTFSTEGTFSTDIDY FT VDHLEGVLDDADLVAGSITADPGLNAVLSGKTIKITGAVSPGKPLNVTYKVKAKTENFG FT DGKAINFVVPNGQTPPEKCGPEDTTCTEHPIAGNLVVEKSSDPESGTSVLPGQRVNYTL FT NFANTGASEVDVNYIDYLADVLDDANFVEGSLETGQGLDATLVGDQIQITGKLKAESAA FT SVSYSVIIKESEFGNGIAKNFLVPDGEDPVCDPEQSNCTEHPVLGSVTWEKVDGGGTAL FT AGSEWELSGPGADGQQVAIEDCIEKTAAECTGADKDPAAGAFKLTGLTWGEYTLVETKA FT PAGYVLDDAEHRFTIGTSDDAKLIWDLGDMENEQRPALALPLTGGMGTQSFIITGSIAL FT MAALGVVAWRRRKAAAQG" FT CDS 294172..295839 FT /transl_table=11 FT /gene="fimA" FT /locus_tag="AARI_02720" FT /product="putative fimbrial structural subunit" FT /function="1.1 Cell wall" FT /note="identified by similarity to protein SP:O68212 FT (Actinomyces naeslundii). Fimbriae mediate bacterial FT adhesion. C-terminal Gram positive anchor (PF00746)" FT /db_xref="GOA:E1VSA4" FT /db_xref="InterPro:IPR001899" FT /db_xref="InterPro:IPR019931" FT /db_xref="InterPro:IPR019948" FT /db_xref="UniProtKB/TrEMBL:E1VSA4" FT /protein_id="CBT74507.1" FT /translation="MGLLPGDAERPRLRGNPGFRLKHQHSIHVLELYQISLAAVTGDIA FT AQKKGTAEMAEIKHTRGKRVLSGLGVLTLAAAGLLGGTGAALADDNSALNTGNIDQGRE FT GSIKIHKHKHQNGTSATQNPAGTGDAINSEGIAGVEFTAYQLTDIDLSDTNDWDQLDNL FT DLSNACTSIPGHTLGTPIVADVTNSQGVSTLTDLKLGAYVVCETDAPASVVDRSQPFVV FT AIPTPYENAWVYDVNVYPKNGTSDITKSIDPQSDLGLGGVVNFPVTVTVPKTKGDELLT FT KFEIVDTFDSRLGLNDDGVASVKLGGADVDSSYYTVSNDGQSVKVTFNEAGRQWLKSQG FT EKKVVVTFSAEVKEVGEISNDATAYINTPGHDGTIESDPVNTNWGDLVIQKLAAGSNAT FT LADAVFEVYAAEAPYAGGSCDTAVATGSALEVNGRTEFTSGPNGVVDIAGLFVSDSVNP FT TINAEQRCYVLKEVKAPTGYVTPTGAKALTGVAVKTGANTANVYDATIVNSQQDVPELP FT LTGANGQILMVIGGTAVLLLAGGLVIVSRRRSAREETK" FT CDS 295970..296908 FT /transl_table=11 FT /locus_tag="AARI_02730" FT /product="putative sortase" FT /function="1.1 Cell wall" FT /note="identified by match to protein family PF04203. FT Sortase is a transpeptidase that attaches surface proteins FT by the threonine of an LPXTG motif to the cell wall. FT Possible role in synthesis of functional type 2 fimbriae" FT /db_xref="InterPro:IPR005754" FT /db_xref="InterPro:IPR023365" FT /db_xref="UniProtKB/TrEMBL:E1VSA5" FT /protein_id="CBT74508.1" FT /translation="MPDTMTPPAGPRPAGVHRARRASRRWRPGLLTIASSLLALVGLSV FT LLYPSAASWMSSYNQSLLIEDMGRSLENASPGVDEQLSLAQRYNEALSTGVNLDANANV FT PTGSGTSSDASLRYEDMLNTGSSDVMARVRIPAIDVDLPIYHGTSDETLLRGVGHLEGS FT SLPIGGADTHSVLTAHRGLAQAEMFTNLDKVDVGDRFTIEVFGEVLTYQVRETKVVDPD FT DTDTLHAVAGEDLVTLVTCTPLGINSQRILVTGERVTPTPIEDVQAAGQAPDIPGFPWW FT ALIFGAGLLLIATYFWRSGYGDARRAAARKR" FT CDS 296956..297372 FT /transl_table=11 FT /locus_tag="AARI_02740" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007351" FT /db_xref="UniProtKB/TrEMBL:E1VSA6" FT /protein_id="CBT74509.1" FT /translation="MAEADKQSVELAWAELCLQLPCSYVDHPFGPDSTVFKVAGPDRSR FT GRMFALLLNLHGETVLNLKCEPALADQQRSEHPQITPGYHMNKKHWNSVRPGLDPHYVR FT ELIEDSYDLVVEGLPRRDQEHIRLQTKIADGSID" FT CDS 297377..297700 FT /transl_table=11 FT /locus_tag="AARI_02750" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007138" FT /db_xref="InterPro:IPR011008" FT /db_xref="UniProtKB/TrEMBL:E1VSA7" FT /protein_id="CBT74510.1" FT /translation="MYFIVVKYQVKPEFAATFMEHVAEFTRATRAEEGNLWFDWSVSVE FT NPNEYVLVEAFRDDDAAAAHVNSDHFAAGIDAMRPLLVSTPDIVSRKVDGEGWDKMGEL FT VID" FT CDS 297933..298043 FT /transl_table=11 FT /locus_tag="AARI_02760" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSA8" FT /protein_id="CBT74511.1" FT /translation="MLGTVLELPEGPVEELLDGLVDSEGCALARVFHEGR" FT repeat_region 298014..298017 FT /rpt_type=DIRECT FT mobile_element 298018..299755 FT /mobile_element_type="insertion sequence:ISAar8" FT /rpt_family="IS1380" FT repeat_region 298018..298035 FT /rpt_type=INVERTED FT CDS 298139..299575 FT /transl_table=11 FT /locus_tag="AARI_34440" FT /product="transposase of ISAar8, IS1380 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VSA9" FT /db_xref="InterPro:IPR002559" FT /db_xref="UniProtKB/TrEMBL:E1VSA9" FT /protein_id="CBT74512.1" FT /translation="MNHSTHVFPAIPTQLTGQSLVSHAGLSVLTSFLNALDFRRLCEDR FT FSQFVPATATHRPGKILGALTLSLAAGGEQATDIDQLRAAPDLFGSVASDATVSRFMGR FT IKEQPEAFSYGFATMTRSLRSKVWNAAGPRNPARLATAANPLIIDLDASLVHVHSEKES FT SAGTYKGGYGFSPMIAMADYGKANGTGEVLAVHLRPGNRGANSAKSHIEVLTQALAQLP FT DDFYDEHGNLHGEKILVRTDSAGSSREFLHHLDSLGLQFSTSYSLPVLKERFIRWIDEK FT KYWEPALDANGDQRDDAWVIDATKVLELRQYPPGTRIYLRAEPLHPGAKANLFDTDGNR FT VTAFLTNAPRFNVAFLDARHRARGRCENRIKTLKSTGLGKLPYWSFAANQAWADLAMFA FT LNLVAWLQLAVLPGGHEASVWDLKRWRYRLFSMAGKIVSGGRQRRLLIPVRAPEAQLLC FT QLQEGIGVFFQRWRRGELAA" FT repeat_region 299738..299755 FT /rpt_type=INVERTED FT CDS complement(299740..301776) FT /transl_table=11 FT /locus_tag="AARI_02770" FT /product="putative 5'-nucleotidase family protein" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.1.3.5" FT /note="5 -nucleotidases are enzymes that catalyze the FT hydrolysis of phosphate esterified at carbon 5 of the FT ribose and deoxyribose portions of nucleotide molecules" FT /db_xref="GOA:E1VSB0" FT /db_xref="InterPro:IPR004843" FT /db_xref="InterPro:IPR006179" FT /db_xref="InterPro:IPR008334" FT /db_xref="UniProtKB/TrEMBL:E1VSB0" FT /protein_id="CBT74513.1" FT /translation="MPAIGRIRTITLSTLTTAALVAAGCTVAQATTTPEADAESTFTLD FT LLDINDFHGRIGASSDSAGAAVLAGAVDQLRAANPYTLFVSAGDNIGASTFASASQDDN FT PTIDALGLGGLDVSAVGNHEFDKGFEDLIGRVTDRYAQASGGDGGDYTLGANVYEKGST FT TPALPEYALREVNGVSVGFIGTVTEDVPSLVSPSGITELDFGSELEAANRVAGQLSDGD FT DANGEADVIVLLTHNGSESADCSTIASETTSYGELVREADAQIDAIVSGHTHQSYDCQI FT AGPDGERPVIQAHQYGTTLGKVSLEIDEDSGEVVSSSTELLALTSQDAEGNWQTNYPAN FT STVQQIVDQAIADSEEVGSIEVGKISEDILRGGQPSGADRGVESTLGNTVADIHQWATS FT NENYGGEPTQIAFMNPGGLRADLLYGEDGTVSYKDAAEVQPFANTLVTFDLTGAQIREV FT LEQQWQPAGSERAKLHLGISEALAYTYLEDAPVGEHIQQITFNGEPLDEAATFHVVANA FT FLAAGGDNFTAFAEGTNHADSGQIDLDATVNYFKSHDVVTPAPLGRAVLAGTEWATVTL FT STSEVAPGEELEVTVSGLAEGAQISASAFAGTTEFTDLPAADAAGTVSFTLPVGDDVDP FT GDYELIVSQTQREDIVTAFSVVAAQPTATPTPTESTSPSPDFS" FT repeat_region 299756..299759 FT /rpt_type=DIRECT FT CDS complement(301894..302091) FT /transl_table=11 FT /locus_tag="AARI_02780" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSB1" FT /protein_id="CBT74514.1" FT /translation="MLGAALLFASIGLFAFALDTSQRSVATACWVTSTLMFICAAMLLL FT SGIVGASSVSAGEARPKRRR" FT CDS complement(302283..302984) FT /transl_table=11 FT /locus_tag="AARI_02790" FT /product="conserved hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.992 FT between position 38 and 39" FT /db_xref="InterPro:IPR018532" FT /db_xref="UniProtKB/TrEMBL:E1VSB2" FT /protein_id="CBT74515.1" FT /translation="MRLPRRALSLVLLASTLTLGACSSLQSLDFTTTDGAQAATSGAYG FT STEDYAAALELLDEIDIKGRAPKTGYSRDQFGDGWKDPDRNGCDARNDILARDLQDVTY FT KGSSSCVVLTGTFDDPYTGTTIEFLRGQGTSTAVQIDHVVALSDAWQKGAQQWDAQTRL FT EFANDPLNLMASDGSANASKGDKDAASWLPPNKSFRCAYVARQTQVKAKYDAWMTQAEH FT DAIEQLLTACV" FT CDS 303239..303493 FT /transl_table=11 FT /locus_tag="AARI_02800" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSB3" FT /protein_id="CBT74516.1" FT /translation="MTSPSLISSDRPQPLSTSSPEKVEILCRVKPQIRGSAPAASLEPH FT KTRSPADWPMNHSVGGRPHGSPATAMIAAQITATRGDKT" FT CDS 303870..304676 FT /transl_table=11 FT /gene="fabG" FT /locus_tag="AARI_02810" FT /product="putative 3-oxoacyl-[acyl-carrier-protein] FT reductase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.1.1.100" FT /note="3-oxoacyl-[acyl-carrier-protein] reductase catalyses FT the following reaction: (3R)-3-hydroxyacyl-[acyl- FT carrier-protein] + NADP(+) <=> 3-oxoacyl-[acyl-carrier- FT protein] + NADPH. It is involved in fatty acid FT biosynthesis" FT /db_xref="GOA:E1VSB4" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VSB4" FT /protein_id="CBT74517.1" FT /translation="MNATTSPAPASTTAALQLKDQLVLVTGGARGLGAAISTAFLEAGA FT RVVINYRNSAQAAAQLAARYPERALAIQADVRDPEQLAALAAAAGAHFGQQITTLINNA FT LVDFSFNGEARSKADELSAEELSAQFAGSVLAPVAAIQAVLPGMRAAGFGRIINIGTNL FT FQHPVVPYHDYTATKAALLSLTRTFADDLGPSGINVNMVSGGLLRTTDASAATPAEVFD FT LIASGTPLRRVTTPEELADAVLFFAAPGSRGVTGQNLIVDGGLVKG" FT CDS 304673..306019 FT /transl_table=11 FT /locus_tag="AARI_02820" FT /product="putative monooxygenase" FT /function="2 Intermediary metabolism" FT /note="similar to nitrilotriacetate monooxygenase component FT A (EC 1.14.13.-); cd01095" FT /db_xref="GOA:E1VSB5" FT /db_xref="InterPro:IPR011251" FT /db_xref="InterPro:IPR016215" FT /db_xref="UniProtKB/TrEMBL:E1VSB5" FT /protein_id="CBT74518.1" FT /translation="MSLKQAHFNLFAYGTGHHQAAWRAADSSAERLGELDYWVQLAHTA FT ERGLFDAFFLADGQSLSPAAAQAGPTWFYEPLTLLSALSQHTEYLGLVCTVSSSFFEPY FT AAARLLASLDHLCAGRAGVNVVTSMWDAEAQNYSRERLGEHAERYARAEEFLTVLRELW FT GSFPRTALETDRAGRFVDPSQLRELNHVGEHFAVRGPLNVPGSPQGHPVIFQAGSSGPG FT RALAARHAEAIYAVAADERMALDYARDIRARAAAAGRAAHPPLIMPGLVAYVAPTEVQA FT RELQRRLDALLPTAQALHQLGVFVQQDTSGWDLDAPVPDLPSVERFTGPAGRYTTILRL FT IELHRPTVRELLGLLAAGGGHCTMVGTPQTLADQIERWLDSGAADGFNLMPPALPGSLE FT DFVDLVIPELQRRGRYRTRYEHHTLRGNLGLPEPTRLAGLTREETAQAG" FT CDS complement(305960..307309) FT /transl_table=11 FT /locus_tag="AARI_02830" FT /product="enterochelin esterase-like protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="possibly involved in the intracellular release of FT iron from iron-siderophore complexes" FT /db_xref="GOA:E1VSB7" FT /db_xref="InterPro:IPR000801" FT /db_xref="InterPro:IPR014756" FT /db_xref="InterPro:IPR021764" FT /db_xref="UniProtKB/TrEMBL:E1VSB7" FT /protein_id="CBT74519.1" FT /translation="MSTRPTFRRPEPRGSGAATPRVPGFFSSRVAAGGIDAVLDALRSG FT QLPYPLVDRRPSDAEATEDDAPAQAYVTFLWVDTPGEDPVRSVILSANALVDHEQLEAC FT EFEPVREGLWAITLQVPTDWVASYRITPHRGAGPAPWRTETERRAIRLAADTGGTDPLN FT PHVSASMNGAPVSVVYGPDAKRNEHLAPATPDRQRTGPAIGGWGGAADAEPAVEHPRLS FT RHVLWDENCARERNLWMYRPPHGGQDSPLVIVHDGATWVNYLNIAASLDAAINAGTLAP FT LHVMFVDSTTVQIRSAELPVASGTTASLATQFLPWAREFFPVSALPEHTLVTGSSFGGL FT AALLAVTEHPQLFGRALAQSPSLWHTDLSSALGDLAPQVHVTIQAGCYETEIFTSCEQV FT LEALAGSESARRIGFEPISGGHDWAWWAPRLLTGLSRFFPGEAREPGRLR" FT CDS complement(307299..308183) FT /transl_table=11 FT /locus_tag="AARI_02840" FT /product="putative siderophore-interacting protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="identified by match to protein family PF04954. Match FT to protein domain PF08021. Possibly involved in removal of FT iron from iron-siderophore complexes" FT /db_xref="GOA:E1VSB6" FT /db_xref="InterPro:IPR007037" FT /db_xref="InterPro:IPR013113" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:E1VSB6" FT /protein_id="CBT74520.1" FT /translation="MPTHVMTVEEVVDYTPHLRRVVFGGRGVADYLAAPPCVPNIKIYF FT PQPGQPLDQPGEDERGRWVFTGDQRARVRTYTVRWADAQAGRLAIDFVRHGDEGLASAW FT VERIVPGDELGALGGGGRVLKPGGYALMFGDETALPAISDTLEHMPADQTGQVFIEVLD FT EAEIHELTKPEGVQVHWLPRGGVPAGRTRLLIEAMERFTLPEGLDYAGVHLWVSAESEV FT VRFARRWAATVGIARENRLIIGYWHLDMNEVAYAQDSNHDRVAGEMAYERPGHEHDHHD FT HDHEHDHEHAHEH" FT CDS complement(308216..309235) FT /transl_table=11 FT /locus_tag="AARI_02850" FT /product="iron-siderophore ABC transporter, inner membrane FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, permease (IM), ISVH-family (iron FT siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VSB8" FT /db_xref="InterPro:IPR000522" FT /db_xref="UniProtKB/TrEMBL:E1VSB8" FT /protein_id="CBT74521.1" FT /translation="MSTQTTSRRRFTPARRRIVLGTLLVLLAAVAVTAMGTGTITLGPQ FT QVLAALFGSGEPKDVMVVQKIRVPRVLTAVGVGAALGAAGACFQSISRNPLGSPDIIGF FT TTGAATGAVAQIVLFNAGAWATGASAMICGLLTAAVVYLLSFSKHATGGQRLVIIGIGV FT GAMLGAVNTILLAKGDADLAAQANLWLSGSLGGRTWADAALVGVALLVLLPLLVAHGRN FT LTMLEMGDDTAQALGVGAETVRRLTIFAAVCLTAAATAAAGPIAFVALASGQIIRQLIG FT NRSVPIWQAALTGSVLLVACDVITQHLPLQAQVPIGLATSLAGGLYLLYLLTRPQTRT" FT CDS complement(309232..310251) FT /transl_table=11 FT /locus_tag="AARI_02860" FT /product="iron-siderophore ABC transporter, inner membrane FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, permease (IM), ISVH-family (iron FT siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VSB9" FT /db_xref="InterPro:IPR000522" FT /db_xref="UniProtKB/TrEMBL:E1VSB9" FT /protein_id="CBT74522.1" FT /translation="MLQRTITGHRSRVSPWLVASAILVLLGLLSCALGTKNISLAETWQ FT AVTAFDPENNNHLLVRELRVPRTLLAVVVGAALGLAGALMQSMTRNPLAEPGLLGVNAG FT AAFAVAVAITLGYVQPAGYLFFAFAGAAAASVIVYLMGRGRGTGNDVVRLVLAGAGMSV FT MLMASTQILVIGGGTETHERFAAWTTGSLQGRGYDVLPLTAVVVLIGAVIALGLCRALD FT ALALGEDSARSLGVNPTRAWLLSAVAVMLLAGAATAATGPISFIGLAAPHTARMLVGPH FT HVRYLPLSMLLGAGVLLIADITGRLVASPLEIGAGAMSALIGAPVFILLARRRLKVGR" FT CDS complement(310274..311296) FT /transl_table=11 FT /locus_tag="AARI_02870" FT /product="iron-siderophore ABC transporter, FT substrate-binding protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, binding protein (BP), ISVH- FT family (iron siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VSC0" FT /db_xref="InterPro:IPR002491" FT /db_xref="UniProtKB/TrEMBL:E1VSC0" FT /protein_id="CBT74523.1" FT /translation="MHSHVFKFASAAAAAALTLSLGACASYSTAETTTDGSSAEAETGT FT WPRTVTDDAGNEVEIPAKPERIVSTTVSTTGSLLALDAPLVGSATAAISPQSDENGWFT FT QWADVAVERDLEPIYQLGNFDLEAVVAQDPDLIVVSTSGADSEIDNLAQLQDIAPTYVV FT NYGDKDWKELTEELGEATGTEANAAAVIDEFDQRAESIKQKLAIPAGTTASIVSYNQGD FT DSPVGKTTGPHAALISSLGFDIVEPPAEYDTSTQVREDFAFTSYEGLAESATGDAVFLI FT SATDEIAKAFKDDATLANLPSVKNDNVFPLANSFRLDYYSSSGILDYFENDFPGLNEAK FT " FT CDS complement(311493..312878) FT /transl_table=11 FT /locus_tag="AARI_02880" FT /product="AraC-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein domain PF00165: FT bacterial regulatory helix-turn-helix proteins, AraC FT family" FT /db_xref="GOA:E1VSC1" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR014710" FT /db_xref="InterPro:IPR018060" FT /db_xref="UniProtKB/TrEMBL:E1VSC1" FT /protein_id="CBT74524.1" FT /translation="MSGSRLQAPGIPGPEPVVVHWKCNLTYSIVVWVSSGTARIHLEDQ FT VRELRAGQALWVPPYVAHMVEHDAESLALSIMVTARRGWGLGSEPVLIDVPPSHAQWMF FT HLMLLTLSPLHSGQVPGKRIVEMLTHFAAHKRSETPPLPLVMPRHPAARQVAARLLSDP FT GSELRLEDFAAQLSVSERTLRRAFRTDTGLGFRQWRQQAQLGGLDRALPLRTQQVPAFT FT TRWMHLTRDDLVLWALRGRASVHRLSPGDHTAAESTQALQAGQFLLVPAGQSLRVEIEQ FT GSLLIPLPLPAGSLPADPAHRMPCQLPADYFQTMLHRAISHITLLRPVHFDRVNTLRLL FT EHVPNFPGLRYPRDPVLRRIAGELTTDVRGKVRAAELAARHGFSLRQLQRRWLAETGLG FT LRPWRQAHRFQHADALLNSGFAVPFVAAQLGFTEPGNFARAYQKLRGYRPKTATHVLPT FT DIF" FT CDS complement(312868..312978) FT /transl_table=11 FT /locus_tag="AARI_02890" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSC3" FT /protein_id="CBT74525.1" FT /translation="MTQQYDSFMWRARARRIPRAGKQSVQVASPGVRHER" FT CDS complement(313047..314282) FT /transl_table=11 FT /locus_tag="AARI_02900" FT /product="putative siderophore-interacting protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="identified by match to protein family PF04954. Match FT to protein domain PF08021. Possibly involved in removal of FT iron from iron-siderophore complexes" FT /db_xref="InterPro:IPR007037" FT /db_xref="InterPro:IPR013113" FT /db_xref="UniProtKB/TrEMBL:E1VSC2" FT /protein_id="CBT74526.1" FT /translation="MSKHHKYNKYGPQVTVSARDGITLDVIRQAEKAGAKAGHDVAKAM FT LYQSIGTGSALTGPQAEELLAAAERAGAAAALSAARKVLDKTVRTSFHGAGAEPAAPTA FT PLAPPAAVPTAFPTAVPAPAAQEAPPALPYAQTYEEPLAEYRPPISYHEAPRGKVTQHV FT LTITRVQRLSDQLVRIVASAPDLDGYRSNGALDEYVKVFVADPALGLVPPYDIKALRQR FT LPREQVPRSKSYTIRWVDPVVDELAIDFVVHGEPGTVGHWAGQVEPGAALVISPARSKH FT SVNLTAPYYVLAADEAGIPAISKVLEALPDTTEGVALLEVADEGAMFDVKHPAGVELRW FT LSRDGSPAGRSDALPYTMQTLQVPGHGLGVIAHAERTTIKNIGRICSGWNTDKRASHIS FT SYWTLREGRLLR" FT CDS 314485..314832 FT /transl_table=11 FT /locus_tag="AARI_02910" FT /product="putative PhnA protein" FT /function="2.6 Metabolism of phosphate" FT /note="identified by match to PF08274 and PF03831. This FT protein family includes an uncharacterised member FT designated PhnA in Escherichia coli, part of a large operon FT associated with alkylphosphonate uptake and carbon- FT phosphorus bond cleavage (alkylphosphonates utilization as FT phosphorus source)" FT /db_xref="InterPro:IPR004624" FT /db_xref="InterPro:IPR013987" FT /db_xref="InterPro:IPR013988" FT /db_xref="UniProtKB/TrEMBL:E1VSC4" FT /protein_id="CBT74527.1" FT /translation="MSETLPPCPQCSSPYTYELDALLVCPECGHEWNAETESAEPTEQV FT IKDAVGNVLQDGDTVSITKTLKVKGAQGALKAGTKVRNIRLVAGNGDHDIAAKVDGFGQ FT MELKSSIVKKI" FT CDS 314988..315602 FT /transl_table=11 FT /locus_tag="AARI_02920" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR019606" FT /db_xref="UniProtKB/TrEMBL:E1VSC5" FT /protein_id="CBT74528.1" FT /translation="MWSHRFARRGIPALLSFCLVLSSCSGGTGSDPSASQLPTANDMTS FT PATSTPATSSPATTDTPTGTSPSQQTAALTLFYVAVGDDGVAGPEIGCGDSIIATYTGE FT KTFSDQLAAAMTSLLADKQDTHGESGLRNALSASDLTYVSAQVADDTVTVDLSGLVVSG FT GVCDDPRIVEQLKYTAMTAAGTGRAEIRVNGVELDEVLSQK" FT CDS complement(315664..317979) FT /transl_table=11 FT /gene="purL" FT /locus_tag="AARI_02930" FT /product="phosphoribosylformylglycinamidine synthase FT subunit smPurL" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="6.3.5.3" FT /note="phosphoribosylformylglycinamidine synthase catalyzes FT the fourth step in the de novo biosynthesis of purines. In FT Bacillus subtilis it is formed from three proteins: PurS, FT PurQ and smPurL" FT /db_xref="GOA:E1VSC6" FT /db_xref="InterPro:IPR000728" FT /db_xref="InterPro:IPR010074" FT /db_xref="InterPro:IPR010918" FT /db_xref="InterPro:IPR016188" FT /db_xref="UniProtKB/TrEMBL:E1VSC6" FT /protein_id="CBT74529.1" FT /translation="MSQEATKEFNIDTVDNAAGTPDVELPWAELGLKDNEFAEIVKILG FT RRPTAAELAMYSVMWSEHCSYKSTKNHLRQFGQKVTPEMKKDLMVGMGENAGVTDLGDG FT WAVTFKIESHNSPSYVEPYQGAATGIGGIVRDIISMGARPIAVMDPLRFGAIDHEDSQR FT VVHGVVSGIGGYGNSLGLPNIGGETVFDPIYQGNPLVNALAVGALRHEDLRLANASGVG FT NKVVLFGARTGGDGIGGASVLASESFDDTKPSKRPAVQVGDPFAEKVLIECCLELFKAS FT LVEGIQDLGAAGISCATSELASNGEGGMQVELTNVLLRDSTLTPGEILMSESQERMMAV FT VTPENIEAFEAVMAKWNVEYSWLGEVTDTDRLIITWDGEVIVDVDPKTVAHDGPVYDRP FT YARPQWQDALQADTFKSSEAGKNLPATGDELKAATLELIASPNMCDKSWITNQYDRYVG FT GNTALAAPDDAGVVRIDESTGLGVAIATDANGRYTYLDPYVGAQLALAESYRNVATSGA FT IPAAVSDCLNYGSPEDPDVMWQLAEGIRGLSDACMELGVPVTGGNVSLYNQTGNKAIHP FT TPVVATLGKFDDVARRTPSGWRAEADGQAIYLIGTTEDELDGSEFANLRGHLGGTPPKV FT DLAAEKELGAILINASRDGMIDAAHDLSEGGLAAALAEMVLRYGVGARVALNEIKERDG FT IDSFTALFSESQARALVAVPRSEEVRFNDMTGARGVTVARLGIVDAQSNALEIQGEFTA FT TVDELRQAHEGTMAKYFG" FT CDS complement(317976..318728) FT /transl_table=11 FT /gene="purQ" FT /locus_tag="AARI_02940" FT /product="phosphoribosylformylglycinamidine synthase FT subunit PurQ" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="6.3.5.3" FT /note="phosphoribosylformylglycinamidine synthase catalyzes FT the fourth step in the de novo biosynthesis of purines. In FT Bacillus subtilis it is formed from three proteins: PurS, FT PurQ and smPurL" FT /db_xref="GOA:E1VSC7" FT /db_xref="InterPro:IPR010075" FT /db_xref="InterPro:IPR017926" FT /db_xref="UniProtKB/TrEMBL:E1VSC7" FT /protein_id="CBT74530.1" FT /translation="MSTELPLIGDYSTPSTELSGARIGVVTFPGTLDDRDAARAVRAAG FT AEAVSLWHADTDLQDVDAVVIPGGFSYGDYLRAGAISRFAPMMAKIADAANSDAKLPVL FT GICNGFQILTESHLLPGSMIKNDHLKFICRDQLLRVENNQTAWTNGFEAGQEITIVLKN FT QDGQYVADEKVLDELEAENRIAFSYVGWNPNGSRRSIAGVSNKAGNVVGLMPHPEHAIE FT AGFGPDHRGTDGLAFFTSVLTHLVGGKK" FT CDS complement(318728..318979) FT /transl_table=11 FT /gene="purS" FT /locus_tag="AARI_02950" FT /product="phosphoribosylformylglycinamidine synthase FT subunit PurS" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="6.3.5.3" FT /note="phosphoribosylformylglycinamidine synthase catalyzes FT the fourth step in the de novo biosynthesis of purines. In FT Bacillus subtilis it is formed from three proteins: PurS, FT PurQ and smPurL" FT /db_xref="GOA:E1VSC8" FT /db_xref="InterPro:IPR003850" FT /db_xref="UniProtKB/TrEMBL:E1VSC8" FT /protein_id="CBT74531.1" FT /translation="MPRIVVDVMLKPEILDPQGKAIAGALPRLGFTSFEAVRQGKRFEL FT FVDGEVTEEILAQAREAAETLLSNPVIEDVVNVEVVED" FT CDS 319162..319611 FT /transl_table=11 FT /locus_tag="AARI_02960" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSC9" FT /protein_id="CBT74532.1" FT /translation="MGHGFVLGAYAETVKNTSQTICACRVLETGELSYENCCKPFHDGR FT KDGSLLPSSAEELMRSRYSAFVLGLAGYLLATWHESTRPKELELDPQMRWTGLEIISTR FT AGGAAASRGVVEFAAHYLDGRIDAQQHEVSTFVKQDGAWYYLDAL" FT CDS complement(319616..320608) FT /transl_table=11 FT /locus_tag="AARI_02970" FT /product="ankyrin repeat protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="contains ankyrin repeats (PF0023). Such repeats FT occur in a large number of functionally diverse proteins FT mainly from eukaryotes. They have been found in proteins of FT diverse function such as transcriptional initiators, FT cell-cycle regulators, cytoskeletal, ion transporters and FT signal transducers The few known examples from prokaryotes FT and viruses may be the result of horizontal gene transfers" FT /db_xref="InterPro:IPR002110" FT /db_xref="InterPro:IPR020683" FT /db_xref="UniProtKB/TrEMBL:E1VSD0" FT /protein_id="CBT74533.1" FT /translation="MALHSGLSAQRRGIALIALPLAAAIGACTGCAPSSPQAQEAVSDP FT VPATSSSISPPKATPSLGNSPASSRGQQSASSQPSTIAPTKAPSSTAAKTSSVAETPKS FT SETSLSPLATGAKTGASLKALPSSAAPMSKATAQLFAAVNAGKPKGVKAAIKNGADLSA FT KDESGRTALMRAVIKKNPAIAKELFEAGADPDVKDDFYESAFLRASANGQVATLKLFID FT GGADITAVNRMGGTALTVASENGQVQAVRHLLRTDIPVDYVNDLGWTALHETIVLGQGT FT NNAITIARLLITNGANPNLKDHSGSDAFKLARERQQKQMLTMLQAASKR" FT CDS 320786..321916 FT /transl_table=11 FT /gene="rumB" FT /locus_tag="AARI_02980" FT /product="23S rRNA (uracil-5-)-methyltransferase RumB" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.-" FT /note="catalyzes the formation of 5-methyl-uridine at FT position 747 (M-5-U747) in 23S rRNA" FT /db_xref="GOA:E1VSD1" FT /db_xref="InterPro:IPR010280" FT /db_xref="InterPro:IPR011825" FT /db_xref="UniProtKB/TrEMBL:E1VSD1" FT /protein_id="CBT74534.1" FT /translation="MECLYFSASRCRSCTLMTVPYAQQLQSKVEDCKRLLADFPDLEFL FT PAQASSEQGFRNKAKMVISGTTDKPTIGILDAEGRGIDLRNCGVVADQLRAVFPLIERF FT IHELKLIPYDVPKRKGELKHVILTVSDTGSVMVRWVLRTKKHFVALRDSLPQFLEQLPR FT HSVVSVNFLPEHKAVLEGEEEIILTRRTTLEFGLNGVPMHLRPQGFFQTNSEVAAALYR FT QARQWINDANPESVWDLYSGVGGFALHCAAEDRTVYGIETSTEAVEAAETSAKAMELDD FT IHFKAQDATEFALGAGWAPEAVIVNPPRRGITADLSTWLNGSDVQQIIYSSCNAKSLAR FT DLERLENYTPTLARVMDMFPQTNHYEVIVKLERKAA" FT CDS complement(321913..323490) FT /transl_table=11 FT /locus_tag="AARI_02990" FT /product="putative Na+/H+ antiporter" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="CPA superfamily, monovalent cation:proton FT antiporter-1 (CPA1) family (TC 2.A.36.y.z). Na+/H+ FT antiporters are key transporters in maintaining the pH of FT actively metabolising cells" FT /db_xref="GOA:E1VSD2" FT /db_xref="InterPro:IPR006153" FT /db_xref="InterPro:IPR018421" FT /db_xref="InterPro:IPR018422" FT /db_xref="UniProtKB/TrEMBL:E1VSD2" FT /protein_id="CBT74535.1" FT /translation="MEFFLLVIALLFATILIVGIGERIKLPYPILMLIFATLAGFLPFM FT PKMHIEPDLILPIFLPPLLFATAQRSSWSVFRFRWKALIRLAVVLIVVTAGTVAATALA FT FSPIASIPLALALGAVVAPPDPVAVDAIATKVKMPRRLTSLLETEGLFNDAMAIVLFQL FT AVQATVDKTQVGLEIIPQFLIGAAGAVALGLAMGWAIGALNRFVPNLAARCAATLVAPY FT AVYVIAEELHTSGVIAVVVTALEMVRRDRPQDSAERLTRQSFWEVLELLATGLAFGLMG FT IEMNQVIQEEGRNLIGFIPGIAAICFVVIAVRALWMLGTYYLPNRKNPKIPARKDALVL FT TWCGMRGLATLALALALPKVTADGSPIEGRNFIVAAACTVLLCTLVVPGLTLPSLMRVL FT KLRNNEQDTKRAKRNLARRAEAVALSALKKNLDLQELPENYQQAVRRRMNSLHTILAKD FT PDPHDAISDEKYTQVRAVIAKADSIQAIALEAARDELLKARREPNVDPHLVDEIVGRLD FT RRTATLDR" FT CDS complement(323538..323969) FT /transl_table=11 FT /locus_tag="AARI_03000" FT /product="conserved hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.735 FT between position 34 and 35" FT /db_xref="GOA:E1VSD3" FT /db_xref="InterPro:IPR023549" FT /db_xref="UniProtKB/TrEMBL:E1VSD3" FT /protein_id="CBT74536.1" FT /translation="MGTTRSFRLVLACIGASSLGLCLASCSTSTTVGSQTRLDITIRAD FT GSEISQQYLLECDGEQSTDASTLPDASKACLQLALDPSVTTEEIDPQQACTEIYGGPQR FT AEIEGTLHGDPVNANFSRHNGCAIERWESASFLLGSVNS" FT CDS complement(324003..324902) FT /transl_table=11 FT /locus_tag="AARI_03010" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSD4" FT /protein_id="CBT74537.1" FT /translation="MPLTATILDPSQWTPRAVEHETRARAFGEPFVDRRMKGKKHPIED FT FLFTYYTQKPGQLYRWHPGMAVVLVGHEARERGTWKFYRSVQTSSGPGYEFDAQAFGQA FT RARAIEFARIILAGTAQRPGNFSCFGLHEWAMAYKSEANGIRHEYLPLRLGAQGTDEVV FT ETHKIRCTHFDAFRFYTPQAIDLNEVQPTRETQRDLEQPACLHANMDLYKWAYKLSPAV FT PSELVMDCFELAWDIRTMDMQASPYDLADWGHDPIRIETPEGKATYVRMQKEFAARADS FT LRLSLLEIANSLPIPRED" FT CDS 324981..325538 FT /transl_table=11 FT /locus_tag="AARI_03020" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007061" FT /db_xref="UniProtKB/TrEMBL:E1VSD5" FT /protein_id="CBT74538.1" FT /translation="MENLPLWEPPMSGTEAQHLFGMLDRLRTTFRYKADKLDIGQLATK FT LPSSQLSLGGLLQHLALVEDEKFTYFIARQRPEVLLALTADGREHFDVDLNDDPEILYQ FT RYDEAVAKSRKIQQSLIEEGALDTDSGLEFDGKHVSVRRIICDLVEEYGRHAGHADLLR FT EAVDGRVGEDAPLDYLPAWYRE" FT CDS 325684..327033 FT /transl_table=11 FT /locus_tag="AARI_03030" FT /product="NAD dependent epimerase/dehydratase family FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF01370: NAD FT dependent epimerase/dehydratase family. This family of FT proteins utilise NAD as a cofactor. The proteins in this FT family use nucleotide-sugar substrates for a variety of FT chemical reactions" FT /db_xref="GOA:E1VSD6" FT /db_xref="InterPro:IPR001509" FT /db_xref="InterPro:IPR010099" FT /db_xref="InterPro:IPR013549" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VSD6" FT /protein_id="CBT74539.1" FT /translation="MTLNRSSQLPASAPVVFDWFSRPGAIQRLLPPWLPLKVMEEATSL FT KDGTAVLGLPGGLLWNAKHQPEGFSENRSFVDQLEPEGLRGIPARVVRWRHEHYFEPAG FT PESTTVRDCIESNMPGRQIESMLAYRHRQLANDFAAHNRAAQSGLEPLVIAVTGSSGLV FT GQALCAFLSTGGHQVIKLVRHAPHTASERRWDPADPDKDLLEGCDAVIHLAGASIFGRF FT SQAHRHAIESSRIEPTRSLALLAARSGVRTFISSSAIGFYGASAGPDPLDESDSAPASN FT QDFLSGVVQRWEQAAREGSGSMRRVQIRTGVVLSPKGGMLAVLRPIFTAGLGGPLGGGQ FT QMLSWIGLDDLLDIYHRALWDSQLAGPVNAVAPQPVSNAEFTRALARAVRRPAVIPVPD FT AAPKLVLGAQGSQLLAMADQRIVPRKLLDGGHQFRNERIELALAHSLGAS" FT CDS 327255..328385 FT /transl_table=11 FT /gene="hemH" FT /locus_tag="AARI_03040" FT /product="putative ferrochelatase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="4.99.1.1" FT /note="catalyzes the last step in heme biosynthesis: the FT chelation of a ferrous ion to proto-porphyrin IX, to form FT protoheme: Protoheme + 2 H+ <=> protoporphyrin + Fe2+" FT /db_xref="GOA:E1VSD7" FT /db_xref="InterPro:IPR001015" FT /db_xref="UniProtKB/TrEMBL:E1VSD7" FT /protein_id="CBT74540.1" FT /translation="MGNMSVAPFDAILLMSFGGPEKPADVLPFLQNVTRGRGIPVERLE FT EVGEHYYMFGGKSPINEQNQALVRALRDEFAARGIDTPLLWGNRNWQPYLAEVVGNHAR FT MHGSRRFLAIDTSAYSSYSSCRQYREDFAGAVAALEEQGIEVVIDKVRQYYNHPGFAQA FT QLDCLRRGLGEFKQLVGGLDRSRHKILFVTHSIPTSMQKSSEKFTVGYQGQHEELMKWL FT SAELDGEEQLDAELVFCSRSGSAHTPWLEPDINDRMRELSDSGTEAVLVVPIGFVSDHM FT EVKFDLDTEAAQTARELGMGFLRADSVGISPSFVSGLVDLVVERAAQVRAEEPEQRTIS FT GSKALGPGSGACSLNCCEGARSKNTVPNWNVDKPAS" FT CDS 328650..328859 FT /transl_table=11 FT /locus_tag="AARI_03050" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSD8" FT /protein_id="CBT74541.1" FT /translation="MHEAAWAFSKWQNPREAELADRMPDAGFPVSLHQYPTQGAGPSLN FT TGLRATRIEKSGWRGARLTTDHRS" FT CDS complement(328865..330289) FT /transl_table=11 FT /gene="citH" FT /locus_tag="AARI_03060" FT /product="citrate transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="identified by similarity to protein SP:Q6M8T2 FT (Corynebacterium glutamicum). IT superfamily, citrate- FT Mg2+:H+ (CitM) citrate-Ca2+:H+ (CitH) symporter (CitMHS) FT family (TC 2.A.11.y.z)" FT /db_xref="GOA:E1VSD9" FT /db_xref="InterPro:IPR004680" FT /db_xref="InterPro:IPR014738" FT /db_xref="UniProtKB/TrEMBL:E1VSD9" FT /protein_id="CBT74542.1" FT /translation="MLVALGFLMVATFMVLIMTKRMTPLLALILVPTIFGLFAGAGFGL FT GDMVIDAVKDMSGTAALLMFAIMYFGIMIDVGLFDRLVSGIQKLVGNDPAKVVMGTSLL FT TAVISLDGDGSTTFIVVTAAMLPIYQRLGMSPVVLTCVAGLTNGTLNIVPWGGPTARAA FT AALGVDASEIFVPMLPSLGIALVVIALFAWQMGVSERRRLQRERPEIWGTELGGGNVAA FT PTGGKAPGGTSPAGGNLAVLESVARKGDGTEFSTMDGTVLDPDRETLRPKTFYFNLALT FT VAIMVLLVVDVMPLSYLFMVGTAIALVVNFPKVSDQVKMIAAHSSEIIAVVSMVLGAAV FT LTGVLSGTGMVDAMSQWLVDVIPTSMGPYMAVLTGLISIPATFLMSNDAFYFGVLPVLA FT EAGAHFGVPAVDMARASITGQPVHMQSPLVPAILLLVSLSRVDLGDHHKKVLWRALVVS FT LVMLASGMLLGVIHMG" FT gene 330465..330749 FT /pseudo FT /locus_tag="AARI_03070" FT /product="truncated CitA signal transduction histidine FT kinase" FT /note="N-terminal section of the CitA signal transduction FT histidine kinase. CitAB controls citrate utilization in FT Corynebacterium glutamicum" FT gene 330781..332172 FT /pseudo FT /locus_tag="AARI_03080" FT /product="truncated CitA signal transduction histidine FT kinase" FT /note="C-terminal section of the CitA signal transduction FT histidine kinase. CitAB controls citrate utilization in FT Corynebacterium glutamicum" FT CDS 332169..332840 FT /transl_table=11 FT /gene="citB" FT /locus_tag="AARI_03090" FT /product="two-component system response regulator CitB" FT /function="1.3 Sensors (signal transduction)" FT /note="identified by similarity to protein SP:Q8NU70 FT (Corynebacterium glutamicum). CitAB controls citrate FT utilization in Corynebacterium glutamicum" FT /db_xref="GOA:E1VSE0" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR005471" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR024187" FT /db_xref="UniProtKB/TrEMBL:E1VSE0" FT /protein_id="CBT74543.1" FT /translation="MNENSSGNYRVLIVDDDFRVGELHADMVNAIPGFHALEPVQDPRV FT IPKLVQSLKPDLVLLDLYLPHVSGIELLRELDVDAIMISAAIEPKNIDKALRSGALAFI FT IKPFDAKTLASKLKGWARYRRQLAGTGEFNQQGVDRLYRSLQGGEETNASVGAAPTEQA FT VLSCVKESAEPMSVAEVAEAVGVARATAQRYLAALVANESLELQLGYGTRGRPEHRYVA FT S" FT CDS complement(332853..333593) FT /transl_table=11 FT /locus_tag="AARI_03100" FT /product="putative phosphotransferase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF01636. This family consists of bacterial FT antibiotic resistance proteins, which confer resistance to FT various aminoglycosides. The aminoglycoside FT phosphotransferases inactivate aminoglycoside antibiotics FT via phosphorylation. This family also includes homoserine FT kinase" FT /db_xref="GOA:E1VSE1" FT /db_xref="InterPro:IPR002575" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR024165" FT /db_xref="UniProtKB/TrEMBL:E1VSE1" FT /protein_id="CBT74544.1" FT /translation="MISGPPPADHPIPPAVRAAAGPEEIEGIWQNALGGVTYRIGNGER FT TRFAKWSPGCPPEEECDLTAEAQRMSWAGEFIRVPEVLSCEDHADGQLLVTAALHGHSA FT ASSLGKSDPARSARAVGQGLRQMHDALPVGACPFDWDLESRIHHLPAGQRAELLAEAPE FT LDLVVCHGDACLPNTIITDDHALSAHVDMGKLGLADRWADLAIAAWSTEWNYGPGFEQY FT VYAGYCTEPDERKIAFYRGVWDAT" FT CDS 333732..335339 FT /transl_table=11 FT /locus_tag="AARI_03110" FT /product="putative secreted alcaline phosphatase" FT /function="2.6 Metabolism of phosphate" FT /EC_number="3.1.3.1" FT /note="catalyses the following reaction : a phosphate FT monoester + H(2)O <=> an alcohol + phosphate" FT /db_xref="GOA:E1VSE2" FT /db_xref="InterPro:IPR006311" FT /db_xref="InterPro:IPR018946" FT /db_xref="UniProtKB/TrEMBL:E1VSE2" FT /protein_id="CBT74545.1" FT /translation="MTSISRRKLLTGTLGASALTLVGPTGAALASSSPRLVRSRLGLTS FT GFSMGDVSTSNAVFWARSSGEGRLRAQLRAVDETGNIIRGRGSFAKTLRGAYARETTDF FT TAKINAQHLPAGTRFAVSIGFEDENGTLGEMQNGWFSTAPALTGRRNQDASRAQSFVWS FT GDTAGQGWGINEEIGRMRAYAAMHATKPDFFVHSGDTIYADGPIAGEVMEPDGQIWRNL FT VTEEVSKVAETLDEYRGRHRYNLMDHNVRAMYAEVPVIAQWDDHETHNNWWPGEVIQDE FT RYTVRDINTLAARGRQAWQEYQPIADPRAMNGGTGFEAARIYRKISRGPVLDLFALDMR FT SYKSENTAGMEEKATAILGEEQLNWLVDGLAKSKATWKVILNDLPLGIIVPDGKAQESI FT SNADHGAPLGRELELARLLKAIKDRGIKNVVFLTADVHYCAAHHYSPERAAFREFNEFW FT EFVAGPVNAGSFGPNEMDGTFGPKVEFSKAGTTNQSPRDGKGQFFGHVDLDEQDLFTVT FT LRNGLGETVYTKTLEPAK" FT CDS complement(335410..336696) FT /transl_table=11 FT /gene="ask" FT /locus_tag="AARI_03120" FT /product="aspartate kinase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.7.2.4" FT /note="catalyzes the phosphorylation of aspartate. The FT product of this reaction can then be used in the FT biosynthesis of lysine or in the pathway leading to FT homoserine, which participates in the biosynthesis of FT threonine, isoleucine and methionine" FT /db_xref="GOA:E1VSE3" FT /db_xref="InterPro:IPR001048" FT /db_xref="InterPro:IPR001057" FT /db_xref="InterPro:IPR001341" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR005260" FT /db_xref="InterPro:IPR018042" FT /db_xref="UniProtKB/TrEMBL:E1VSE3" FT /protein_id="CBT74546.1" FT /translation="MGLIVQKFGGSSVSDAEGIKRVARRIIDTKSKGHDVVVVVSAMGD FT TTDDLLDLAGQLTDEAPAREMDMLLSAGERISMSLLAMAINQFGEQAASFTGSQAGLIT FT DSTHGKARIMEVSPQRVRRAIDRGFIAIVAGFQGMSKESKNITTMGRGGSDTTAVALAA FT ALGADVCEIYTDVDGIYTADPRVVHSAKKIETITSEEMLEMAASGSKILHLRCVEYARR FT FGVPLHVRSSFSTNEGTWVLPDPEDKIKIQEGEPLEQPIISGVAHDHSEAKVTIIGVPD FT IPGKAAQIFGVIAAAQANIDMIVQNISTRGSGATDISFTLPMTETKHVLEALNTAKPEI FT GFEDIEHNDEVGKLSLIGAGMRSNPGVSFTFFEALHRAGVNVDMISTSEIRISVVTDAD FT KLNDAVRAIHTAFDLDTDVEATVYGGTGR" FT CDS complement(336878..337429) FT /transl_table=11 FT /locus_tag="AARI_03130" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSE4" FT /protein_id="CBT74547.1" FT /translation="MAIKSSNLAAIAKATGIEWDQWCSKLRAGGADKLTHKQIAELAFT FT HIPPAVDNPGWWAQSVAVAYEQQISRRLPGQAQDGTFQGSVSSTIDADLDTALERWVVC FT VQGRNEFNGHKLSEPARTSGSERWRYWRADFSDGTKAQVDIGLKGEKSSVAINITKAET FT PEQVSEWKSFWRQILAEFKG" FT CDS complement(337450..337605) FT /transl_table=11 FT /locus_tag="AARI_03140" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSE5" FT /protein_id="CBT74548.1" FT /translation="MEEWAGIMDAAGLRGMKQNERVQMLLPLMQDQQECGRLLWARRIA FT SEYRQF" FT CDS complement(337846..338322) FT /transl_table=11 FT /locus_tag="AARI_03150" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VSE6" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VSE6" FT /protein_id="CBT74549.1" FT /translation="MQVSSKAEDAPTAERPDLYASAEQELFSLIALTARAKRELATRLD FT SRLTPGYLPVLGMILRSQRITQSEICEHLLVDKAALSRMITKLEQLALVKREVDPEDRR FT VFHLLPTELAVERWHECFQGWRTELRSRMTNWDNEDLSALIDLLSRLNLEIKSL" FT CDS complement(338331..339953) FT /transl_table=11 FT /locus_tag="AARI_03160" FT /product="putative EmrB/QacA subfamily drug resistance FT transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily, drug:H+ antiporter-2 FT (14 spanner) (DHA2) family (TC 2.A.1.3.z). Identified by FT match to protein family TIGR00711" FT /db_xref="GOA:E1VSE7" FT /db_xref="InterPro:IPR001411" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VSE7" FT /protein_id="CBT74550.1" FT /translation="MTATAPVAKPKMTHREILTALTGILMGMFVSILASTVVSSSLPVI FT VSDLNGSQTAFTWVVTATLLATTISTPIWGKLADLGNRKLLLQIALGIFVLASAAAGFS FT QNTSFLIAMRVIQGLAGGGVGALAQIVMADFLSPRERGKYMGLFGAVMAVGTVGGPLIG FT GFVTDAINWRWNFFIALPFAVAAVILIQRTLHLPAIPKRKVKIDYWGILLLSAGVSLLL FT IWMSLGGSQFEWASMTSYLMISGAVVMLALFVVVEAKSSEPLLSLGLFKNRTFTYAVIA FT SLAVGVSMFGTSVFLSQYMIMARGASATMAGLMTFPLMGGLLVISTIGGAMISRTGKWK FT ALVVTGSVLIVIGLFLLGTIHYDTNYALVATYMFILGAGMGLVMQNMVLVVQNSVHVKE FT LGVASSAVNFFRTLGGTAGTAGLGAVLAATVPNMIADRQSDLAAALATIGDQAKELTAA FT LGSGTLPSVATMPEPVRVIFESIYGDAVPSLFTLAAPLSLIVVIAVCLIPNQSLKTQTA FT TERMQDLAAEDQGGTKPESPAGS" FT CDS complement(340137..340949) FT /transl_table=11 FT /gene="recR" FT /locus_tag="AARI_03170" FT /product="recombination protein recR" FT /function="3.3 DNA recombination, and repair" FT /note="may play a role in DNA repair. It seems to be FT involved in an recBC-independent recombinational process of FT DNA repair. It may act with recF and recO" FT /db_xref="GOA:E1VSE8" FT /db_xref="InterPro:IPR000093" FT /db_xref="InterPro:IPR003583" FT /db_xref="InterPro:IPR006171" FT /db_xref="InterPro:IPR015967" FT /db_xref="InterPro:IPR023627" FT /db_xref="InterPro:IPR023628" FT /db_xref="UniProtKB/TrEMBL:E1VSE8" FT /protein_id="CBT74551.1" FT /translation="MYEGAVQELIDELGRLPGIGPKSAQRIAFHILDADAEDMTRLAAS FT IQLVKEKVKFCEICFNISEQEICAICRDERRDGTKICIVEESKDVLAIERTRAFSGKYH FT VLGGSINPLAGIGPEQLHIRELVTRLADDSITELILATDPNLEGEATAVYLVRALAPLG FT IHITRLASGLPVGGDLEYADEVTLARAFEGRRAAGRTAPGPARLKAEKQEATEKDEQEE FT SEDPAQKPKAQLPEPRLLHVGGKPVDSGTGCEASSHPVVPEMDNRRSQ" FT CDS complement(341040..344486) FT /transl_table=11 FT /gene="dnaX" FT /locus_tag="AARI_03180" FT /product="DNA polymerase III, subunits gamma and tau" FT /function="3.1 DNA replication" FT /EC_number="2.7.7.7" FT /note="DNA polymerase III is a complex, multichain enzyme FT responsible for most of the replicative synthesis in FT bacteria. DNA polymerase III contains a core (composed of FT alpha, epsilon and theta chains) that associates with a tau FT subunit. This core dimerizes to form the POLIII complex. FT PolIII associates with the gamma complex (composed of FT gamma, delta, delta, psi and chi chains) and with the beta FT chain to form the complete DNA polymerase III complex" FT /db_xref="GOA:E1VSE9" 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:E1VSE9" FT /protein_id="CBT74552.1" FT /translation="MTALEKNRVNHAYLFSGPRGCGKTTSARILARCLNCEQGPTPVPC FT GTCASCVDLANGGPGSLDVIEIDAASHGGVDDARDLRERATFAPTRDRYKIFIIDEAHM FT VTAAGFNALLKIVEEPPAHIKFIFATTEPEKVIGTIRSRTHHYPFRLVPPEALLAYLQL FT LCERENVQVAEGVLPLVIRAGGGSVRDTLSVLDQLIAGARDGNLDYETAIALLGYTHST FT LLDEVTLSLHESDGAGLFGAIDRIIQTGLDPRRFVEDVLERFRDLIIAKAMPEGLEKIL FT RGVPEDQLEALRLQAGLVGAGELSRWADVTNKALSEMTGATSPRLHLELLAARLMLPGS FT QNSDSSFAARLDRLERHAMTGGALPALDEDEASGAPGAINAAPNPAAARQGAAAVREAL FT AAAKSRLGGAPAESQGAPAAQEQPAQVQPEQAQPQQQSSQAQQPAAQATPVQNQHPEQS FT EENSSSATAAQPVRSAQPAASAQPQQAEDGDPNAPLDPGAAASLNTGEAADWGATWGPK FT GDVHPVTTEVQPGPSTPAARPEGVAPFSLVPDPSSGEDLSFGTGVSIDDVKQNPAMAEF FT ARRAAANRGPQAPAPAGAQPQPAENASQPGVDAQQEHAQRAQAEREAQQRAAQEQAQHE FT QAEREAQQRAAQEQAQREQAQHEQAEREAQQRAAQEQAQRQQGQPQQHAPQQAAPNGMP FT QDHQQAPQGSGSPVAKFQQAWPMILQQLQGNSRVLHSMVATYGSVAGFDGRTLTLAFSN FT TGPIVNLRNRPDLMSTLTGVLSQVHGSPLEVVLTEGGSNPNGGGSPKGERRPIPAPIPA FT PTKFTKAVSSAGAAARAAARAQAAAPAPQQRPAVAAPSSAPVAPAPRAHDGYASAYEDV FT PPPADEPYFDESPYPDDPYFQPAGSAPPAPPAQPQPQAAAPAAAAPPSPVAPAPATGAP FT RNFGGPPVAPKPRMTAGMTARQAEGGMPNIERPVSSTPLHPGSTTGSFENLAAPAPETQ FT ASSAPASPEVASAAAAPMPERPAAPRPQEQPRQEPGAPVQQPATPESAPSWGAPQAEAE FT PASAPAPLGRMSRYQQLMDQAKNAPSAPAPAQAATGWGGQASRPAPAPVQEPEEFVPSD FT DDIEVEDSALIGVPAVERLLGGMVIEQRDVNGNVVEIKRSL" FT CDS complement(344577..345497) FT /transl_table=11 FT /locus_tag="AARI_03190" FT /product="putative glutamate--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.17" FT /db_xref="GOA:E1VSF0" FT /db_xref="InterPro:IPR000924" FT /db_xref="InterPro:IPR001412" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR020058" FT /db_xref="InterPro:IPR020061" FT /db_xref="InterPro:IPR022380" FT /db_xref="UniProtKB/TrEMBL:E1VSF0" FT /protein_id="CBT74553.1" FT /translation="MGAGRFAPSPSGPLHLGNLRTAILAWLFARSTDRDFLLRIEDLDR FT VRSGAETTQINELASLGLDFDGEMLRQSDRLPVYLEAVERLKDRGLVYECFCSRKDIAE FT AGSAPHAAPGAYPGTCRELSPSEREAKAKNRPAALRLRSQVNEFSVHDELFGDYTGAVD FT DFVLIRNDGAPAYNLAVVVDDAFSGIDQVVRGDDLLSSAPRQAYLATLLDYEVPVYAHV FT PLALNSKGQRLAKRDGAVTLEEITEQGLLPANVVTILLESLGLPSTSLQAALQAFDPAA FT LPREPWIVDPENIVQQLMPPASRNR" FT CDS complement(345728..347260) FT /transl_table=11 FT /locus_tag="AARI_03200" FT /product="HNH endonuclease domain-containing protein" FT /function="3 Information pathways" FT /note="identified by match to cd00085: HNH nucleases; HNH FT endonuclease signature which is found in viral, FT prokaryotic, and eukaryotic proteins" FT /db_xref="GOA:E1VSF1" FT /db_xref="InterPro:IPR002711" FT /db_xref="InterPro:IPR003615" FT /db_xref="InterPro:IPR003870" FT /db_xref="UniProtKB/TrEMBL:E1VSF1" FT /protein_id="CBT74554.1" FT /translation="MSKREVFHSSDDPRRLPISPPGTRNIPGVDGLWAANLDKDNLFTQ FT IAATATRLYEQSPVTSSAQGLDRLKAIARLRSMLDAAEAAVLADSYEYAVADAVSQGTQ FT ESLLGEPEESDEGQSAYYYGVNRSDESLIRSCFVAEVAAAMRTTEKKAQDKLFFAEGLR FT HLCAETLEALSIGEITTKSAQEIVKHCQDLAPEDVKLLQHTLLPIARHATDSAIIQRAR FT KMRERLHPKPIEERHKKGAEDRKVTYWHEANGMSVIQLYMPVEKALSIINTVNWHAVRN FT LDSADERTEQQRRLDIICDALLDGWPATEGTALKARVAVTIPALEMLADPKRALADLEG FT YGPIPMGTALLIAKDAPSFIKVLTDPWSGAAIDVGREKYRPSKALRDLLRHRDVVCRFP FT GCNRPAETSEIDHIDAWGNGGHTTRSNTHLLCKRHQMFKHVMGWQATYLPDGSVNWRSP FT NGVMCVELPGSVTTVQNFDFEKEQTPMLPTAQLDDRVRRVLGWVEPPERETG" FT tRNA 347449..347536 FT /locus_tag="AARI_36450" FT /product="transfer RNA-Ser" FT /anticodon=(pos:347483..347485,aa:Ser) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 347668..348033 FT /transl_table=11 FT /locus_tag="AARI_03210" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSF2" FT /protein_id="CBT74555.1" FT /translation="MASVLGEICLDCNNPMLLARFWCEALNYEVLMEEAGLVSIGPKFQ FT GDGGLSLTFAQVPETKSIKNRLHLDLRPHSTAQADEADRLLSLGASYADVGQHEDEGWI FT VMADPEGNEFCVLAAND" FT CDS complement(348140..349180) FT /transl_table=11 FT /locus_tag="AARI_03220" FT /product="2OG-Fe(II) oxygenase superfamily protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF03171. This family contains FT members of the 2-oxoglutarate (2OG) and Fe(II)- dependent FT oxygenase superfamily" FT /db_xref="GOA:E1VSF3" FT /db_xref="InterPro:IPR002283" FT /db_xref="InterPro:IPR005123" FT /db_xref="UniProtKB/TrEMBL:E1VSF3" FT /protein_id="CBT74556.1" FT /translation="MNNVVTKIPLLDISTSRNADGSFNEEFVAALRDAAHRVGFFQIVG FT YSSQLGQDQELLDTIAEFFSKPVEQKIKLDNRNSAQFRGYTRMGTEITRGRADAREQID FT YGPQRETLAVVPKDKPYLNLQGPNQFPEDFPQLEQRAMAWAELMNKTGHELLSAIAVGL FT GLPEDHFDEPFANTPSWMGKLVHYVSGDVVPESGNQGVGLHADYGFVTLLLQDQVGGLQ FT VQPYGQEEWIEVPPTPGALVVNLGEMLEVATNGYLMATIHRVIAPPAGVDRYSVPFFYS FT PRLDAVIDKVELPADLAAEARGVSDDPENPMLASYGANVLKGWLRAHPQTAAIHYPELA FT KNRKSA" FT CDS 349456..349758 FT /transl_table=11 FT /locus_tag="AARI_03230" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR014447" FT /db_xref="UniProtKB/TrEMBL:E1VSF4" FT /protein_id="CBT74557.1" FT /translation="MIFRAVGDGRPYPDHGYSSTRDWSELPPQQVKLADLVTTKSTLDL FT ETLLSEDSTFYGDLFPHVVRYRDVLYLEDGMHRALRSALHHRSVIHARILDLDAS" FT CDS 349840..350460 FT /transl_table=11 FT /locus_tag="AARI_03240" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSF5" FT /protein_id="CBT74558.1" FT /translation="MRDREDPGQWHGAHIVDEQELSFSSDGQAKKRARKRQNIVFTVMA FT LLVIAVLTGAVLVFNGTLKLGGEPTAAQSPTPSETKIENAKCPAVNFKYQKPGDVEIRV FT LNTTDISGLASDTAKALEERGFKIFSLTSGWKSLAGTTGAVIAGPDGYAQAFTVQRQVP FT GTVFIYDEKKWGSRVDLALGEKYEGLEKERKLDTSDGKLVCAK" FT CDS complement(350465..351154) FT /transl_table=11 FT /locus_tag="AARI_03250" FT /product="DSBA-like thioredoxin domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF01323" FT /db_xref="GOA:E1VSF6" FT /db_xref="InterPro:IPR001853" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:E1VSF6" FT /protein_id="CBT74559.1" FT /translation="MSENTAAPSAQDKRIRVDIFSDIACPWCFIGKRRFEKGVESFEYS FT QNVDVYWHSYQLDPSLPDNYDGSEAEYLSKMKGLGQEQVMQMLDHVTAQAAGEGLNYDF FT ENLKVANSFTALRVLEYAKQHGAGNEMKEALLSAHFEKGLNTGDEETLLQLAGQLGLDT FT DELRTNLASGAYAEEVNADIAQARELGISGVPFFIIDGKYGISGAQPAEVFANALTQVH FT SGNVQGA" FT CDS 351220..351999 FT /transl_table=11 FT /locus_tag="AARI_03260" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR010699" FT /db_xref="UniProtKB/TrEMBL:E1VSF7" FT /protein_id="CBT74560.1" FT /translation="MEVALQGTAGVDDREKAVQVAKNLRWRGILFAGTITAMAGFVDGV FT GFVHFGGYFLSFMSGNSTRSSAALMTGDFAGWGMAMSLVGCFVGGVILATLITYPLKKM FT RRPVAMYFSAMLLLAAAISGYFLPQLTALLLAAAMGVVNVSYSRSGEVSLGLTYMTGTL FT VKLGQALGGAIIGLATGSDRGVYRLLWTRYALLWLMITLGSLGGVLAYLRLGLGSLWIV FT AAGMLIWASLAMIQELRTPDDPDEPSGPRAGTLTEIS" FT CDS complement(352064..353470) FT /transl_table=11 FT /gene="hutT" FT /locus_tag="AARI_03270" FT /product="putative histidine-specific permease" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="amino acid-polyamine-organocation (APC) superfamily, FT amino acid transporter (AAT) family, histidine permease (TC FT 2.A.3.1.9). Identified by similarity to protein SP:Q9H86 FT (Pseudomonas aeruginosa)" FT /db_xref="GOA:E1VSF8" FT /db_xref="InterPro:IPR002293" FT /db_xref="InterPro:IPR004840" FT /db_xref="InterPro:IPR004841" FT /db_xref="UniProtKB/TrEMBL:E1VSF8" FT /protein_id="CBT74561.1" FT /translation="MNEIKASLARGLTARHIRFMALGSAIGTGLFYGSSSAIQAAGPAV FT LFAYIIGGAAVFIVMRAMGEMAVKHPVSGSFAHYASRYLGRFAGFVTGWTFAFEMAIVA FT IADVTAFGIYMGFWFPQVAQWIWVLAVVLLIASINLMKVKVFGETEFWLAAIKVTAIIA FT MIIGGAALIIFGFNAPDTETATGLATLMSAGTLFPNGFVGLLLSFAVVMFAFGGIETIG FT ITAGEAADPAKAVPAAINTVPWRILLFYVASLAVVMMLFDWRQIDGSASPFVQIFDGLG FT IPAAAHVLNAVVITAAVSAINADTFGAGRMLYAMSEIGHAPKSFGRISRNGVPWMTVVI FT MAVVLLVDVVLNALLPEALFTIIASIATFATVWVWIMILTSYLAMRRKEAAAGRGPAVA FT REYAVPGGTVAAWIALVFMVFVVVLLALSPATRVALYTGIAWLVLLALLFKLLVRPAAP FT VKHDSDSLLG" FT CDS 353597..354223 FT /transl_table=11 FT /locus_tag="AARI_03280" FT /product="phosphoglycerate mutase family protein" FT /function="2 Intermediary metabolism" FT /note="identified by match to protein domain PF00300" FT /db_xref="InterPro:IPR013078" FT /db_xref="UniProtKB/TrEMBL:E1VSF9" FT /protein_id="CBT74562.1" FT /translation="MVSLATSLYLPHWFRWDNGRMKLGFVRHGQTQWNLEGRLQGSSDI FT PLNDTGRSQAREAVGVLDGGQWDAIVSSPLSRARETAQIIAEGLGLELGPSYDLLIERD FT YAQGEGMVETEALALWPDKHGGGIEPLESVVDRGLRAMAQIASDYPGKNVAVICHGTII FT RYTLSHFAGYKLDTIRNGSVAIIGNETGKWQLELVNDQVPEQLAR" FT CDS complement(354230..355294) FT /transl_table=11 FT /locus_tag="AARI_03290" FT /product="putative hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00561: alpha/beta hydrolase fold. This FT catalytic domain is found in a very wide range of enzymes" FT /db_xref="GOA:E1VSG0" FT /db_xref="UniProtKB/TrEMBL:E1VSG0" FT /protein_id="CBT74563.1" FT /translation="MAFQFKNPAEDLWQPDLLGEQFSQRPLPMSDGSTATLIRHRARKS FT LRLPPPLRGIAVLYVHGWSDYFFQKELAEFLTDAGADFYALDLRHYGRNLPVDRATGIA FT ELSSPGFTTDLEEYFEEFDAAHRIISSAHPGTRFVLLAHSTGGLSASLYAAADPQKVDA FT LALNSPWLEFQASEIGRTALARIMQVASTRNPHRFLPSVDPGFYTRTVSSQFSGEWDYD FT LGWRPVNGFKLTAGFISAVFNAQAKVKKGLDLQMPTLVMLSAEDYLLPRWNDSATRADV FT ALNVQAVAQRSIDLGRELHLVRLPGALHDVFLSSPKIRSKAYMALGSWLAVVKNRQRDS FT QLASSVRRIVPASS" FT CDS complement(355426..357063) FT /transl_table=11 FT /gene="aceB" FT /locus_tag="AARI_03300" FT /product="malate synthase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="2.3.3.9" FT /note="catalyzes the aldol condensation of glyoxylate with FT acetyl-CoA to form malate, the second step of the FT glyoxylate bypass, an alternative to the tricarboxylic acid FT cycle in bacteria, fungi and plants" FT /db_xref="GOA:E1VSG1" 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:E1VSG1" FT /protein_id="CBT74564.1" FT /translation="MNSPITLNNITITATPVRYQEQILTSEALDFLSALHTAFEPRRAE FT LMQRRQVNRARIANGRDPKFLDETRAIREDDSWQVAPIAPGLEDRRVEITGPIERKMAI FT NALNSGAKVWLADMEDASSPSWQNVIKNQVNLIRILDKELDFTAPDGREYKLNSYELTE FT LPTIVVRPRGWHLPEKHLLVAGTPMSGALVDFGLHFFHNAKRLLAAGRGPYYYLPKLEN FT HLEARLWNEVFNMAQDLLDIERGTIRATVLIETITAAFEMEEILYELREHSSGLNAGRW FT DYIFSIIKNFRSRGPRFVFPDRDTVTMTAPFMRAYTEQLVRACHRRGASAIGGMSAFVP FT NRKDASINEIAFGKVREDKAREAADGFDGSWVAHPDLVSVAREVYDEVLGENPNQLQRT FT REDVQVSGPALLNVESVTGKITERGIRDNIDIGIRYIESWLRGNGAVALRNLMEDAATA FT EISRSQLWQWIHQSAITDEGEIITRRWVQELTEETMDNLERFEGDRFEEAVEIFEACAL FT RDDFPTFLTKNAYLRYLDAPARTLEMAG" FT CDS complement(357144..358457) FT /transl_table=11 FT /gene="aceA" FT /locus_tag="AARI_03310" FT /product="isocitrate lyase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="4.1.3.1" FT /note="catalyzes the conversion of isocitrate to succinate FT and glyoxylate. This is the first step in the glyoxylate FT bypass, an alternative to the tricarboxylic acid cycle in FT bacteria, fungi and plants" FT /db_xref="GOA:E1VSG2" 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:E1VSG2" FT /protein_id="CBT74565.1" FT /translation="MTTENTNETSIDNRIAAIETDWENNPRWNSVTRDYTAADVVKLQG FT RVQEEHTLAKRGSEKLWKQLTEETPTGGYTNALGALTGNQAVQQVKAGLRAIYLSGWQV FT AADANLSGQTYPDQSLYPANSVPQVVRRINNALQRADQIEFSEGIHSVEDWMVPIVADA FT EAGFGGPLNAYELMKSMITAGASGVHWEDQLASEKKCGHLGGKVLIPTQQHIRTLNAAR FT LAADVAGTPSVVIARTDAEAATLITSDVDERDQQFITGERTPEGFYKVRNGIEPCIARA FT KAYAPYSDLIWMETGTPDLELARKFAEAVKKDFPDQMLSYNCSPSFNWKKHLDDATIAK FT FQRELGAMGFSFQFITLAGFHALNHSMFDLAQGYAKDGMSAYVELQEREFASEAAGYTA FT TKHQREVGTGYFDAISTALNPNASTLALVGSTEEGQFH" FT CDS complement(358984..359586) FT /transl_table=11 FT /locus_tag="AARI_03320" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR010282" FT /db_xref="UniProtKB/TrEMBL:E1VSG3" FT /protein_id="CBT74566.1" FT /translation="MSEAQASFAPGSIFELAQSTKKQWELGQVRLIASGVLAQDGTLQP FT SEPREATWQLSIRSIEKAASFTPAPSAQVFTLIAGDFVQLDVDGQQHGLEPLRPLKFET FT ANPVEASQPTEELLIVHVAATPQQVRPTVRIVELSKKREQHLFDGQLGVLVQGSAKLLL FT GENEQSLNLRDTVVGSDADDPRITGRGFMAVVSFDLP" FT CDS complement(359596..360216) FT /transl_table=11 FT /locus_tag="AARI_03330" FT /product="putative dTMP kinase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.7.4.9" FT /note="identified by match to protein domain PF02223. dTMP FT kinase (thymidylate kinase) catalyzes the phosphorylation FT of thymidine 5-monophosphate (dTMP) to thymidine 5- FT diphosphate (dTDP) in the presence of ATP and magnesium" FT /db_xref="GOA:E1VSG4" FT /db_xref="InterPro:IPR018094" FT /db_xref="UniProtKB/TrEMBL:E1VSG4" FT /protein_id="CBT74567.1" FT /translation="MHAISTRPLPATSHGHDPPQTLVILGPDGAGKSTLIEALTRQLLN FT ERIRARRLANAAARSWLTKFCRRSGITFPTFTQDFFETSIRGFNVARNMVSAAHSGGLS FT VMDRHLYCQLVLRRLRGHPSGLLLPWLAAKSTECARIILLDIDPHLAYERIVSRGKDHE FT TLEYLSESRDEYLRLAQLHGWIILDASLSTSLLVEQLRLVIGK" FT CDS 360294..360392 FT /transl_table=11 FT /locus_tag="AARI_03340" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSG6" FT /protein_id="CBT74568.1" FT /translation="MGEAQRENSEESELFDSEALKNGGLADLKMKI" FT CDS 360453..361916 FT /transl_table=11 FT /locus_tag="AARI_03350" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domain PF01381: helix-turn-helix" FT /db_xref="GOA:E1VSG5" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010359" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VSG5" FT /protein_id="CBT74569.1" FT /translation="MNFSGNGAGSEDTELDAIALGRRIRFLRKSKQLTLDDVSTLVDTA FT PSQLSLIENGKREPKLSLLKSLAGALGVGVDDLLGTEPPSRRAALEIELERAQRGPLYE FT SLGLPTVRVGTRLPMDVLESLVGLQHELERRLNEQAATPEEARRANTALRHEMRQRNNY FT YKDIEQEATKVLTAVGHDSGPLSHHRAADIAEHLGFSLRFVGNLPHSTRSVTDQKNKRI FT YLTQANRSEHDPRSVLLQALGHHVLGHKTPTDYFDFLSQRVATNYFAAALMMPEKSTVE FT YLQRAKNNRELAVEDLRDAFAVSYESAAHRFTNLATEHLGMTCHFQKVHESGILHKAYE FT NDRVNFPADHTGAIEGQSICRYWTSRVVFEQMDKFRSFEQYTDTVNGTFWCTARTERHS FT SGLYSLSIGVPFEHVKWFRGRDTKERCQSTCPDENCCRRPPADLSNQWFGNAWPAMRAN FT THLLAAMPTGAFPGVDETEVYRFLQKQMG" FT CDS complement(361927..362589) FT /transl_table=11 FT /locus_tag="AARI_03360" FT /product="putative hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VSG7" FT /db_xref="UniProtKB/TrEMBL:E1VSG7" FT /protein_id="CBT74570.1" FT /translation="MTQELSIPFEELELSALWDPAENAKAVVVLAHGSGAGKDHEFMAG FT FALALANLDASVLRFNFPYMDAGKKFPDKAPTAIAVWRQVRDWVEENMAEGLPIFAAGK FT SFGGRMASLAVAEGMPAQGLIFLGYPLHAPKKEEKLRDEHLYPLDLPMLFLEGTRDPFA FT TPEKMEEVASKLNQHSELSWFEGGNHSFKVARSGRSAAQDGAWLADAATAFIAKHTD" FT CDS complement(362644..363543) FT /transl_table=11 FT /locus_tag="AARI_03370" FT /product="hypothetical secreted protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.454 FT between position 41 and 42" FT /db_xref="UniProtKB/TrEMBL:E1VSG8" FT /protein_id="CBT74571.1" FT /translation="MRVRSVLAICALIVFLAGCSAAGSSHNPSTPTPTKSMSAAAASST FT LAEEAATPAAPESSPVVASPSSGQAWADSKIEMWKENSGIKSTKGFLYPYNLMTSWESP FT EPGALNIYLDNSMEFGVQSPEPHQTREDELRLMGRIMFESVGEASPELESVTFSTEDGK FT NSGTYSRARTGADPKDREAWADEKYTQWITAMNDTYESFCGAEITKLEIYRSCIPDDPH FT AYISKVHSPAFGELVVTIDDGPWMDGTYDMPASSFVSSNMMIKINSKAATGEKVQKLKV FT VARDGEDVDVALRKDWEM" FT CDS complement(363603..364022) FT /transl_table=11 FT /locus_tag="AARI_03380" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VSG9" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VSG9" FT /protein_id="CBT74572.1" FT /translation="MELSTTKLPPGEQILSLYDSVGWSAYTDDPEVLIQALSNSTFAVY FT AYDQQQQLAGLIRVISDNATICYVQDILVRPSAQRSGIGRALFDAVLQKFQHVRQLVLI FT TDDMPQQRAFYESMGLTEGAEFEHGVIRVFARFAQ" FT CDS complement(364052..364408) FT /transl_table=11 FT /locus_tag="AARI_03390" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSH0" FT /protein_id="CBT74573.1" FT /translation="MAQIGMITLDTVDEQSAAAWWRAVLGGKYAGQYPGFTMIRVPGFS FT AMLGFQKVPEVTAGKNRVHLDLSATSDRAREVEIFVKAGATRLEEHCDDPDFGWSVLRD FT PYGIVFCISDPHDQ" FT CDS complement(364496..364993) FT /transl_table=11 FT /locus_tag="AARI_03400" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VSH1" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VSH1" FT /protein_id="CBT74574.1" FT /translation="MPSDLLQAHLQHTAISSPECSYAQLLPLDPARALDLADAYFTAYP FT PGMAAASRAEAREEMASTFTQEYGKVLENASFMAVRKGKAVGAIMVVAESIWEEQLSGP FT FIIDLFTAPAHQGHQLGRSLIAAAMLACKEQGARTLSLRVGEGTSPAAHRLYAQAGFLP FT IP" FT CDS complement(365165..367723) FT /transl_table=11 FT /gene="clpC" FT /locus_tag="AARI_03410" FT /product="ATP-dependent Clp protease ATP-binding subunit" FT /function="3.9 Protein folding" FT /note="ATP-dependent Clp proteases act as chaperones to FT target the proteases to substrates" FT /db_xref="GOA:E1VSH2" 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:IPR018368" FT /db_xref="InterPro:IPR019489" FT /db_xref="InterPro:IPR023150" FT /db_xref="UniProtKB/TrEMBL:E1VSH2" FT /protein_id="CBT74575.1" FT /translation="MPAFFGAPSDGSFEEFLSRFLSARAQAARPIDITRLLSARTHEAV FT ATAAAISHEHGHDEIDSLHLLMALLRTEPIGEHLGAMGVDIDALGADAIARMPKSQEKA FT EKPTRLSSSAQRSLFDAYQVARNYGSTYIDPDHLFLAFVFNPESPVSQLLAQHGITGQS FT LQQAAMEQAQRAQNGGQEQGSEESDVSMLERYGTDLTALAADGQIDPVIGRDDELDQVV FT EILARRTKNNPVLIGEAGVGKTAIAEGLARAIVDDQVPEQIRGSRLISIDLPGMLAGTR FT YRGDFEQRLTGLLEEIADAEGQVLVFIDEMHLLVGAGSGESGNMDAANILKPRLARGEL FT HLIGATTLDEFRKVEKDSALARRFGKVTVAEPSEEVSLAILEGLRESYEDHHQVQYTPA FT ALKAAVALSARYLTDRQLPDKAIDLIDIAGARRSIAAGDTEDVQSLRAELVDAEREKSR FT AIGEERYEDASAWRDHITELTARITAAEEAGDAGITRVVDEAQISEVISRSTGIPTSRI FT TGDDKTRLASLEESLHASVIGQKDAVSAVARAVRRNRTGMSPAGRPIGSFLFLGPTGVG FT KTELAKALATNLFGSADSLLRVDMSEYGEKHTVARLIGAPPGYIGHDEPGQLTEKVRRN FT PYSVILLDEIEKAHPDVFNVLLQVLDDGRLTDSAGRTVDFSNTLILMTSNLGGEYLANK FT AGNFGFTSTNATSEAHEVRAKVMGKVREFMRPEFLNRLDEVLLFSKLSQSEISQIVKLV FT IAETEARLNDQELQLEISDAAVQFLASEGYDPEFGARPLRRLVQRKVQDAIADLLIDDS FT LAAGDTVLVDYAANKLSVQKKAEMPTPPAHSEQVPSYFGN" FT CDS complement(367853..368527) FT /transl_table=11 FT /locus_tag="AARI_03420" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VSH3" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VSH3" FT /protein_id="CBT74576.1" FT /translation="MEKIKVLIVDDEPLIRHALGTILATAHGIAMVNSVENGQAAVDYC FT KDNHVDVVLMDLQMPIMDGVSATKIIKSVQDSPSVLAITAFSSDEYLVPVLTAGASGYL FT VKDSEPDEIIRAIHAVHQGTAAISPSVSSDLVSAVREAYRDNSGDIQELVYDLGITNRE FT FEILKLLAKGLNNPEISKTLAISETTVKTHMAKIFVKLDVRDRVQALVAATRMGLIEIP FT RD" FT CDS 368629..368796 FT /transl_table=11 FT /locus_tag="AARI_03430" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSH4" FT /protein_id="CBT74577.1" FT /translation="MLAVAALVLAPLTAVAAPASAATSSAQSSGAVATPAGFGSAFSEW FT ICNRYGVGCP" FT CDS 368856..370028 FT /transl_table=11 FT /locus_tag="AARI_03440" FT /product="putative signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions. 5 FT transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VSH5" FT /db_xref="InterPro:IPR011712" FT /db_xref="UniProtKB/TrEMBL:E1VSH5" FT /protein_id="CBT74578.1" FT /translation="MNGTLTKLFAGRGVIVWTGITVLVAVSSSEFVTLLEEGFSGSSDV FT SVRGALLGLGLCVILALGLRWPAVSIGLFVAVAYFFLTDSSLFFWTIVSFMIFSSLAAT FT ARALSVRALFLTLSAAWMVQFGIQSGKDAVLLVALAPLAAMAFFLTRNIYLLREKNAVA FT VHQMQAVREQTRLAVDRERKNIARDLHDIVAHDITVVAMQSKAAKFANDGQKALEALDV FT IAKLSTETLHDLRLMLNVLRADGTMADSLTQNVDKPAATTVYALQGAELFVQRLRDANF FT KVTSATDEKISDLPRSAQTAIYRVMQEGTTNVIKHGLTGGTCTFNLIVSGSEAILEIAN FT QMSNSRKKSGDLPSGGTGLIGMGDRMSAFGGKFATNAEDGIWKLRASIPL" FT CDS 370382..371002 FT /transl_table=11 FT /locus_tag="AARI_03450" FT /product="dihydropteridine reductase family protein" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="identified by match to protein family PF00881. FT Members of this family utilise FMN as a cofactor. Possible FT characteristics include 6,7-dihydropteridine reductase FT (EC:1.5.1.34) and NADH dehydrogenase (EC:1.6.99.3)" FT /db_xref="GOA:E1VSH6" FT /db_xref="InterPro:IPR000415" FT /db_xref="UniProtKB/TrEMBL:E1VSH6" FT /protein_id="CBT74579.1" FT /translation="MSIQVETNHYESLTIPQDAADQLFFDARSANSFSDEPVSDEVLDA FT IYEATKMGPTMMNNQPLRITWIKSEQARQAIAGSMAGRNAEKALSAPALAVLSFDTEWH FT EEFENFFPHAPERKEMFQDLAMRTAVGNNNAWLQAGYFIMGVRAAGLAAGPMGGFDSTV FT VDAAINAENNHKSFLIVNVGKPGENAWHDRLPRHDASLATRSV" FT CDS complement(371071..372276) FT /transl_table=11 FT /locus_tag="AARI_03460" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSH7" FT /protein_id="CBT74580.1" FT /translation="MASRKPAKKKPAQGHPARRSGASNVPFESEVRQALQPFKSSLFRH FT FHEEGQAASETRAALEGLTTLLTVHAQLRKSVDVKTLDPSILGEQLGHLTSLGKEVSEA FT SAAILKHYLTFLGTTANFGGSVDDFKQTFEFLSRMAGDSPIVAPYLEDEEANGILESMP FT FVFAARELISWVGDGKPTTPAGVLTGATLQDAAGALGLFVKVDESAEVPQESEWEPEDG FT TVVPSLADIPRLSAYWDALIGTAMLRYQAPNATPTESLSDALLASSGQGARLVKELIAE FT VLYSHILINTLQKPGKAQIAEMVAGVLSNAASSTPPRTEFALQVPSEDDLPAEQHHLIA FT SLEEVVPQVESLLRVFEREGLVEINEEITVPVALRSSLERALTKVSDHVLNDSQQDSDA FT DA" FT CDS 372582..373877 FT /transl_table=11 FT /locus_tag="AARI_03470" FT /product="putative D-amino-acid dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.4.99.1" FT /note="catalyzes the following reaction: D-amino acid + FT H(2)O + acceptor <=> 2-oxo acid + NH(3) + reduced acceptor. FT Acts to some extent on all D-amino acids except D-aspartate FT and D-glutamate" FT /db_xref="GOA:E1VSH8" FT /db_xref="InterPro:IPR006076" FT /db_xref="UniProtKB/TrEMBL:E1VSH8" FT /protein_id="CBT74581.1" FT /translation="MLGGWIVAGVTVPDHVVVVGAGFVGLSTAWYLQEAGVKVTVVDRG FT GVAAGSSWGNAGWLTPALTLPIAEPAIFKNGLKMMLDPASPLYIPLKADAKLLRFLIGF FT AWHSTPRKWEEAMRVYSEIGATGLDAFDEIAQATTAGPGVQELTKPADPFLTGFTSLKD FT RDGLLHEFEMIEKTGGEVDYELLTGDELRGIEPTLSNKVAAGVAIKNQRYLNPPKFMES FT LAESVVARGGDIIGNFNVTDVRDNGKSVTIIGSEGRSITADHVVLATGAWMTDMANKFG FT VNVVVQAGRGYSFTVEPEDMPTHPIYFPAQRVACTPLGDRFRIAGTMEFRDVNHKLEPK FT RIEAIVAAATPVYKGINWENRKEEWVGGRPCTADGMPLVGQTGSARVSVGGGHGMWGVA FT LGPLTGKILAAQITGQQAPSIARHFNPLRKGF" FT repeat_region 374061..374068 FT /rpt_type=DIRECT FT repeat_region 374069..374091 FT /rpt_type=INVERTED FT mobile_element 374069..375517 FT /mobile_element_type="insertion sequence:ISAar23" FT /rpt_family="ISL3" FT CDS 374204..375511 FT /transl_table=11 FT /locus_tag="AARI_34450" FT /product="transposase of ISAar23, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VSH9" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VSH9" FT /protein_id="CBT74582.1" FT /translation="MHHSIYTPANLTTFTNLDGLGLTAIGQRLTPKKAEILCQVTNPDP FT WCQTCGTPGNPRDTVTRRLAHEPFGWRPTVLVIKHRRYRCNHCQRVWREDLSQAVAPRQ FT KISRTGLRWALAGLVTQHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFNGVKV FT LGVDEHVWRHTKSGDKYVTVIVDLTPVKAGTGTARLLDMIPGRSKAVFKTWLAERGEAW FT KNNVEVVAMDGFTGFKSAAAEELPQAVEVLDPFHVVKLGSEALDQARQRVQREQYGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKQRVEDLFNVAKHEPVQLVWSVYQRMVDAYRQKKP FT EIGRWAMEQLINEIGTKVPKGLPELKKLGGTLRRRKPDVLAYFDHVGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRSRLHPES" FT repeat_region 375495..375517 FT /rpt_type=INVERTED FT repeat_region 375518..375525 FT /rpt_type=DIRECT FT CDS complement(375571..376425) FT /transl_table=11 FT /locus_tag="AARI_03480" FT /product="putative NAD dependent epimerase/dehydratase FT family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF01370: NAD FT dependent epimerase/dehydratase family. This family of FT proteins utilise NAD as a cofactor. The proteins in this FT family use nucleotide-sugar substrates for a variety of FT chemical reactions" FT /db_xref="GOA:E1VSI0" FT /db_xref="InterPro:IPR005913" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VSI0" FT /protein_id="CBT74583.1" FT /translation="MKVLLVSCGDVATEAGLRFHAHGHEVTAWRRQADKLPGLFTGHSV FT DLLVPAKWPAIDPETDIVVLTPVPVTRDAEGYQRSYLNVAKELATRVAADCPKLRRFIY FT VSSSAVMGGEAGQWVDESAPLAPTRETSKVLAQTEIALAGSGLPVTILRASGIYGPGRT FT RLVDIVRSGTAQLPIQSHWTNRIHRDDLAQAIVHVAALGEQAAELYLASDSAPAQLGEV FT YEFLAKQLDLPVPPGASEAPTRSAADRRLDNARLLASGLQLEYPSYAQGYRHILEGTST FT RHQ" FT CDS 376541..377746 FT /transl_table=11 FT /locus_tag="AARI_03490" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VSI1" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="UniProtKB/TrEMBL:E1VSI1" FT /protein_id="CBT74584.1" FT /translation="MGASARCVIFAAVAFFSMLGEGMAVFALTLATADELGSWGVTALF FT LAGLVPPVVFAPWVGRWVDGSALWRVWIINLGLHVLVFAAMALAGSIIASLALLSVASV FT CAVVNGAVIFKLIPRIRGGFSVARASSFLVVATSLAGIIAPAVASFVFAARGLGVVLWC FT AALGFVILAVAAVLLFSSQRSNPDETAASAAPTAPHAAAAARSTAVLLHDWRLRVLLLP FT MAAIVLFTAAEGVAGVFYLREVTATDTGYAVLLGAWSLGAVAGSLVGGNQRFGARSALP FT ILLGGAGVGAAILVEGLWANPAGLAVVFLLGGVGNGLHNTGVRTAIYDYVPESRHGAAW FT AQLRMMINIMVALGYLVGTPGLFVEPAQLVIVFSGAGTLLAIALSLVLLKRRNGQSPIS FT NR" FT CDS 378017..378433 FT /transl_table=11 FT /gene="umuD" FT /locus_tag="AARI_03500" FT /product="putative DNA polymerase subunit UmuD" FT /function="3.3 DNA recombination, and repair" FT /EC_number="2.7.7.7" FT /note="in Escherichia coli umuD and umuC genes have been FT shown to encode E. coli s fifth DNA polymerase, pol V FT (consisting of a heterotrimer of UmuD (2)C). The main FT function of pol V appears to be the bypass of DNA lesions FT that would otherwise block replication by pols I-IV" FT /db_xref="GOA:E1VSI2" FT /db_xref="InterPro:IPR006197" FT /db_xref="InterPro:IPR011056" FT /db_xref="InterPro:IPR015927" FT /db_xref="InterPro:IPR019759" FT /db_xref="UniProtKB/TrEMBL:E1VSI2" FT /protein_id="CBT74585.1" FT /translation="MADEQEMMPPGASHGPVQAVSAMGFPSPARDYFDGGLDLNRLLVR FT DRVSTFIMRVSGNAMQSAGIHDGDEVIVDRSLSVRHGSVVIVNLNGQMLVRRWQIDGQE FT VGLLSDESPLPVVLTEGDEVNVFGVITRCLHHVR" FT CDS 378423..379715 FT /transl_table=11 FT /gene="umuC" FT /locus_tag="AARI_03510" FT /product="putative DNA polymerase subunit UmuC" FT /function="3.3 DNA recombination, and repair" FT /EC_number="2.7.7.7" FT /note="in Escherichia coli umuD and umuC genes have been FT shown to encode E. coli s fifth DNA polymerase, pol V FT (consisting of a heterotrimer of UmuD (2)C). The main FT function of pol V appears to be the bypass of DNA lesions FT that would otherwise block replication by pols I-IV" FT /db_xref="GOA:E1VSI3" FT /db_xref="InterPro:IPR001126" FT /db_xref="InterPro:IPR017961" FT /db_xref="InterPro:IPR017963" FT /db_xref="InterPro:IPR024728" FT /db_xref="UniProtKB/TrEMBL:E1VSI3" FT /protein_id="CBT74586.1" FT /translation="MSADHVALVDVNNFYVSCERAFDYSLRNRPVVVLSNNDGCVVARS FT QEAKDLGIPTGEPFFKVQRYMDSHNLAVRSSNYELYGDMSARVMELLGRYGTWHEVYSI FT DESFVGLEGNLEQVRSVAAQIRAAIDQSIGLPVCVGVSSTKTLAKLANHIAKHNPGLGG FT VCVQQLMDPEVLENILHRVPVTDVWGVGRKTGAKLAAMGIESIADLQAADPLAIRKKFS FT VVLQRTVFELNGQRCIGPVEERADRGQVMFTRSFSTPVRTHEAMEEVMSIYAQKAASRL FT AREGRYAALLTVTAGTSRFARGEASFPSAQVRLPRPTRDPILLSKLAIAAMRDLMQPGI FT DYVRGGVILSGLSDSPGEQQLDLFGQSTDPAAEEQENVSSVVQDISVRFGAKSIGLGHA FT GMAKSPEWSMKREHISQRYTTDWDELLVVQA" FT CDS 379788..381107 FT /transl_table=11 FT /locus_tag="AARI_03520" FT /product="glycosyl hydrolase, family 3" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="3.2.1.-" FT /note="identified by match to PF00933. Glycoside hydrolase FT family 3 comprises enzymes with a number of known FT activities; beta-glucosidase (EC:3.2.1.21); beta- FT xylosidase (EC:3.2.1.37); N-acetyl beta-glucosaminidase FT (EC:3.2.1.52); glucan beta-1,3-glucosidase (EC:3.2.1.58); FT cellodextrinase (EC:3.2.1.74); exo-1,3-1,4-glucanase (EC:3. FT 2.1)" FT /db_xref="GOA:E1VSI4" FT /db_xref="InterPro:IPR001764" FT /db_xref="InterPro:IPR017853" FT /db_xref="UniProtKB/TrEMBL:E1VSI4" FT /protein_id="CBT74587.1" FT /translation="MTTRAKQLLSAGMLMTLMLASCSAPNAGKPAPSTPTTSVNISSGP FT TAPAQPTAPSQTSASSSHLDTMPTQSQQPSPREQAEALANELSVSEQASSLVMAGVPAT FT GASAAEISALKKQGISNVFLRGRSQLSVKQTSVKVQQITQSLEANVPADLPVWVATDQE FT GGFVRVQQGPGFTELPTALTQGGWSPSKLKRELGAVGKQLVEAGINVNLAPVADVVPAE FT LGTGNAPIGYFGREYAHGATAVAKTMATVNEALHSQGVQPVVKHFPGLGRVAKNTDTNS FT GVADTKIDANSSDLQPFERAIEQDKSWVMVSNARYAKLDAKNDAPFSSKIITGLLREQM FT GYEGIVISDDLCEAKQVSYLQVGERAVKFVAAGGTLPLCVESAPAITMAKALAAEAKAD FT GKFAAKVKEAAVKILEEKLSARQAARRQIKRVGPGCFLTR" FT CDS complement(381145..384426) FT /transl_table=11 FT /locus_tag="AARI_03530" FT /product="secreted subtilase family protease" FT /function="3.10 Protein degradation" FT /EC_number="3.4.21.-" FT /note="identified by match to PF00082. Subtilases are a FT family of serine proteases. The vast majority of the family FT are endopeptidases. Signal peptide predicted by SignalP 3.0 FT HMM (probability: 1.000) with cleavage site probability FT 0.964 between position 32 and 33" FT /db_xref="GOA:E1VSI5" FT /db_xref="InterPro:IPR000209" FT /db_xref="InterPro:IPR015500" FT /db_xref="InterPro:IPR023827" FT /db_xref="InterPro:IPR023828" FT /db_xref="UniProtKB/TrEMBL:E1VSI5" FT /protein_id="CBT74588.1" FT /translation="MVTRRTQKVPHLILGSATALALAVTLSGPASAAGIPQPGDGENAA FT SLPITSSSALSNLKVSGPLAKATGEVSVYVQLQGDGAFETVEKSGKKKDAAKVKKIGKE FT VKAKGKQLAAEANSKVIYTTHNALKGVALTGDAADLRKLAQRSDVAKISSIVPKKPSNR FT SSVVDTGALESWKSLDKTGDGVKVAVLDTGVDYTHASFGGPGTLEGYKEAQASEELPSA FT DSGLIDSNKFIGGWDLVGDDYNADSSADTYQPIPHPDSNPLDCQAAGHGSHVAGTTAGY FT GVNADGSTFTGDYSSLDADALSEMKVGPGSAPNAQLIGIRVFGCGGSSSVVGQALDYVL FT DPNGDGDFSDRADVVNMSLGSDHSPTEDPENDIVDALSAAGILSVVASGNAGDVTDVGG FT SPGNSRSSLTVANSIGSHVTLEKIQIDGPEDVAGAASGQYSANFNYTNADPAALSGEAV FT MAPADNAFGCDAFEPGSLEGKWVWLQWSENGEFPCGSGVRFNNAEAAGATGVLLDAELN FT LFDAGIAGNATIPGAQFTLDESNKLRPAAEAGTLKVTLSPDFVGGSSSESGVADTLNSS FT SSRGVHGSNGVVKPDVAAPGTQIGSVGVGTGTGTAVMTGTSMATPLVAGIAALVLEDSD FT YSPYEAKSVIMNTAATDIKDANGNAYGPNRVGSGRVMADAALETPAFAYDSEAADLTSV FT VFGVIEVDGKKNFSAKREITVENTSDKAQTYDANYVAATTIPGATFTLDRNSVTVPAGG FT SAKLNVTLSVDPQQWAKTIDPTMATTQSGLARAWVADVSGRVELSASDVPTLRIPVQAA FT PKLSADMEGKLKKLKKGADTTTLSLKGNDITAGAGATSVTSLLGAFELGASSERGDDSL FT DNIPAARSMDLKHVGASSTAPRTGIADGQLNIGISTWDNWAHLAGGTELDVEIDTNGDG FT EADFVTFNTAFDEVDLDLAATFNLATGEQVDLQPVNGVLGDVDTNTYDTNVAILPVSLS FT ALGLDEDSKEISYRVLGYSWYNTDDNGAMIPVDQTDWIEFNVAEPQVDFGAEGSLFTDL FT KGTKIPVTVADSSKASKALLLHMHNASGDRAQVLEVTDGKVKGKK" FT CDS complement(384780..385268) FT /transl_table=11 FT /locus_tag="AARI_03540" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR010841" FT /db_xref="UniProtKB/TrEMBL:E1VSI6" FT /protein_id="CBT74589.1" FT /translation="MQPLTEKTIRSSFVNASRQEAKKLTLPENFDSLDWDSLEYLGWRD FT PKMMQRGYLFHTDDSGRTRGILLRPTDGGRKPTNAAMCEMCRDVNIPCAVGMWTTKRAG FT QAGRDGDTLGTLICLNFECSRNVRIPPPKNPIYPDPMVVVAQRIELLDERVQSFLSRL" FT repeat_region 385567..385574 FT /rpt_type=DIRECT FT mobile_element 385575..386990 FT /mobile_element_type="insertion sequence:ISAar13" FT /rpt_family="ISL3" FT repeat_region 385575..385598 FT /rpt_type=INVERTED FT CDS 385681..386958 FT /transl_table=11 FT /locus_tag="AARI_34460" FT /product="transposase of ISAar13, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VSI7" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VSI7" FT /protein_id="CBT74590.1" FT /translation="MFKDTGGNDAASILLNLTDYRVIDATQEPAGRQVLIEPKATEAAC FT PTCGVITTRIHARPVHRVKDLPTGGNDIKVLVRKRRMACQETACERRSFVQTTEQLPLR FT ARITTRLSQKLVDEMSCELRAVSRVASAYQVSWPTVMARANMVGELVGNVDRMFIRRLG FT IDEHRFRKVRYARGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRCAAVKKWLKSRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKISVDHFHVIQRANLMITQVRRRRSHEVLQRR FT GRAADPAYKYRKLLTCNLENLSIRQVERLKLILEADPELGVIYGIKEHVRELLKTRDIH FT DFQSRWAVLEKSVKTTKMVEAKSLFRTLTAWRRELLVFIRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRVRILLYTAGLRPC" FT repeat_region 386967..386990 FT /rpt_type=INVERTED FT repeat_region 386991..386998 FT /rpt_type=DIRECT FT CDS complement(387055..387876) FT /transl_table=11 FT /locus_tag="AARI_03550" FT /product="putative phosphomethylpyrimidine kinase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.4.7" FT /note="EC 2.7.4.7 is involved in thiamin biosynthesis. It FT catalyzes the phosphorylation of HMP-P to HMP-PP" FT /db_xref="GOA:E1VSI8" FT /db_xref="InterPro:IPR013749" FT /db_xref="UniProtKB/TrEMBL:E1VSI8" FT /protein_id="CBT74591.1" FT /translation="MTNTNTASPAMTLTIAGSEATGGAGAQADLKTFQELGTYGIVALT FT CIVSFDPKDSWNHRFVPVEQQVIADQLEAIQTCYEDKLGTVKLGMMGSPATINTVATAL FT KSQKWDNVLLDPVLICKGQEPGHALDTDEALKANLLPLATFVTPNHFEAEQLSGIKITT FT ESDLIEAAKKIHEVSGAAVLAKGGVRIAGEDAIDVFYDGTTLEVLREKKIGEVAVSGAG FT CSLAAAVTAELAKGATPLEAARTAKAFVTEGIRNRVSGNTPFDALWQGGRR" FT CDS complement(387918..388532) FT /transl_table=11 FT /locus_tag="AARI_03560" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSI9" FT /protein_id="CBT74592.1" FT /translation="MSPMARELPSWTHDYATVRDRLASFPNQYEIRSVNQDGDDVEILR FT YWPEASWTAPADAQRLIFLGAPNDSTAAALSESGWQPVTTMHLLAGKPDDVEQVVKLAD FT TSGLFEAPMDNYDVVEVTDFDRPVARGRMHYGENYALLTDPDLFAPADPDTARRAVLAN FT FAGAAFGHGLPWLLLVANAEHADQLPEGWSKATMLSFWQHC" FT CDS complement(388666..389373) FT /transl_table=11 FT /locus_tag="AARI_03570" FT /product="putative TetR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00440: bacterial regulatory FT proteins, tetR family" FT /db_xref="GOA:E1VSJ0" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:E1VSJ0" FT /protein_id="CBT74593.1" FT /translation="MTTQPRTEKGRQTQAKLLATALECFAQDGYKASSMRAIASNAGVS FT LSHAYYYFKSKEDIVAQLLLNLRKEQYDQCSGILDEGNTLETNIRTVLDAGVRTLSGYH FT DFGPPFLRLLLSRDLSNDEISSIELELWEKVVSGSRPLPPLGIRRDLPKFLLLVSRQVF FT SAWAFDQSPQQRRSRLLMKNMAPVVAKFAVLCRLPVVRSLFEDVLALMDPGPAEIAEAA FT VPKPVPLRKQKAS" FT CDS 389732..390442 FT /transl_table=11 FT /locus_tag="AARI_03580" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR003744" FT /db_xref="UniProtKB/TrEMBL:E1VSJ1" FT /protein_id="CBT74594.1" FT /translation="MGDSNADNKLIRTKSAVFASAGSPYFSTVLTMMGAVVILSNIGAS FT KGVSFGPLITDGGFFLFPLAYILGDVISEVYGLKAARRSILVTFALAFFAVFCFWVMIQ FT LPSAEFYDGQEALERTLGPIWQIVVASACGFLVGQLANSWVLVKLKERSGERGLILRLI FT GSSGVGEFLDTLIFCAIAAPVIGIADAPSFINYVAVGFVYKTAVEIIFVPVTSVVIRWF FT KKREPSYGETVATS" FT CDS 390509..391204 FT /transl_table=11 FT /locus_tag="AARI_03590" FT /product="putative ABC transporter, ATP-binding subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily (TC 3. FT A.1.y.z). ABCISSE: ABC transporter, ATP-binding protein FT (ABC), DRI-family" FT /db_xref="GOA:E1VSJ2" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VSJ2" FT /protein_id="CBT74595.1" FT /translation="MQMGQRAKGQLEVHSLTIGYPNRVICRPINLQLARGTGLGIIGAN FT GSGKSTLVRTILGHLPPIEGTVEFQGLPVDDSSAHFRRTVAVQVTDGAFFEELTVREHL FT EMVARGHGVAEWGQAVQNELDFFEFSTVSDHLPNELSSGQRRKVLLAACLIRPAELVIL FT DEPEQRLDLRIRNKLYQRLAAIRANGTSVFAVTHDPLMLRSCMEQVLLLDEDEGQLLDP FT DSGAQWLER" FT CDS 391212..392777 FT /transl_table=11 FT /locus_tag="AARI_03600" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="12 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSJ3" FT /protein_id="CBT74596.1" FT /translation="MPQLIEFNPKELLARARSRRNFSERFDSFSDAYIWVLSALVALAY FT LFSALFGVLFVLLGEGVPHQELPTAVWGMRDLSLVLLVLAALAIFRVMLFIGPCGLSAA FT KAHWWLPLPIRLRNIRRSTWRNAVLAGLFASSFLGALWLIIMLGLAGSLQLPVAGLALG FT SFAVMGIGIANVATVIQSLNMHATARRISGWAMSTIALVLVVLWLLMMGKAQWAQALVE FT ELSSATLNQQVWLNVLLVLVVLCVASSYWAYRQFEQITGQALRAAGQQQQFAMGTLMQL FT DSRGLAAPAQTAIHRRRAHGARLTAKLPVAWRILILRLLRGGRWQATALCLTLMLLLAA FT AVQQIANPLSAAAFYLLLCVVLPLSISRIVAPLLGEQQLTQMLGLSESQLARAATCFAL FT LFAATALVFLTGGLGILDMIQIVHPWQWGAALSIASLGCAAASSAHAQRGERDWGTLLG FT SASNEMTIATVLFLEAVTYIRVAATFSPLVVLVLNPAATISWVLWACALLLGGSALLQI FT FRKN" FT CDS 392806..393261 FT /transl_table=11 FT /locus_tag="AARI_03610" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VSJ4" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VSJ4" FT /protein_id="CBT74597.1" FT /translation="MTVSISIFKPAELPQQLFYAVLKLRADVFIVEQQSCYPDIDGHDL FT DEDTVHLCALEDGKVLCTVRIMEIGSPSPRIGRVATASSARGRGLAGELMKQAVGLCQP FT HAQIQLSAQTQLESWYGKFGFQRSGADYDDDGIMHLPMIRDGGKAAL" FT CDS complement(393333..394631) FT /transl_table=11 FT /gene="tgt" FT /locus_tag="AARI_03620" FT /product="queuine tRNA-ribosyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.4.2.29" FT /note="exchanges the guanine residue with 7-aminomethyl-7- FT deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, - FT Asn, -His and -Tyr). After this exchange, a cyclopentendiol FT moiety is attached to the 7-aminomethyl group of FT 7-deazaguanine, resulting in the hypermodified nucleoside FT queuosine (Q) (7-(((4,5-cis-dihydroxy-2- FT cyclopenten-1-yl)amino)methyl)- 7-deazaguanosine)" FT /db_xref="GOA:E1VSJ5" FT /db_xref="InterPro:IPR002616" FT /db_xref="InterPro:IPR004803" FT /db_xref="UniProtKB/TrEMBL:E1VSJ5" FT /protein_id="CBT74598.1" FT /translation="MPEKNFDPSAPHARQDEFGFEVGTRLTATDGSPMLGRTGVIRTPH FT GEIKTPAFIAVGTKATVKAVTPVQVEQLGAQAVLSNAYHLYLQPGADILDEAGGLGKFM FT GWRGPTFTDSGGFQVMSLGSGFKKVIDMKSVDQSGPDDAVAPGKERLANVDEDGVWFKS FT HLDGNKHRFSPEISMGVQHQIGADVMFAFDELTTLQNSRGYQVESLERTRRWAERCIAE FT HFSLTDSRVGKDYQALFGVIQGAQYEDLRRKACQDLGAMAFDGFGIGGALEKENLGTIV FT GWCSEELPENKPRHLLGISEPDDIFTAIENGADTFDCVSPTRVARNSAFYTPWGRFNLS FT GARYKRDFTPLVEGCPCYACENFSRAYIHHLYKAKELLSHTLISIHNEHFTVSLVESAR FT QAIEDGTFFELKDKVLSSYYAGTPDPQGKPATA" FT CDS 394765..395862 FT /transl_table=11 FT /locus_tag="AARI_03630" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="10 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSJ6" FT /protein_id="CBT74599.1" FT /translation="MGLEKLKDSVAALVKLGPARKDHWIGLRTGVGVFAPLITLFAVDR FT LDLVVFAVFGAFTGVYGRVDGYWNRLRMQVRSGALFFVVIALALAASYWWIDHANPEVK FT QWQIVGATTLVAGACSVLVGFMRLRPGGSLFHIFAFAAIASIPEPAPFGEALLVSALTV FT LLSIAIGAAGALGQWANVWKRTPLPPLSDNVRRAIWWEGLFYILSAGVAGALANTVGSR FT LEAGHNYWAMVAAVVPLVGHTTTLRIRRGMHRMLGTLAGMILMAILIFLNPQVWVLLAF FT NALCQFMAEMLVMRNYFLAQIFITPMALVGVSLVTGLSGAVMYDRVIETLIGCAVGMLG FT VLLGSWVGTILKRRRGIVPKRETEI" FT CDS complement(395859..396398) FT /transl_table=11 FT /locus_tag="AARI_03640" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VSJ7" FT /db_xref="InterPro:IPR000086" FT /db_xref="UniProtKB/TrEMBL:E1VSJ7" FT /protein_id="CBT74600.1" FT /translation="MNVRTPDPYPGWLSEEDLYEARQRLPILYVEAIPVRLDPLGYVNE FT VGLLLTGDDDGQMLRTFVSGRVMYRETIRAALIRHIEKDLGTMVLPQLPASPVPFTVAE FT YFPAPSETGLTDDRQHAVSMCYIVPVRGESSPRSDALELTWLSPSEALSSDIQGEFAGG FT RENILRQALAHVGLNI" FT CDS 396607..398055 FT /transl_table=11 FT /locus_tag="AARI_03650" FT /product="putative EmrB/QacA subfamily drug resistance FT transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily, drug:H+ antiporter-2 FT (14 spanner) (DHA2) family (TC 2.A.1.3.z). Identified by FT match to protein family TIGR00711" FT /db_xref="GOA:E1VSJ8" FT /db_xref="InterPro:IPR001411" FT /db_xref="InterPro:IPR004638" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VSJ8" FT /protein_id="CBT74601.1" FT /translation="MTNAPERLSKQNFTTIAVLIVSSFVVILNETIMNVALPVLMNEFN FT VTADAIQWLSTIFMLTMAVVIPMTGFLLQRMSIHKVFILAMGLFTVGTILAAAAPGLTV FT LLVARVIQASGTAIMMPLLMTTILHLVPPARRGVLMGNVSIVISVAPAIGPTLSGLILQ FT YLSWRFMFIVIVPIAVVALLVGSPRLPRDVEGVSTPLSVPSLILAIPGFGGLVYALSGL FT SAGVTPLNLGILIGAVLCLLAFVFLQLNLQKEDKALLDLRPLGYKSFSLSLVLMMFSMI FT ALFGVIILLPMFFTNVLGIETLTTGLIMLPGGLLMGILAPMVGKLYDKVGARPLIVPGA FT LVLLASLLGYAMILDADTPIWLLVVLHLVMSLGLAFIFTPAFTTALNPLPHHLHSHGSA FT LLSTLQQLAGAMGTALLVGVVASATAAKIAAGTDELTAMVEGFQPGFLIGAACSVGIVV FT IGFLLGGRKQAVAAEAEPSKVPSH" FT CDS 398204..398980 FT /transl_table=11 FT /locus_tag="AARI_03660" FT /product="short-chain dehydrogenases/reductases family FT protein" FT /function="2 Intermediary metabolism" FT /note="identified by match to PF00106. The short-chain FT dehydrogenases/reductases family (SDR) is a very large FT family of enzymes, most of which are known to be NAD- or FT NADP-dependent oxidoreductases" FT /db_xref="GOA:E1VSJ9" 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:E1VSJ9" FT /protein_id="CBT74602.1" FT /translation="MQLQDSVALVTGGLSGLGRATAQKLASQAKHVLVLDLPRDDGDEI FT SAQIGANVRFVPADVTDAQQVATAIERAKELGTLRVLVNCAGVATPGKVLGREGVLPLE FT RFSKVLEINVNGTFNVIRLAAEAMAHSEAEVDEHGTSERGVIINTASVAAFDGQIGQPA FT YAASKGAVAAMTLPLARELASHQIRVMTIAPGIFHTPMMAGLPQAAQDSLGAQVPHPSR FT LGRPEEYAALVEHIVANPMLNGETIRLDGAIRMAPR" FT CDS complement(399005..399421) FT /transl_table=11 FT /locus_tag="AARI_03670" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSK0" FT /protein_id="CBT74603.1" FT /translation="MPQLNQHTARTKFERWATDAPLGFFAGFSMVYALQLWFATAGWTG FT REHAMQVALVAVGVSLIAAGFAHTERGRHALASGFGISMVAAAIQGWFHESTPLWVSAV FT WIFMALLVFLLAENRRFQISHAEHRAQRGKPIEF" FT CDS 399461..401104 FT /transl_table=11 FT /locus_tag="AARI_03680" FT /product="site-specific recombinase" FT /function="3.3 DNA recombination, and repair" FT /note="serine recombinases demonstrate functional FT versatility and include resolvases, invertases, integrases, FT and transposases. This protein may be a resolvase (match to FT PF07508 and PF00239)" FT /db_xref="GOA:E1VSK1" FT /db_xref="InterPro:IPR006119" FT /db_xref="InterPro:IPR011109" FT /db_xref="UniProtKB/TrEMBL:E1VSK1" FT /protein_id="CBT74604.1" FT /translation="MNTSRHQPGVNARPGRTGRSTVYPAYAQTGPESPTPGTKPIFLYL FT RLSKYHKDKADAIERQRIDLTRMLTAEGGWTIMGEYIDNDSASSAAIKTRKGWRQLNAD FT IKAEKIGAVAFWKLDRTNRIASQCIEWIGDCQRAGVQLRSHQDSTDELNTATAGAKLVT FT GIKALLAEVETDSMSERQLASKRHLAEAGFHHGGMRPFGWMQGPRVTDAMGRTGIRLIP FT HPVEHQALKDAVDLVLAGKSLAQIGRYWKEQYGITTASGAYVYEATIYRSLVSPRMIGY FT RMRQVPEHQRGVKIDLLDYIARDASGEPVISQEPVCDRATWLRVRRLLEEAKTSKARKP FT WGSHEWLLTGLIYCQCGGRLYGHQKTRHRASGEKQVEYVYRCLTNRHRGAGNCPGSCTI FT NANKAEAYVLGWFFSQITDEALAKARARRRAARSDAAVDDLLAQLDEATAEKNALLAKQ FT GTSAYKGAMVTVLLGLIEDAQNRIDVLQRRVDAVELDHLVITDGPEVIRSWESKGIKEK FT RNFLRRMIQQIDALPGRGTIDQRIQITPVA" FT CDS complement(401281..401850) FT /transl_table=11 FT /locus_tag="AARI_03690" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSK2" FT /protein_id="CBT74605.1" FT /translation="MNDHPLPEIDPDESTIEDFELTATDLEAAGPPHPVNWNLLSADDL FT EAEWLELNRWVDWLRKTYGLPASVIPPFWHHHPELVWELSALHLHWLCAYDPEQNGSAP FT LGWHRDFVDARQRLRDWVAASGTRLDRDRPTRQTTWPGEEPAPQIEDIVIEDRDDEFTD FT FVLAEVAQRRAEEEAFYRHVAGDDHD" FT CDS complement(401860..402321) FT /transl_table=11 FT /locus_tag="AARI_03700" FT /product="single-stranded DNA-binding protein" FT /function="3 Information pathways" FT /note="identified by match to PF00436. The Escherichia coli FT single-strand binding protein binds tightly to single- FT stranded DNA (ss-DNA) and plays an important role in DNA FT replication, recombination and repair. Closely related FT variants of SSB are encoded in the genome of a variety of FT large self-transmissible plasmids" FT /db_xref="GOA:E1VSK3" FT /db_xref="InterPro:IPR000424" FT /db_xref="InterPro:IPR011344" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="UniProtKB/TrEMBL:E1VSK3" FT /protein_id="CBT74606.1" FT /translation="MAIRTQESLSGFIATDPQLTYTERGEARFYARFGQENYRREQDGT FT FTKLEPDFGNLVMYRATAERAYERFSKGDQFVAEGYTHDYEYERDGQQITGTEFVVKKI FT GHDTARTRYDVDRSPRAQAVDREGSSRETPGFKSPQQTDRSQGAPAMGM" FT CDS complement(402407..404173) FT /transl_table=11 FT /locus_tag="AARI_03710" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSK4" FT /protein_id="CBT74607.1" FT /translation="MNRQAASMSDGLANLGIGLLIAAAGLAAILRVAGTIAAFLTGTPQ FT PQAGITAGLMVLLNPADPAPALEADGLNSIAYWITTTLLIVVLGAGVWWGWTKVRHHSQ FT SVQTDPRRLQGIATSGEVSRVASDTALIKRAGTLRPSLGAPKPSDVGYLLGRSRGKRVW FT ASVEDSILLVGPPRSGKGLHVVINAILDAPGAVVTTSTRPDNLTATLRARQRIGPVAVF FT DPQHLAEGLPAGLRWSPVRGCEDPLTAMIRATGLASGTGLSAGGVEGGGFWEGKTRTAL FT QALLHAAALDNRPPAELFRWTLDPTAAAEAVAILTNSSQAAAGWAESLEAMIDADPRTR FT DSIWQGVSLALAALADPRVLDAVTPRAGEHFDPEAFLTESGTLYLLATGAGAGASSALV FT AALVEDLIETARRMAARSAGARLDPPVLLALDEIGNLAPLPSLPTLMAEGGGTGITTMP FT VLQSLAQARDKWGENAANAIWDAAIVKIILGGASNSRDLQDLSTLIGERDEYTDSITIG FT DHGTRSNQRSIRRVPILPPDRLRTLPFGTGITMLRSAPPIVTNLRSWVTRDDAKTLRAD FT RTEIETLLQQRP" FT CDS complement(404170..404709) FT /transl_table=11 FT /locus_tag="AARI_03720" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSK5" FT /protein_id="CBT74608.1" FT /translation="MSRREIRAQQQQGQPPVTLPLVVVTVEKGGTLIVTVDGSLFAPEA FT FAPAWRRSDFGRIMDRITDQRRTPVRVEVHESDGTSFTDIITPSPSRRTRPEPETANTE FT TALETPAAPQLVEVAAEGFIPGEDIGVAIIVTHTDASHTGHARALLETAQFDASPTGEV FT VLIGRVSGNYEIVRHP" FT CDS complement(404706..406262) FT /transl_table=11 FT /locus_tag="AARI_03730" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSK6" FT /protein_id="CBT74609.1" FT /translation="MNRHADERLHTSVLVGPDGERRKHRKARRNAAAALHAEERRARAA FT EAKARADVERAERRGTRYLPAAGEPGRAALATPGRFRLPRHQDTSAALAGAYPFLAEGG FT LGSDGVFVGQDLYSGGSFVYDPWVLYQRGLITAPNVVLAGIVGSGKSSLAKSLYTRSIP FT FGRRVYVPGDPKGEHTPVAEMVGGQAIVLGHGLRNRLNPLDEGHRPSGLSDHEWATQVA FT SRRRDLIGALAATVLERSLTPLEHTAIDVALTAVVAGNDVPILPMVVDLILTPDPADNE FT DGRLAEDGRMVGHALRRLVAGDLQGLFDGPSTVAFDPSLPMISLDLSRVAENSTLISVL FT MTCSSAWMESALMDPNGGQRWVIYDEAWRLMSHPALLKRMDAQWRLARHYGIANMLIFH FT KLTDLDNVGDHGSAMRALASSLLANAETRIIYRQESDQLGITARTLGLTGTEQKLLPGL FT GTGQGLWRIKDRSFVIQHQLHPAELDAFDTTTRMITKSEKSIDADETSPSLSLNRGGEG FT V" FT CDS complement(406259..407074) FT /transl_table=11 FT /locus_tag="AARI_03740" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSK7" FT /protein_id="CBT74610.1" FT /translation="MPTFDNPLSDAAEASEALRGLAHATRTFDNPADTYAVIGDLLSGL FT RSLRQVFDQLATTHLTHRNRAFNDAGDHKIGAGDALAASDELHHAGSLLDAANDRLDAA FT SQASGRIAWHPATSVAETVQRYVSVVFLQGEDADRVLDQIETDGITAGIQHLQGWDYGN FT ETTDTALAHGHVYDAVPTGALDWTAEHGDYVLVANRHLGHVSLLRKTAFDTNVLATPDG FT VSTDIAPARPDDPPARHAPGAPSAREDAFGHPFRPAHISAVIQGRGLGL" FT CDS 407333..409069 FT /transl_table=11 FT /locus_tag="AARI_03750" FT /product="putative drug resistance ATP-binding protein" FT /function="4.2 Detoxification" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT (putative) drug resistance ATPase-1 (Drug RA1) family (TC FT 3.A.1.120.z). ABCISSE: fused ATP-binding protein (ABC2), FT ART-family. Duplicated ATPase domains (PF00005)" FT /db_xref="GOA:E1VSK8" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VSK8" FT /protein_id="CBT74611.1" FT /translation="MPHLLPTSSFTATGSHLRVDGISFSYPDRRVLTDVSFVVSAGDRV FT GLIGENGSGKSTLLRVIAGALEPATGAVTVNAPDSHMPKIGLLHQEPPFSTSATIAEAL FT EQAVAPLRRVVEEVSALGVALSSRPEDQAASDAYAHALDTAERLGAWDVDARISAMLTG FT LGLDGIDRNRLTGSLSGGQRARLALAWLLLKAPDVLLLDEPTNHLDDAATAYLVGVLSS FT WRGPLLVASHDRTFLDEVVTSLLDLDPSPIPHAVAGPLVQDGTGTAIGATRFTGNYTDY FT LIVSADVRRGWERQYRDEQAELSRLRATVKDQQTVGHADWKPRSEVRMAQKFYADRNAQ FT VVARRVNDARARLEELEDRQIRKPPQELEFMGLTAAGEPHIVGALEPVFTTANVTVRNR FT LTATSLSISRGEKWLITGPNGSGKSTLLSLLAGTLEPSAGQVTRSPNDRIRLLAQETTL FT PDPHNRGPGRTTGQTYVDLVGAELAAKVPLSTFGLIPARDLNRSVVELSVGQQRRLALA FT ALLADPPEILLLDEPTNHFSLSLVTALENALTDYPGTIVIASHDRWLRRRWTGRQFEIP FT AR" FT CDS complement(409105..410085) FT /transl_table=11 FT /locus_tag="AARI_03760" FT /product="putative Zn-dependent alcohol dehydrogenase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /EC_number="1.1.1.-" FT /note="identified by match to PF08240. Zn-dependent alcohol FT dehydrogenases catalyse the following reaction: an alcohol FT + NAD(+) <=> an aldehyde or ketone + NADH" FT /db_xref="GOA:E1VSK9" FT /db_xref="InterPro:IPR002085" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR013149" FT /db_xref="InterPro:IPR013154" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VSK9" FT /protein_id="CBT74612.1" FT /translation="MLMQAVLAERPGILSDVLALHNIPDPGVPGEGEVTVRMIASTINP FT SDAVTVSGAYGSRTQFPFIPGFEGVGIIESVGPGVPVEALGKRVLPIGSAGNWQEVKLT FT AYSWCVPVPDDIPDTKACFAYINPLTAWLMVEQHCSDQTGQVAITGATTTIASHLAEFL FT YIRGIQPVGIIRGTPGSTVANRDHWSDVIETSHANWAKQLQKHNGKKFDLIFDCVGGQL FT GATLMRHLAPGGVLVHYGLLSGEPLPSECFTSGESKRVEMFRLRDTIHSHARERLPALF FT TPVFEHMRAGRLHTEIAASVPLSGLPAMLTDQSGVTPGKVLISYA" FT CDS complement(410151..411626) FT /transl_table=11 FT /locus_tag="AARI_03770" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSL0" FT /protein_id="CBT74613.1" FT /translation="MARKHEHDRRRDDYELSAVKFSRLTRRGILLGLSLPQLITLAIGI FT LSIVAALYAGGGLLIAYAAPIWLLAAVLTWVPAGGRKLIEWVPVGFRWVWRVSIGQLLY FT RRRIVKPRPAGTLALPGDAAALREYVDPETGAAMIHDPHQHTLTAIIGLSHPAFVLLDP FT GEQERRVTAWGRVLATTCRSGRIARLQVLERTLPDSGSGLAEWWASHGHHDDSWTATTY FT AELIERAGPAGERHATTLSLALDMRTAARQIRTAGGGLRGAAAVLRQEMTTLVAALRAA FT DLTPSEWLTPGEIAVILRSAYDPAIAATLERHGDLGRDLATAGPVAVTETWDQLRSDSA FT HHAVLWISEWPRSLVYPGFLAPILLSTGIQRSFSLVCTPIRSDQAARDIRKKKTEYISD FT AAQRQKIGQIEDAGQTAEYQDVLQQEADLTSGHGILRYTGLINISAPSQDDLEAAVAAV FT EQAAIQASCETRRLVGHQAQAFTVAALPLARTV" FT CDS complement(411633..413063) FT /transl_table=11 FT /locus_tag="AARI_03780" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="7 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VSL1" FT /db_xref="InterPro:IPR007688" FT /db_xref="UniProtKB/TrEMBL:E1VSL1" FT /protein_id="CBT74614.1" FT /translation="MAICDIPVISNVCDVAGEAAATLVSAPFDWLAQAMGQAAGWLFEA FT VWSVFDTTTLVDVSDPGYIGVYNVLFGVAVFIMLIFFCLQLITGLIRRDPTALSRAALG FT LAKAVLGSFVAISITGLLLEITDQLTIGIVQATGNTMEGMGDRIALLAAGLVGINIAAP FT GVGAIITIFLAGLAISAAAIVWFSLLIRKALLLVAIVFAPIALAGASWDATKGWFTKWA FT AFVIALIASKLVLVVIFLVAITQVSAPIDLDLASIADPIAGIVLMLIAAFAPYMAYKFI FT SFVGFDMYHAMSSEQEAKSAMNRPVPTVAKPAGDGPKKVLDDAGSSGGKSGGGSSASAR FT TGGGGSSSGTAAGAGKGAAAGGTSAGASAGSAGAGAGGAGASAGAGAAAAGPAAAAVIG FT AQVVKGAATAGPKAGSAVGGQAEAHAGAAQDTAPPPAPNAPAQPTPGTARSASPAPPAP FT PAKATPPPAPPSSPKPKE" FT CDS complement(413107..413466) FT /transl_table=11 FT /locus_tag="AARI_03790" FT /product="putative TonB-box containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PS00430: TonB-dependent receptor proteins FT signature. In Escherichia coli the TonB protein interacts FT with outer membrane receptor proteins that carry out high- FT affinity binding and energy-dependent uptake of specific FT substrates into the periplasmic space. 2 transmembrane FT helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSL2" FT /protein_id="CBT74615.1" FT /translation="MLPLIEGASIVNTLTVLAEATPVLSALLPMQIDIDPNSSGLPGIN FT QLRTIVGAVMTVGLILSVLALIVSAIVWGFGANSSNPHLAGRGKIGVLVSCGAAIICGA FT SVTLINFFWNVGQSV" FT CDS 413569..414174 FT /transl_table=11 FT /locus_tag="AARI_03800" FT /product="SAM-dependent methyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.1.1.-" FT /note="identified by match to protein domain PF08241" FT /db_xref="GOA:E1VSL3" FT /db_xref="InterPro:IPR013216" FT /db_xref="UniProtKB/TrEMBL:E1VSL3" FT /protein_id="CBT74616.1" FT /translation="MTVDRVRDAYAYRASEYIDLLGSIDATATEDQELVGAWSQKRDGL FT ILDVGCGPGQWTNFLHATGAEVVGIDPVHEFVVDAQARYPQVDYRLGQAENLDVPDASV FT AGILAWYSLIHTNPSDLGAVLDEFARVLRPGGSLLLGFFEGPELMPFDHAVTTAYFWPI FT PELTHRLDQARFTVTETQTRTDEGSRPHGAIIARREHV" FT CDS complement(414175..414441) FT /transl_table=11 FT /locus_tag="AARI_03810" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSL4" FT /protein_id="CBT74617.1" FT /translation="MDVFPDFGGVGGAGGLTAVIGALLTFVLIIAVLMLIICGVTWAIA FT TANGHHGAASKARIGAWTALGAAVLAGGAVTWVNWLINLGSTL" FT CDS complement(414444..416066) FT /transl_table=11 FT /locus_tag="AARI_03820" FT /product="putative secreted M23 family peptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.-.-" FT /note="identified by match to protein family PF01551. FT Members of this family are zinc metallopeptidases with a FT range of specificities. Peptidase family M23 are also FT endopeptidases. Signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0. 740 FT between position 37 and 38" FT /db_xref="GOA:E1VSL5" FT /db_xref="InterPro:IPR011055" FT /db_xref="InterPro:IPR016047" FT /db_xref="UniProtKB/TrEMBL:E1VSL5" FT /protein_id="CBT74618.1" FT /translation="MSGMRKILAALVIAAVCFGPTVVLLGIGLVMNPAAQASCLPGMSL FT TVGPIPDSLDVTTKNGERYTLNRKQLTHAATINTVGGQTDGIDTRGVTIALMAALTEST FT LRQLANTGTYPESGDYPNDGNGSDHDSLGLFQMRPQAGWGTVADLMDTTYQARAFYGGP FT TGPNYPSPRGLLDIPGWQQMDMGAAAQAVEVSAYPDRYQNYQPVAEAILTALTRPAPGA FT GGEAGSVPETSRIVFPLPAGTWTRTSAWGWRSDPFTGERSFHSGSDYGAADGTPIYAAA FT DGRVTVAEFTGGYGGLIIIEHTVSGQALRTAYAHMWQHGIHVTPGQTVTAGTHIGDVGS FT SGRSTGAHLHFEVRPGSTGSDTIDADAWLSEHGATETGGGQTPGPGCAAGGDAPAPGGM FT AGEPDVMVDDPTSGGQITARMLHVMTHTRIAFAGTGWGCYSPRPGTRSEHPLGRACDVT FT FGNRIGQAATGASLESGWAVTNWLKTHAETLGVEYLIWQGRIWSLAQDVEGWRPYHGGG FT MHDPADITGGHFDHLHITVKEGA" FT CDS complement(416073..416720) FT /transl_table=11 FT /locus_tag="AARI_03830" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSL6" FT /protein_id="CBT74619.1" FT /translation="MLIAAIAGALAVVVLAGIGVYGLIRGPHTSSLDPEPSGQTDTVAP FT SPRHPATKTGPNEIRDTTRAEDFARDVALALFTWDTASGYQSSEYAQVIVDVGDPTGTE FT TAGLAADVRTYLPSPEQWAQLRTHQTSQWLTIDDLYIPAAWADAEAQAAPGQLLPGTTA FT YTVTGTRHREGIWGTEPVESSRPVAFTMFITCQPTFDHCRLLRLSRVDEPLT" FT CDS complement(416796..417902) FT /transl_table=11 FT /locus_tag="AARI_03840" FT /product="ParB-like protein" FT /function="3 Information pathways" FT /note="match to protein family PF02195. Proteins containing FT this domain, appear to be related to the Escherichia coli FT plasmid protein ParB, which preferentially cleaves FT single-stranded DNA" FT /db_xref="GOA:E1VSL7" FT /db_xref="InterPro:IPR003115" FT /db_xref="UniProtKB/TrEMBL:E1VSL7" FT /protein_id="CBT74620.1" FT /translation="MVVVSERNGFIGLERTVDSITIGTRHRTDYGDLAQLIASIKRDGL FT LQPVTITPDGVLVCGARRLAAIKQLGWRTVNVWVRSGITDRLGALLAEQDDNLLHKPLT FT PTEQATLYRELKEIMAEEAAQRQAATQFGTGGKQPGQAGAGESPGPYGMKGDAREQAAR FT LITGTDSSQRLERIAHLQTLAENPDQSEEVRQRARAELAAIDTGSPVSPAFQRLNAHTS FT VAELERIANDTDVDEIVRHHAQVAAHSLRETPADVKAAELERLAVEALRRVKEQTKTQK FT PRPLRPAPKPDEGTVPQFPVRAFRVMWSEMAAWWLHYDVADIAHALTDEEHEAFQETIE FT GTVNFARQIAEHRTTARVAQDAAARVIA" FT CDS complement(417886..418812) FT /transl_table=11 FT /locus_tag="AARI_03850" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSL8" FT /protein_id="CBT74621.1" FT /translation="MTSTAIVLDQDLWEVVRTCLSGGATIMTTTAAAHIDFTTGEGLRS FT LLTRIHDAGKAAWRSDRDVPALMDYTATKYAPLARKHGLDAWEAASAAFDVMRTPSVLR FT ANDPWGVVTRAVQITCIAEARANGMLCSTHQARRPQFSVFHDAERFSDRENPLTDYHPA FT FHHHDHDSEVGHDPVSPESEQVLAVSAVSDTVALFTALGWPEPTVKASIDYICERLARA FT GNRATAFEALRRDKHARALLDLPASSWHGLLRTVLGNPEPVYVGTSHGRGVLLRLLIGE FT PVPVLLRDDDLVLTITASIPVRGGGRE" FT CDS complement(418819..419253) FT /transl_table=11 FT /locus_tag="AARI_03860" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSL9" FT /protein_id="CBT74622.1" FT /translation="MNTKQPAHVTYETEPPQTTSRATEPGTAGGSPHEDVSELARRNDP FT SLKSRTVTARGVDRFDPRSVAWMRLSDALSASTAQLAGRGISFEAELHRRIRRFPVQTV FT AASRTAISNRVSKLPPLSAFGRPRPHGVSAPQRSGVGMAR" FT CDS complement(419250..419981) FT /transl_table=11 FT /locus_tag="AARI_03870" FT /product="putative phage excisionase" FT /function="4.4 Phage-related function" FT /note="similar to putative excisionases from Mycobacterium FT phages" FT /db_xref="GOA:E1VSM0" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR021235" FT /db_xref="UniProtKB/TrEMBL:E1VSM0" FT /protein_id="CBT74623.1" FT /translation="MTTPMLRRGGRLAVSTAVAGTVLIALGAFWLSFTALADLARRSGI FT SEDQAWAWPLIVDGIIVVATVSVVALAGHRAAWYPWMLLAAGALVSVTANALHAVIAAD FT AGVPGLLAAAVAAVPPLVLLAITHLTVILTRPIAPNNFPSTAATTLELVDEADSDNDQE FT DAAWLPVPDSCSAATPPSTDEASAVSPDPGELDRRAVAAGLREQGWSNKRIATHFGVHP FT STVGRWLPQQLSITNEQETSP" FT CDS complement(419978..420883) FT /transl_table=11 FT /locus_tag="AARI_03880" FT /product="putative bifunctional primase/DNA polymerase FT protein" FT /function="3.1 DNA replication" FT /note="match to protein family PF09250" FT /db_xref="InterPro:IPR015330" FT /db_xref="UniProtKB/TrEMBL:E1VSM1" FT /protein_id="CBT74624.1" FT /translation="MATVFNALARIQHLRLPDAARSLASAGVPVFPCVPGEKRPLTRRG FT FHDAANDLDQVSAWWDRWPSANLAIPTGPASGIDVVDIDIGSTGSGVPAFQRARREGLV FT HGWAALVRTPSGGLHVYFPAGTSREQPSWQAPMAHIDFRGTGGYVLAPPSQVRQPDGHL FT RPYELQSTGLVEPSPVDASRLRNFLDPRPALTHRDQMTTRRGLDVQRLGQWVAALGEGE FT RNLGLFWAACRLAENNTAVGDTLAVLGPAAAHAGLGAREITTTIRSAYRTTDPAYHRST FT SDEPAPRRSPPQPAVGRVIA" FT CDS complement(420885..421976) FT /transl_table=11 FT /locus_tag="AARI_03890" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR010359" FT /db_xref="UniProtKB/TrEMBL:E1VSM2" FT /protein_id="CBT74625.1" FT /translation="MAKNWEEARVAREAKLDGLQERLASAVDGLVTGEDWQRAMAFAAR FT FRSRSFNNILLIWSQHLGAFEAGRVQVTEPSYVAGFRQWQTLGRQVDKGQSGYMIFAPV FT TARFASATPADAASWRRLERGEKPRAGEVARSKIVGVKPAYVWDVSQTSGEPIPERPMP FT VLLEGEAPAGLWEGIAAQIEARGFTVLRVPHEGMIHGANGVTDYGANTVAVRENMPPAA FT QVKTLAHELAHVMLHGPNNPDASGHRGVGEVEAESVALMVGAAHGMDTTGYTIPYVTGW FT ASTVKDSSPVEVVQAAGERVRKAATEILDQLNTAQVGAGDPPGLVRDTSRREARQRFAP FT QPLPEPSPSPSSAVGSREPVRGL" FT CDS complement(422211..423167) FT /transl_table=11 FT /locus_tag="AARI_03900" FT /product="AraC-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein domain PF00165: FT bacterial regulatory helix-turn-helix proteins, AraC FT family" FT /db_xref="GOA:E1VSM3" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR018060" FT /db_xref="UniProtKB/TrEMBL:E1VSM3" FT /protein_id="CBT74626.1" FT /translation="MDPACSWSAKAQYEFRQGESAHGFHPVLARTRTLHRPIGPIAYDC FT VKVIIVRDGSALLFSEFGQRIVTAGDVVVLGANVLCGSEPEGHITATTIYLDTDYVIDQ FT VFWQHAWLLHDRLDAQRFTKALYSEPSQVLRLGEDRTGMLMPWLDELVARSIDGGFAHH FT FHRMQALWFAIADVVTPFVKVTPIRQSRTQRAHSRPTLPRCRNFAPARDEAHQTRATLA FT SDIATNWTLDVLSARVHLSPKQLSRVFTEAYGKTPLAYLTMLRVEEMAHLLRETHLTID FT ASARRVGWASRSRANEAFQQCVGMTPSEYRRMHRSEK" FT CDS complement(423172..424479) FT /transl_table=11 FT /locus_tag="AARI_03910" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690" FT /db_xref="GOA:E1VSM4" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VSM4" FT /protein_id="CBT74627.1" FT /translation="MQKPEDRDSAAGYDAVVSAEPDSIMKTRGRSASQIPIIFVTVFLT FT YTAMTVMNPLIAPLSRVIGMPEWQIGVGVSVAALCVAVASPFWGRLSQRVGARLILTST FT ICSATLAMVVFAAVAHARFLGIASAGVVFVVLLLVRGVWFGLSEAAVLPTAQAYVASIT FT PDPTERVRGMAAIGAGVGASSIAGAIIGGLLGGFSLPVALWAVPILLVLTLAIVTIWMK FT RTSVPVQEKPPRKVSATDSRVRPYLIVSFGLYTALGFIQILVGFLVQDRLFLGTEQAVL FT VTGIAFVCAGVGLLLSQAIAVTRLRWQPVRYIRVGAVISAIGILFLVPDWGASSVLVAM FT FITGVGIGMAIPGVAAGVSLAVGSSEQGSVAGLVAATNALTFIIAPTAATALYALSPLV FT PLIATAIATVLVMTFSPTNRRLAVTPESVHDDEARI" FT CDS complement(424558..426144) FT /transl_table=11 FT /locus_tag="AARI_03920" FT /product="iron-siderophore ABC transporter, ATPase and FT permease components" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT siderophore-Fe3+ uptake transporter (SIUT) family (TC 3.A. FT 1.21.z). ABCISSE: ABC transporter, permease and ATP- FT binding protein (IM-ABC), DPL-family, SID-subfamily FT (siderophore uptake)" FT /db_xref="GOA:E1VSM5" 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:E1VSM5" FT /protein_id="CBT74628.1" FT /translation="MNTQHTQTLPAAARRRLVLISLGWALVALAEATAYTVLALAIAKH FT QPPGMVIATAAVALFITVLVSRSGYLTGARLAGDLFQGVGAAFSHAKLSWFTEKNRTLV FT GTVAGQSIPALMSVPAHQLQTFILSPLIPLLLLVGIAIVAGPLTMLLVAGLVIIAFVAQ FT LFAQRALSRADAGRNTVEQAATEASLEFIDHLELLRTAAGPDRAVSRLEDTWDTHEAAL FT ARTNQVSTPATFVSSLASILPLAGLLLFIASTAMENPATALALIILTARASAPLDALAL FT AGVSINELRTTINRYRAVLSAPVLPEPTKSVQSVGHAMTVNDVSHITVLQGVSTEVPEG FT STTIITGPTGSGKSTLLSLLMRFDDPDNGRIELGGVDLTDMRYEDLAKQIGYVPQDPVV FT FDGTLADNIRLGDPSATDEEIIHAAKQAALGQVIEQSPLGIQQSVGHHGNALSGGERQR FT VAIARALLKQAPILILDEATSALDTATEAKIAKAIRALPCTKIVVTHRDAETTWQPTIR FT IALGESSGTNK" FT CDS complement(426141..427748) FT /transl_table=11 FT /locus_tag="AARI_03930" FT /product="iron-siderophore ABC transporter, ATPase and FT permease components" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT siderophore-Fe3+ uptake transporter (SIUT) family (TC 3.A. FT 1.21.z). ABCISSE: ABC transporter, permease and ATP- FT binding protein (IM-ABC), DPL-family, SID-subfamily FT (siderophore uptake)" FT /db_xref="GOA:E1VSM6" 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:E1VSM6" FT /protein_id="CBT74629.1" FT /translation="MPALNNDPAAAPASPIAAALRPAIPVLTAAVTAAALGGLTMVGAL FT WFTVQVVAAVTLTHAISACVCWLIGGLLLSVSSWLAHHGEARFSARLRRDTARHLAHMP FT MSTVSRYGADALRRLVGEDIAALHHTVAHLPAEIATLAVVPLATVTLLVAVAGPLTLIA FT LIPGLLAAAYYLFIVPRSSAKHGTETVRVMTDIRTAVDDYARGIRVSRIYSAQAGATAN FT YADAARRFTENMVAWVRRVATLSSVAVALLQAVATYAIAYAIGYDQEPAVLAAMLLFGL FT AVVTPALRLGHGLDYVRAGSAAAERIAAVLREPTVTGSTDHSDDPGLELVDVRIGQDDR FT TLIHSLSHTFSPGLVTAITGPSGSGKTTLLRTIAGLETLESGVIRYPHRETNSEKTSPD FT SVLLIPQGGDVLSGTIRENIALSTPEATDDEISTALRRAQLDLPLDTATTTLSGGERQR FT VGLARAFLTDARVILLDEPTSALDKDTSGRLVSELHTFVMEESKTLLIVTHDHGLAEGA FT TAQLKLTGNSVTVAGGTR" FT CDS complement(427748..428623) FT /transl_table=11 FT /locus_tag="AARI_03940" FT /product="iron-siderophore ABC transporter, ATP-binding FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, ATP-binding protein (ABC), ISVH- FT family (iron siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VSM7" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VSM7" FT /protein_id="CBT74630.1" FT /translation="MDTHPLATANTAELTVPTSRLWTVNATIGYDKRVINENLSVSIPD FT ESFTVIVGPNACGKSTLLRGLSRLLKPGSGRVVLDGQDIHSYKAKEVARKLGLLPQTSL FT APDGIRVADLVARGRYPYQKLIRQWTPDDEQAVSTAMAATGIHELSDRLVDELSGGQRQ FT RVWVAMALAQQTEILLLDEPTTFLDLTHQIELMELFTDLHLAGHTLVAVLHDLNQAARY FT ATHLVAMKDGGVVAEGPPAEVLTSDLVEQVFGLRCLVVPDPVAGTPQVVPLGRDRHRNK FT ETPIKEGGTE" FT CDS complement(428629..429708) FT /transl_table=11 FT /locus_tag="AARI_03950" FT /product="iron-siderophore ABC transporter, inner membrane FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, permease (IM), ISVH-family (iron FT siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VSM8" FT /db_xref="InterPro:IPR000522" FT /db_xref="UniProtKB/TrEMBL:E1VSM8" FT /protein_id="CBT74631.1" FT /translation="MKSTIQIPRQIDFGYRNRTIRTQRAVALRFSARSIAINSILAVVA FT VTVAVMSLGIGDYPLTTAQVVQSLFGQGDDFHRLIVTEWRLPIAIAAILFGALLGIGGA FT IFQSLTRNPLGSPDVIGFDAGSYTAVVLTILVIGANQYWYIAAAALVGGLLTAIVVYLL FT SYRGGVQGFRLIIVGIGVSAMLGSINAYLITRAEITDAMSVGFWAAGSLSRVGWHSLVP FT VIIGGLIVFIGVTMLAPALRQLELGDDAALAQGVNASVARPLLLILGVATTALVTAAAG FT PIGFVALSAPQLARRLTRTPGVTVAASAFMGAALLSLAQLLSLVIAQVYRPVPVGLITV FT SLGGLYLIWLLIRETRRSI" FT CDS complement(429705..430670) FT /transl_table=11 FT /locus_tag="AARI_03960" FT /product="putative iron-siderophore ABC transporter, FT substrate-binding protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, binding protein (BP), ISVH- FT family (iron siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VSM9" FT /db_xref="InterPro:IPR000522" FT /db_xref="UniProtKB/TrEMBL:E1VSM9" FT /protein_id="CBT74632.1" FT /translation="MLLALLVVVLAASLSFGANPLPISEIWRVVLSPDSSEASSIVWTL FT RVPRTVVGIAAGVAFGVSGALIQAITRNPLADPGILGVNAGAGFAIVVGVTLFGVGGIT FT GYIWFSFIGAILATVLVYLIGSAGRGASSPVTLVLAGIALAAVLSAFSTFLTLMDQETF FT RSFRAWGLGSLSRASLDDTASVAPFLAVGILLAALISSSLNAVALGDDQATALGASVTR FT TRILGIIAVTLLAGGGTALTGGIAFVGLMVPHIVRWFTGPDQRWIIAYTALAAPSIVLI FT ADVLGRVITRPGEIEAGVLTALIGAPVLIALVRRRKASGL" FT CDS complement(430844..431908) FT /transl_table=11 FT /locus_tag="AARI_03970" FT /product="iron-siderophore ABC transporter, FT substrate-binding protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, binding protein (BP), ISVH- FT family (iron siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VSN0" FT /db_xref="InterPro:IPR002491" FT /db_xref="UniProtKB/TrEMBL:E1VSN0" FT /protein_id="CBT74633.1" FT /translation="MKKTRRSRVIASIGATLATILLIAGCSTSPDSNGSPEEPGASESS FT LLPAAEGKTSYPLTLESPYGETILEERPERIAAIVPNAIDTELLLSLGVTPVLTSNFVS FT EGGYLEEHGSAELDTYEFMMGEDIPIEAIAASNPDLIVTVGWVPGYGELRDYYQQLSKI FT APVVTSPESSQRIIPWQDSIRVLGETLDLSGAAEAVIAEHDERFAQVRADHPEFDGLTA FT TWAIYYGPTNGLQYFSQPGSAPAAFLADLGFSENPNATEFVTDTKVSDELLSKIDADVL FT ILGQSAAASEAEMQELTGRDLFQNLGAVSSGQFVQLPPKTDDGGDLLWAITSGGPIGNA FT WAVERVVPQIADVF" FT CDS complement(431953..433041) FT /transl_table=11 FT /locus_tag="AARI_03980" FT /product="iron-siderophore ABC transporter, FT substrate-binding protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, binding protein (BP), ISVH- FT family (iron siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VSN1" FT /db_xref="InterPro:IPR002491" FT /db_xref="UniProtKB/TrEMBL:E1VSN1" FT /protein_id="CBT74634.1" FT /translation="MSRSKAKHSRILSSICVVFTISLFAAGCSAKPESDAATRPSEQAS FT LLPAAEQTTSYPLTLESPFGETVLPERPERIAAVAPTAIDTELLLALGVTPILTSSLVS FT EGGYLDDHGAAEIETYEFISGEDIPIETIAASDPDLIVAVGWTDGLSGVNLGDYYDRLT FT SIAPVLTSPDTSSQQLIPWQDSLRLLGSTLDLEDAATQVIAHHQEHFAEIRNEHPEFAG FT LTASWVLHFGAANNLRYMSPSGSGTELFLSELGFIPNPKAEQFVGDPWVSNELLTQIDA FT DVLLLGQTVNASDEEMHELVTENDLFMNLGAVMSGHLVQLAPKTEDDRDLLWTVTVGGP FT IGQEWAADYLVPRIADVLTKTS" FT CDS complement(433038..434225) FT /transl_table=11 FT /locus_tag="AARI_03990" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690" FT /db_xref="GOA:E1VSN2" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VSN2" FT /protein_id="CBT74635.1" FT /translation="MSNTLTARRLALCALFLLPGLAMSSWVTRTPAIRDLLGASTAQMG FT LVIFGLALGAMVGILGSGPLLARLGAKPLIAFGTLGVAVSVPLIALGAAAQIDGVVIAA FT LGLFGLSMGGSEIAMNVEGADVEAITGRPFLPALHGSFSLGTLIGAILGIVATAADFSV FT IVHLLTVGLCGVLILIVCIRFLPPATGRRQKPKSPVYRAERAVWRDSSVWFIGVIVLAM FT AFAEGTANDWLPLIMVDGHGLNPTLSSTVFAVFAAAMTLGRFLGGPVVQRFGRAWVLGA FT SALSAVIGISLVAFVDNSLVAGFAVVLWGLGASLGFPVAISSAGASGENPATRVAFVTV FT IGYVAFLVAPPLLGFIGERAGLRGALIIPLLVLFVSIFLSPVARTRPSSIQIGTP" FT CDS complement(434316..435137) FT /transl_table=11 FT /locus_tag="AARI_04000" FT /product="putative siderophore-interacting protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="identified by match to protein family PF04954. Match FT to protein domain PF08021. Possibly involved in removal of FT iron from iron-siderophore complexes" FT /db_xref="GOA:E1VSN3" FT /db_xref="InterPro:IPR007037" FT /db_xref="InterPro:IPR013113" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:E1VSN3" FT /protein_id="CBT74636.1" FT /translation="MSVSARTLRLVPVALRQLVVGRVVDVTTGMKRITLSGGQLGEFTS FT PAGEPQPAFASPGFDDDIRLLFPYPGEIEPVLPVIEDGRVTFAEGRRPLARAYSVRRYD FT SQSRELDVDFVLHGHGVAADWARRTRPGDPIHIAGPGKTQSLPTGRDWFLVAGDDTAIP FT AISRLLEELPHDTRGQVLIDVADDDHRQELIAPEGIEISWIPRHAGTRHPLLNAIQNLR FT WPEGEPFAWLAGEQAEVQKMRRFLVKERAVPKSDIDFTGYWKRGAAGLVGS" FT CDS 435302..436891 FT /transl_table=11 FT /locus_tag="AARI_04010" FT /product="AraC-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein domain PF00165: FT bacterial regulatory helix-turn-helix proteins, AraC FT family" FT /db_xref="GOA:E1VSN4" FT /db_xref="InterPro:IPR003313" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR014710" FT /db_xref="InterPro:IPR018060" FT /db_xref="InterPro:IPR018062" FT /db_xref="UniProtKB/TrEMBL:E1VSN4" FT /protein_id="CBT74637.1" FT /translation="MLFDPPPVPASQTVAVRNTRDPSLLWVHAGTAEVRAAQQQYPLSS FT GQGIWLPAGIPYTLEVGADSVAFPIFPAAGTRAPTLDRPQRIDLPSSWSEWLIYQFARS FT IGYLRGATSDTSLLDLVAGSHYSTPREADRPFEQVPLPPMPRSLEAVTVGRSLLQRPDD FT PADTADHARSVNNSVRTLQLQFLQETGLPFVRWRTAVRVAASAALMDAGHTIGQAGRQV FT GFSTPAGFTRAFHTRTGMTPRQYKQARPAIARRDGNFPGTLGELMLPQLQPQEAPNEAS FT PPPIPAAQTWNRINDFHVLVWVYRGTARVTVGERTRRLRRGDAIWLPAGVRNSVTLSRG FT ALLLPLGSRHGTPETRLPRNLVQRFPDEAELYLLHTFVANYSLVRPRSHDPNGITHSFL FT KHATRTRARAAEDPAGTTPVYKIIRAVRNDPADRRTLTQWAQVLNADARDLGRAFLATT FT GQNYVAWRSEVRMTEARRYLEEGLGVAQVSRKLGYAHPSTFTTVFTRAHDMSPREYQRH FT GWQHTDESLIIR" FT CDS complement(436993..438168) FT /transl_table=11 FT /locus_tag="AARI_04020" FT /product="DNA (cytosine-5-)-methyltransferase-like protein" FT /function="3.2 DNA restriction and modification (and FT repair)" FT /EC_number="2.1.1.37" FT /note="C-5 cytosine-specific DNA methylases are enzymes FT that specifically methylate the C-5 carbon of cytosines in FT DNA. They are found as a component of type II restriction- FT modification systems in prokaryotes and some FT bacteriophages" FT /db_xref="GOA:E1VSN5" FT /db_xref="InterPro:IPR001525" FT /db_xref="UniProtKB/TrEMBL:E1VSN5" FT /protein_id="CBT74638.1" FT /translation="MINPAASTEWLRLELTNHPEPRMHDSTTGRRLRVGSLFSGYGGLD FT LAVEYQFIAETIWFSEINEPVARVFSHHWPDVPNLGDITAIDWTTVPSVDIVCGGFPCQ FT DVSTVGKQAGLAPGTRSGLWANMAAAIEVLQPEWVVIENVRGLLSAPATRPPTQGAPDG FT ERNPFTATLGATTLCEVESDPWGLGDESARSLRALGSVLGDLADLGFNAEWVGLPASLI FT GAPHHRFRIFILAHRQTLPNPAGFGLLSRQRDLGSGESQTRNDCTLTPDHRLRTPRTGW FT LTDQTSRIGHVVDTGRADIRQWGKYAPAITRWKHVTGHDAPAPALLDEFDKPRPAPEFV FT EWLMGLPRGWVTDVGHKLTANEQLMTLGNGVLLLQATTAIAVVRSCTGLGD" FT CDS 438399..441944 FT /transl_table=11 FT /locus_tag="AARI_04030" FT /product="putative conjugal transfer protein" FT /function="3.1 DNA replication" FT /note="match to PF08751: TrwC relaxase. Similar to proteins FT involved in the conjugal tranfer of plasmids" FT /db_xref="InterPro:IPR014862" FT /db_xref="UniProtKB/TrEMBL:E1VSN6" FT /protein_id="CBT74639.1" FT /translation="MTVSMRVMSAGDGYKYLLRTVAAGDGDRSLSTPLTRYYTEKGSPP FT GRWIGQGLVGVGAGQLSTGDQVSEAQLQLLVGMGRDPVTGDPLGRAYQSFTPVTERIEH FT RVSELDASLSPAARAEEVAQFEAEETERGTRRAVAGFDYTFSIPKSASVWWAVADAGTQ FT GLIAQAHHAAIAEVVAFIEREVASTRVGATGPDGAAAQVDVTGVIATAFDHYDSRAGDP FT HLHTHVVISNKVKTAQDGKWRSLDGRPMHAAVVALSELHEAVFADHMTRTFGVEWEARE FT MGRDRNPAWAISAVPETLVSEFSTRSRHIEVEKNRLIEAYVQRQGRQPSTATILKLRAQ FT ATLATRPEKQVRSLSELTTDWRTRATRLLGNDAPLWAQGVAVNPPAMLLRADDVPLDTV FT AEIGQSVVEVVGEKRSTWRRWNLHAEASRQLMGWRFASMLDREAITGLVVDAAENASLR FT LTPPELASSPIVFQRADGTSRFRPKHSTLYSSETLLQAEDRLLTRSRTTTAPTVPLATV FT EQITQRPDADGRMLSDDQSVALAAIAVSGRGIDVLVGAAGAGKTTAMNALRRAWELEHG FT AGSVVGLAPSAVAAQVLADDLGIATENTAKWWHSHLTHGTTFTAGQLVIIDEASLAGTH FT SLDRITGLAETAGAKVLLVGDYAQLQSVDAGGAFALLAGDRDDAPELIDIHRFTHEWEK FT TASLDLRHGRTDIIDTYLDQGRIHDGDEDTMTDAAYAAWREDTAAGLVSVLITETNETV FT TALNNRARADLILDGSLHPSREVELNGGSLAGIGDTIITRRNDRRLRTKDTWVRNGARW FT QITQVRDDGSLTVRAVGRRFGGALVLPATYVADHIDLGYAVTAHRAQGITTDTAHTVVT FT ATTTRENFYVAMTRGRNANHAYVTVNRADDAHSQPHPGDNTDATARSVLYGVMQHVGAE FT LSARETITAEQELWGSIAQLAAEYGTIAQAAQHDRWAALLHASGLTPEQTEDVLTSDAY FT GALSAELRRAEANHHDVDRLLPRLVQARSVEDADDIASVLHARLIKASARPAGSGRTRK FT QPRLIAGLIPHADGTMSPEMRQALNERRELIEQRADALVDQAVDEAADWMQPLLPQGQS FT EDMMAGWRRRARVIAAYRDRHQITAGDPLGPMPERTAQKIDYARAQAAVRQLRPSAEPP FT QHREPRRQVGRSLGL" FT CDS complement(442008..443009) FT /transl_table=11 FT /locus_tag="AARI_04040" FT /product="putative smf family protein" FT /function="3 Information pathways" FT /note="the SMF family (DNA processing chain A, dprA) are a FT group of bacterial proteins. In Helicobacter pylori, dprA FT is required for natural chromosomal and plasmid FT transformation" FT /db_xref="GOA:E1VSN7" FT /db_xref="InterPro:IPR003488" FT /db_xref="UniProtKB/TrEMBL:E1VSN7" FT /protein_id="CBT74640.1" FT /translation="MANLADLATDERTARMALSMIAEPNDSTTGRLLTRVGAVETIRLL FT EADSMVPVLGRVDGTMWRERHGSRVSAESVTERLREVDRLGIGVLIPGDQDWPASVDDL FT GDSAPFVLWTQGAASFLARPPSDLVTVTGARAATSYGEHVVAEIAGDLAQEERVIVAGG FT AYGIEGVAHRAALASGGDTIAVLAGGVDRPYPAGHSELLGRIADTGLVVSEMPPGATPT FT RHRFLARGRLMAALSQTTVLVEAGARSGTLHTALQARLLGRSLGAVPGPVTSAASSGTN FT GLLRDQSARLVTGSGDVRQLLDEHAQSELRQSREFAQTMQTSQAVTSQPPGL" FT CDS complement(443069..443413) FT /transl_table=11 FT /locus_tag="AARI_04050" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSN8" FT /protein_id="CBT74641.1" FT /translation="MFRLLWIASVHTRYFLRRFMPTNILLDLIRSRRGLKWGLPAMLLA FT LPYLYLASLFNLLAMDGGPGWFYLLVLLSYWNTAKFVIMGPISVVLLLRVRAHEWRVRR FT TEPQVLSSVT" FT gene complement(444021..444320) FT /pseudo FT /locus_tag="AARI_04060" FT /product="transcriptional regulator fragment" FT /note="AraC family transcriptional regulator fragment. FT Disrupted by insertion of a IS3 family insertion sequence" FT gene 444417..444743 FT /pseudo FT /locus_tag="AARI_34470" FT /product="partial transposase of IS3 family" FT /function="4.5 Transposon and IS" FT gene 444743..445423 FT /pseudo FT /locus_tag="AARI_34480" FT /product="partial transposase of IS3 family" FT /function="4.5 Transposon and IS" FT CDS 445497..446579 FT /transl_table=11 FT /locus_tag="AARI_04070" FT /product="phage integrase family protein" FT /function="4.4 Phage-related function" FT /note="match to protein family PF00589. Possible phage FT integrase or tyrosine recombinase subunit" FT /db_xref="GOA:E1VSN9" 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:IPR023109" FT /db_xref="UniProtKB/TrEMBL:E1VSN9" FT /protein_id="CBT74642.1" FT /translation="MNTQQELVLLPSHGAWNLHGSAAARFSQANDYLGYLSDRNYSPAT FT TRAYGYDLLAFCRWLHEQNLTIEAVDTNTLINYLKFCKQSSVPGRPGPNVMTLDGQRAD FT GYAPATVNRRMAAVSGLFTFLAMRDPCLPNPMPKGQESRWVSSAQRSGLLGHLATPAAR FT SPLRVREPRRLPRSLESDEVIALFQGLRTYRDRAMAGLMLYCGLRAGEVLALRIRDVDI FT GGRWLLVLGKGSRERRVPLDVDVAGVIQTYLLAERPESDEQRLFLVAKGANRGLPLTAA FT GLRTIFRYHREISGVPDGHPHALRHTFGSALAASGVDLSIMRELLGHAHVNTTARYIHL FT VPAHVKSEYDAAINRQKQSH" FT CDS 446671..448464 FT /transl_table=11 FT /locus_tag="AARI_04080" FT /product="phage integrase family protein" FT /function="4.4 Phage-related function" FT /note="match to protein family PF00589. Possible phage FT integrase or tyrosine recombinase subunit" FT /db_xref="GOA:E1VSP0" FT /db_xref="InterPro:IPR002104" FT /db_xref="InterPro:IPR011010" FT /db_xref="InterPro:IPR013762" FT /db_xref="UniProtKB/TrEMBL:E1VSP0" FT /protein_id="CBT74643.1" FT /translation="MLRYSDPAKWSQEPLERRLEENSSTRAFILYLMVTKRIRGDFPYL FT LERKLANIFVEVQGTDYEDDLRFFSAQARKVGFSERVSAAMTTSVIAKILLRTQQPLTQ FT ITSADLEEFETCCRAREAQTGMSARPLLVLSSSTRQVLFHAHLLANPPLSRTQRVPLKD FT RVGAVNGPFAQFLLRYLERKEVTCTRKTVSSLATRLAHFGQFVTEADPSLASPAELTRR FT SHIEPYLVSLPRSPNTKSSGTLSVAEQSRRVRAAGNFLREITEWGWPEAPPRQLFFRSD FT VPRLPRPLPRHLPPDADRLLAQELLASDYRQAADALLLQRACGLRIGELLDLELDCVHE FT IPEAGTWLKIPLGKMKTERMVPLDPDTLALVDRIIAERSPGQPLAHPRTGKPAQFLFTH FT HGRRLGESAVRLELNRAAQAAGLGKITPHQLRHTYATALINAGVTLQSLMALLGHVSAE FT MSLRYASLFDSTVRTEYERALDLAKSRIGLPDLKEHRSLLPLSDVSVGSWHDTATIKSR FT LAGGHCLRSPAQQACQYANICEHCPSFRTEDSNLPVLEAQRKDALILAQDAKRRGWDSE FT VQRHEALVTQLDLLIERTRTA" FT CDS 448461..448769 FT /transl_table=11 FT /locus_tag="AARI_04090" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="GOA:E1VSP1" FT /db_xref="InterPro:IPR012287" FT /db_xref="UniProtKB/TrEMBL:E1VSP1" FT /protein_id="CBT74644.1" FT /translation="MKRSESQRVVDKALLTLRMQGRTVTFRAVAELAGLSRSTLYRSAG FT LRELIQACREGSARLGGRAILLGSPARVDVFGSGSWNQGKPLLQSDDRACNRECREK" FT gene complement(449044..449601) FT /pseudo FT /locus_tag="AARI_04100" FT /product="transcriptional regulator fragment" FT /note="AraC family transcriptional regulator fragment. FT Disrupted by insertion of a IS3 family insertion sequence" FT CDS complement(449892..450773) FT /transl_table=11 FT /locus_tag="AARI_04110" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSP2" FT /protein_id="CBT74645.1" FT /translation="MITSELLRIRYSLTSKILLTLVLLEALLVGLLLAFLPSLIDGVIA FT LNEVIPNATNADQFSDEQLAALTLASSPFQVLISDVLGNTGIGTSLPVIAATLFGALTI FT TGEFRRGSVTNAALHQPLRAKLILTKATAIAATAFAAAIVLIVVRGGVLAIGLAVQGEP FT LLIEMPELLTVWARGIIALLAYSLLGLGLGLLVRNQVATVSVIFAVIVGESILRPLALL FT IFGGINPTLYLPFGLVPDIIGSNPLAVLGTSASLTASLSSLVALVTLTLWAGAVVGLAV FT FRFARTDIPSST" FT CDS complement(450770..451483) FT /transl_table=11 FT /locus_tag="AARI_04120" FT /product="putative drug resistance ATP-binding protein" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TC 3.A.1.y.z. ABCISSE: ABC transporter, ATP-binding FT protein (ABC), DRI-family, DRB-subfamily (drug resistance, FT putative). Possible function in drug efflux" FT /db_xref="GOA:E1VSP3" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VSP3" FT /protein_id="CBT74646.1" FT /translation="MPLVIENLTKSYGTRKVLDAVSFTATPGRVTGFLGPNGSGKTTTV FT RVALGLANTEAGTALFAGHPFRMLTQPGSSVGVLLENSGLHPGLTPVQHLRIAAAATHT FT HQGRITEVIDEVGLTDAATRKVRGFSQGMRQRLGLALALLANPRLLILDEPANGLDPEG FT MIWLRNLLSEYAKTGATVLVTSHVLNELERFIDDIVIITGGKISAQVTLSDLPTGANLE FT AFYLDTLRHMNQENS" FT CDS complement(451486..452190) FT /transl_table=11 FT /locus_tag="AARI_04130" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="5 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSP4" FT /protein_id="CBT74647.1" FT /translation="MTNHSVRRRDAATSIIPWAGAAVSLGGVLTISAVTMLLPLFGWKA FT ESPQADWAGAFAPSGLMFALALLIVSALICVVPLMVRQFPQLRSPLFYGTATQLRRFLN FT WFLSGLTVFALIAYAGLIGLLEPWGISITGTVFLGLGLLLVAIGIGYPPGGPDYDGPLP FT FTAEVTKEFARSAPLQKYGTSTLGIVLIVTGTWASSFWLFALCVISAVALWLVPWIIAL FT VKVSQSEQENQN" FT CDS 452342..453586 FT /transl_table=11 FT /locus_tag="AARI_04140" FT /product="putative signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions. 6 FT transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VSP5" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR011712" FT /db_xref="UniProtKB/TrEMBL:E1VSP5" FT /protein_id="CBT74648.1" FT /translation="MNSSLPQLTGLDPKPAERSRVLTVTIVGGLSVLVGGFYIWAIQLA FT AQSDAQLVTPQVWAYVVWAAGTVIAAGLLWWHQRYPIIVFAAVFALHLTGAVLLGNGGL FT GGVALPLWFSVYALAAFARPRIALTLVAGAWIIAALVQFLLAAAAGLSLTAPEAVVAAL FT GQGFFFVACFMIGLGMRAQRHRARDAAERAELAEARTRAETAEAISRERNRMARELHDL FT AAHQIMDVLLTTRAALLTDPHPVLESIEHRTAEALDNVRSVVGALREADADTPDQPLAD FT GATHVITQVARERNLHVEHNIQAVHEPPPALIATTLSVLTEALVNAATHAPGMPVTVTL FT HSNIDAVTLHVRNSLAPHAITTESDPPDSGYGLIGAAERAHILNGSVTTGIDTNGDWVL FT SLTLPHLHNAAEVSQ" FT CDS 453583..454257 FT /transl_table=11 FT /locus_tag="AARI_04150" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VSP6" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VSP6" FT /protein_id="CBT74649.1" FT /translation="MITVLIADDQPSVRRALRTFLETQPDIKVISEASSGPEAVTQARI FT RRPDVVLMDVRMPAGDGITATATLAGPDATDPIPVVVITTFDLDEYVFGALENGAIGFL FT LKDAPPTHIIDAVRAAATGEGLVAPAVTRRVISEFARRRAPAARESADADLTPREREVL FT AALAEGSSNAEIAEQLFIEIGTVKTHVSSIILKLGVRDRVQAIVWAYQHHGWQTKLEGE FT DP" FT CDS 454254..454814 FT /transl_table=11 FT /locus_tag="AARI_04160" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSP7" FT /protein_id="CBT74650.1" FT /translation="MTSTPQTQSRPSRTGAIITLVIGAILTITGPIFGVLAGAFSMVPA FT AIEVGDNTAEISPSGIVALDAEASVFLLAPVAELEHLNHDICSVTGPNGEAAPVSFAPA FT SALNTLVNGQRYESFAQVTAATTGPHDITCDTDSIPVVAVPPFTGLFGTFAWWSIGGLA FT VSLIGVVLVIIGIVRVARKPSIQ" FT CDS complement(455296..455838) FT /transl_table=11 FT /locus_tag="AARI_04170" FT /product="conserved hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VSP8" FT /protein_id="CBT74651.1" FT /translation="MSLASDAALSVQLSKLAAAMGAALPAEESDQSPEIFLHSVATFGD FT IARVSALLQAQAVSAAQESGLSWAKIGNALGISRQAAQQRFDSRRADAIQESPAIRIVG FT PVSRDKEIEQINAAGKQNWKLIKSLHGEHVLELDNNNWQVKRVSIFSLRPLPSASEGWV FT PASTRFPDCFYVRKLGS" FT CDS complement(455835..456035) FT /transl_table=11 FT /locus_tag="AARI_04180" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VSP9" FT /protein_id="CBT74652.1" FT /translation="MILLILGIFLVVFAALVGLGLPGFIISVAGWIALIAGLVGFVAML FT IQKSNAASRTNAWRPADKDKQ" FT CDS complement(456087..456707) FT /transl_table=11 FT /locus_tag="AARI_04190" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSQ0" FT /protein_id="CBT74653.1" FT /translation="MAEQQPTPQLKSLVESAQEALTAGSRQPTFELPYAAPDLRPNPAV FT EPFDKVRSYLFGASSVLLLCTSLAFSFGLDGRSRQNLLDPSLVQSILWPAIAIALILSA FT AFSLRRDQRSARRQRKVAIIATAAVALMACAITLASSFLTAGSAVLATISALLALYCVH FT QPPMESAPRGLDLKFTAVPCSTCHKYITQLKRQRILDITVVST" FT CDS complement(456750..457802) FT /transl_table=11 FT /locus_tag="AARI_04200" FT /product="pseudouridylate synthase" FT /function="3.6 RNA modification" FT /EC_number="4.2.1.70" FT /note="identified by match to protein family PF00849. FT Pseudouridylate synthases catalyze the isomerization of FT specific uridines in an RNA molecule to pseudouridines (5- FT ribosyluracil, psi)" FT /db_xref="GOA:E1VSQ1" FT /db_xref="InterPro:IPR006145" FT /db_xref="InterPro:IPR020103" FT /db_xref="UniProtKB/TrEMBL:E1VSQ1" FT /protein_id="CBT74654.1" FT /translation="MAMQSPLPVRNGVNATRLRLPRTGSWATVAEYLLERFGHVDPEGI FT LRRFDDQQIVGLGGVPLTRQTPLGEHEFIWYYRSLPVETPIPFEARILHQDEHLLVVDK FT PHFLPTTPGGRFIQESALVRLRNQTGIDDLVPMHRLDRATAGVILFAVNPQTRGDYQML FT FERREIAKRYKAVVALQPGEGLETGRVLQPNGEHSQVKSQSELRELLAGMPLAFENRMT FT KVKGQLRSVVEDGHPNAQTLINVEAIGTSSGFHAGLEVALMDLEPRSGKTHQLRVHLAS FT LGLGIINDAFYPRLWDLAPDDYQRPLQLLAHTISFTDPLTGIERSFSSEQQLLESPQLS FT SALLNGGELP" FT CDS 457863..458699 FT /transl_table=11 FT /locus_tag="AARI_04210" FT /product="PhzC/PhzF phenazine biosynthesis family protein" FT /function="4.6 Miscellaneous" FT /note="identified by match to protein family PF02567. FT PhzC/PhzF is involved in dimerisation of two 2, FT 3-dihydro-3- oxo-anthranilic acid molecules to create FT phenazine-1- carboxylic acid (PCA) by P. fluorescens. This FT family also contains a putative thymidilate synthase from FT Mycobacterium tuberculosis. Many phenazine compounds are FT found in nature and are produced by bacteria such as FT Pseudomonas spp., Streptomyces spp., and Pantoea FT agglomerans. These compounds have been implicated in the FT virulence and competitive fitness of producing organisms. FT For example, the phenazine pyocyanin produced by FT Pseudomonas aeruginosa contributes to its ability to FT colonise the lungs of cystic fibrosis patients. Similarly, FT phenazine-1-carboxylic acid, produced by a number of FT Pseudomonas, increases survival in soil environments and FT has been shown to be essential for the biological control FT activity of certain strains" FT /db_xref="GOA:E1VSQ2" FT /db_xref="InterPro:IPR003719" FT /db_xref="UniProtKB/TrEMBL:E1VSQ2" FT /protein_id="CBT74655.1" FT /translation="MVLRNYSEVDVFSPTAYRGNPLAVVHDAQGLTSEQMQGFAKWTNL FT AETTFLVQPENPAADYRVRIFSATQEFPFAGHPTLGSAFAWLKAGGVTKDPGRIIQECG FT AGLVEVRVEQQRLWFAAPRLTRYEPVAESLVQRIAEILGVSRERIQDTSWLVNGPEWIG FT VRLASAQQVLELAPDPNALGELSIGVAGPHQPGAETQFEVRAFVGGDPVWEDPVTGSLN FT AGLARWLTDSGMAPERYVAAQGTAIGYQGRVHIRVENGGIWVGGDVSSCVQGEVDL" FT CDS complement(458721..459545) FT /transl_table=11 FT /gene="nei" FT /locus_tag="AARI_04220" FT /product="DNA glycosylase" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.2.2.-" FT /note="involved in base excision repair of DNA damaged by FT oxidation or by mutagenic agents. Acts as DNA glycosylase FT that recognizes and removes damaged bases" FT /db_xref="GOA:E1VSQ3" FT /db_xref="InterPro:IPR000214" FT /db_xref="InterPro:IPR010979" FT /db_xref="InterPro:IPR012319" FT /db_xref="InterPro:IPR015886" FT /db_xref="UniProtKB/TrEMBL:E1VSQ3" FT /protein_id="CBT74656.1" FT /translation="MPEGDSVYRATARLHQALAGEVLLASDLRVPALATVDVAGYEVRE FT VIPRGKHLLMRLQPPARANPDFAQPALTLHSHLLMEGRWDLYAPGERWKRPAHTARVVL FT QTARITAVGFDIAQVKLLPTEQEADVVGHLGPDLLGVDWDAQVALENLRAEPQLGIGQA FT LLDQRIMAGVGNVYRSEILFLSRVHPLTAVREVQNLPALIDLAHRLLVVNKDRPRRVTT FT GQPGTRDPLWVYGRAAKPCLRCGTRIELLRIASTPTGIERDCYLCPSCQPAG" FT CDS complement(459570..464234) FT /transl_table=11 FT /locus_tag="AARI_04230" FT /product="putative ATP-dependent DNA helicase" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.6.1.-" FT /note="may be involved in DNA repair" FT /db_xref="GOA:E1VSQ4" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR013701" FT /db_xref="InterPro:IPR014001" FT /db_xref="UniProtKB/TrEMBL:E1VSQ4" FT /protein_id="CBT74657.1" FT /translation="MSDVLSRFGAATRKWFTDVFSAPTVAQSGAWESISDGKHTLVIAP FT TGSGKTLAAFLWALDRLHHAELDAPTLPGMDSDADHPTGNGTKVLYISPLKALGVDVER FT NLRSPLAGIRATAHEMGLSQPSVSVGVRSGDTPANDRRKLLKDPPEILITTPESLYLML FT TSQARKTLAEVHTVIIDEVHAIASTKRGTHLALSLERLDALLPAPAQRIGLSATVEPPE FT EVARFLAGSAPVNIVRPPSTKKWELAVRVPVEDMTDLPSAAGAHDLGPGSSPTASASIW FT PHVENQLVDLVLDNHSTIIFANSRRLAERLTGRLNEIYAEREGFSAENASTSTPAALMA FT QAGSTAAAHPEAPLLARAHHGSVSKDSRAQIEEDLKLGKLRAVVATSSLELGIDMGLVD FT LVIQVESPNSVSSGLQRVGRAGHQVGSVSQGIFFPKHRADLLSTALVVTRMRQGAIEKM FT VIPANPLDVLAQQTLAAVAMDDLDVEQWFDTVRRSAPYQQLPRSAYLATLDMLSGKYPS FT DEFATLKPRLIWDRDAGTLSARPGAQRLAVISGGTIPDRGLFGVFLAGSEDDKAPKRVG FT ELDEEMVYESRVGDIFALGATSWRIEDITHDRVLVTPAFGQPGKLPFWHGDGLGRPVEL FT GAALGEFTTSLLASERAEAAEVLHGSGLDPFAANNLLNYLDEQRRATGQVPNHQNFVIE FT RFHDELGDWRVILHSPFGLAVHAPWALAVGARVRERWGLDASAMAADDGIVLRIPAMDD FT EPPGADLFAFEADEIIEVVTSQVANSALFASRFRECAARALLLPRINPTKRTPLWQQRQ FT RASQLLDVARNYPDFPIILETVRECLNDVYDLPALSRILSSISSRAIRLVEVTTELPSP FT FAQSLLFGYVAQFLYESDAPLAERRAAALSLDPVLLGELLGRNDVREVLDPKVIATLQE FT QLQHLAPNRRLAGMEGCADLLRLLGPLSAEQLAQRLRDPADEETALDIDSARAHAEALV FT STRRAFTLRQSGELAYAAIEDAGKLRDALGTPLPTGIPAAFLEPAASPIQDLASRFART FT HGPFTIGEMAAQLGLGVAVLRPVLDQLVAAGRLSLGAFRPLEIVPAGVSGDEYCDVQVL FT RTIRTRSLAALRAEVEPVDQDTYGRFLPAWQQIGSSLQGADGAYEIVAQLAGAEVPASA FT LESFVLPARMKGYQNSWLDELCSSGDILICGAGAAGGKDGWLSLHTAEHAALSLPQPDA FT STLQALDLRVLQAFESTGAYFAEELAGRIHRSDEPAASSHEVAESCWRLFWAGYISPDT FT MAPIRGYLAGGSTAHKIAKPAPRARAARLNRLSGLNRLAREQAGGPARGSRGAARWSLL FT PAPVADPTISAHATAEIMLERYGVLTRGSVAAESVPGGFGQLYRVLSKLEEAGHARRGY FT FVEKLGAAQFSTSTTIDRLRGFQLADDPRRQPVATVLASTDPANPYGAALAWPATETGH FT RPGRKAGAIVGLLDGALSLYLERGGRTVLTFGELSEPAWNIIAMQLVATLRTAQVDKIA FT IATVDGQPVQDHPVGIALQGAGFYSTPQGIRFRR" FT CDS complement(464274..464576) FT /transl_table=11 FT /locus_tag="AARI_04240" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domain IPR011991: winged helix FT repressor DNA-binding" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VSQ5" FT /protein_id="CBT74658.1" FT /translation="MNKPSSNAQFDELIHAPIRLRICASLAPVQWAEFAHLRGILDVAD FT SVLSKHLKQLADAGYIGIERFTKLGRSHMRVSLTKSGRQAYVSHVAALREITAGG" FT CDS complement(464560..465021) FT /transl_table=11 FT /locus_tag="AARI_04250" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSQ6" FT /protein_id="CBT74659.1" FT /translation="MNNSQIPSEREAASQLAAAEEAASGTVSATEAPGAFMIVLGLVTA FT AIFSLYGVIDIALWYWSPVLFVPLIAWYAYWSRQRPKRRPALRHSGKYIAVMLFMMLAL FT QLCTFWIPQTWLFAIPKFLALAAVFTGSLWIMRRETIKSRIKDGNEQAI" FT CDS complement(465026..465490) FT /transl_table=11 FT /locus_tag="AARI_04260" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSQ7" FT /protein_id="CBT74660.1" FT /translation="MADGQERIDKLTAAERLASADQASNKMVAAGTSSRATLFVYVVLG FT SIAMSLEHVLSPKMALGLFAVAVVAALVHYMIMRSRATMRPLLSSSATYGWYAFLASMI FT VMCLRFWVAEDPWSIGAKLVVSCTALWHLLSAAQTAWDKDRVQDAQEMAG" FT CDS complement(465554..466012) FT /transl_table=11 FT /locus_tag="AARI_04270" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VSQ8" FT /db_xref="InterPro:IPR003742" FT /db_xref="UniProtKB/TrEMBL:E1VSQ8" FT /protein_id="CBT74661.1" FT /translation="MTIKVLAVGKKHESWVDEGISRYEKRLKKPFNLTWQLLNHSSREN FT DAARTEESARILAKIDDRDFVVLLDERGKNVDSPALANTLRTPIDASRNVVIIIGGAYG FT VDASVHARANFIWSLSKLVFPHQLVRLILTEQLYRAQDILAGGKYHHV" FT CDS 466076..466789 FT /transl_table=11 FT /locus_tag="AARI_04280" FT /product="PAP2 family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF01569. This family FT includes the enzyme type 2 phosphatidic acid phosphatase FT (PAP2), Glucose-6-phosphatase (EC 3.1.3.9), FT Phosphatidylglycerophosphatase B (EC:3.1.3.27) and FT bacterial acid phosphatase (EC:3.1.3.2). The family also FT includes a variety of haloperoxidases that function by FT oxidising halides in the presence of hydrogen peroxide to FT form the corresponding hypohalous acids" FT /db_xref="GOA:E1VSQ9" FT /db_xref="InterPro:IPR000326" FT /db_xref="InterPro:IPR016118" FT /db_xref="UniProtKB/TrEMBL:E1VSQ9" FT /protein_id="CBT74662.1" FT /translation="MRSSWYFRQGGRSRGTQALWMVFGLIVAMFYFTRRVLVSLHAGGW FT ARDLDEPVYRWIAENQSPFLFSASDFLYFWGSTPGMIMIMLVIIALLSWKTRSFWPLAT FT VAFTALVSVLLTVILKTSLQMPRPQGVPGGPAPPQTFSFPSGHTLNSAALIGISCYLAI FT VYGLRRYAYLISIVAALFVLAMGASRIYIGHHWVSDVLVGLLIGAAWAAVVAILHYYFV FT PRPRVTSSVRGSVRR" FT CDS complement(466758..467729) FT /transl_table=11 FT /locus_tag="AARI_04290" FT /product="D-isomer specific 2-hydroxyacid dehydrogenase FT family protein" FT /function="2 Intermediary metabolism" FT /EC_number="1.1.1.-" FT /db_xref="GOA:E1VSR0" FT /db_xref="InterPro:IPR006139" FT /db_xref="InterPro:IPR006140" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VSR0" FT /protein_id="CBT74663.1" FT /translation="MRIAILDDYHNVARSLADFDGLAVALDAEVTVFTEHLGHEDSTVV FT QALQPFDAIVAMRERTPFPAARLAALPNLKLLVTTGRRNGSIDLQAAKNQGIVVSHTGY FT VATDAAEHTWALILSAARRLDVELFSADRPLAAGTGWQTTFGLGLSGKTLGVYGLGNLG FT AKVAKVGLAFGMRVIAYSQNLTKARATEVGVELVSEAELFSTSDIVTVHLKLSERSTGV FT IGPKQLAWMRPDSILVNTSRSRIVQTDALIDALDSRQLHLAAVDVFDVEPLPAKDRLAA FT TRGVIATPHIGYVTIEQFEMFYRDAVEDIRAWASGAPIRVLS" FT CDS complement(467826..469673) FT /transl_table=11 FT /locus_tag="AARI_04300" FT /product="metallophosphoesterase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00149. The metallophosphoesterase motif FT is found in a large number of proteins invoved in FT phosphorylation. These include serine/threonine FT phosphatases, DNA polymerase, exonucleases, and other FT phosphatases" FT /db_xref="GOA:E1VSR1" FT /db_xref="InterPro:IPR004843" FT /db_xref="UniProtKB/TrEMBL:E1VSR1" FT /protein_id="CBT74664.1" FT /translation="MKIFARPGKTNHLTPLHLTAGSLVAIAASTAFIGATPELEAVPAA FT KSAADWSSSTYRGSVEVIPAGTGRSGTAQETLDGVVFEDRNKNSTQDANEPGLPNVTVS FT NGRDVVATDGQGRYELPAYNNMTAFLTQPRGFQVPVDDDHVAQFFYTHLPEGSPDLKYD FT GIAPTGPLPEAVNFPLVASSATQSPEQSCVIGADVQTYTQQEVEYAREGAFADLAARTD FT YTGCGALFIGDLVGDDLTFFHQTRELASMLNGPARFLPGNHDIDYDSLDGQHEFDSFRA FT QFGPEYYSYDTGKTHVIALSTIEYPTAVPAKKSDYTYGLGKRQLQWLRADLAEVPKNKA FT IVLAGHSPLLEFFYSDEHSTKQLKEIYKLLDGREVIALGGHTHMSENLRAGDLMDGWRE FT KVGEEGLPFTHLTVPAISGQWYDGRVTENGYPTSIQRDGTPPGVLTLDIKNTKITESFT FT VTGGDSSKQMSLGLNTPAYRQWYEENLEKERGTVPALDDPLAVSRQGLAEDTWLTTNFW FT MGSTGSAVEVSIDGQDPVAAERTQKMAGERPLSGAEYSDPAAIAEQFVHGGGFAEKTSH FT LWRLELPDDLSVGAHTATVTATDVHGRSFTEELDFTVIG" FT CDS 469854..470981 FT /transl_table=11 FT /locus_tag="AARI_04310" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSR2" FT /protein_id="CBT74665.1" FT /translation="MELVQALMAGARGRRMLWEFATASEEKLLPAFGEHPLHAAMFYAA FT YHVAVERGESVGLFGADESSMPETSVQQIARRLDSTTLVPATAALLQQALVRSVDSARY FT WQEPDGEDTLLALPELAAPLERVARHLADSGLAAGWMDPVDLRNQFQVEFDQHDPQGRT FT QAPGSNALGLLQEWRAGILATEARDAAEMSSTPLGSFSGEWWSKPSSRLPSTTGVFPDR FT EPVGLSCVEDGFGWEQASVRFTSVPPAAKVLEIATAEDWIRLCREHGIEVTAHKRHDWY FT LSTGRDGAWKIPDWLAVARDYDGVHLGIGAYLALAGQCLDIDEEYASVIAGWDPDQTFW FT FTDELRCYGPAREWICKDANNEDARWLPAGNDPSS" FT CDS 471031..471462 FT /transl_table=11 FT /locus_tag="AARI_04320" FT /product="thioesterase family domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF03061: thioesterase FT superfamily" FT /db_xref="InterPro:IPR006683" FT /db_xref="UniProtKB/TrEMBL:E1VSR3" FT /protein_id="CBT74666.1" FT /translation="MSETTNDELAAATEVILQLRWSDQDALGHVNNARIVTLMEEARIR FT WTREDGTTGRFEFGTVVASIQIDYLRPLYYQPEMLIRMGISRLGNKSFTVRGIGYQDGQ FT PVFDSTTVMVPLAADGISSRPLNELERSWLGKSLIPARS" FT gene complement(471459..471782) FT /pseudo FT /locus_tag="AARI_04330" FT /product="truncated transcriptional regulator" FT /note="C-terminal section of a transcriptional regulator" FT gene complement(471810..472310) FT /pseudo FT /locus_tag="AARI_04340" FT /product="truncated transcriptional regulator" FT /note="N-terminal section of a transcriptional regulator" FT CDS 472554..473849 FT /transl_table=11 FT /locus_tag="AARI_04350" FT /product="putative benzoate permease" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="benzoate:H+ symporter (BenE) family, benzoate FT permease (TC 2.A.46.1.1). Identified by match to protein FT family PF03594" FT /db_xref="GOA:E1VSR4" FT /db_xref="InterPro:IPR004711" FT /db_xref="UniProtKB/TrEMBL:E1VSR4" FT /protein_id="CBT74667.1" FT /translation="MPKPADNLPTRESTPAAAGAPREPLLERAVQRPAGIRALLRDLGG FT TYASNGVIGLVFSASGPIAVTLAVGVAGGLSQAEMASWVCGIFLSAGLATIVMSLLYRQ FT PLGFAWSIPGTVLLGPSLQHLSFPEVVGAFFVSGVLVLALGATGVVRRIMAAIPMPIVM FT AMVAAVFLRFGTDIVSSTQANPVVAGPMVLVFVLLAAVPALGRRLPPVLGTLIAGVIAV FT AASGQFALDAAGGPVLATPVFTAPEFTWAAQLELVVPLAITVLIVQNGQGVAVLRSAGH FT RPPVNAFALASGGFSILNACFGAVSACVTGPTNALLTSSGEKHRQYTAAVVYGLLSLLF FT ALFAPTLTRFMLATPEAFVLALGGIAMLKALQQAFVTAFATKFTLGALVTFVVTISGLD FT LFNIHAAFWGILFGYAASRLMERTDHATVSGP" FT CDS 473971..474762 FT /transl_table=11 FT /locus_tag="AARI_04360" FT /product="putative aspartate dehydrogenase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="1.4.1.21" FT /note="catalyzes the first step in NAD biosynthesis from FT aspartate. Specifically catalyzes the NAD or NADP- FT dependent dehydrogenation of L-aspartate to iminoaspartate" FT /db_xref="GOA:E1VSR5" FT /db_xref="InterPro:IPR002811" FT /db_xref="InterPro:IPR005106" FT /db_xref="InterPro:IPR011182" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VSR5" FT /protein_id="CBT74668.1" FT /translation="MATGSMYRVGVLGHGAIGSVVAEQLAAGTVHGAQLEGVILRRPQA FT GLEHEQLSWEAALERCDLVVECAGQQALRENAVCILASGVDLLASSMGALADPEFAAQV FT QAAGPGRLSSTAGAIGGLDLLGAAARMGGIDQVLVTTRKLPAILVQPWMDAQLRGELEQ FT AAGPVEVFRGPAAAAAQDFPKSLNVAAAVALAVGDWDAVTARLIADPEAGLTEHRIEAR FT GPAGEYSFSIKNHPSPRNPRTSGIVPWALLHSIRQAAAARR" FT CDS complement(474779..475186) FT /transl_table=11 FT /gene="pcaC" FT /locus_tag="AARI_04370" FT /product="4-carboxymuconolactone decarboxylase" FT /function="4.2 Detoxification" FT /EC_number="4.1.1.44" FT /note="involved in protocatechuate catabolism" FT /db_xref="GOA:E1VSR6" FT /db_xref="InterPro:IPR003779" FT /db_xref="InterPro:IPR012788" FT /db_xref="UniProtKB/TrEMBL:E1VSR6" FT /protein_id="CBT74669.1" FT /translation="MADSPRLPGDTYDAGMEVRRQVLGNEHVERSTRNSNEFTDEFQEM FT ITRYAWGTIWTRDGLPHTTRSAITLTAMIAGGYWEELEMHVHAALRNGMTPEEIKEVFL FT QCAIYCSVPAANVAFKIGKKVLEEYAAAEGD" FT CDS complement(475205..475975) FT /transl_table=11 FT /gene="pcaD" FT /locus_tag="AARI_04380" FT /product="putative 3-oxoadipate enol-lactonase" FT /function="4.2 Detoxification" FT /EC_number="3.1.1.24" FT /note="3-oxoadipate enol-lactonase catalyses the formation FT of 3-oxoadipate from 3-oxoadipate enol-lactone. It is FT involved in aromatic acids catabolism" FT /db_xref="GOA:E1VSR7" FT /db_xref="InterPro:IPR000073" FT /db_xref="UniProtKB/TrEMBL:E1VSR7" FT /protein_id="CBT74670.1" FT /translation="MLHTDKALPTLIVGPSLGTAALPLWAPALPYLKDKFQVIAWDLPG FT HGESKPSTEAFSLAELATGVTKAVEALRADGVISEGSKLYYAGVSVGGATALQLAVDHT FT GFFNALSSICSAAKIGTPEGWTDRAELVAKAGTPTMVAGSAERWFAPGFIEKEPVISTE FT LLHSLQDADRFAYAHACGALAGFDVRGQLASTSDPIIAINGAQDQVCPPADAEFIAENA FT PRGTMAVIDSASHLAPAEAPEETAALLAEFLLSN" FT CDS complement(475984..477390) FT /transl_table=11 FT /gene="pcaB" FT /locus_tag="AARI_04390" FT /product="3-carboxy-cis,cis-muconate cycloisomerase" FT /function="4.2 Detoxification" FT /EC_number="5.5.1.2" FT /note="catalyses the cyclization of 3-carboxy-cis,cis- FT muconate to 4-carboxy-muconolactone. Involved in aromatic FT acids catabolism" FT /db_xref="GOA:E1VSR8" FT /db_xref="InterPro:IPR000362" FT /db_xref="InterPro:IPR008948" FT /db_xref="InterPro:IPR019468" FT /db_xref="InterPro:IPR020557" FT /db_xref="InterPro:IPR022761" FT /db_xref="InterPro:IPR024083" FT /db_xref="UniProtKB/TrEMBL:E1VSR8" FT /protein_id="CBT74671.1" FT /translation="MDGADYGVLAPAWAGTAAAALASDASFVQAMLDAEAGWVQVQADA FT DLCSVQDAQAVREVASVDRYDLALLASRTPDGANALIPLLGMMRDLLKHDGAAATAGTA FT LHRGATSQDIIDTALMLVLSKTLTLTLADLRSTAGGLSALAQAHRGTVCIARSLTQHAL FT PTTLGWKAASWLSAVLDAEHQLDAAARQLRLQWGGAVGTLASLEQLLSGQPETTATSQS FT LSSDLAALLGLEDPGTPWHTNRMPILQLGSALGAAIAALGTLGADVLTASRPEIGELSE FT PREAGKGGSSAMPQKQNPVRSVLLRNAAFSAPGLLSTLFTAAGTAVDERPDGGWHAEWS FT ALRELARLAAGAAQHGAFLANGLSVNHQAIERNLALGGDAVLSERVATVLAPLVVGGKP FT AIQALVRRSLDEGISLRDLLRLEISVHDLGDQHLYELFDPAGYLGAADRFTETVLADYS FT ARKESWQSRN" FT CDS complement(477536..478114) FT /transl_table=11 FT /gene="pcaG" FT /locus_tag="AARI_04400" FT /product="protocatechuate 3,4-dioxygenase subunit alpha" FT /function="4.2 Detoxification" FT /EC_number="1.13.11.3" FT /note="catalyses the following reaction: 3,4- FT dihydroxybenzoate + O(2) <=> 3-carboxy-cis,cis-muconate" FT /db_xref="GOA:E1VSR9" FT /db_xref="InterPro:IPR000627" FT /db_xref="InterPro:IPR012786" FT /db_xref="InterPro:IPR015889" FT /db_xref="UniProtKB/TrEMBL:E1VSR9" FT /protein_id="CBT74672.1" FT /translation="MAQAPELKLTPTPGQTIGPFYGYALPFEKDNELVNQAHPNSVRLH FT GVVCDGNGEIIPDALLEIWQADEHGNVVSREGSLVRDGYTFTGWGRVAVDNAGHYTFTT FT VNPGATEEGKAPFIMLAVFARGLLNRLFTRIYLPEDTEALASDPLLSSLGEAERATLIA FT AREDDGSLRFDIRLQGGNETVFLSYPRES" FT CDS complement(478116..478964) FT /transl_table=11 FT /gene="pcaH" FT /locus_tag="AARI_04410" FT /product="protocatechuate 3,4-dioxygenase subunit beta" FT /function="4.2 Detoxification" FT /EC_number="1.13.11.3" FT /note="catalyses the following reaction: 3,4- FT dihydroxybenzoate + O(2) <=> 3-carboxy-cis,cis-muconate" FT /db_xref="GOA:E1VSS0" FT /db_xref="InterPro:IPR000627" FT /db_xref="InterPro:IPR012785" FT /db_xref="InterPro:IPR015889" FT /db_xref="InterPro:IPR024756" FT /db_xref="UniProtKB/TrEMBL:E1VSS0" FT /protein_id="CBT74673.1" FT /translation="MSTETTQKDGTGAESFENSHALDPAATTASQEEISGEITGIHEAY FT RQEVLAGKKAEIQPRVDFAPYRSSLLRHPTKNLHHVDPETIELHSPAFGQRDVHALESD FT LTIQHNGEPIGERIVVAGRVLDGDGRPVAGQLVEIWQANAAGRYIHKRDQHPAPIDPNF FT TGVGRAITGPNGEYSFTTIKPAPYPWKNHHNAWRPAHIHFSLFGTDFTQRMITQMYFPG FT DPLFALDPIYQSITDADARDRLVATYDHSITSHEWATGYNWDIVLTGSNRTWMEDEEGD FT H" FT CDS complement(479005..480201) FT /transl_table=11 FT /gene="pobA" FT /locus_tag="AARI_04420" FT /product="4-hydroxybenzoate 3-monooxygenase" FT /function="4.2 Detoxification" FT /EC_number="1.14.13.2" FT /note="catalyses the following reaction: 4-hydroxybenzoate FT + NADPH + O(2) <=> protocatechuate + NADP(+) + H(2)O" FT /db_xref="GOA:E1VSS1" FT /db_xref="InterPro:IPR002938" FT /db_xref="InterPro:IPR003042" FT /db_xref="UniProtKB/TrEMBL:E1VSS1" FT /protein_id="CBT74674.1" FT /translation="MVQNPRILKTKVGIIGGGPAGLMLSHLLAKTGIENIVVEMRDHEA FT IRNTHRAGILEAQAVKMLTESGVDGRVLTHGDEHAGIDLRFNGESHPLDFRDLVDATVT FT LYAQNEVFVDLAAARQRDQGDVRYSCEVTEILDMETSTPKFRFTDAQGNLFEVHADVIV FT GADGSRSFARRQMPETLRKDFKVAYPFAWFGILTEAPKSAPELIYANSPHGFALISQRS FT ETVQRMYFQCDPNEDVNAWSDDRIWAELQKRVDGPDNFQLKTGEIFDKTVLSFRSFVRE FT PLSHGRLFLIGDAGHTVPPTGAKGLNLAFADVKVLFEALDSYFSTGSEQLLDGYSDLAL FT KRVWKAQNFSYWMTSMLHTPVGGDPFMAKRALGELETVTSSRFGQQYLAESYTGWPHS" FT CDS complement(480419..481165) FT /transl_table=11 FT /locus_tag="AARI_04430" FT /product="IclR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF09339: IclR helix-turn- FT helix domain. This family of bacterial transcriptional FT regulators groups several proteins, including gylR, a FT possible activator protein for the gylABX glycerol operon FT in Streptomyces, and iclR, the repressor of the acetate FT operon (also known as glyoxylate bypass operon) in FT Escherichia coli and Salmonella typhimurium" FT /db_xref="GOA:E1VSS2" FT /db_xref="InterPro:IPR005471" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014757" FT /db_xref="UniProtKB/TrEMBL:E1VSS2" FT /protein_id="CBT74675.1" FT /translation="MANSPSGDSMLDRLVRILSSFDLNNQSLSVSSLARRADIPKATMY FT RLLDELVSHDLLARDGSGQVRLGLRLWELANRSAATQDLRTAALPFMEDINQLLGQNTQ FT LSVLHQDEVLIIERLSRPGSVVNQANVAGRMPVHRTSMGMALLAFSRPETIHGFLERHH FT ELMTDAHPELRAEMAEIRRNGFASFDGFIDPETTGAAAPILDEAGYQVAVISVVVPRDS FT GTLQSAALALRTAARGIARALRLDNI" FT CDS 481414..482082 FT /transl_table=11 FT /locus_tag="AARI_04440" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.321 FT between position 26 and 27" FT /db_xref="UniProtKB/TrEMBL:E1VSS3" FT /protein_id="CBT74676.1" FT /translation="MVRNHQVKIAALMAALTLAASGCVSASQGGAGDPSAGTVSPTPSS FT PEQDAKVPQRPAVLSEKTEEGLQGAMEYWVQLLNYSVASGDTAALKGFSAAHCTLCQEL FT IAQTDQAYANGGSIDEGEFRVIETMSTLDKYQASPGEPKVVFASFGIERAAGQVLGADG FT KVTSEIEPVSCMDFEENWDEIAYDEDGNFIGSICSLAVQDPAFDESSGWQPLNVAINAQ FT " FT CDS 482258..483469 FT /transl_table=11 FT /locus_tag="AARI_04450" FT /product="acetyl-CoA C-acyltransferase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.3.1.16" FT /note="acetyl-CoA C-acyltransferase (also named 3-ketoacyl- FT CoA thiolase or thiolase I) has a broad chain-length FT specificity for its substrates and is involved in FT degradative pathways such as fatty acid beta-oxidation" FT /db_xref="GOA:E1VSS4" 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:E1VSS4" FT /protein_id="CBT74677.1" FT /translation="MQQAYLYDAIRTPFGKIGGALSSHRPDDLAAHVVRELVARSPKLD FT VADIDESIFGNANGAGEENRNVARMATLLAGLPTSLPGTTMNRLCGSSLDASIAASRQI FT ATGDADLVLVGGVESMSRAPWVLPKTERPFPMSNLELANTTLGWRLVNPAMPGEWTVSL FT GEATEQLREKHGISREDQDEFSAASHQRAAAAWQAGKYDNLVVPVPPANKRGTEVTRDE FT TIRADSTAQTLSKLRTVFRTGENATVTAGNASPMSDGASAAFIGSERGGELLGAAPIAR FT IASNGAAALDPQFFGFAPVEAANKALAKAGLKWSDIAAVELNEAFAAQSLACIRAWDID FT PAIVNAWGGAISIGHPLGASGLRILGTVARRLAESGERYGLAAICIGVGQGLAVVVENI FT NATK" FT CDS 483489..484160 FT /transl_table=11 FT /gene="pcaI" FT /locus_tag="AARI_04460" FT /product="3-oxoadipate CoA-transferase subunit A" FT /function="4.2 Detoxification" FT /EC_number="2.8.3.6" FT /note="identified by similarity to protein SP:Q01103 FT (Pseudomonas putida). Catalyses the following reaction : FT succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA" FT /db_xref="GOA:E1VSS5" FT /db_xref="InterPro:IPR004163" FT /db_xref="InterPro:IPR004165" FT /db_xref="InterPro:IPR012792" FT /db_xref="UniProtKB/TrEMBL:E1VSS5" FT /protein_id="CBT74678.1" FT /translation="MAPRIATSAADAVAEITDGATVLIGGFGNAGQPMELIDALMDCGA FT KDLTVVNNNAGQADAGLALLIKERRVKKIICSFPRQSDSWHFDEAYRAGEIELELVPQG FT NLAERIRAAGTGIGGFFTPTGYGTLLAEGKETRVIDGKGYVLETPIHADFALIKALKAD FT TLGNLVYRKTARNFGPIMATAAKAAIVQVDEVVQPGAIDPENVITPGIFVDTVVELGGQ FT K" FT CDS 484160..484807 FT /transl_table=11 FT /gene="pcaJ" FT /locus_tag="AARI_04470" FT /product="3-oxoadipate CoA-transferase subunit B" FT /function="4.2 Detoxification" FT /EC_number="2.8.3.6" FT /note="identified by similarity to protein SP: P0A102 FT (Pseudomonas putida). Catalyses the following reaction : FT succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA" FT /db_xref="GOA:E1VSS6" FT /db_xref="InterPro:IPR004165" FT /db_xref="InterPro:IPR012791" FT /db_xref="UniProtKB/TrEMBL:E1VSS6" FT /protein_id="CBT74679.1" FT /translation="MTTTEAKLTRDEMAQLVAADIPAGAFVNLGIGQPTNVSNYLTKEQ FT GVTLHTENGMLGMGPVATGEDIDPDLINAGKIPVTQLPGASFFHHADSFAMMRGGHLDV FT CVLGAFQISKDGDLANWHTGAERAIPAVGGAMDLAIGAKATWVMMSLFTKAGESKLVET FT LSYPVTGLGCVSRIYTEVAVFELRDAKVFVRSTHGISFEELAAKVPVELTQA" FT CDS 484829..485671 FT /transl_table=11 FT /locus_tag="AARI_04480" FT /product="IclR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF09339: IclR helix-turn- FT helix domain. This family of bacterial transcriptional FT regulators groups several proteins, including gylR, a FT possible activator protein for the gylABX glycerol operon FT in Streptomyces, and iclR, the repressor of the acetate FT operon (also known as glyoxylate bypass operon) in FT Escherichia coli and Salmonella typhimurium" FT /db_xref="GOA:E1VSS7" FT /db_xref="InterPro:IPR005471" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR012794" FT /db_xref="InterPro:IPR014757" FT /db_xref="UniProtKB/TrEMBL:E1VSS7" FT /protein_id="CBT74680.1" FT /translation="MRIRVPEVHPRNHFQRARSTVSEQAATTTSVQSLARGLAVISSFD FT ADHASMTLSEVAGRTALSRATARRFLLTLVELGYVRTDGKHFELTSKVLQLGYSYLSSA FT TLPQLIEPVLEELSAAVHESASASILDGSQIVYIARVHTRSIMRVGISVGTRFPAANTS FT MGRVLLAYQPEEISEAVIAAGVHSMTGLGIDDPDQLRVELQRIRTQGYAVVDQELEIGL FT RSVAVPVFSADGTVVAAMNVSMSVRPDTTQSAEQAAEVVLPQLLEAAAQVREALAASR" FT CDS complement(485760..486152) FT /transl_table=11 FT /locus_tag="AARI_04490" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain IPR011588: FT glyoxalase/extradiol ring-cleavage dioxygenase domain" FT /db_xref="UniProtKB/TrEMBL:E1VSS8" FT /protein_id="CBT74681.1" FT /translation="MDVLSSRVLLRPIDLAATQQFYRDVLQLAVAREFGPAQQPGMVFF FT LGNGLLEVSGHRPPGKPSTLVLWLQVRDVQAELEQLTARGATVQREARKEDWGLIEAWI FT QDPDGTRIVLVQVPEGHPIRRDVREP" FT CDS complement(486247..487128) FT /transl_table=11 FT /locus_tag="AARI_04500" FT /product="putative triacylglycerol lipase precursor" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.1.3" FT /note="triacylglycerol lipase hydrolyzes ester bonds in FT triacylglycerol giving diacylglycerol, monoacylglycerol, FT glycerol and free fatty acids. Signal peptide predicted by FT SignalP 3.0 HMM (probability: 1) with cleavage site FT probability 0.991 between position 34 and 35" FT /db_xref="GOA:E1VSS9" FT /db_xref="InterPro:IPR002918" FT /db_xref="UniProtKB/TrEMBL:E1VSS9" FT /protein_id="CBT74682.1" FT /translation="MQRRILSVLGALCLAAATLTAPAIMPSAGSTAQAETVSSLNISPS FT GANDWDCAPDAEHPYPVVLVHGTFTTMDVNWISLSPKLKRNGYCVFALNYGLENGISGA FT AHVPDSAAELRDFIDRVRQATGANKVDIVGHSQGGMMPRWYMGHMGGAKHVNELVAIAP FT SSHGTQGILVPSATGVKIAGNYAGWICDACADQVAGSEFMTELNSIGDTVAGPDYTVIS FT TKYDEVVMPYKSQFLQGNSARVTNVLLQDKCPLDVSGHAGVAVDPVVHRWVLNALSTDG FT PADPGYRPSCYL" FT CDS 487599..488249 FT /transl_table=11 FT /locus_tag="AARI_04510" FT /product="phospholipase/carboxylesterase family protein" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.-.-" FT /note="identified by match to protein family PF02230. This FT family consists of both phospholipases and FT carboxylesterases with broad substrate specificity" FT /db_xref="GOA:E1VST0" FT /db_xref="InterPro:IPR003140" FT /db_xref="UniProtKB/TrEMBL:E1VST0" FT /protein_id="CBT74683.1" FT /translation="MSNLLSDVRSGNWSSTPESGAMLVFLHGFGSNEHDLGSLSEPLGL FT DLPWASLRAPLELGHGGAAWFQITTPGVPDAAPVQAATAAIWAWIDANVDPATRIIPVG FT FSQGGLMASQLLRTRPERVLATTILGGFVLGGAQPADEIIAAQRPAVLWGRGTEDRVIA FT PVAIERTTKFLPEHSTLTARTYPGLAHGINMDELNDVRSHITAQLDLIPLGKS" FT CDS 488299..488592 FT /transl_table=11 FT /locus_tag="AARI_04520" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VST1" FT /protein_id="CBT74684.1" FT /translation="MDNVEQALGRIRAAIEKLHLAAAQDHDAQRAHAARWLDGLFEDVE FT SREQLREAARKALELYRGGMGSFQDVGTAVMDDAVSGLRRALGSARSWLLRS" FT CDS complement(488634..489740) FT /transl_table=11 FT /locus_tag="AARI_04530" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="7 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VST2" FT /protein_id="CBT74685.1" FT /translation="MLMTLTDNAPRQSPASKHAVNPAAKKSPAAKPAPLGWGKLVLTML FT IPFFLCAIMGLFYLGAFHAPSPHNVQVAVVGDSAQAKVFAQTLQDGSEGALNVRTVADA FT DQARELVEQRELVAAYETSGGTATLYSSSAASETSANIAQKIFSDVAYEQGQPLRIEDV FT VPTGEQDTTGQGLFFLLVALSIGGYASAVPLAGFMGKVKLPVRFAMAAVAAAVVATIAV FT LVAGPVYRIIEDHYAGIWLISWVYAAGITLLGLGLHPLLRHWTTPALTLCFVALNFTSS FT GGIFQPQMQPGFYGALNTFWNGAGWLHAVQTLVYFPEQSIGMDILRLILWLVPGILLVI FT LTHAWSVRRTRVADENAKIRDVEETVAA" FT CDS 489813..490244 FT /transl_table=11 FT /locus_tag="AARI_04540" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VST3" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VST3" FT /protein_id="CBT74686.1" FT /translation="MGKEQREADIQSIFHHMQMITRRANTRSRQLAEPLTLVEHSLLRF FT IADTPGTRATDIAEAFSLNRSTVSRQVGTLLDLGYIAYDDAESGRGRVLELTEVGRERL FT QASAAVHRAAVTDRLDGWSEEQISAFAEALERYNVADSQ" FT CDS complement(490269..490478) FT /transl_table=11 FT /locus_tag="AARI_04550" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR023387" FT /db_xref="UniProtKB/TrEMBL:E1VST4" FT /protein_id="CBT74687.1" FT /translation="MSIEPGIYQHFKGQRYEVLAVGKHSETEEPLVFYRKLYDDYSFWA FT RPLEMFAEHVERDGYNGPRFARIA" FT CDS complement(490517..491008) FT /transl_table=11 FT /gene="mog" FT /locus_tag="AARI_04560" FT /product="molybdopterin adenylyltransferase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="involved in molybdoterin cofactor biosynthesis. FT Catalyses the following reaction: molybdopterin + ATP --> FT molybdopterin-AMP + diphosphate. The function of several FT enzymes, such as xanthine oxidase, sulfite oxidase, nitrate FT reductase, depends on the molybdopterin cofactor" FT /db_xref="GOA:E1VST5" FT /db_xref="InterPro:IPR001453" FT /db_xref="UniProtKB/TrEMBL:E1VST5" FT /protein_id="CBT74688.1" FT /translation="METSRTAAVVVASTSAAAGTAEDKTGQLITRWLSERGFETGEPTV FT VADGQPVRFAVDDLLANDAQVVIVTGGTGVSPDDQSPEMVAPLLDVQLPGIIEAIRRRG FT EASTALSIITRGVAGFSGNSFVITLPGSTGGVKDGLAVLDPILEHLLVQRSGGTGHGPR FT " FT CDS complement(490998..491474) FT /transl_table=11 FT /gene="moaC" FT /locus_tag="AARI_04570" FT /product="molybdenum cofactor biosynthesis protein C" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="is involved, together with MoaA, in the conversion FT of a guanosine derivative (5 -GTP) into the molybdopterin FT precursor Z. The function of several enzymes, such as FT xanthine oxidase, sulfite oxidase, nitrate reductase, FT depends on the molybdopterin cofactor" FT /db_xref="GOA:E1VST6" FT /db_xref="InterPro:IPR002820" FT /db_xref="InterPro:IPR023045" FT /db_xref="InterPro:IPR023046" FT /db_xref="UniProtKB/TrEMBL:E1VST6" FT /protein_id="CBT74689.1" FT /translation="MSEKLTHLREDGSAHMVDVSDKAVTKRVATAEAIFATRPDVVPML FT MTGDLPKGEALGTARVAGIMAAKRTWELIPLCHPLPISKVSIDFTAEESAVRVTAQVTT FT KGVTGVEMEALTAASVAALTLYDMVKGVDKHAEVRSVKVLAKSGGKSGDWVRGD" FT CDS complement(491467..492699) FT /transl_table=11 FT /gene="moeA" FT /locus_tag="AARI_04580" FT /product="molybdopterin biosynthesis protein MoeA" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="involved in the biosynthesis of a demolybdo- FT cofactor (molybdopterin), necessary for molybdo-enzymes FT such as xanthine oxidase, sulfite oxidase, nitrate FT reductase: molybdopterin-AMP + molybdate --> molybdenum FT cofactor + AMP + H2O" FT /db_xref="GOA:E1VST7" FT /db_xref="InterPro:IPR001453" FT /db_xref="InterPro:IPR005110" FT /db_xref="InterPro:IPR005111" FT /db_xref="InterPro:IPR020817" FT /db_xref="UniProtKB/TrEMBL:E1VST7" FT /protein_id="CBT74690.1" FT /translation="MSCTLESHRAELEELLSPVFACLDSEVLRIDSPEAIDRILSEDQN FT ALLPIPAFTNSQMDGYAARSADLAAASLRSPISLPLGFTAAAGDRQIPLAEGTVSPVMT FT GAMIPLGADTVIPIEESGSGAFPELVRAGVGTPSGHAEFSAPSAEGRFIRPAGVDLETG FT ALVAKAGTRLTPTMIAALVSSGLREVPVRRALKVAVCTTGDELSDGQCSQGQIPDSNSP FT MLAAWLRRYQVQVRTLQLPDDPQRFTLAIDALQEQVDLIVTVGGISAGAYEVVRQALSP FT LGGVFHHVAIQPGGPQGFAQLPKAAVLCFPGNPVSALLSAELFLAPLLRQLNALPEPLP FT RHYPLAADASSPEHKHQVRRALIRDGQVTILDPGSHLVHDLARADALVHIPVGVSQLAA FT GQSIETWSMNV" FT CDS complement(492703..492954) FT /transl_table=11 FT /gene="moaD" FT /locus_tag="AARI_04590" FT /product="molybdopterin-converting factor small subunit FT MoaD" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="molybdoterin synthase converts molybdopterin FT precursor Z into molybdopterin. This requires the FT incorporation of two sulfur atoms into precursor Z to FT generate a dithiolene group. Heterodimer of 2 MoaD subunits FT and 2 MoaE subunits" FT /db_xref="InterPro:IPR003749" FT /db_xref="InterPro:IPR012675" FT /db_xref="InterPro:IPR016155" FT /db_xref="UniProtKB/TrEMBL:E1VST8" FT /protein_id="CBT74691.1" FT /translation="MSKITIRYFAAAAAAAGCEQESWERPDTLAKLRSELIDSYGPDMA FT QVLRAGSFLINGVVRRDAGELGTADDLTVDVLPPFAGG" FT CDS 492992..494173 FT /transl_table=11 FT /gene="moeB" FT /locus_tag="AARI_04600" FT /product="molybdopterin biosynthesis protein MoeB" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="involved in the biosynthesis of a demolybdo cofactor FT (molybdopterin), necessary for molybdoenzymes. Plays a role FT in the activation of the small subunit of the molybdopterin FT converting factor (MoaD)" FT /db_xref="GOA:E1VST9" FT /db_xref="InterPro:IPR000594" FT /db_xref="InterPro:IPR001763" FT /db_xref="InterPro:IPR007901" FT /db_xref="InterPro:IPR009036" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VST9" FT /protein_id="CBT74692.1" FT /translation="MKSERDFPALVAPGPPLSEERVARAARQLSLPGFDQAAQRRLAAA FT RVLVIGAGGLGSASVPYLVGAGVGTIGIVDDDLVELSNLHRQVTHTTANIGLAKTASLA FT QAATALDPNVKIIEHNLRLDSSNALEIFANYDLVIDGSDNFPTRYLSNDAAQLSGIPLI FT WGSILQHHGQVSVAWHEHGPGYRDLFPVPPAPGTVPDCAAGGVLPGLCGTVGSLLATEA FT LKLIAGIGTPLVGKVLIYDALAASTRTLEYSRDPQAPEISELIDYVLFCSGTLPEAEGI FT DAESLAELLAGTDAPVLLDVRNDDEHAQQHITGSLHLPLPELEAAIESGTELEQIPAQV FT TVYCARGPRSQRAASLLASRGIKTNYLEGGLPALAAVEPQLLAKPATTEGNRS" FT CDS 494170..494577 FT /transl_table=11 FT /gene="moaE" FT /locus_tag="AARI_04610" FT /product="molybdopterin-converting factor large subunit FT MoaE" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="molybdoterin synthase converts molybdopterin FT precursor Z into molybdopterin. This requires the FT incorporation of two sulfur atoms into precursor Z to FT generate a dithiolene group. Heterodimer of 2 MoaD subunits FT and 2 MoaE subunits" FT /db_xref="GOA:E1VSU0" FT /db_xref="InterPro:IPR003448" FT /db_xref="UniProtKB/TrEMBL:E1VSU0" FT /protein_id="CBT74693.1" FT /translation="MSYALITEEPIDEAAVRAAVQSDTAGALVMFHGIIRNHDGGQSVN FT SLDYSHHPQAQEFLEKIIAEEEERTGLKVSAVHRVGPLKIGDAALVAASAAAHRKEAFE FT AIENLVERIKAEVPIWKKQHFTSGSSEWVGL" FT CDS 494626..495042 FT /transl_table=11 FT /locus_tag="AARI_04620" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSU1" FT /protein_id="CBT74694.1" FT /translation="MTDYRLGIGSKTDYREVIPREIPRNEFLVSRLRQECLPLPDTDTA FT ILAMQRTLGQPTQKTLSKQDIRKLTVGYLLAFRDVELARASQNAAISNVASALLALHYE FT STIGKSVDDVLLAIHAYFWLGNITAEALLESLEH" FT CDS complement(495175..496131) FT /transl_table=11 FT /locus_tag="AARI_04630" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="GOA:E1VSU2" FT /db_xref="InterPro:IPR001034" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR013196" FT /db_xref="InterPro:IPR018356" FT /db_xref="UniProtKB/TrEMBL:E1VSU2" FT /protein_id="CBT74695.1" FT /translation="MSTSTRFLRLLSLLQTHRYWSGDELAQRLDVSLRTVRRDIDRLRD FT LGYPVQADRGVGGGYQLASGTALPPLVLDDEEAVALVVALQSTVHGGSSALAEAALRAM FT GKVVPVLPARLRKRAQALTASTVPLNSQSCTADPVDPTVLVALAQACRDHERIAFEYKD FT AKGAATSRRVEPLQLVNVGNRYYLVAFDLDRDDWRSFRVDRAQNPSPRALRFTPRPVPG FT GDAAGFVRAALRGSGQQEMSARIHASSEKLEPLIGRWFQIKQIDANSCLVRTENMDLRW FT AAFGLAMSEARISDVQPQELSALLDSWSSNLAYQNPS" FT CDS 496236..496784 FT /transl_table=11 FT /locus_tag="AARI_04640" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007061" FT /db_xref="UniProtKB/TrEMBL:E1VSU3" FT /protein_id="CBT74696.1" FT /translation="MSTMAITNTATLSGERADLFQALANARHFLRFTAQGLNDEQASKR FT TTASELTLGGLIKHVTGVEEQWQEFIVKGRAAMAWDGADFSQMPPEAIEAFHNEFRMQP FT GETLEALLESYTQVADRTDALLAKVDLDTVHELPSAPWFVDTHWSVRRTLLHIISETTQ FT HSGHADIIRESLDGQKSMG" FT CDS complement(496781..497821) FT /transl_table=11 FT /gene="moaA" FT /locus_tag="AARI_04650" FT /product="molybdenum cofactor biosynthesis protein A" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="is involved, together with MoaC, in the conversion FT of a guanosine derivative (5 -GTP) into the molybdopterin FT precursor Z. The function of several enzymes, such as FT xanthine oxidase, sulfite oxidase, nitrate reductase, FT depends on the molybdopterin cofactor" FT /db_xref="GOA:E1VSU4" FT /db_xref="InterPro:IPR000385" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR010505" FT /db_xref="InterPro:IPR013483" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:E1VSU4" FT /protein_id="CBT74697.1" FT /translation="MKAPLAGEILDARSRPLHDLRISVTDRCNFRCVYCMPKEIFGRDF FT QFRERSELLSFEEIERLARISVSLGVTKLRLTGGEPLLRRGIVDLVAMLSNLRTPEGKR FT IDLAMTTNGSALPVLAPALKEAGLNRVTISLDSLDDEKFKAINDVNFPVSKVLEAIQVA FT REVGLGPVKINTVIKRGVNDSEILSLAEHFRGTGNILRFIEFMDVGTTNGWKLDEVLPS FT AEVVSMINERWALEPVTKTEPGETANRWRYKDGAGEIGVISSVTNAFCGNCSRARVSAE FT GQLYTCLFAGSGYDLRQLMRDGISDEDLAKALTGHWRKRDDNYSELRAALTPGNRKRIE FT MSYIGG" FT CDS 497954..498724 FT /transl_table=11 FT /gene="modA" FT /locus_tag="AARI_04660" FT /product="molybdate ABC transporter, substrate-binding FT protein ModA" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, MolT- FT family (molybdate uptake transporter), molybdate porter (TC FT 3.A.1.8.1). ABCISSE: ABC transporter, binding protein (BP), FT MOI-family, molybdate import. Part of the ABC transporter FT complex ModABC involved in molybdate import" FT /db_xref="GOA:E1VSU5" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR005950" FT /db_xref="UniProtKB/TrEMBL:E1VSU5" FT /protein_id="CBT74698.1" FT /translation="MRVRWPLALRCTVLAAVAGLSLTGCSASGNSTGEPITIAAAASLQ FT GAFEQISEEFTAEHPEVQISSITYDGSSTLATQILEGANVDVFASADERNMSEVTEAGF FT GHEPVIFASNTLVIAVPQDNPADIDSLQDLSQATMVLCAPQVPCGAASQRLLEASGVQV FT TPASQEQNVTAVLQKVAAGEADAGLVYATDVLDDGNVAAIVPDGAEDIVNTYPIAALGE FT NPGAQAFVDFVSSERGQQILEEHGFGTGAAQANG" FT CDS 498717..499523 FT /transl_table=11 FT /gene="modB" FT /locus_tag="AARI_04670" FT /product="molybdate ABC transporter, inner membrane subunit FT ModB" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, MolT- FT family (molybdate uptake transporter), molybdate porter (TC FT 3.A.1.8.1). ABCISSE: ABC transporter, permease (IM), FT MOI-family, molybdate import. Part of the ABC transporter FT complex ModABC involved in molybdate import" FT /db_xref="GOA:E1VSU6" FT /db_xref="InterPro:IPR000515" FT /db_xref="InterPro:IPR006469" FT /db_xref="InterPro:IPR011867" FT /db_xref="UniProtKB/TrEMBL:E1VSU6" FT /protein_id="CBT74699.1" FT /translation="MASDTGVRVPGFAIAPALLGVALLVLPLLALISRASWSTLVADAT FT SEEALAALWLSLRTGVAATVLCVLLGVPLAVLMARSSTRVAQLLRALIAVPLVLPPMVG FT GVALLFLFGRTSPIGQFIDSIWGISLPFSTAAVVIAQSFVALPFLVLSVEGSLRAAGAG FT YEQAAATLGAGRWMVLTRITLPLAAPGLVAGIILCFARAIGEFGATALFAGNAPGVTQT FT MPLAIYTAFNGAGAGRDSAVALSLLLLATAVLVLLLVRAWRPGALK" FT CDS 499520..501517 FT /transl_table=11 FT /locus_tag="AARI_04680" FT /product="putative molybdate transport/synthesis fusion FT protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.-" FT /note="N-terminal section of the protein: ABC transporter, FT ATP-binding subunit ModC; TCDB: ATP-binding cassette (ABC) FT superfamily, MolT-family (molybdate uptake transporter), FT molybdate porter (TC 3.A.1.8.1). ABCISSE: ABC transporter, FT ATP-binding protein (ABC), MOI-family, molybdate import. FT Part of the ABC transporter complex ModABC involved in FT molybdate import. C-terminal section of the protein: FT molybdopterin biosynthesis protein MoeA; involved in the FT biosynthesis of a demolybdo-cofactor (molybdopterin), FT necessary for molybdo-enzymes such as xanthine oxidase, FT sulfite oxidase, nitrate reductase: molybdopterin-AMP + FT molybdate --> molybdenum cofactor + AMP + H2O" FT /db_xref="GOA:E1VSU7" FT /db_xref="InterPro:IPR001453" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005110" FT /db_xref="InterPro:IPR005111" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VSU7" FT /protein_id="CBT74700.1" FT /translation="MTLKVNLQVPRTGFDVDVEFAVPAGSTLAMMGPSGSGKSTIVHAI FT AGIQKITRGRIELSGTVLADAKLHRPPHLREVGLLGQDPHLFPHLDALKNIAFGARAGG FT LEKSAATAAASEWLARLGLEEIASHRPEALSGGQRQRIALARALAAKPKILLIDEPFAS FT LDVEAAMDMRALVREELARTATSAIVVSHSAADTLALADDLLVLERGQIIQQGTVAEVF FT AAPANRFVRAVVATLPAQHPISIQEEPIMSTGNDPIELEVHRSRLLSQVVPVAPQRIAV FT AGGFTALHGAVLAQDVASAHPLPLWDNSAMDGYAVRSADTATAPAALDVIGEVPAGSGW FT NPMLEAGQCVKIMTGAPIPSDADAVVRIEDTSAAVDGWDVKTVQVNVQVPAGKDIRRSG FT EDKNAGEPMAYAGEELTAARLSALAAAGSSTLQVRTMPKVAVLITGAELRTPGQALTRG FT QIPETNSLLMAGLLAESGIQATTVVHCVDDIEAVHEQLVILGATHDAVLSTGGVGPGAY FT DVMRQALEAEPQVQAVRVKIRPGQPQCAGRLAAGAMVFALPGNPVSAAVSFELFVRPCL FT RAMQGHRDVLRPTLRAVAAVGWRAAAGRVQVIPVVFEHGEQLRCAPAVQAQSISHSVGG FT FGAAQGYALVPAGITQVNPGDEVEVLRMVP" FT CDS 501514..502392 FT /transl_table=11 FT /gene="mobA" FT /locus_tag="AARI_04690" FT /product="molybdopterin-guanine dinucleotide biosynthesis FT protein A" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="links a guanosine 5 -phosphate to molydopterin, FT forming molybdopterin guanine dinucleotide: molybdenum FT cofactor + GTP = molybdopterin guanine dinucleotide + FT diphosphate + 2 H2O" FT /db_xref="InterPro:IPR006812" FT /db_xref="UniProtKB/TrEMBL:E1VSU8" FT /protein_id="CBT74701.1" FT /translation="MSNSNAIGFDALVLAGGRGTRLGGAGKAELQLHGQRLVDRVVAAT FT RKAGAARVIVVGPDTAGTKADWVVREDPPFAGPLAGIAAGLKELSSETASEWTMVLACD FT LQRPVAVSTALTKNFERRETDGLLLVDAQGHTQWLAGIYRTAALALACDELGENLVDAP FT VRRALNQLHLAQVPVDDETSSDIDTPQALESARRNERTRMAQHLPPEALNEWLEAAAKE FT LGLDAGGVDIATVLDVAKHVAHEVARPAAPLSTFLLGLAMGNGKGDLDGLSQQLVSRAH FT RWADEHPEGIA" FT CDS complement(502481..503380) FT /transl_table=11 FT /locus_tag="AARI_04700" FT /product="putative disulfide bond formation protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF02683: Cytochrome C biogenesis protein FT transmembrane region" FT /db_xref="GOA:E1VSU9" FT /db_xref="InterPro:IPR003834" FT /db_xref="UniProtKB/TrEMBL:E1VSU9" FT /protein_id="CBT74702.1" FT /translation="MDIGLLSAFLGGMLALLSPCSALLLPAFFASTVGSGPRLYLHGLV FT FYLGLALVLVPAGLGVGAVGLFLATERELIVLIASLMLIAMGIIYFAGFGFDLSRWIPG FT FSKLQHRASGGKGLLKTLALGAVGGVSGFCAGPILGAMLTLAAVQGDAVSGGVLLAVYG FT AGMVVPMFVLARIWNRLGANGRSNLRGRTTKVFGRELHVVSILTGSLLIVVGVIFWLTN FT GLISAPQLVPIGVQDWLQRNSAALSSPMVDVAALVVLAVIVFWGWMRRGRKSAQKPTMP FT EELAPGQAQSKDEDRQES" FT CDS complement(503380..504129) FT /transl_table=11 FT /locus_tag="AARI_04710" FT /product="DSBA-like thioredoxin domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF01323" FT /db_xref="InterPro:IPR001853" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:E1VSV0" FT /protein_id="CBT74703.1" FT /translation="MENSSTAKPKRRWIGLAMALAAIAALVFVALNLGDINSDGPATPK FT DQPISQQTETPADATEQAPDLSQFELRSPDDLLAAGPVDAPVGVVVFSDYQCKFCAKWS FT SETLPLILDYAKEGKVRVEWRDVNIFGDDSERAALASYAAAKQGKFWEYHDELFADGKS FT RKGSGLSEKSLAKLAADLGLDTKQFTTDVKSEEAAKMIDSNAQLGLQLGVYSTPAFLVD FT GEPVMGAQPKSVFIDKIEAALAAKDAS" FT CDS complement(504458..505471) FT /transl_table=11 FT /locus_tag="AARI_04720" FT /product="putative permease" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /db_xref="GOA:E1VSV1" FT /db_xref="InterPro:IPR004695" FT /db_xref="UniProtKB/TrEMBL:E1VSV1" FT /protein_id="CBT74704.1" FT /translation="MGTGIASTLTQLHAGQTTLGADLARFFLVAGWAFAVIFTIGFAIR FT CLRTTGAWAASMHGVGASAWGMVSMGILSIGSATATVLADWAPQFTTVSWGVDGALWVI FT GTALGLITTFGFSLALIRRRNAEPRPAWGLAVVPLMVSATCGAPFIAKLDSPVLAATLL FT AVLIFCFVTSLMLGIIIFAAAYCHHARVDRIPAELSASSWIPLGVVGQSTAAAQAISSQ FT MHRFILPEAMPGIQAVANVYGIVMLCAAIPVVIFAVSTTTFGIANKMSFSPGWWALTFP FT VGTLSLGALNLGHSLQSNGYSAVGIGAWILLLSTWTVCAIASLRHPFLAKSPAPAN" FT CDS 505636..506529 FT /transl_table=11 FT /locus_tag="AARI_04730" FT /product="LysR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00126: bacterial regulatory FT helix-turn-helix protein, lysR family. 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 /db_xref="GOA:E1VSV2" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VSV2" FT /protein_id="CBT74705.1" FT /translation="MSDWPELSSLEVLVAVAEHGSLSAAARELHMEQPNVSRSISRLER FT RLNLALLRRSTTGSRLTPEGLLFVEWARELLSSADSLMRNARALGNDNFGELKISASQT FT IAEYLLPRWLSSLRVALPNTQISLRVSNTTDVLNELHTGVCGLGFVEGPVAKESTHSAF FT VGEDRLVLVVASSHPWADRDSVQPKEIMDSCLIARESGSGTRKVLDEALKAPVVPRIVL FT ESNAAVRVAVLSGAGPAVLSRFAVSDAVAAGTLVELPIDGVQLQRRLRAVWTGPRQLTG FT AAEKLVGIAIASSRTI" FT CDS complement(506703..507473) FT /transl_table=11 FT /gene="narI" FT /locus_tag="AARI_04740" FT /product="respiratory nitrate reductase gamma subunit" FT /function="2.8 Metabolism of nitrogen/nitrate and nitrite" FT /EC_number="1.7.99.4" FT /note="the respiratory nitrate reductase enzyme complex FT allows the bacteria to use nitrate as an electron acceptor FT during anaerobic growth. The gamma subunit is a b-type FT cytochrome that receives electrons from the quinone pool. FT It then transfers these via the iron-sulfur clusters of the FT beta subunit to the molybdenum cofactor found in the alpha FT subunit" FT /db_xref="GOA:E1VSV3" FT /db_xref="InterPro:IPR003816" FT /db_xref="InterPro:IPR023234" FT /db_xref="UniProtKB/TrEMBL:E1VSV3" FT /protein_id="CBT74706.1" FT /translation="MSTSAILLWVVLPYAAAVVFIVGHIWRYRYDKFGWTTRSSQTYEN FT RLLRWGSPMFHFGILMVIAGHVVGLLIPREWLYAIGVNEHIYHLGATWMGTAAAILTVA FT GLIILIYRRRTVGPVFLATTVMDKVMYVFLGATLGFGTLATLVYQVFGPGYSYRESISP FT WIRQMIIFQPHPEMMVEVPLFFQLHVATACVLFALWPFTRLVHVFSAPIPYFFRPYIVY FT RSRDESRGAGSRPVRRGWDPVAAPQPRGKRGSNR" FT CDS complement(507470..508168) FT /transl_table=11 FT /gene="narJ" FT /locus_tag="AARI_04750" FT /product="respiratory nitrate reductase delta subunit" FT /function="2.8 Metabolism of nitrogen/nitrate and nitrite" FT /EC_number="1.7.99.4" FT /note="the respiratory nitrate reductase enzyme complex FT allows the bacteria to use nitrate as an electron acceptor FT during anaerobic growth. The delta subunit is not part of FT the nitrate reductase enzyme but is most likely needed for FT assembly of the multi-subunit enzyme complex" FT /db_xref="GOA:E1VSV4" FT /db_xref="InterPro:IPR003765" FT /db_xref="InterPro:IPR020945" FT /db_xref="UniProtKB/TrEMBL:E1VSV4" FT /protein_id="CBT74707.1" FT /translation="MIPRLFNRATPRRKLAGTLEPVAMKRAERARVHTLASLLLDYPDQ FT KWFARLDELETHLGSVPAPIAQLLADFIEASRSLGSTQVQRLYVQTFDLKRKCSLYLSY FT FATGDTRKRGTALVTFLEAYRATGWEFDADELPDYLPAVLEFSARCDDPIAEALLSSHI FT EGIEVLRTALESMGSHWAGLIRSITLSLPPVDQETQERVLALVSEGPPTETVGLSFLGN FT LPPFSPRGNG" FT CDS complement(508165..509802) FT /transl_table=11 FT /gene="narH" FT /locus_tag="AARI_04760" FT /product="respiratory nitrate reductase beta subunit" FT /function="2.8 Metabolism of nitrogen/nitrate and nitrite" FT /EC_number="1.7.99.4" FT /note="the respiratory nitrate reductase enzyme complex FT allows the bacteria to use nitrate as an electron acceptor FT during anaerobic growth" FT /db_xref="GOA:E1VSV5" FT /db_xref="InterPro:IPR006547" FT /db_xref="InterPro:IPR017896" FT /db_xref="UniProtKB/TrEMBL:E1VSV5" FT /protein_id="CBT74708.1" FT /translation="MKVMAQMSMVMNLDKCIGCHTCSVTCKQAWTNRTGVEYVWFNNVE FT TRPGVGYPRTYEDQEKWRGGWTLNKRGRLTLRDGGRFKKLSRIFSNPKLPEIHDYYEPW FT TYDYDMLLNSPSGEHTPVATPKSLLTGKDMKIGWSANWDDNLGGSLETMDQDPLLAKMS FT EEVKAEYEKAFMFYLPRICEHCLNPSCVASCPSGAMYKRAEDGIVLVDQDACRGWRMCV FT SGCPYKKVYFNHRTGKAEKCTFCYPRIEVGLPTVCAETCVGRLRYLGLVLYDADAVAAA FT ASVEDEHDLLDAQRGVLLDPHDPAVIEAARAGGIPEDWIESAQASPIWKLIRDYEIALP FT LHPEYRTMPMVWYIPPLSPVVDVVTNTGNDGEDADNLFAAIDKLRIPIGYLAELFSAGD FT TAPVDLSLRKLAAMRSYMRGVSMSDRRDESITEAVGMSGPQMEEMYRLLAIAKYEERYV FT IPPAHAEQAHDLEEMGCSLDFEGGPGMGGAGPFGSSSGESVPVAVENFQSLKNRQTSDR FT PSTPGRVNLLNWDGNGTPEGLFPPEDGK" FT gene complement(509799..512129) FT /pseudo FT /locus_tag="AARI_04770" FT /product="truncated respiratory nitrate reductase" FT /note="C-terminal section of a respiratory nitrate FT reductase alpha subunit" FT gene complement(512108..513517) FT /pseudo FT /locus_tag="AARI_04780" FT /product="truncated respiratory nitrate reductase" FT /note="N-terminal section of a respiratory nitrate FT reductase alpha subunit" FT CDS 513815..514966 FT /transl_table=11 FT /locus_tag="AARI_04790" FT /product="putative nitrate/nitrite transporter" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="major facilitator superfamily, nitrate/nitrite FT porter family, 24 TMS, 2 domain, NarK1-NarK2 porter (TC 2. FT A.1.8.11). In Paracoccus pantotrophus, this transporter FT comprises 2 domains: NarK1, a NO3-/H+ symporter; and NarK2, FT a NO3-/NO2- antiporter" FT /db_xref="GOA:E1VSV6" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VSV6" FT /protein_id="CBT74709.1" FT /translation="MPAPWVSGHGCSFPPIQRFYAEGMDLSEGQVSLMLATPVLVGALG FT RIFTGALTDRFGARKMFTVVLLATVPAVLLVALAGSIGSFALLIIAGTYLGVGGSIFAV FT GVPFASAWYPPHKRGFANGVFGMGMIGTAISAFQTPRLLQSFGYWGTHLFLAGLLVVTA FT ALVWFLMRESPAWKPNNQPLFPKVFGALKLAITWEMAFLYGIVFGGFVAFSTFLPKYLM FT TIYPENVDPIGAGTRTALFALAAVIARPIGGVLADKFGPKIIALISLAGIVSLAYIVGQ FT QPSEGILTGVTFILMASAMGLGMGAVFAWIGPSTPPEKVGAVSGVVAAAGGLGGYFPPL FT AMGMTYHAETNSYALGLWLLVLVGTFALVVAGMLRGTRGRGGM" FT CDS 515046..515588 FT /transl_table=11 FT /locus_tag="AARI_04800" FT /product="YaeQ family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF07152. This FT family consists of several hypothetical bacterial proteins FT of around 180 residues in length, which are often known as FT YaeQ. YaeQ is homologous to RfaH, a specialised FT transcription elongation protein. YaeQ is known to FT compensate for loss of RfaH function in Escherichia coli FT and Salmonella typhimurium" FT /db_xref="InterPro:IPR009822" FT /db_xref="UniProtKB/TrEMBL:E1VSV7" FT /protein_id="CBT74710.1" FT /translation="MAIGATIHTFEVQLADVDRGVYEDLSLRVAQHPSETDAYMVTRVL FT AYCLELEEGIAFSAGGVSTGEEPAILVKDLTGLITAWIEVGAPDAQRLHLGSKRADRAA FT VYTHRDPAKLLATWRGKTIHRSQDIVVRSFDSKFIDAAAQALTRRNTMSLSVTEGQIYL FT ELNGTNLETQISTHEIE" FT CDS 515686..516762 FT /transl_table=11 FT /gene="glpQ" FT /locus_tag="AARI_04810" FT /product="putative glycerophosphodiester phosphodiesterase" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.4.46" FT /note="glycerophosphoryl diester phosphodiesterases display FT broad specificity for glycerophosphodiesters; FT glycerophosphocholine, glycerophosphoethanolamine, FT glycerophosphoglycerol, and bis(glycerophosphoglycerol)" FT /db_xref="GOA:E1VSV8" FT /db_xref="InterPro:IPR004129" FT /db_xref="InterPro:IPR017946" FT /db_xref="UniProtKB/TrEMBL:E1VSV8" FT /protein_id="CBT74711.1" FT /translation="MKLRNITFGTATLALAVTMAMPAVAAQIEPTGADPLLIGHRGAAG FT VAPENTLPAIKAGSQSGAEFTEIDVQLSKDGVPFIFHDSTASRTTNIAEVFPERVDDPI FT TSFTWDELQQLDAGSYFSEEFEGTKIPHFDEVPGALTDDTGVFIEIKDPAKSPGVEKLV FT ADALAQNPEWKELADANKIEVLGFDAVSNQRFAQIAPEVPLQQLSGTVPSVAELANYAS FT YADSFGTSYRTLDAAGAQRVKDAGLGLGVYTVNADAAADEALALGVERITGDFPQQINR FT HLDGQKIFPANNGVIIADSINDVPGSDTTPEKGEHVILENTGKRTIDVSGNILRDAANN FT ILEIGEGYELEPGQKLRV" FT CDS complement(517349..517741) FT /transl_table=11 FT /locus_tag="AARI_04820" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSV9" FT /protein_id="CBT74712.1" FT /translation="MLEVMEEIPDSALVSDKALEQYLNSVNVAEQNNSSKFELAQAAGI FT DWGNTAKCAQALGTAVLGFAVPAVKLIRIKALIKELGGVWKSAKLLVGAGTAAEKGEAA FT VTALASLVAELAGIPGIVGACPKVWK" FT tRNA complement(518344..518434) FT /locus_tag="AARI_36460" FT /product="transfer RNA-Ser" FT /anticodon=(pos:518398..518400,aa:Ser) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(518529..519005) FT /transl_table=11 FT /gene="codA" FT /locus_tag="AARI_04830" FT /product="putative cytosine deaminase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.5.4.1" FT /note="catalyzes the hydrolysis of cytosine into uracil and FT ammonia" FT /db_xref="GOA:E1VSW0" FT /db_xref="InterPro:IPR002125" FT /db_xref="InterPro:IPR016192" FT /db_xref="InterPro:IPR016193" FT /db_xref="UniProtKB/TrEMBL:E1VSW0" FT /protein_id="CBT74713.1" FT /translation="MVHEFETWMDLALAEARAALATDDVPIGAVILSPAGEVLATGRNE FT REAGNDPTAHAEVVAIRNAVKALEAKGEDDGWRLSDCTLVVTLEPCAMCAGAIVLSRIP FT KLVFGAWDEKAGACGSVFDIVREPRLNHWVEVYSRVKEEECAELLREFFRGKRA" FT CDS 519175..519822 FT /transl_table=11 FT /gene="upp" FT /locus_tag="AARI_04840" FT /product="uracil phosphoribosyltransferase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.4.2.9" FT /note="catalyses the formation of UMP and diphosphate from FT uracil and 5-phospho-alpha-D-ribose 1-diphosphate" FT /db_xref="GOA:E1VSW1" FT /db_xref="InterPro:IPR000836" FT /db_xref="InterPro:IPR005765" FT /db_xref="UniProtKB/TrEMBL:E1VSW1" FT /protein_id="CBT74714.1" FT /translation="MRVQVVDHPLVAHKVSVLRDKNTPSSIFRQLTDELVTLLAYEATR FT EVKTESVQVQTPVATTIGTAIAKPTPLVVPILRAGLGMLEGMTRLVPTAEVGFLGMARN FT EETLDIITYADRVPNDLTGRQVFVLDPMLATGGTLAEAIKFIFDRGADSVTCICLIAAP FT EGVARLEEIHGDDDRVHVVLANLDEKLNEKSYIIPGLGDAGDRLYGVTPPIA" FT CDS complement(519859..521370) FT /transl_table=11 FT /locus_tag="AARI_04850" FT /product="signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VSW2" 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:E1VSW2" FT /protein_id="CBT74715.1" FT /translation="MSFFSPNTKVSSPHALQRKLLLILLTSVTAVSVLLGLLYNAGMRQ FT TLMDQLNSQLRLATERALNYSQGAPAVNSRLDAPGQAAGTLTARFVDKYVFNGGVLDER FT TGVLEQLSQEDAIPMVDLELSTLREGGPFKPVRAHLTVGDYYLVAVKDSGSNGILIVGL FT PLHSTDLALRGMAWLTLFIALILIAGAGLAGSWLISRSLASLKRVATVAASVAAEELDS FT GKVDLAQRVPAQDAIPGTEVGNVGNALNAMISNVSTALTSREKSQAQMRQFVADASHEL FT RTPLSAIRGYTELLSATEHFSPDGQRSVDRVLQQSARMSSLVESLLLLARLDEENAFKR FT SEVDLCELTADITEDFKLTASDHHWIFDCRTPQTIIHADSASLRRVITNLLANARKHTT FT AGNTVTVSVDQDDQTDEAILRVHDTGEGIAPEFLPRVFERFTRADKARSGSDGTTGLGL FT PIAKSIVEAHGGKITVASKPGDTVFEVRLPLIDPEIAEEMPKAAV" FT CDS complement(521367..522107) FT /transl_table=11 FT /locus_tag="AARI_04860" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VSW3" 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:E1VSW3" FT /protein_id="CBT74716.1" FT /translation="MNESRFSPSQLPRLTHPDGTAIKVLVVDDEPSLAELVAMGTRMLG FT WEATMAHDGPEAVATARSLAPDVLVLDWMLPGFDGPEVLRKVRTHFPEIPVLFLTAKDA FT VEDRIEGLGAGADDYVAKPFSLEEVLIRLHRLVERSGAATADSAELVVGDLVLNTDSHD FT VSRAGREISLTATEFDLLSYLMNNARRVVSKSQILDNVWHYDFDGQANIVELYISYLRK FT KIDVDAEPMIHTVRGVGYVLKPAA" FT CDS 522722..523507 FT /transl_table=11 FT /locus_tag="AARI_04870" FT /product="putative two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VSW4" FT /db_xref="InterPro:IPR001867" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:E1VSW4" FT /protein_id="CBT74717.1" FT /translation="MSAGSGYVHVSIRNAQNRAAAAQRAASGNYAPAGYRPLRAVSTAH FT ETREPMHSSTTAPVQSTGQPSTDTSARGFVLYVGLDETTAQAQGTSLGKLATQVRAFLA FT TLSPQAQTHAAVALAPTSAQGDPIDVVRQALGDPTVSRRPRAEARPSTPRPSGVLIDLS FT RREVYLDGETLNLTFKEFELLNFLVENGTRTVGREELLENLWRNAEEVPNERTIDVHIR FT RLRSKLGRLANTVRTVRGQGYRFYEHPEVVVWAAPEYSI" FT CDS 523577..524104 FT /transl_table=11 FT /locus_tag="AARI_04880" FT /product="putative regulatory protein" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="3.1.3.-" FT /note="COG2062; phosphohistidine phosphatase SixA from FT Escherichia coli exhibits phosphatase activity towards the FT HPT domain of the ArcB sensor involved in the multistep FT his-asp phosphorelay" FT /db_xref="GOA:E1VSW5" FT /db_xref="InterPro:IPR013078" FT /db_xref="UniProtKB/TrEMBL:E1VSW5" FT /protein_id="CBT74718.1" FT /translation="MNTMHSRKLILMRHAKADYPLGVSDHDRPLAARGHREAPAAGAWL FT VDNELIPDYIICSDALRARSTCAWVLSELGEKGPTPYIDSRIFSAGTAQLCSIINEVPD FT TVSNLLVIGHQPILQELALRLASRDSDEEAVYELAMNYPTLGTTVLETSHPYSHLDARD FT ARVTHFIAPRPA" FT CDS 524331..525458 FT /transl_table=11 FT /locus_tag="AARI_04890" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSW6" FT /protein_id="CBT74719.1" FT /translation="MAIIAESLPTQSAAARNEVQQQIDAQRARTIRAAYTTRFAAAELQ FT RNPQDFEIVRRANMVPRSGDVVIANVAELGKHTRLQSPVSRRQLMFVGQEIMVAYGHRY FT APDQFLAHVPDNLGPCQLVAGGGVASEVIEQHASIDKATQLEPVGLLMRQGKVVNLLDF FT APLSIENESPRAAQIDAPRPPVIAVLGTSMNSGKSTTLGCLVNGLVNSGMQVAAGKATG FT TGAGNDPNLFTDAGAFSVCDFTDFGFPTTYRLDYETVRDLLVAMIREQSATGAGTVVIE FT IADGLFQGETSRLLRDPIFTAQVDRVLFSAQDALGAQAGERILLDAGLDVAAVSGVLTA FT SPLAAMEAQAQLATPVIGTFDLCQAEVAAALLPTR" FT CDS 525467..527080 FT /transl_table=11 FT /locus_tag="AARI_04900" FT /product="putative drug resistance ATP-binding protein" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TC 3.A.1.117.z. ABCISSE: ABC transporter, permease FT and ATP-binding protein (IM-ABC), DPL-family, antibiotic FT resistance or production (ARP) subfamily. Possible function FT in antibiotic resistance or production (export)" FT /db_xref="GOA:E1VSW7" FT /db_xref="InterPro:IPR001140" FT /db_xref="InterPro:IPR011527" FT /db_xref="InterPro:IPR017940" FT /db_xref="UniProtKB/TrEMBL:E1VSW7" FT /protein_id="CBT74720.1" FT /translation="MLDQKIAVAPPAQPGRLPALVAPGRRMLLAGLLSLGILAGLLSIA FT IGWLIGQLSASISLGALGAVLGLVACFFLAKYAERVLAEKLGQHYVAQLRRGLVTHALR FT SARGPSMGITIARSTNDLSSIRNWIVQGMVPLVAGLPLLAVSGAGLWFLHPLLALSLAA FT TLVLEGILLAALAGGTFLSARTLRRHRGNLASRIADTVAARTAIAAGGGVEREVQRVQD FT ASQKVIDASVHRARFAAALRGGALAIPLLGTALVVAAASMAQLPAAAMATALTLMGICA FT GTLGEWGRVVEYRQNYKAGRRIIAPLLAEQDRWQAREETPASTRDAKELMLQPSSVRIQ FT VPAGMADQFSTLRAQPGERIALRGSQSQCAALLSAIATGSLVHGADPQAGVWIAEGRSE FT DLPATGRRKLVGSALDSMVPERGSVARALRYRHPGASLRKAVALAETCGLKMADLPGGE FT ETRLRRGGEPLNSAQQASLLVARALLREPPLLVVDSLLARLPDDAYGDVAELLNGYPGV FT LLFSAGLPGIKETASWESQA" FT CDS complement(527077..527688) FT /transl_table=11 FT /locus_tag="AARI_04910" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00440: bacterial regulatory proteins, FT tetR family" FT /db_xref="GOA:E1VSW8" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:E1VSW8" FT /protein_id="CBT74721.1" FT /translation="MTTPTGQRRRVRATDSKEKLFEAAMKLLGSRSPESVSVDEIAAAA FT GVSKGTVYYNFGSKNELVSQILSYGAHKLMGELARAASGEDPYLALRQMLEFSMDFVAN FT YPSFAHLWMQEQLNADTTNALADTPLHTQVTGLIIEVLERLVVLEPDQKLSVATSIFGA FT ALFTARMRASGRTGLDREQTVRAVLLTVDGLRPTRPAAGS" FT CDS complement(527685..530015) FT /transl_table=11 FT /locus_tag="AARI_04920" FT /product="PIP family transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TC 9.B.74.y.z. The phage infection protein (PIP) FT family is a putative transport protein family. Identified FT by match to protein domains TIGR03061 and TIGR03062" FT /db_xref="GOA:E1VSW9" FT /db_xref="InterPro:IPR013525" FT /db_xref="InterPro:IPR017500" FT /db_xref="InterPro:IPR017501" FT /db_xref="InterPro:IPR023908" FT /db_xref="UniProtKB/TrEMBL:E1VSW9" FT /protein_id="CBT74722.1" FT /translation="MTTLRLALSELKRMSRGTLPKLALIAVTCVPLLYGALYLYANWDP FT QGNLDKVTAAVVNLDEGAEQDGERTRVGDDVVEELEDDGTFSWAHLDSKTEAEQAVATG FT QYAFALILPEDFSAALVSPGDFEDAEQANIELLTNDANNFMVSNFAKTLATTVRTSVAE FT EVGTETASAMIAGFVDIHDSMGEAADGAGQLYDGTLRLGDGVVTLTDGTTKLVDGSTEL FT NSGTKTLKDGTAELSGGLGKLVDGQTQLRDGSAELATGTAQLADGSKELSDGLHTLKTK FT TQALPGSVSKLDKGAASAKKAADQLAAGSQQVADGNQQLASTADDAIAVIDQLQANTKT FT QLDSVKADTQQRLDQLVSSGALTQEQADSIQSTVSQSVENSTLSNALDNKVTQVNTELS FT TLQTQLHTLADGSAQVAEGNQQLATGLGTLADGTKALDNAMPALVKGIDSAAQGSAKLA FT SGAAEANTGAKTLAKGQQAALNGATDAADGASQLDHGAGTLLAGTGSLHDGLVQLSDGV FT GELSDGTHDLQEGSDELATGLKDGTGKVPNPDKSTSERLADVMGNPVAVSNSKQAEAQA FT YGGGLAPFFMTLATFIGVLILTQVMRPMTKRALASNGSNWKISIGGWLPFAAIAVLQTS FT LLYAVVRFGLGLHAAHPWLIWALLACSALCFSALIQGCFALLGTAGKFVVLVLMVLQLV FT TSGGTFPWETLPDSLHLLHRILPMSNVVIGMRHLMYGADLGVLPSVAGSLLLYTAIGLA FT LSMLAVRKNKTWSLKTLQPELKE" FT CDS complement(530019..530801) FT /transl_table=11 FT /locus_tag="AARI_04930" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSX0" FT /protein_id="CBT74723.1" FT /translation="MLTADSITVKGRHDQLVAPTSVQLQRGELQLLVAEPQISRTALAL FT VLSGRMEPSSGVVAWNADPKMRSLRRHSALVDSPGINEPESHLKVRDLVAEDLGLIPGP FT SWRKPGARKWMAQHGFGDIANCWIDAIDPGRLFELQLLLAAENPCLELLIVDSPDRHDL FT EDEHWLETLENFASSHREFAVLAIVSRPPRHWDQQTGQADAPEPAALQLSDPSTGFIQE FT ELDLGLDPLAVNEDSPENHDIFLPADELADAVQCEAKE" FT CDS 531023..532939 FT /transl_table=11 FT /locus_tag="AARI_04940" FT /product="putative extracellular nuclease" FT /function="3 Information pathways" FT /note="match to PF03372: FT Endonuclease/Exonuclease/phosphatase family. This large FT family of proteins includes magnesium dependent FT endonucleases and a large number of phosphatases involved FT in intracellular signalling. Signal peptide predicted by FT SignalP 3.0 HMM (probability: 1.000) with cleavage site FT probability 0.974 between position 28 and 29" FT /db_xref="InterPro:IPR005135" FT /db_xref="UniProtKB/TrEMBL:E1VSX1" FT /protein_id="CBT74724.1" FT /translation="MINRRPTRIAAAVLGTALAVSSFSVAHADTAEITPIEQIQGTGGS FT SPMAGQDATVRGAVTGAYAEGGFRGFYVQSAGSGVDPSGQASSAIFVYAPDEVSSVNVG FT DHVQVSGEVSEYYGLTQLKAGSVAVLDEPAESVKPLAIPLPSSDAERERFESMLIEPQG FT EFTVSDNYSLNQYGELSLAMGTSEILPGERLLRQPTDVFRPGSAEAEALAAENEQRSIV FT VDDGATLNFATSKNKQIALPYIDAQQRVTVGADATFIAPVILDYRYDTWRLQPQGQVVG FT ADDGDIAVNFEQLESDAPQEVGGNVSVGSFNVLNYFTTTGDMLDGCSYYTDREGNPINV FT RGGCDARGAATAESFERQQSKIVSALGEFTADVVVLEEIENSARFGQNRDAALANLVNE FT LNEEAGDEVWSYVPTPSVVPADEDVIRTAIIYRDKAVKPIDESVILDDPAFSNARDPLA FT QAFQRVGGNQNTRFLVVANHFKSKGSNPDDGSGNADKGDGQGAWNVARVAQAEALVGFA FT DELKKLRNTDQVLLAGDFNSYAAEDPMQVLIEAGYVDLGAAADSQSYLYDGFVGSLDHI FT FASEKLAGKVTGEDIWNINAIESVGYEYSRYNNNITNLFTADQYRSSDHDPVLVGLQLD FT KKN" FT gene 533267..533515 FT /pseudo FT /locus_tag="AARI_04950" FT /product="truncated sugar ABC transporter, FT substrate-binding protein" FT /note="N-terminal section of a sugar ABC transporter, FT substrate-binding protein. Carbohydrate uptake transporter- FT 1 (CUT1) family (TC 3.A.1.1.z)" FT gene 533551..534594 FT /pseudo FT /locus_tag="AARI_04960" FT /product="truncated sugar ABC transporter, FT substrate-binding protein" FT /note="C-terminal section of a sugar ABC transporter, FT substrate-binding protein. Carbohydrate uptake transporter- FT 1 (CUT1) family (TC 3.A.1.1.z)" FT CDS 534691..535854 FT /transl_table=11 FT /gene="bglA" FT /locus_tag="AARI_04970" FT /product="cellobiose ABC transporter, inner membrane FT subunit BglA" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="identified by similarity to protein SP: Q9LAV7 FT (Thermobifida fusca). TCDB: ATP-binding cassette (ABC) FT superfamily, carbohydrate uptake transporter-1 (CUT1) FT family (TC 3.A.1.1.z). ABCISSE: ABC transporter, permease FT (IM), OSP-family (oligosaccharides or polyols), cellobiose FT import" FT /db_xref="GOA:E1VSX2" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VSX2" FT /protein_id="CBT74725.1" FT /translation="MSTTTHDAPEQDRDASAPSPQPQRWNKGNNAPAGAKPAETRDERK FT TRRRHLRGRWDFKYSPYLYISPFFILFGLVGLFPLIYTFVVSINDWDLLGGAGAWIGLE FT NYKAELTSPLFWNSLFNTYSIFLLSAIPQLVIATFIAAMLDQNIRAKTFWRMSVLVPYV FT VTPVAVTLIFSSAFDEQYGVLNNLLAAVNIDPIAWKTEVFPSHMAIATMVNWRWTGYNA FT LILLAAMQAVPRELHESAAIDGAGVIRRFFSITLPSIRPTMIFVIITATIGGLQIFTEP FT KLFNPSSSVPGGPDRQYQTTVLYLWDLAFNRGDFGRASAVAWILFLIIIVIGVINFLIS FT GSIASSADKKCAGSTGRTRAARRAAARAEAKAAKPANGTQSGSAANE" FT CDS 535862..536734 FT /transl_table=11 FT /gene="bglB" FT /locus_tag="AARI_04980" FT /product="cellobiose ABC transporter, substrate-binding FT protein BglB" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="identified by similarity to protein SP: Q9LAV6 FT (Thermobifida fusca). TCDB: ATP-binding cassette (ABC) FT superfamily, carbohydrate uptake transporter-1 (CUT1) FT family (TC 3.A.1.1.z). ABCISSE: ABC transporter, binding FT protein (BP), OSP-family (oligosaccharides or polyols), FT cellobiose import" FT /db_xref="GOA:E1VSX3" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VSX3" FT /protein_id="CBT74726.1" FT /translation="MERPARQVRAPQRRGKNFSMDRRPGFLTYGILLAFLIGSTYPLWY FT SFVIGSSTGAVFASAYPPLLPGGQFWTNVAEVLDSVDFWAALGNSIIVSSVITFSVVSF FT STLAGYAFAKLRFRGRQGLLVFVIATLAVPTQLGIIPMFMMMKQFGWTGSLGAIIIPTL FT VTAFGVFFMRQYLVENIPDELIEAARVDGASMIGTFWHVGVPAARPAMAILSLFTFMTA FT WTDYLWPMLVAPQNPTLQVALSQLQSARYVDYTIVMTGALLATIPLLVLFILAGKQLVS FT GIMAGAVKG" FT CDS 536734..538152 FT /transl_table=11 FT /gene="bglC" FT /locus_tag="AARI_04990" FT /product="beta-glucosidase BglC" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="3.2.1.21" FT /note="identified by similarity to protein SP:Q9LAV5 FT (Thermobifida fusca). In Thermobifida fusca, bglC is most FT active against cellobiose" FT /db_xref="GOA:E1VSX4" FT /db_xref="InterPro:IPR001360" FT /db_xref="InterPro:IPR013781" FT /db_xref="InterPro:IPR017736" FT /db_xref="InterPro:IPR017853" FT /db_xref="InterPro:IPR018120" FT /db_xref="UniProtKB/TrEMBL:E1VSX4" FT /protein_id="CBT74727.1" FT /translation="MMNHLSQKFAWPKEFLWGSATAAAQIEGAGHSYGKEDSVWDAFAR FT KEGAIAGGENLEVAVDHYHRYRDDVQLMRELGLDSYRFSTSWARVVPGGRNVNPEGLDF FT YSRLVDELLENGILPWLTLYHWDLPQALEEHGGWTNRETSYKFVEYAEAVYEKLGDRVK FT HWTTFNEPLCSSLIGYAAGEHAPGRQEPEAALAAVHHQHLAHGLATSRLRELGAEQIGI FT TLNLTNAVPNDPTDPVDLEAARRIDALWNRMYLDPILRGSYPEDLLEDVKGLGLAEVIE FT PGDLEIIAQPIDFLGVNHYHDDNVSGHPLPAGQPEAVVPTDSPKSSPFVGSEYVTFPAR FT DLPRTAMGWEVNPEGLRVLLNRLNQDYGNIPSLYITENGASYTDTVTEEGTAEDTEREE FT YILNHLDAVARAMQDGVDIRGYFVWSLLDNFEWAWGYAKRFGIIHVDYQSQVRTIKNSG FT RTYAGLIAANRTMA" FT CDS 538247..539266 FT /transl_table=11 FT /gene="celR" FT /locus_tag="AARI_05000" FT /product="LacI-family transcriptional regulator CelR" FT /function="3.5.2 Transcription regulation" FT /note="identified by similarity to protein SP:O87590 FT (Thermobifida fusca). In Thermobifida fusca, CelR Binds to FT the 14-bp operator sequence 5-TGGGAGCGCTCCCA-3 in the FT upstream regions of cellulase genes; these operator FT sequences are modulated by cellobiose" FT /db_xref="GOA:E1VSX5" FT /db_xref="InterPro:IPR000843" FT /db_xref="InterPro:IPR001761" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VSX5" FT /protein_id="CBT74728.1" FT /translation="MSMHDARNPKPTLELVAEHAGVSRATVSRVVNGSDRVKPAARAAV FT ELAIRELNYVPNRAARSLAQGRTNSIALVIPENTAKFFADPYFAKVVQGAAQYLADTEF FT MLTLLLSTEADPVKTTRYLQGSNVDGALVLSHHADDRSYADLGSVLPMVYGGRTMSTDQ FT KDIYVVDVDNVAAARQATEVIIDRGRTKLAIIAGPQNMGAGLDRLIGFKQAVEEAGLEP FT VAIEIGDFTPASGRRIMRQLLDADVRVDGLFAASAQMGFGALQALGEAGMKVPEDISVT FT SVDDDSFARNSTPPLTTIAQNPERQGEIMAELLIKRINGEQVPAWSIVDTRLVLRASH" FT tRNA complement(539342..539418) FT /locus_tag="AARI_36470" FT /product="transfer RNA-Arg" FT /anticodon=(pos:539382..539384,aa:Arg) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT gene complement(539597..539839) FT /pseudo FT /locus_tag="AARI_05010" FT /product="truncated GNAT-family acetyltransferase" FT CDS complement(539984..540097) FT /transl_table=11 FT /locus_tag="AARI_05020" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VSX6" FT /protein_id="CBT74729.1" FT /translation="MPQIALPDQLRLRLLEVSDAKQVTGSYTRNRTHLEQW" FT tRNA complement(540156..540232) FT /locus_tag="AARI_36480" FT /product="transfer RNA-Arg" FT /anticodon=(pos:540196..540198,aa:Arg) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 540550..542382 FT /transl_table=11 FT /gene="pckG" FT /locus_tag="AARI_05030" FT /product="phosphoenolpyruvate carboxykinase (GTP)" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="4.1.1.32" FT /note="catalyzes the formation of phosphoenolpyruvate by FT decarboxylation of oxaloacetate while hydrolyzing GTP" FT /db_xref="GOA:E1VSX7" 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:E1VSX7" FT /protein_id="CBT74730.1" FT /translation="MSTSSDQNVISAAPTSHEKLASWVEEVAALTKPDRVYWVDGSAEE FT NDRLTAELVEAGTLVKLTDPNFPNSYAGFSDPKDVARVEERTFICSEKEEDAGFTNNWE FT DPVKMKSMLSGLFDGSMRGRTMYVIPFVMGPLDAEQPAYGVEITDSAYVVASMRIMAKI FT GDEVLRKMEAEKAFFVPALHSVGAPLEPGQEDVAWPCNEDKWIVHFPEERAIMSYGSGY FT GGNALLGKKCYSLRIASAMARDEGWLAEHMLILKLISPENKAYHIAAAFPSACGKTNLA FT LLDPTIEGWKTETLGDDINWMRIGKDGELRGVNPEYGLFGVAPGTGWSTNPNAMRAITK FT GNNIFTNVALTDEGGVWWEGMTDEAPAHLIDWLGNDWTPESGRVAAHPNSRFCTPIDQV FT DMLSADYYSPNGVKIDAILFGGRRKTTIPLVTEARSWTNGIFMGSTLSSETTAAAAGAT FT GQVRRDPMAMLPFIGYNAGDYLNHWDKISAKLNPEQMPKIFLVNWFRRTADGGFAWPGF FT GDNSRVLKWAVERIEGTADAKETVIGNVPTGDSLDLTGLDGFTAADVEAAVAVNKDEWA FT TEVEGIEEWYANFGDALPASLRAELDGLKARLGA" FT CDS 542551..543078 FT /transl_table=11 FT /locus_tag="AARI_05040" FT /product="PadR-like family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF03551" FT /db_xref="InterPro:IPR005149" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR018309" FT /db_xref="UniProtKB/TrEMBL:E1VSX8" FT /protein_id="CBT74731.1" FT /translation="MVLARLILGLLCLSPMTGYELKKHFDSSINHFWNADKAQIYRTLA FT QLVDKGYATVRTVAQSNYPDRQEHHITEEGRAALAQWLSSGAVQSPERDPFMGQVFFAA FT ELERDEIQDLLAERRQATQLILDDYLSQREGIDMRAAADRRSFLMAATLDHAIRQQAAE FT LEWLDAVLEYLP" FT CDS 543075..544157 FT /transl_table=11 FT /locus_tag="AARI_05050" FT /product="putative hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /EC_number="3.-.-.-" FT /note="match to PF00561: alpha/beta hydrolase fold. This FT catalytic domain is found in a very wide range of enzymes" FT /db_xref="GOA:E1VSX9" FT /db_xref="UniProtKB/TrEMBL:E1VSX9" FT /protein_id="CBT74732.1" FT /translation="MTSAKDQNKTPAKTVARDATDYPEVHPGRQHQSQRPAPTLVFLHG FT GNVGNWSWDPQVLAFGDYNILTLHLPAFGARFEETWDGMESAADDVAALIADEVSEGGV FT HLVGISLGGVIALHVAARHPELIESLMITGTPVTGVGQAAKAFQRMQLKLIGSEWFWRF FT QAGAYGMVDDERELFTEHGVKLKPENMRAIMDEMDPGGLPDKLSSYQGPMLALVGSKEP FT KLVQKSFEALRATLPQAITRVVPGMHHQWNIENPILFNSVLRKWVSETGLHQILVDPQA FT VKPGRAAKVASEEQEGAAAEGQQPDADKAAPPAQPSSQKKPGKIAGRLDPRRLDPKKFE FT FMKKPQPPAGKPDKSVDGDN" FT CDS complement(544225..545400) FT /transl_table=11 FT /locus_tag="AARI_05060" FT /product="putative flavohemoprotein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="flavohemoproteins from bacteria (e.g. Escherichia FT coli hmpA) and fungi consist of two distinct domains, an N- FT terminal globin domain and a C-terminal FAD-containing FT reductase domain" FT /db_xref="GOA:E1VSY0" FT /db_xref="InterPro:IPR000971" FT /db_xref="InterPro:IPR001221" FT /db_xref="InterPro:IPR008333" FT /db_xref="InterPro:IPR009050" FT /db_xref="InterPro:IPR012292" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:E1VSY0" FT /protein_id="CBT74733.1" FT /translation="MLSTKSFPVIEATLPIIAERISSITPNFYNRLFTAHPELLDGIFS FT RSNQKNGTQQQALAGSIAVFATYLVKYPETTPETMLARVAHKHTSLGVVEEQYPIVYKH FT LFDAIAEDLGDALTPEIAEAWTEVYWLMAHALIKIEKGLYAQQANAEIYTPWKLVKRTE FT TGVDSVSFSFEPADSTPATVAKPGQFVSVRMPMTDGVRQVRQYTLSDNIEQTDLRTITV FT KLDVNGEFSPAIHNDLKIGDVVELSNPYGDLVIENDGSPLVIATAGIGCTPSAAALQTL FT AANGSSRKITVLHADQEFGAWPLREQMLESISKLPEASISTWFERGELPEGLNAKSGYM FT NLTEALTEDAQVYLCGPLPFMHAARTQALEAGIPAERIHYEVFGPDVWPAA" FT CDS complement(545546..546004) FT /transl_table=11 FT /locus_tag="AARI_05070" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF02082" FT /db_xref="GOA:E1VSY1" FT /db_xref="InterPro:IPR000944" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VSY1" FT /protein_id="CBT74734.1" FT /translation="MKLSAFTDVCLRTIMVLATPGTGQLTSREISESVGVPYNHVAKAV FT LELRTLGILQVTRGRNGGAMLTGAALESSLGGLLRKLDKRTDIVDCSDHDAQSNCPLAG FT NCRLRAVFRQAREAFYASLDALKIQDICPTSPAAAFTALPFPTVRDIA" FT CDS complement(546082..546552) FT /transl_table=11 FT /locus_tag="AARI_05080" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSY2" FT /protein_id="CBT74735.1" FT /translation="MKLEELDEGVKDALNKVLGTALGVAREQLEEQGVFLPFAIALEPK FT EGEDEPELRLIAVPPTDDPEDPEADIDTEAMASDLMQVLNQQGTHFLAIAIASDVLLQE FT NDQDAIHIVAEHRVGAALAIVQPYTMPAEPGGEWVFEDPAAESAEALWANAL" FT CDS complement(546565..547989) FT /transl_table=11 FT /gene="manB" FT /locus_tag="AARI_05090" FT /product="phosphomannomutase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="5.4.2.8" FT /note="catalyses the following reaction: alpha-D-mannose 1- FT phosphate <=> D-mannose 6-phosphate" FT /db_xref="GOA:E1VSY3" FT /db_xref="InterPro:IPR005841" FT /db_xref="InterPro:IPR005843" FT /db_xref="InterPro:IPR005844" FT /db_xref="InterPro:IPR005845" FT /db_xref="InterPro:IPR005846" FT /db_xref="InterPro:IPR016055" FT /db_xref="UniProtKB/TrEMBL:E1VSY3" FT /protein_id="CBT74736.1" FT /translation="MSEEIDLKQSFKAYDIRGVVGENLNAEAIEAIGAAFVDVLSLSGK FT DVLVGGDMRPSSGEFAQAFARGATYRGANIIMLGLISTDELYFASGKLNAAGVVFTASH FT NPAQYNGIKMSKAGARPISSATGLFDIRDLAQQYLDEGLPVSGDVPQGSISERDVLADY FT AAYLRELVDLSSMRQLKIVVDAGNGMGGLTTPAVLGDTVLPGLPLEIVPLYFELDGTFP FT NHPANPLEPENLKDLQAAVLEHGADLGLAFDGDADRCFVIDERGLPLSPSAITALVAVR FT EIARVQAAGEQSPVIIHNLITSKAVPEFVTKSGGTPVMTRVGHSFIKAEMATQGAVFGG FT EHSAHYYFRDFYNADTGMLAAMHVLAALGEQQLPLSELGAEYEPYAATGEINSEVEDKA FT GATARVVAHFEGQPVDVLTMDGTTISASDGSWWFNLRPSNTEPFLRFNGEGRTAEIIEP FT IRDAVLAIVRETNVAN" FT CDS 548166..550286 FT /transl_table=11 FT /locus_tag="AARI_05100" FT /product="putative ATP-dependent DNA helicase" FT /function="3 Information pathways" FT /EC_number="3.6.1.-" FT /note="match to protein family TIGR00614: recQ family" FT /db_xref="GOA:E1VSY4" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR002464" FT /db_xref="InterPro:IPR004589" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014001" FT /db_xref="UniProtKB/TrEMBL:E1VSY4" FT /protein_id="CBT74737.1" FT /translation="MDGSTQVNLKTLALQKLRALVQNPDAQFHDGQYESISALVAERRR FT ALVVQRTGWGKSAVYFIASLLLREQGYGPTLIVSPLLALMRDQVAAAERAGVRAAAINS FT ANVLEWREILEKLQRDELDVLLVSPERLNNPSFREQQLPMLMQRLGLLVIDEAHCISDW FT GHDFRPDYRRIRDLIAQLPKGLPVLATTATANSRVVQDVAEQLGGGTEEVFTLRGTLAR FT DSLRLGVLRLASPRMQLAWLLSHINDFKGSGIIYTLTVSAAEDIARLLKDAGHEVAAYT FT GRTDLEERERLEQALKNNEVKALIATSALGMGFDKPDLGFVLHIGAPSSPVAYYQQVGR FT AGRGSINADVLLLPGPDDSEIWEYFATSSMPDQVRATQVLEALTRANGAMSVPALESAV FT NLRRSPLELLLKVLAVDGAVERVAGGWMRTDMPWVYDADRYKRVAQSRIHEQNLMVSYE FT NTRGCRMQFLTDALDDPKSAPCGRCDNCAGVWFDDHIPDDSKDSAQAALGRVGVPIEPR FT KLYPSGLDRLGHTLKGKIPVDEQVATGRALARLTDLGWGNRLRQVFADPTDNPIDKAMF FT DACVKVLAEWNWEERPVGVVAMPSNKRPQLITSLAQGLAEVGRLCYLGQLAYRAGGPQN FT GPGGNSAFRVAAVADAFELPPQLEELIANAPGPVLLVDDLVDSRWSMAMAGRALRIAGA FT PGVMPFTLGVAG" FT CDS 550317..551225 FT /transl_table=11 FT /locus_tag="AARI_05110" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VSY5" FT /protein_id="CBT74738.1" FT /translation="MEIIIWLVVLIAVIALGYFGLQALRKKNTAQIAEAISREAAQEAN FT AKLDDASRNSVYRNLAKGDVRGAVKDFRAATGESVKNCVIAVRSLDKYPQSAPAKELPS FT DDAQIKALSDKLEAQVEREDREAAGAADATPASADDTWVVPQEWSEQFGSLEEPSATHF FT KMAFELDGESREFSSEQLPPNEYDQLFSMLRDSNFEEAAKILHGYTDLPVDDLERMIAA FT SPMSGANANGNVADFRFEGQGPDGPVHFDAAELPESEREALFDAIADTDLDRMSEIIVR FT HTSLPEDIVQNMLRSFVKRDD" FT tRNA complement(551613..551704) FT /locus_tag="AARI_36490" FT /product="transfer RNA-Ser" FT /anticodon=(pos:551668..551670,aa:Ser) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(551768..553855) FT /transl_table=11 FT /locus_tag="AARI_05120" FT /product="prolyl oligopeptidase family protein" FT /function="3.10 Protein degradation" FT /EC_number="3.4.21.-" FT /note="identified by match to PF00326 and PF02897. Prolyl FT oligopeptidase family consist of a number of evolutionary FT related peptidases whose catalytic activity seems to be FT provided by a charge relay system similar to that of the FT trypsin family of serine proteases, but which evolved by FT independent convergent evolution" FT /db_xref="GOA:E1VSY6" FT /db_xref="InterPro:IPR001375" FT /db_xref="InterPro:IPR002470" FT /db_xref="InterPro:IPR004106" FT /db_xref="UniProtKB/TrEMBL:E1VSY6" FT /protein_id="CBT74739.1" FT /translation="MTEHVSDTATADAYSWLEGTHDEKALAWVRQHTERTEAELYDDAF FT RQSVQQINTVLDAQDRIPMVNKRGEHYYNFWRDSQHRLGLWRRTDWESYLTDEPQWEIL FT LDLDALALAEGREWHFAGSALLRPDNNEPYRRALVRLSPDGGDQVRIREFDLESKTFVQ FT DGFDLPVAKTQASWIDPDTLLVGTASSDQFTTRSTYASTLRKVGRGMDIEAAPIIFEVG FT KEHVAAFGYYDSTPGYQRIVTTDAIDFYNSKTGVFIDGVHRELQVPTDVSVSLHRQWVL FT FAPRTDWEHQGQLIPAGALAIASLEVFLDTGAVDQVVFTPDAHTALESLSFTANYLLLT FT VLHDVASQVRIIDLNAGFAQSEMPLEDRMLSVSVAAVDDEDQAHGDDYWMTITGFTTPT FT TLLRGQVGKQAVAIKKSPDRFDAQGFEVTQHFATSADGTRVPYFQVADRELEFDGMNPV FT LMDGYGGFQHSMTPGYAAAMGTGWLSHRTSDGRKPVYVMTNIRGGGEYGPDWHRAALRE FT NRHRAYEDFAAIAQDLVARGVTTRAHLAATGRSNGGLLMGNMIAGYPQLFGAISCGVPL FT LDMKRYTQLAAGHSWIAEYGDPDVPEDWKFLRTFSPVHRLSDQHHAADDYPASLIWTTT FT SDDRVGPSQARIMAAKMMDMGIENVRYHEPESGGHAGSTDNESTAKMLATSYEFLWRQV FT R" FT CDS 553912..555927 FT /transl_table=11 FT /locus_tag="AARI_05130" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSY7" FT /protein_id="CBT74740.1" FT /translation="MSTSTQNPKNEFNLAIVGAGPRGTSTVERLAHLANNLERTANRIN FT ITVFDPYRPGSGHVWSPKQSEHFLMNTPASFPTVAPERTSDEPGLSFRQFVALHGDGRR FT LSEEHARMLSQVEAGTYPSRALYGEYLEHVYDSSVALLAAHESFSVEHLAAEVIGVRPL FT GNGYQLDYRTAQGEGEAAQKTFDAVVLALGHQSAELNPWQKQLQEAAQQADATYLPPNV FT PADLDYSLFAESQPALIRGLGLNFFDGMAELTLGRGGLFRETGKEPGHRLEYIASGREP FT ELVVASRRGTPYWGKPVVEQFIPEEISLRYFDVPELIGQLAEARATNPAATLVFSRHIW FT PKLHRDILFAYYSTWAESCGAPEGFSAEEFIEQLDELLTAEHREGSQVWLGELRKFIAQ FT IPECEWLDVPKLAKPFDEVGFGSDAEYQQAVRDYLVDNARHSVGGLKDPLSCAIMTMNA FT GRMLIKELVVTGVIDEQSRIEEIQAHFEPLVEGLSSGPPLERIEQLLALSRAGLVSFIG FT PEPEFGFDEVSQMFTASSPWVDSEVYTARTMCEAMMPSNRVLQNDTQLIRQLLKDHVAR FT AHTWRNEEGESLPGSGFDVVGEPYRLVNNEGLAHRGIFVLGVQLSSAQWGTAIAAQAGN FT MKNPAAQTLHDAANVVNEVARLAGLQGKEALSAAQD" FT tRNA complement(555975..556062) FT /locus_tag="AARI_36500" FT /product="transfer RNA-Ser" FT /anticodon=(pos:556026..556028,aa:Ser) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 556113..557102 FT /transl_table=11 FT /gene="qor" FT /locus_tag="AARI_05140" FT /product="putative NADPH:quinone reductase" FT /function="4.6 Miscellaneous" FT /EC_number="1.6.5.5" FT /note="NADPH:quinone reductase catalyzes the following FT reaction: NADPH + quinone <=> NADP(+) + semiquinone. FT Quinone or similar compounds may act as acceptor" FT /db_xref="GOA:E1VSY8" FT /db_xref="InterPro:IPR002085" FT /db_xref="InterPro:IPR002364" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR013149" FT /db_xref="InterPro:IPR013154" FT /db_xref="InterPro:IPR014189" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VSY8" FT /protein_id="CBT74741.1" FT /translation="MNDVMKAYIYNGSGGPEILELVDRPVPSLASGEVLIKVEAFGLNR FT ADVQQRKGVYPPPPGASDIPGLEVSGRIVEIGDGVSGWKTGARVAALLAAGGYAQYVNV FT PAELLIEVPQSVSDIDAAALPEVAATVVSNLFVEGELAQGQTLLLHGGAGGIGSMAIQL FT AKAAGARVIVTASSAQKLEYCCALGAEEGINYREEDFAERVKEITQGQGADLILDVVGA FT KYLAQNLKSLAVGGRLVVIGLQGGAKAEANLGLLLAKRAQIIGTTLRARPVHEKEEIIR FT QTITRVIPLLEKGQLALNVTKTFDYSEVSSAHEYFDSGKHTGKIVIKV" FT gene 557423..558193 FT /pseudo FT /locus_tag="AARI_34490" FT /product="partial transposase of IS982 family" FT /function="4.5 Transposon and IS" FT CDS 558231..558422 FT /transl_table=11 FT /locus_tag="AARI_05150" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007423" FT /db_xref="UniProtKB/TrEMBL:E1VSY9" FT /protein_id="CBT74742.1" FT /translation="MATLFERLGQAKKFVDGVLGADKYQHYLEHHERNHPGAKPMTERE FT FWKDYTDWQEKNPEGRCC" FT CDS 558576..559025 FT /transl_table=11 FT /locus_tag="AARI_05160" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSZ0" FT /protein_id="CBT74743.1" FT /translation="MAFFSRLRAERAATRELGEGVWRRAHDRFQRSLDRVFQVVEGITD FT DQVYNELVKEANEMAVLLPTVRQLCCAAQRITPSNDDTIPQLTSAAHRSLTKAANDLAT FT TAQVIAMMRMQAEAGQPIDIEAVRHRAKLVEEDVSRAAQMLASSE" FT repeat_region 559107..559114 FT /rpt_type=DIRECT FT mobile_element 559115..560332 FT /mobile_element_type="insertion sequence:ISAar1" FT /rpt_family="IS1595 group ISSod11" FT repeat_region 559115..559138 FT /rpt_type=INVERTED FT gene 559227..559541 FT /pseudo FT /locus_tag="AARI_34500" FT /product="transposase of ISAar1, IS1595 family, ISSod11 FT group (pseudogene)" FT /function="4.5 Transposon and IS" FT gene 559546..559911 FT /pseudo FT /locus_tag="AARI_34510" FT /product="transposase of ISAar1, IS1595 family, ISSod11 FT group (pseudogene)" FT /function="4.5 Transposon and IS" FT gene 559915..560298 FT /pseudo FT /locus_tag="AARI_34520" FT /product="transposase of ISAar1, IS1595 family, ISSod11 FT group (pseudogene)" FT /function="4.5 Transposon and IS" FT repeat_region 560309..560332 FT /rpt_type=INVERTED FT CDS 560320..561162 FT /transl_table=11 FT /gene="dkgA" FT /locus_tag="AARI_05170" FT /product="putative 2,5-didehydrogluconate reductase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.1.1.274" FT /note="catalyzes the reduction of 2,5-diketogluconic acid FT to 2-keto-L-gulonic acid, a key intermediate in the FT production of ascorbic acid. Can also reduce ethyl 2- FT methylacetoacetate stereoselectively to ethyl (2R)-methyl- FT (3S)-hydroxybutanoate and can also accept some other beta- FT keto esters. Identified by similarity to protein SP:Q46857 FT (Escherichia coli)" FT /db_xref="GOA:E1VSZ1" FT /db_xref="InterPro:IPR001395" FT /db_xref="InterPro:IPR018170" FT /db_xref="InterPro:IPR020471" FT /db_xref="InterPro:IPR023210" FT /db_xref="UniProtKB/TrEMBL:E1VSZ1" FT /protein_id="CBT74744.1" FT /translation="MDTPFSELKFLDGNTIDQLGYGVWKVADADAEVVVGKAIDAGYRH FT IDTARIYGNEAGVGRAVAASNVPREELFITTKVWNSDQGFEKTMAAADASLQRLGLEYV FT DLYLIHWLQPKRGTYVDTWKALIQLQKDGKAKSIGVCNFTKEALEELYTETGVRPVINQ FT VETHPYFPQNELRSYEAEHGILHESWSPLGHGGELLSDPVLVDIAKKHDASVAQVVIAW FT HLAVGNVVIPKSTTDSRIVENFESLNVKLDEEDLAAIATLDRGAEGRISADPATADFE" FT repeat_region 560333..560340 FT /rpt_type=DIRECT FT tRNA complement(561363..561437) FT /locus_tag="AARI_36510" FT /product="transfer RNA-Thr" FT /anticodon=(pos:561403..561405,aa:Thr) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(561520..563037) FT /transl_table=11 FT /locus_tag="AARI_05180" FT /product="putative secreted peptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.-.-" FT /note="match to protein family PF08386. This is a C- FT terminal domain associated with putative hydrolases and FT bacterial peptidases that belong to MEROPS peptidase family FT S33 (clan SC). Signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.604 FT between position 25 and 26" FT /db_xref="GOA:E1VSZ2" FT /db_xref="InterPro:IPR000073" FT /db_xref="UniProtKB/TrEMBL:E1VSZ2" FT /protein_id="CBT74745.1" FT /translation="MMRLAAVGTALAMGLAGCSSSTADSQPEDAQSSQPAAKSSAPEGL FT ESFYTQELDWEMCGSIIECATIKVPMDYANPEGQSIDLALNRRAVDGATGNILVNPGGP FT GGSGLDMVSSTVPSMFSNDLQRAYNVIGFDPRGVGESSPVTCQSAAETDKGRQENLRAW FT VPEDQHEIIESTEDYAADCASNTGELLDHVDTVSAARDMDVIRAVLGDAQLDYLGVSYG FT TFLGATYADLFPQNVGRFVLDGAMDPSLPAAEVTLAQAVGFEKETDAWLASCLESDACP FT FTGTVEEAKVQLQQFFAQVENEPMTASDGRVVPIIDFVNGFVLPLYDDSSWSYLTDAMN FT AAINDADVDMILGFADLSADRQSDGTYASNSSDAFTAINCLDRPMDSSAETMQDEATEL FT MRMAPTLGKYLAYGSITCEAWDYDSTGTPEILDAPGSNEILVIGTVGDPATPYKWSEAL FT AKQLDNATLLTYEGHGHTAYGRSNECITKAVDEYLIDGKVPEAGTRC" FT CDS complement(563079..564233) FT /transl_table=11 FT /locus_tag="AARI_05190" FT /product="putative DNA polymerase III subunit delta prime" FT /function="3.1 DNA replication" FT /EC_number="2.7.7.7" FT /note="DNA polymerase III is a complex, multichain enzyme FT responsible for most of the replicative synthesis in FT bacteria. The beta chain is required for initiation of FT replication once it is clamped onto DNA. DNA polymerase III FT contains a core (composed of alpha, epsilon and theta FT chains) that associates with a tau subunit. This core FT dimerizes to form the POLIII complex. PolIII associates FT with the gamma complex (composed of gamma, delta, delta FT prime, psi and chi chains) and with the beta chain to form FT the complete DNA polymerase III complex" FT /db_xref="GOA:E1VSZ3" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003959" FT /db_xref="UniProtKB/TrEMBL:E1VSZ3" FT /protein_id="CBT74746.1" FT /translation="MIRPVFADLAGQERVISTLTAEVDRGNPTHAWLVTGPPGSGRTTA FT ARAFAAALQCTQTPAGCGQCANCKMVMNSEHPDVSFVSTDKFEYQIADVRHLITRAQES FT AGTGRWRIIIIEDADRMSERSTNVLLKAIEEPPAKMIWILCAPSPADVLVTIRSRCRAV FT NLSVPAAQDVADLLVRRDGLEPEQAMFAARVSQSHIGVARLLARDEQARIQREKVVTLP FT LRTTTLPQAMAAAAEISKLASERAENITGTDLQNKIAQLRHANGLGLEENIPAGLRGQF FT KALEDDAKRFARRTAFDALDRTLTDLTTFFRDVLSIQLHADIELINEHLREKLERFAAA FT QSSEKSLAQLDAINETRSRLAANVNQLMALEALMTRLLPQPGRR" FT CDS complement(564230..564883) FT /transl_table=11 FT /gene="tmk" FT /locus_tag="AARI_05200" FT /product="dTMP kinase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.7.4.9" FT /note="catalyzes the phosphorylation of thymidine 5- FT monophosphate (dTMP) to thymidine 5-diphosphate (dTDP) in FT the presence of ATP and magnesium" FT /db_xref="GOA:E1VSZ4" FT /db_xref="InterPro:IPR018094" FT /db_xref="InterPro:IPR018095" FT /db_xref="UniProtKB/TrEMBL:E1VSZ4" FT /protein_id="CBT74747.1" FT /translation="MSIESSAPTRGLFIVFEGGDGAGKTTQVAMAQQWLESRGATVRTT FT REPGGTQISEELRSLVLEHGHGEIDARTEALIYSAARAAHVQQVIRPSLEAGTHIICDR FT FVDSSLAYQGMGRELGFAAVASINDFATGGLKPDVTIILDISAEHGRARRIAASGGVED FT SDRLEAEPDDFHERIRNAFLELAAQDPQRYLVLDATASVEQLHQSIVEHLAGLL" FT repeat_region complement(564970..564977) FT /rpt_type=DIRECT FT repeat_region complement(564978..565001) FT /rpt_type=INVERTED FT mobile_element complement(564978..566194) FT /mobile_element_type="insertion sequence:ISAar1" FT /rpt_family="IS1595 group ISSod11" FT gene complement(565012..565395) FT /pseudo FT /locus_tag="AARI_34530" FT /product="transposase of ISAar1, IS1595 family, ISSod11 FT group (pseudogene)" FT /function="4.5 Transposon and IS" FT gene complement(565396..566082) FT /pseudo FT /locus_tag="AARI_34540" FT /product="partial transposase of ISAar13, ISL3 family" FT /function="4.5 Transposon and IS" FT /note="pseudogene" FT repeat_region complement(566171..566194) FT /rpt_type=INVERTED FT repeat_region complement(566195..566202) FT /rpt_type=DIRECT FT CDS 566256..567413 FT /transl_table=11 FT /gene="metB" FT /locus_tag="AARI_05210" FT /product="cystathionine gamma-synthase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.5.1.48" FT /note="catalyzes the conversion of cysteine and succinyl- FT homoserine into cystathionine and succinate. Several other FT reactions may also be catalysed in some organisms" FT /db_xref="GOA:E1VSZ5" FT /db_xref="InterPro:IPR000277" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:E1VSZ5" FT /protein_id="CBT74748.1" FT /translation="MNPRNADSARTPAWDPKTLLVAGGRPAHGYDAPVNHPVTFTSTYH FT SKGQAAPGERVYARFSNPTWDPFEQVLGELEAATLPALVFSSGMAAIAAALSIVPEAGV FT LVMPRHSYNGSLALSSELQEAGRLSIRPVDIANTEEVLAALDGADVLWVESPTNPMLEV FT ADLPALLAAAKAKNTVSIVDNTFATPLLQQPLNHGADLVVHSVTKYLSGHSDVIMGALV FT TSDEQLHSRLHGYRTLHGAIAGPMDTFLALRGVRTMSVRIDRSQSNSQVLAERLADHPK FT VQAVRYPGLPSDPGHERAAKLMGGFGSVIALEAGSSAQEADRVLDALKLITGATSLGGV FT ESLAERRARHASEPASVPASLIRLSVGIEDVEDLWADLDQALEQL" FT CDS 567485..567802 FT /transl_table=11 FT /locus_tag="AARI_05220" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR019662" FT /db_xref="UniProtKB/TrEMBL:E1VSZ6" FT /protein_id="CBT74749.1" FT /translation="MNMMYAAQLIEYYLMIALSVVIVALAVWALVDCLRRGADRFAQEG FT KRTKGFWLGMTVASTAVALLGVFSQGGIGFLQLIGACIACVYLADVKPAVSGKGGGWYN FT Y" FT CDS 567935..568681 FT /transl_table=11 FT /gene="gpmA" FT /locus_tag="AARI_05230" FT /product="2,3-bisphosphoglycerate-dependent FT phosphoglycerate mutase" FT /function="2.1.2 Main glycolytic pathways" FT /EC_number="5.4.2.1" FT /note="catalyzes the interconversion of 2-phosphoglycerate FT and 3-phosphoglycerate" FT /db_xref="GOA:E1VSZ7" FT /db_xref="InterPro:IPR001345" FT /db_xref="InterPro:IPR005952" FT /db_xref="InterPro:IPR013078" FT /db_xref="UniProtKB/TrEMBL:E1VSZ7" FT /protein_id="CBT74750.1" FT /translation="MSHTLILLRHGQSEWNEKNLFTGWYDVSLTEKGRAEAARGGQLLT FT EAGYKPEVLHTSLLTRAIVTANLALEAAGRSWIPVNRDWRLNERHYGALQGKDKAQTLA FT EFGEEQFMEWRRSYDTPPPALDDSSEFSQINDERYAALGDSAPRTECLKDVLDRMLPYW FT ENNIKADLSAGKTVMVTAHGNSLRALVKHLDGISDEDIAGLNIPTGIPLVYELDDNFQP FT ITRGGTYLDPEAAADAIKAVANQGRK" FT CDS 568880..569182 FT /transl_table=11 FT /locus_tag="AARI_05240" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VSZ8" FT /protein_id="CBT74751.1" FT /translation="MATDYDEVRPDVAEARKASLDAVKSANAPDAKSVVRELDETDHTD FT GMDLPGADLSNEELTVTVVPQKDDEFICGSCFLIRHRSQLVREEGNVGFCVECEG" FT CDS complement(569427..570080) FT /transl_table=11 FT /gene="phoU" FT /locus_tag="AARI_05250" FT /product="phosphate transport system regulatory protein FT PhoU" FT /function="2.6 Metabolism of phosphate" FT /note="probably involved in phosphate transport and/or FT metabolism. Identified by match to PF01895" FT /db_xref="InterPro:IPR008170" FT /db_xref="UniProtKB/TrEMBL:E1VSZ9" FT /protein_id="CBT74752.1" FT /translation="MRKVFQADLQQIGEELIEMANQVAVAMDRAWDSLATVDVDLAQEV FT IAADAKIDFLQNQLDERAIDTLALQGPVASDLRMIVGSLRMSASLERMGDLARHLAQLT FT RLRFPNPAIPEKISGTFAQMAKIDIDIAKAVARLLDTRDLQIATEIIELNHELDRLHSS FT VFTQVAADDWDSNAPTTVDVSLTSRYLERFGDHGVSVARKVTYLVTGEWDPTEI" FT CDS 570317..571522 FT /transl_table=11 FT /locus_tag="AARI_05260" FT /product="signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VT00" 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="UniProtKB/TrEMBL:E1VT00" FT /protein_id="CBT74753.1" FT /translation="MISTLIAGILGLALGIVGIIAFRLSQARSSRLPQVDEPVLPEGAA FT AVLSVIGRAFVILDDVDGVVRANPASYAYGLVRGHTLVHNELLTLVRQVRADGVIAESQ FT YELQRSTLGAGQLIVHVRVAPLGDEYILLLADDRTEITRTEAMRNDFVANVSHELKTPV FT GAIGLLAEAITEAADDPKAVRRFSTRMDKESRRLAALVQDIIELSRLQASDAIVQGQEV FT NVDSVVAEAVDRNHLIAEEKGITITVGGHLDEPILGDADLLMTAIRNLIDNAVRYSPEN FT TTVGVGIRQRDGYAQISVTDQGPGISAEEQERVFERFYRVDSARSRQTGGTGLGLSIVK FT HVLANHGGEVSLWSQPGHGSTFTIRLPLADEEPATSNAPAGPKMKERTIEDSASDREGG FT RR" FT CDS 571519..572199 FT /transl_table=11 FT /locus_tag="AARI_05270" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VT01" 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:E1VT01" FT /protein_id="CBT74754.1" FT /translation="MTRILIVEDEESLSDPLSYLLEREGFEVRIADDGLKAVTEFERHG FT ADLVLLDLMLPGQPGTEVIRQIRLNSQVPVIMLTAKDSEIDKVVGLELGADDYVTKPYS FT SRELLARIRAVLRRQGEGEELISNVVTAGPVRMDVERHVVSVENTEVSMPLKEFELLEM FT LLRNAGRVLTRGQLIDRVWGSDYVGDTKTLDVHVKRLRSKIEADPAVPERLVTVRGLGY FT KFVV" FT CDS complement(572284..572823) FT /transl_table=11 FT /locus_tag="AARI_05280" FT /product="conserved hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.991) with cleavage site probability 0.479 FT between position 35 and 36" FT /db_xref="UniProtKB/TrEMBL:E1VT02" FT /protein_id="CBT74755.1" FT /translation="MITARMTAGRRIAASLAVAALAFGVTSCGAINEQATNTDYAASDG FT VNVDVADAKVRNLMFVTNSDDTQARLIGTVVNAGDSALTLSVKAESASPVSIPVPADGT FT VKLEDDENEQIIKNLGIRAGEHADSVFTVSGEEVEFSVPVVDGTLAEYRDFVPGGADAS FT VTEHLTPEETHSTSGH" FT CDS 573179..573664 FT /transl_table=11 FT /locus_tag="AARI_05290" FT /product="CarD transcriptional regulator-like protein" FT /function="3.5.2 Transcription regulation" FT /note="CarD is a Myxococcus xanthus protein required for FT the activation of light- and starvation-inducible genes" FT /db_xref="InterPro:IPR003711" FT /db_xref="UniProtKB/TrEMBL:E1VT03" FT /protein_id="CBT74756.1" FT /translation="MVFEVGETVVYPHHGAAMIEEIKMRKIKGEEKMYLKLKVAQGDLT FT IEVPAENVDLVGVRDVVGQEGLDHVFDVLRAEFTEEPTNWSRRYKANVEKLASGDVIKV FT AEVVRDLWRRENDRGLSAGEKRMLAKARQVLISELALAKDLDEAKAESLLDEVLASA" FT CDS 573769..575010 FT /transl_table=11 FT /gene="ispDF" FT /locus_tag="AARI_05300" FT /product="bifunctional 2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase/2-C-methyl-D-erythritol FT 2,4-cyclodiphosphate synthase protein" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.7.7.60" FT /EC_number="4.6.1.12" FT /note="bifunctional enzyme catalyzing non-consecutive FT reactions in the 1-deoxy-D-xylulose 5-phosphate pathway of FT isoprenoid precursor biosynthesis" FT /db_xref="GOA:E1VT04" FT /db_xref="InterPro:IPR001228" FT /db_xref="InterPro:IPR003526" FT /db_xref="InterPro:IPR018294" FT /db_xref="InterPro:IPR020555" FT /db_xref="InterPro:IPR023423" FT /db_xref="UniProtKB/TrEMBL:E1VT04" FT /protein_id="CBT74757.1" FT /translation="MKQSETQNSSLILVAAGMGTRLGAGIPKAMVHVAGKSLAQHAVER FT ILQVPQITEIIVVTPPNDNRLAATMEQYGAKVRTVPGGASRVASVRAGLAEASLAAANI FT LVHDAARAFTPAQIFAQVLEALSAKECSAVIPALKVTDTISVVERDAAGGHEIITQTPD FT RSTLRAVQTPQGFDAQLLRDAHAQLDTYTEAELDKVTDDASIVRAFGAKVQVVPGSQQA FT MKVTHPEDLDTASKLARPEAEANGAAKEENMILPRVGNGIDVHAVSEDPSRQMWLAGLH FT FPEDIGLSGHSDGDAVAHAACDALFSAAGIGDLGTHFGVDRPEFAGASGVSLIAEAARL FT VREAGFEIGNVAVQFVGRRPRFAARREEANKVLSDAIVAPVSVTATTSDGLGYEGEGKG FT VTAYATALVYPVSH" FT CDS 575098..576549 FT /transl_table=11 FT /gene="cysS" FT /locus_tag="AARI_05310" FT /product="cysteine--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.16" FT /note="activates cysteine and transfers it to tRNA(Cys) as FT the first step in protein biosynthesis" FT /db_xref="GOA:E1VT05" 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:E1VT05" FT /protein_id="CBT74758.1" FT /translation="MSLRFYDTKTASVRDFQPLAEGEVKLYYCGATVQGMPHVGHVRSA FT IVFDVLVRWLEYRGFAVTTVRNVTDIDDKILEKSANSFAEDFEADAHYRPREEWYALAY FT RFEQEFARAYEALGVRRPTYEPRATGHITEMHELISQLIERGHAYPAADDSGDVYFDVR FT SYEQYGALTRQKIDDMQDAPDSDPRGKKDPRDFALWKGLKDIDPPTASWPSPWGRGRPG FT WHLECSAMAGKYLGSEFDIHGGGLDLRFPHHENEMAQSNAAGHGFANFWMHNGMVTYEG FT EKMSKSIGNTISPEEMLALADARVVRYFLGQAQYRSMLDYRPDSLTEAGAAVERIDTFI FT SNARYRLGAAAEAIAATEVPEAFGTAMDDDLNVPMALAALHETVRLGNASRDSRDDAAT FT AKALGQVLAMTQVLGLDDAGSHESQDSSAEHAALDQLVQAQLAERAKARAAKDWARSDA FT IRDALGSAGITVADSADGARWTLDD" FT CDS 576600..577547 FT /transl_table=11 FT /locus_tag="AARI_05320" FT /product="putative RNA methyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.-" FT /note="identified by match to protein family PF00588: SpoU FT rRNA Methylase family. Possible role in rRNA modification" FT /db_xref="GOA:E1VT06" FT /db_xref="InterPro:IPR001537" FT /db_xref="InterPro:IPR004441" FT /db_xref="InterPro:IPR013123" FT /db_xref="UniProtKB/TrEMBL:E1VT06" FT /protein_id="CBT74759.1" FT /translation="MNKKGPTKGSGGKGRRSLEGKGPTPKAEDRPYHKAYRAKQLSERS FT AAKRSTGRQADRIKVNAEFVTGRNSVVEALRAGIPAKALHVAIRIDVDDRVRESLKLAA FT EQGIPLMEASKPELDRMTDAAIHQGMALQIPPYEYKDAVQLATKAIKDFDKGYTKTQPL FT FLALDGITDPRNLGAIVRSASAFGADGVIIPERRSVGMTASAWKTSAGAAVRVPVAKCN FT NLTSALKEIKAAGIFVIGLDAGGDMDLPNFELATGPLCIVVGSEGKGLSRLVRENCDAI FT VSIPIDSAMESLNASMAVGISLYEVSRLRAEQAK" FT rRNA 578113..579631 FT /locus_tag="AARI_36520" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 580265..583387 FT /locus_tag="AARI_36530" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 583544..583659 FT /locus_tag="AARI_36540" FT /inference="ab initio prediction:rRNAScan:1.0" FT CDS 583851..584060 FT /transl_table=11 FT /locus_tag="AARI_05330" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT07" FT /protein_id="CBT74760.1" FT /translation="MVEKASHLSAGSAIASIVFAVIAIGIALLTLNIPSTSIRVLLIVV FT AIALIAAAGAATAITLRRIKQPKN" FT CDS 584530..585906 FT /transl_table=11 FT /locus_tag="AARI_05340" FT /product="FAD linked oxidase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF02913 and PF01565" FT /db_xref="GOA:E1VT08" 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:E1VT08" FT /protein_id="CBT74761.1" FT /translation="MSDAYSDLVETLRRELPEDSIVLSDSVLRENSRDFGQISGEPVMP FT LAVVFPTEVGHVQAVMRVATANRIPVISRGAGTGVSGGVHVQGDAVILNLSKMDKIIEI FT RPHDEVAIVEPGVINHHLNTAVAQFGLMYAPDPASYKMSTIGGNIATNAGGLRCAKYGV FT TRESVLSLDVVLADGRLIRVGKNTFKGVAGYDLAALFTGSEGTLGVVVRAFVRLRYLPV FT DERDLSMVFPSLEAAVEGVQQIAKSRIQPAILELIDYSTICVLDQQYSTDYASLGGAML FT LVRLDGYGAEREEAAVRDAFMSSDVQLSKSGDAAATRLIEMRRTSRGDTKDDAYRTGED FT VAIPKSRMVEYVHRLQDLAREENVNMRMISHAGDGNLHPTFFVDPTEGEQLLARLHRAV FT EGSVKEALALGGTITGEHGVGLIKKDWLAWEQSDEVLQLQHQIKALLDPLNILNPGKAI FT " FT tRNA 586015..586091 FT /locus_tag="AARI_36550" FT /product="transfer RNA-Pro" FT /anticodon=(pos:586049..586051,aa:Pro) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 586292..586927 FT /transl_table=11 FT /locus_tag="AARI_05350" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT09" FT /protein_id="CBT74762.1" FT /translation="MEQPEHHHSSNEDGLNNEALPSDAQAFMRLRRHIQHLGSAVRRLV FT MQDGDIAMDADNKNLRTRPSRFLGGNKAVSQDQREFDRPEVSNLTIEDMAKSVFLAALE FT RAKPWRLVAAGELDPGILDIPESLQDYMRSDDGLALLEFWHETLHGSFDGDFREFEGWI FT LSGRNFDSSESSGLLELADLIDGWIAYLRKLMLQGTQAEGQNDDLGSN" FT CDS complement(587613..588047) FT /transl_table=11 FT /locus_tag="AARI_05360" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="GOA:E1VT10" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR012287" FT /db_xref="UniProtKB/TrEMBL:E1VT10" FT /protein_id="CBT74763.1" FT /translation="MVEVLAGYSKQAHRKMDRLSTAARALQRLKSGEIRPRASQSERHS FT RRYRIADRFSSDELVAIGQRYQAGEQSTDLAKEHGIAKSTLLRLLAERGIQTRQRGLTP FT AKEREILRLRKQGFIIRDIAQRVGCSYDTARKFLLTASNA" FT tRNA 588321..588392 FT /locus_tag="AARI_36560" FT /product="transfer RNA-Gln" FT /anticodon=(pos:588354..588356,aa:Gln) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 588441..588516 FT /locus_tag="AARI_36570" FT /product="transfer RNA-Glu" FT /anticodon=(pos:588475..588477,aa:Glu) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT repeat_region complement(588628..588634) FT /rpt_type=DIRECT FT repeat_region complement(588635..588661) FT /rpt_type=INVERTED FT mobile_element complement(588635..589974) FT /mobile_element_type="insertion sequence:ISAAr5" FT /rpt_family="IS256" FT CDS complement(588703..589902) FT /transl_table=11 FT /locus_tag="AARI_34550" FT /product="transposase of ISAar5, IS256 family" FT /function="4.5 Transposon and IS" FT /db_xref="InterPro:IPR018289" FT /db_xref="UniProtKB/TrEMBL:E1VT11" FT /protein_id="CBT74764.1" FT /translation="MGIESISVKLTGQSHTCIICHSRLKKNGTTSKGTQRWRCITCNAS FT TVFKREDTTARNQLTGFVSWLMSKHSQAEFGGGTGRTFRHQTAWCWNVHPYLHHTGEVF FT DEIQVDGIYLRQGWCLLIAIAHGRVIGWQWCDREKAEAWTVLLQHFPEPKVAVTDGGSG FT LMKALKEFWPNVKIQRCLVHIQRNVRTYLTLNPRLPAGKSLRRLSLKLTKIRTQEAAAE FT WIAAFAAWHAENHELINERTYAADWSGAWPRGLRRNRKWWYTHDRLRSAYESMNKALRR FT GHLFTYLDKDLNGLGINATTNMIEGAVNSGIRAMIFYHRGMPIEHRRRACEWFCWTHAD FT EGNRPALRTLLRPEHYTPEAKKKAQHMVDEAPIGPELYGTGPSAEDGQFIRSGWMRNIY FT " FT repeat_region complement(589948..589974) FT /rpt_type=INVERTED FT repeat_region complement(589975..589981) FT /rpt_type=DIRECT FT rRNA 591247..592765 FT /locus_tag="AARI_36580" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 593399..596521 FT /locus_tag="AARI_36590" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 596678..596793 FT /locus_tag="AARI_36600" FT /inference="ab initio prediction:rRNAScan:1.0" FT CDS 597118..597414 FT /transl_table=11 FT /locus_tag="AARI_05370" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VT12" FT /protein_id="CBT74765.1" FT /translation="MLFMSFLASIGLVASTFLLGLFFAGLHETRAESESTSTTSVAFTA FT LVMLFVAVCAAFILVEPALINPLWLQYTLMAGAPLVVGYAMRRALARSMDRSQ" FT CDS 597710..598492 FT /transl_table=11 FT /locus_tag="AARI_05380" FT /product="putative dehydrogenase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VT13" FT /db_xref="InterPro:IPR001509" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VT13" FT /protein_id="CBT74766.1" FT /translation="MRTYVVTGAASGIGAATAELIRERGHKVIGVGLRDADVTADLSTA FT EGRQSAVSRTLELSEGKIDAVIAAAGISAPKAVTVAVNFFGVTNYLEGLLPALAQAQSP FT RVAVVSSMASIQQNSAELVEALLSGDEEQALAIGASLEAEGPRAGYLNYPSSKRALGRW FT VRRECITEKWAGAGIPLNAVAPGTVITNMTRELLSTDEGKAMVDQNVPMPLNYHSEAVV FT IAKLLLWLTSEENTHVTGQTIYCDGGAEATLRGDDIWA" FT CDS complement(598883..599950) FT /transl_table=11 FT /gene="msiK" FT /locus_tag="AARI_05390" FT /product="cellobiose/maltose ABC transporter, ATP-binding FT subunit MsiK" FT /function="1.2.4 Transport/binding of carbohydrates" FT /EC_number="3.6.3.-" FT /note="identified by similarity to protein SP:P96483 FT (Streptomyces reticuli). In Streptomyces reticuli, MsiK FT assists the cellobiose and maltose ABC transport systems. FT TCDB: ATP-binding cassette (ABC) superfamily, carbohydrate FT uptake transporter-1 (CUT1) family (TC 3.A.1.1.z). ABCISSE: FT ABC transporter, ATP-binding protein (ABC), OSP- family FT (oligosaccharides or polyols)" FT /db_xref="GOA:E1VT14" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR008995" FT /db_xref="InterPro:IPR013611" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VT14" FT /protein_id="CBT74767.1" FT /translation="MATVTFEKATRIYPGALVPSVDAIDLEIQDGEFLVLVGPSGCGKS FT TTLRMLAGLEEVNSGRILIGDKDVTNVPPKDRDIAMVFQNYALYPHMTVAENMGFALKI FT AGVDKEERKKRVLEAAKLLDLEKYLDRKPKALSGGQRQRVAMGRAIVRSPQVFLMDEPL FT SNLDAKLRVQTRTQIASLTRRLGVTTVYVTHDQVEALTMGDRVAVLKDGELQQVGTPRE FT LYDRPRNVFVAGFIGSPAMNLVKLQSENGKIAFGSTLIDAPGSKGGTTLGFRPEDIELV FT GPGEGIELIVDVVEELGADAYIYGSAELAGETQVVVVRVDGRTPPARGQRINIAPDLQH FT AHMFDTESGLRLADA" FT CDS complement(600016..600795) FT /transl_table=11 FT /gene="otsB" FT /locus_tag="AARI_05400" FT /product="trehalose-phosphatase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="3.1.3.12" FT /note="synthesis of trehalose from trehalose-6-phosphate" FT /db_xref="GOA:E1VT15" FT /db_xref="InterPro:IPR003337" FT /db_xref="InterPro:IPR006379" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:E1VT15" FT /protein_id="CBT74768.1" FT /translation="MPELAPALHAALADFAAHERVLVALDFDGTMSPLVDRPQDARPLP FT ASAAAFEQLATSPGVYTAVVSGRNLQSLNQAYPEPRPEICIGSHGAERLLPEHLGALWH FT DEPLSTKQLQLLKELTGRLEQIAAAHANVTVEHKPSATVLHVRQAAPDTALKALAQAKS FT ALQQLDGVALLEGKAVLEATVHHGDKGQSLQWLREVLDVQAVLFVGDDVTDENGFKVLG FT SADLGIKVGAGPTVATYSIPSPAELPDLLNILIFMRH" FT CDS complement(600838..602301) FT /transl_table=11 FT /gene="otsA" FT /locus_tag="AARI_05410" FT /product="alpha,alpha-trehalose-phosphate synthase FT (UDP-forming)" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="2.4.1.15" FT /note="synthesis of trehalose 6-phosphate from UDP-glucose FT and glucose-6-phosphate" FT /db_xref="GOA:E1VT16" FT /db_xref="InterPro:IPR001830" FT /db_xref="UniProtKB/TrEMBL:E1VT16" FT /protein_id="CBT74769.1" FT /translation="MGIPALNPKTENSYDFVVVANRLPVDRITNPDGTQGFQRSPGGLV FT TALEPVMASSEGAWVGWHGGIGEELESFDKDEIHLVPVPLDEDDLSLYYEGFSNSTLWP FT LYHDVIVPPEYHRTWWDRYKKINQRFADAVLKIAAPNATVWVHDYQLQLVPQMLRLARP FT DLKIGFFLHIPFPAASLFSQLPWRTQILQGLAGADLVGFQRETDASNFLRCLRRFTGYS FT TKGDVATPPADSDMQNLCRANAHPISIDTKTIAKLSRDPQIIARAAQIRHELGNPKTIM FT LGVDRLDYTKGIRHRLKAYGELLTDQTLRAGDVCLIQVASPSRENVESYMELRDQVELM FT VGQITGQHDTLSHTTLRYLHQSYPLREMIAMYLAADVLLVTALRDGMNLVAKEFVAAHQ FT DGRGVLVLSEYTGAADQLPQAVLVNPHDIDGMKAKIVEAVQMNESEQERRMKRMNRQLA FT VNDVSKWSNDFLAALAEINAASSVHGSVR" FT CDS 602701..603567 FT /transl_table=11 FT /locus_tag="AARI_05420" FT /product="DSBA-like thioredoxin domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF01323" FT /db_xref="InterPro:IPR001853" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:E1VT17" FT /protein_id="CBT74770.1" FT /translation="MSTNNPRPSKAERTASAREKAAQMRAAQEAAAKRKSLFVKLGVLA FT AVIVVIALVVTLIVQNNNAKIEDSGAVPQGGTAAGGIMVTSADTVAEKTIDKVDIKKLE FT APDEAPAPATPRDLTVAEKGEPINIALYVDVNCVHCADFEATYGDQMQQWLADGKVTIE FT YRNVGYLDRGSATNFSSRAANALACVADESPAAYLGFVKALWGHYPEGEMKNAELADMA FT IQNGAAESVADCIDDDKFRPFVKYATTAGQYDGVAGTPSIFVQGKEVDLAKQDFPTAVE FT EAMAANK" FT tRNA 603741..603814 FT /locus_tag="AARI_36610" FT /product="transfer RNA-Thr" FT /anticodon=(pos:603775..603777,aa:Thr) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 603981..604931 FT /transl_table=11 FT /locus_tag="AARI_05430" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR008526" FT /db_xref="UniProtKB/TrEMBL:E1VT18" FT /protein_id="CBT74771.1" FT /translation="MAGGLAALLDDVAALVKVTAASLDDIALGAGKASTKALGVVVDDA FT AVTPQYVDGISPKRELPIIWKIAKGSLRNKLLFILPVALLLSTFAPWALTPILMLGGAY FT LVFEGAEKLMEAFGWIKHHGVELEGKDRDEKAIIGSAVRTDLVLSAEILVISLNEVADQ FT PFLMRTAILLVVAIMMTVVVYGAVGLIVKMDDIGLRLAAKPRELSQKIGRGLVKAMPIV FT MSVLSKVGVVAMLWVGGHLLLVGMDELGWHAPYGFVHHMELLVHDATGQAGAVLGWLVN FT TAFSCLAGFIMGTVITVIILGIKKLRHKGKAETAH" FT CDS 605042..606691 FT /transl_table=11 FT /locus_tag="AARI_05440" FT /product="putative site-specific DNA-methyltransferase FT (adenine specific)" FT /function="3.2 DNA restriction and modification (and FT repair)" FT /EC_number="2.1.1.72" FT /note="match to PF02384. This domain is found in N-6 FT adenine-specific DNA methylase from type I and type IC FT restriction systems. These enzymes are responsible for the FT methylation of specific DNA sequences in order to prevent FT the host from digesting its own genome via its restriction FT enzymes. Match to PS00092 pattern: N-6 Adenine-specific DNA FT methylases signature" FT /db_xref="GOA:E1VT19" FT /db_xref="InterPro:IPR002052" FT /db_xref="InterPro:IPR002296" FT /db_xref="InterPro:IPR003356" FT /db_xref="UniProtKB/TrEMBL:E1VT19" FT /protein_id="CBT74772.1" FT /translation="MLSKELNDQATARHARGAYFTPEPVASFMAQWALGQQGSRVLEPS FT CGEAQFLAAAHSVLDEQREQLDMLGLELHEPSVQAARQRMRAAGINARIEQANFFEVSG FT HGDFDAVIGNPPYVRYQLHRGADRQLSRAAAKASGVELNELASIWAAFVVHATSFLAVG FT GRLALVLPAELMFVNYAGPVRQMLLERFADVHLAVFEERLFADAQEEVVLLLAKGYREG FT ASGSFNLHQFRNAQDLQTLGEGVRHTPVRMSDRWTGSLAGLEAQGILATALAAGRMAPL FT QSWGETSLGAVTGNNKWFTLSAGQIHQLGLVREDLIRISPPGSRHLRGLELSEEDWEKL FT TEHGAATYMFRPAAEPSAAGARLVASGELQNVDQAYKCRVRSPWWRVPVLSVPDLFMTY FT MNADTPRLTANEAGVHHINSIHGVYLGADVRQLGRELLSVASLNTLSMLGAEMVGRSYG FT GGILKLEPREADQLPVPSIDLVQRHAKRLRSIKPTVRELLQQGRKQEATDLVDNVVLKQ FT MLGLDRAAVAAVHAARTSMLERRKARSKAVKG" FT CDS 606688..607620 FT /transl_table=11 FT /locus_tag="AARI_05450" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VT20" FT /protein_id="CBT74773.1" FT /translation="MNVANPVVEKTLAFAEFDTTLMSAAKDSPWLNNGAVTEAFNPSFS FT VLERLLSIPVRNKAVTRSGRFAQGVDAWLAHELRRAGFDADLVWPRPEAPRVLSSDILE FT LLRKLPERLADEVHESIMSGKAGSTDARILGRAYMKQTDVVMTHWSTGPELLLSTKAMT FT SSFGKNLANRYEEAYGDAANLRARYPLAAVGFFFVQRATILESEPAAFRRTVDMIRKLR FT DFGDGFGYTATGLLLVDWDDTAENPEVKCVHAPVPADIAAPQFLNAMVDAVLKVTPIDL FT HEAARARRAGEVAPLPGHDAVDEQQDALF" FT CDS complement(607625..608242) FT /transl_table=11 FT /locus_tag="AARI_05460" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VT21" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VT21" FT /protein_id="CBT74774.1" FT /translation="MFENLNFSLSSLCVQPAQRAELASLYTVVDQRWNQKFDRLSLLVT FT VRDQGTLVAAGLVHDSIVAPTSSMNAVELGCMAVRADYRRLGIRQHVTSLRLAHALRAG FT RTPISVIDSQNPASWAFYERSELWERERSFEHEGQLKFIYRATEAAWQWAAQLPQASED FT QVAIRLSQAPAPSAPFTLAPALAYPHAARYGSDDSASPVPVM" FT tRNA 608653..608729 FT /locus_tag="AARI_36620" FT /product="transfer RNA-Val" FT /anticodon=(pos:608687..608689,aa:Val) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(608787..609833) FT /transl_table=11 FT /locus_tag="AARI_05470" FT /product="putative luciferase-like monooxygenase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00296. Bacterial luciferase FT is a flavin monooxygenase that catalyses the oxidation of FT long-chain aldehydes and releases energy in the form of FT visible light, and which uses flavin as a substrate rather FT than a cofactor. There are structural similarities between FT bacterial luciferase and nonfluorescent flavoproteins FT (LuxF, FP390), alkanesulfonate monooxygenase (SsuD), and FT coenzyme F420- dependent terahydromethanopterin reductase, FT which make up clearly related families with somewhat FT different folds" FT /db_xref="GOA:E1VT22" FT /db_xref="InterPro:IPR011251" FT /db_xref="InterPro:IPR022290" FT /db_xref="UniProtKB/TrEMBL:E1VT22" FT /protein_id="CBT74775.1" FT /translation="MSTKLPLPEIGAETFGDITEDAQGNPLSHAQVIRNVIAEGQQAEA FT SNLDFFGVGEHHRDDYAISSPEVVLAALASITQRIKLGTAVTVLSSDDPVRVYERFATL FT DAISNGRTEIIAGRGSFIESFPLFGLDLEDYEDLFEEKLHLLAKLRHGKPVSWQGKHRA FT ALRNQQVYPLLEDRPLTTWVGVGGSPQSVVRAARHGLPLCLAIIGGQPSAFEGLASLYR FT RALEEFGQEQLPISAHFHGLVASTDEEALETLWPHYQRTMNRLGAERGWPPASKMRLQA FT SMGPEGAMMAGSPQTVAQKMAKVTTQLGLSRVDIKYSAGSLPHEVMMESIKLLGEEVKP FT RVHQLLGS" FT CDS 610034..611704 FT /transl_table=11 FT /locus_tag="AARI_05480" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="9 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR010619" FT /db_xref="InterPro:IPR024528" FT /db_xref="UniProtKB/TrEMBL:E1VT23" FT /protein_id="CBT74776.1" FT /translation="MAYRSDEERSTSSNAVGEDPAPIAGAMPRIVTSEINMGFHPEEPV FT EEPLMASELPLNTAVSANVAAADATDIEWRTGQVHTTDEGITLMPTRANPVARRLLAKM FT WISDAPPTEALNIVERLQGTPYANPKINVDQDASNRRTMEFALDLGETLIRYGAGALEV FT ETSVIAVTAALGLSHLDVDITNQSLHLNYSPPDGESYSVLRVVRSYTSNYAGMVLVHEL FT VSDIIAGGVSRTASAARLKQITRKPKPFPRWIAATSRAVFAAAFVLFIGGSWAGALVAM FT VSSSLVTQISRYGSRWRVPEFFTIAASTLTVTVIALLGHQFHAPLDPALVVSGGILLLL FT PSGRFVSALQDAINGFPVTAVGRLFSASLIYGAILCGIATALVISDLLGGEKVDVHKIV FT QTEYPTWLLVVLVGVAIVAGAVTEQSALRLLLPTAGIAVGGYLVMLLAESIGLGDRATP FT ALVATVIGFAARFAADKLRSPQLVLAAPAVMFLLPGLMIFRAMYGIVINVDETAAGLVE FT MFNAMAIMLSIAGGVVFGDTLCRPLTSNARRERRRIRRR" FT CDS complement(611701..612375) FT /transl_table=11 FT /gene="ung" FT /locus_tag="AARI_05490" FT /product="uracil-DNA glycosylase" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.2.2.-" FT /note="DNA repair enzyme that excises uracil residues from FT the DNA which can arise as a result of misincorporation of FT dUMP residues by DNA polymerase or due to deamination of FT cytosine" FT /db_xref="GOA:E1VT24" FT /db_xref="InterPro:IPR002043" FT /db_xref="InterPro:IPR005122" FT /db_xref="InterPro:IPR018085" FT /db_xref="UniProtKB/TrEMBL:E1VT24" FT /protein_id="CBT74777.1" FT /translation="MADLGFIAPDWVQALQEQDSLLKSLASLLAARSAAGEQILPAPEV FT MFRALSLPLSEVKVLIIGQDPYPTPGHPNGLAFAANKQVRPLPRSLSNIYKELQADLGI FT APVPHPDLSPWLSQGVLLLNQVLSVTAGDAGSHQNLGWSPIVQSILKALNELPHPPVAL FT LWGKHAQKLSQALPNAEQLHSAHPSPLSASRGFFGSKPFSNINRLLSEKGQKPIDWSLP FT KA" FT CDS 612631..612921 FT /transl_table=11 FT /locus_tag="AARI_05500" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021678" FT /db_xref="UniProtKB/TrEMBL:E1VT25" FT /protein_id="CBT74778.1" FT /translation="MAENELLVDFVMNPDSELDERSQQILTLEKLWWKYAGAKEQAITK FT QFSMSPTNYYQLLNQLIETDAALAYDPMLVKRLRRARSTKRRVGGKVGTGR" FT CDS 612964..613569 FT /transl_table=11 FT /locus_tag="AARI_05510" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VT26" FT /protein_id="CBT74779.1" FT /translation="MTNYPRDEFDRVPEFSTRVGSHHAHGWAQSAASKSTGGKLRWVVL FT TAVLVLVIGALSFIFGPQLKETLATSTGSESSQSQEETPQSSEEATPSESESPSSTIDD FT EDVLYGQLIGVYNAANIAGLATAGEDAMTEAGFTSIVADNWTKPAEVSAVYYMSESYRT FT TAEKAAEVLKVEEVLQTTNIPNRVTVVLGTDDTLGLNE" FT CDS 613868..615505 FT /transl_table=11 FT /gene="groEL" FT /locus_tag="AARI_05520" FT /product="chaperonin GroEL" FT /function="3.9 Protein folding" FT /note="chaperonins are involved in productive folding of FT proteins. With the aid of cochaperonin GroES, GroEL FT encapsulates non-native substrate proteins inside the FT cavity of the GroEL-ES complex and promotes folding by FT using energy derived from ATP hydrolysis" FT /db_xref="GOA:E1VT27" FT /db_xref="InterPro:IPR001844" FT /db_xref="InterPro:IPR002423" FT /db_xref="InterPro:IPR018370" FT /db_xref="UniProtKB/TrEMBL:E1VT27" FT /protein_id="CBT74780.1" FT /translation="MAKMIAFDEEARRGLERGLNTLADAVKVTLGPRGRNVVLEKKWGA FT PTITNDGVSIAKEIDLEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLR FT NVAAGADPIALRRGIDKAVEAVTAELFAAAKKIESKEQIAATASISAGDKEIGGLIAEA FT LDKVGEQGVITVEESNTFGLELELAEGMRFDKGYISAYFVTDAERQETVLEDPYILIVN FT SKISSVKDMVTLLEKVMQSNKSLLIIAEDVEGEALATLILNKIRGLFKSVAVKAPGFGD FT RRKAMLTDIAILTGGQVVSEEIGLSLDNVGLEVLGTARKVVITKDETTIVEGGGEADAI FT EGRKSQIAAEIKNTDSDYDREKLQERHAKLSGGVAVLKAGAATEVELKERKHRIEDAVR FT NAKAAVEEGIVAGGGVALIQAGAAAFEKLVLEGDEATGANIVRVGIEAPLKQIALNAGM FT EPGVVADKVKGLPAGHGLNAATGQYVDLLEAGVNDPVKVTRSALQNAASIAGLFLTTEA FT VVAEKPAPAGAAPAGGDDMGGMGGMGGF" FT CDS complement(615609..616499) FT /transl_table=11 FT /locus_tag="AARI_05530" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VT28" FT /db_xref="InterPro:IPR003607" FT /db_xref="InterPro:IPR009218" FT /db_xref="InterPro:IPR023279" FT /db_xref="UniProtKB/TrEMBL:E1VT28" FT /protein_id="CBT74781.1" FT /translation="MSILIDPPRWPAHGTLFAHLVSDTSLAELHQFAEQQEISRRAFDR FT DHYDVPREHYDRLVAAGAQEVSGGELVRALLSSGIRIPAKYRPEKLGTILSRRWARTLP FT TEPQLGSELLERWSQSHRHYHDRVHLLSVLEALDWLAKDNTDPEELMLLQLAAWFHDAV FT YEGTSEDEFKSAILARERLWGVLSPGAVSKVSDLIMLTAGHSPADTDRLGNILCDADLE FT VLARPTVAYQRYAEAIYKEYEHLPRPLLASGRSKILTGLLEKDKIYGTPAGIQRWEPGA FT RINLSNELELLRSWL" FT CDS complement(616543..616833) FT /transl_table=11 FT /locus_tag="AARI_05540" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR010310" FT /db_xref="UniProtKB/TrEMBL:E1VT29" FT /protein_id="CBT74782.1" FT /translation="MSTFSTNTGEMQVKSQAVMNTIDRLRHEVSTMQMNLDQLQSTWQG FT SAAASFQSIVAEWRSTHVQIEEALSSIATALNHASMQYEEVEQVNTSLFRY" FT CDS complement(616947..618485) FT /transl_table=11 FT /locus_tag="AARI_05550" FT /product="signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VT30" 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:E1VT30" FT /protein_id="CBT74783.1" FT /translation="MKSFRAQWRRTSLRTKLVTVMLGLMIVAIFATAVGSAHTLRIAMT FT NQIDKQLNVSKSTMAYGLNKAYLYSLNEDSGSHDALDVDATLLGLSSAYADIRDQDGEI FT VYVMPRSRVGPSNGTDLPLLNMEEIQQLAAHPNSPATVPGAFPTSAGWRTVMIPLKSSE FT LNLFLSMPLDNVNRTVNQTAVLVLSTGTLTALLMSMIAYGLTGRSLKPLINVERTASMI FT ADGDLSQRVKDYPAETEVGRLSRSLNAMLAQIEKAFNDREASERKMRRFIQDASHELRT FT PLVTIQGYSEFYRYGGLAEPEAMDSAMGRIESESKRMARLVEDLLMLARLDEQRPMEKQ FT PVDLLVLGQDAVEDTKVRAPDRTVKLVGLVSDRPSPASTVGDDARIRQVIANLITNALR FT YTPEGSPLEVAVGVRSLVAGTMDAVVEIRDHGPGIPAEDAKRIFERFYRSDSSRQRETG FT GSGLGLAIVAAIVQQHGGSVALADTPGGGATMSISLPYEPLREPKEPEVDDIED" FT CDS complement(618538..619245) FT /transl_table=11 FT /locus_tag="AARI_05560" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VT31" 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:E1VT31" FT /protein_id="CBT74784.1" FT /translation="MSPKTAEAKLLVVDDEPNIRELLSTSLRFAGFEVVAAANGREALA FT AVEADEPDLAVLDVMLPDMDGFTITRKLRAAGRHFPVLFLTARDDTSDKVTGLTVGGDD FT YVTKPFSLDEVVARIRAVLRRTASGEDENATISVADLELDDDAHEVRRAGEIIDLSPTE FT FKLLRYLMMNPNRVLSKSQILDHVWEYDFNGDASIVESYISYLRRKVDRPEWPALIQTK FT RGVGYLMRTPDRR" FT CDS complement(619304..619522) FT /transl_table=11 FT /locus_tag="AARI_05570" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT32" FT /protein_id="CBT74785.1" FT /translation="MSASSKTMSFLSRLAIAIAVLSALALIGILVFYFQGIAIPPLLML FT CARFGLPTAFILAAVVIFGNVARRRSN" FT CDS 619775..620158 FT /transl_table=11 FT /locus_tag="AARI_05580" FT /product="putative cold shock protein" FT /function="4.1 Adaptation to atypical conditions" FT /note="N-terminal section of the protein: match to PF00313 FT (cold-shock DNA-binding domain). The so-called cold shock FT proteins are thought to help the cell to survive in FT temperatures lower than optimum growth temperature, by FT contrast with heat shock proteins, which help the cell to FT survive in temperatures greater than the optimum, possibly FT by condensation of the chromosome and organization of the FT prokaryotic nucleoid" FT /db_xref="GOA:E1VT33" FT /db_xref="InterPro:IPR002059" FT /db_xref="InterPro:IPR011129" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR016027" FT /db_xref="UniProtKB/TrEMBL:E1VT33" FT /protein_id="CBT74786.1" FT /translation="MPSGKVKWYEKAKGFGFITAEDGKEIYVNAAALPEGVHDLRPGTR FT LEFGVAEGRRGPQALSLRLLEEAPSVARAKRKKPEAEAVLIEDLIKLLDNVSNSLHKGR FT YPEQAYGKKVATVLRAVADDLDA" FT CDS 620162..620773 FT /transl_table=11 FT /locus_tag="AARI_05590" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021391" FT /db_xref="UniProtKB/TrEMBL:E1VT34" FT /protein_id="CBT74787.1" FT /translation="MARKPKLDTILAEAVDTARGALAEIAGVSEIGEHLGVTAEGERLV FT THRFVSHKKGYQGWTWFATLARVSRAKSKDLTVCEVGIIAGEHSLLAPAWVPWADRLAK FT EEIEAASAEEAGETSGEDTGTAASAERAETQPDAAVAEDSTSATEKQPESDEAEDAESD FT QETVQTHKSPARRQVRRRRTAQRTAARRRAAQRNRTRKEN" FT CDS complement(620850..621971) FT /transl_table=11 FT /gene="serC" FT /locus_tag="AARI_05600" FT /product="phosphoserine transaminase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.6.1.52" FT /note="catalyzes the reversible interconversion of 3- FT phosphonooxypyruvate and glutamate to phosphoserine and 2- FT oxoglutarate to. It is required both in the major FT phosphorylated pathway of serine biosynthesis and in FT pyridoxine biosynthesis. Also catalyses the third step in FT the biosynthesis of the coenzyme pyridoxal 5-phosphate : FT (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate FT <=> 4-phosphonooxy-L-threonine + 2-oxoglutarate" FT /db_xref="GOA:E1VT35" FT /db_xref="InterPro:IPR000192" FT /db_xref="InterPro:IPR006272" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="InterPro:IPR022278" FT /db_xref="UniProtKB/TrEMBL:E1VT35" FT /protein_id="CBT74788.1" FT /translation="MSTDIKIPENLLPADGRFGAGPSKVRAEQVQAIVDAGPELLGTSH FT RQAPVKNLVASVQDGLKEMFNAPAGYEVLLGVGGSTAFWDAAAFSLVRSKAQHLSFGEF FT GSKFAKATDKAPFLEASSIIVGEPGTVPEPVAEADVDLYAWPHNETSTGAAAPIQRVAG FT ANADALVVIDATSAAGGLDVDLAETDVYYFAPQKNFASDGGLWLAFVSPAAIARIEEIA FT ATDRWIPDFLNLKTALDNSLKNQTYNTPSLTTLVGLDAQIKWINANGGLKWAAARTAES FT AGKIQAWAEASEIAAPYVANPAHRSNVISTVDFADSVDASAIAKVLRANGVVDVEPYRK FT LGRNQLRIATFVAIEPNDVESLLKCIDYVIEQL" FT CDS 622233..622928 FT /transl_table=11 FT /gene="ideR" FT /locus_tag="AARI_05610" FT /product="iron-dependent repressor IdeR" FT /function="3.5.2 Transcription regulation" FT /note="identified by similarity to protein SP:P0A672 FT (Mycobacterium tuberculosis). Iron-binding repressor of FT siderophore biosynthesis and iron uptake. Synonym: DtxR FT (Corynebacterium glutamicum)" FT /db_xref="GOA:E1VT36" FT /db_xref="InterPro:IPR001367" FT /db_xref="InterPro:IPR007167" FT /db_xref="InterPro:IPR008988" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR022687" FT /db_xref="InterPro:IPR022689" FT /db_xref="UniProtKB/TrEMBL:E1VT36" FT /protein_id="CBT74789.1" FT /translation="MSDLIDTTEMYLRTILELQEEEIVALRARIAERLGHSGPTVSQTV FT ARMERDGLVIVSTDRHLALTEKGHELATGVMRKHRLAERLLSDIIGLDWEYVHDEACRW FT EHVMSERVERRLFDLLGKPTVSPYGNPIPGLEVLGGPNVGEISHDVENLDDALLSGNIG FT PLAIERLAEPIQTDPILLGQLNEGGIRPGAIVTLERADDYVVVRVQGIEGALELPVEVS FT AHVFVKSQK" FT CDS 623191..624237 FT /transl_table=11 FT /locus_tag="AARI_05620" FT /product="putative M23 family peptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.24.-" FT /note="identified by match to protein family PF01551. FT Members of this family are zinc metallopeptidases with a FT range of specificities. Peptidase family M23 are also FT endopeptidases" FT /db_xref="GOA:E1VT37" FT /db_xref="InterPro:IPR011055" FT /db_xref="InterPro:IPR016047" FT /db_xref="UniProtKB/TrEMBL:E1VT37" FT /protein_id="CBT74790.1" FT /translation="MVETKTAGRRRVADVEVDVIAEVTASATERTGGRRAARAAATVPM FT IAPAKPVHEDFVGRRFDSVHRYGVAPTQSMLAATDVASNVVLLPNAAPASASKPKPVEA FT AGNVAFIASFKSKVQKTAHRGFAHKVAAVAAVSGLALAAVTPQLSGNSEEQKAVEVAAQ FT RTATSAVVDVTAPSSNAELSVERAALSSELNTEVAKEEKFAEVMTASGGSITAIKDTSG FT LLGSPVTTQRITSSFGHRKNPTGAGYMIHSGTDYGVPSGTKVYAAADGIVTVSGWAGHS FT GNRITLDHGNGLETGYSHNSKLVVKVGQKVKRGDVVALAGSTGNSTGPHVHFEVIVDGQ FT FKDPAGWL" FT CDS 624535..625362 FT /transl_table=11 FT /locus_tag="AARI_05630" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR000064" FT /db_xref="UniProtKB/TrEMBL:E1VT38" FT /protein_id="CBT74791.1" FT /translation="MTKSHAHGRRRADVPRTNSLQAISQAVASNAGSVGRQAAVVAAAS FT GLIVTLGVPGQATAPRDVSASPVDTINPERVAVKAVKVAADKKADIAIERASFTAEEKP FT EPVVIAVSNDITPTTRSNNSGSSDSMAPMTRQSRSGGQESAPQQKAQPKAETTVQSSNL FT SGIAATAAKYVGVPYVWGGNGPSGWDCSGFVKYVYAQHGINIARGTSAILGSGQFVRTS FT NPKPGDLVFQNGGGHVGIYLGGGQMIGAQNPTVDTMIHSVSRNPLYGYYTLAG" FT CDS 625966..626088 FT /transl_table=11 FT /locus_tag="AARI_05640" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT39" FT /protein_id="CBT74792.1" FT /translation="MLSQLGWQLRITPHRPRVAGHLVSGLQHVDAAWNEYLHAS" FT CDS complement(626126..626536) FT /transl_table=11 FT /locus_tag="AARI_05650" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VT40" FT /db_xref="InterPro:IPR000086" FT /db_xref="InterPro:IPR015797" FT /db_xref="InterPro:IPR020084" FT /db_xref="UniProtKB/TrEMBL:E1VT40" FT /protein_id="CBT74793.1" FT /translation="MRKNLTISAACLINNQGEILLVRKRGTTKFMQPGGKPETGETALQ FT TIIREIREELGIDFTAEQLHFDGEWTGPAANEADTLIHASLYSARYDGALTPLAELEEL FT LWIDPQQALERDDLAPLLRDHVLPLAIARAKA" FT CDS 626725..627954 FT /transl_table=11 FT /locus_tag="AARI_05660" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00480: ROK family" FT /db_xref="InterPro:IPR000600" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VT41" FT /protein_id="CBT74794.1" FT /translation="MRRGTNLGRLGDFNQAVILESIRRAAEGISRVELAGSTGLSPQTI FT SNVVRRLLDDGIVREDRTIVSGPGKPRTVLELEGNRLVSIGIHLDPSVLTFVAMNLRGE FT VLRERRIEVPNLEVATETVQLMATTVKELIAEIRVPKKHIVGVGIAVPGPVNVEEGVVL FT NPPLLDGWADVELVNPLRKLLRLQVIIEKDTIASAVGELWQAKEEKNNDFVFVYCGHGF FT GAGLVLNGDVHHGSSNNAGEIGHYSTGYKSVKCEECGADDCLAAGTSYEFIAAQAKERG FT LELPSFEIVGPEQRAAGMNRLYELAHEGNKVAKDLVIEAMVKVGEVAGQLANSLDVREV FT VLGGPQWDKVRELVADEVNDAIGRRFALRGVHEIEMRTSELGSNVGAIGGACVVMDASL FT SPKATALLLR" FT tRNA complement(628074..628150) FT /locus_tag="AARI_36630" FT /product="transfer RNA-Arg" FT /anticodon=(pos:628114..628116,aa:Arg) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(628217..628879) FT /transl_table=11 FT /locus_tag="AARI_05670" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VT42" FT /protein_id="CBT74795.1" FT /translation="MAKKVRKSKEYRKPNQFEQLQNQRIESNARSGKVQSTSHENKSNP FT MLLISVGLIIGVALFVYYHLLTLVQMQDLSGSLPMPDQRIFGYTLGDIEALRNAMDDDA FT VGQLNYLHKTAGFLFPMFTAIFSMLLFIYWIPNRQTRWLAWIAPLGFAAIDIWENFAID FT ALFTGELSESAVVLASILTTTRWALFIITAGLVLGLGAVRANRALKAKMLAIREGTD" FT CDS 628964..631342 FT /transl_table=11 FT /gene="pcrA" FT /locus_tag="AARI_05680" FT /product="ATP-dependent DNA helicase PcrA" FT /function="3.1 DNA replication" FT /EC_number="3.6.1.-" FT /note="an ATP-dependent DNA helicase which facilitates the FT progress of replication forks. Non-essential in FT Escherchichia coli, PcrA is an essential DNA helicase in FT Bacillus subtilis, fulfilling functions both in repair and FT rolling-circle replication" FT /db_xref="GOA:E1VT43" FT /db_xref="InterPro:IPR000212" FT /db_xref="InterPro:IPR005751" FT /db_xref="InterPro:IPR013986" FT /db_xref="InterPro:IPR014016" FT /db_xref="InterPro:IPR014017" FT /db_xref="UniProtKB/TrEMBL:E1VT43" FT /protein_id="CBT74796.1" FT /translation="MDFLFDDFAPDTTQQVMPSAEELLVGMNPQQEEAVRYAGGPLLIV FT AGAGSGKTRVLTHRIAYLMATGRARPHEILAITFTNKAAAEMRERAAELIGEDQAKKMW FT ISTFHSSCVRILRREAATIGMKSNFSIYDSTDSLRLITLVAKSLEIDPKRFTPKAIAHK FT ISSLKNELIDDEDYASTINANDPFSRAVSEVYRGYTRRLRAANAMDFDDLIGQVVYMFR FT AFPRVADNYRRRFRHVLIDEYQDTNHAQYSLVRELTGVEGDTTPGELTVVGDSDQSIYA FT FRGADIRNIIDFEKDYPNAATIKLEQNYRSTQTILSAANEVIKRNPDRNDKKLWTASGD FT GEKITGYVGESESDEARWIAEEILRLNDDDEVRPGDVAIFYRTNAQSRALEEQLMRVDL FT KYRVVGGTRFYDRKEIKDALAYLRALVNPDDDINVRRILNEPKRGIGDRAEGAVAALAE FT RDRISFMDALRRSDEAPGLGTRGIKMTAAFVSMMDDLKTVAEGSGPAEALEAVLEQTGY FT LETLRLSSDPQDESRVENLAELVAVVRDYVNDEPEGGLEGFLERVALVADADQIPEAPS FT DDEGAAMAAQEGVVTLMTLHTAKGLEFPVVFLTGMEHGVFPHQRSMTDEKELAEERRLA FT YVGLTRARERLYLTRAEQRSLWGQAQYNPASQFLEEVPSELIDWKREGSGGGMGFGFGN FT TAVNFATSRYERGSHWGAGSGTVQPTRGHNAAPISKKRVVQNKDITIPEVGQNVKHSSF FT GLGTVIALEGAGDKTVAKVQFPDSEKRLLLRYAPLEIVD" FT CDS 631585..632757 FT /transl_table=11 FT /gene="sucC" FT /locus_tag="AARI_05690" FT /product="succinyl-CoA synthetase beta subunit" FT /function="2.1.3 TCA cycle" FT /EC_number="6.2.1.5" FT /note="succinyl-CoA synthetase, which is composed of alpha FT and beta subunits, catalyzes the interconversion of FT succinyl-CoA and succinate. Involved in the TCA cycle" FT /db_xref="GOA:E1VT44" FT /db_xref="InterPro:IPR005809" FT /db_xref="InterPro:IPR005811" FT /db_xref="InterPro:IPR011761" FT /db_xref="InterPro:IPR013650" FT /db_xref="InterPro:IPR013815" FT /db_xref="InterPro:IPR013816" FT /db_xref="InterPro:IPR016102" FT /db_xref="InterPro:IPR017866" FT /db_xref="UniProtKB/TrEMBL:E1VT44" FT /protein_id="CBT74797.1" FT /translation="MDLYEYQARDLFEAHGVPVLAGIVAYTPEEAKAAAEKIGGVVVVK FT AQVKVGGRGKAGGVKVAKTADEAFEHASNILGMDIKGHTVNKVMIAQGADIAEEFYFSV FT LLDRANRNYLAMCSVEGGMEIEVLAVERPDALAKVAVDPIVGIDAAKAAEIVEAANFPE FT ELRAKVAETIQKLWVVFKEEDATLVEVNPLVKTGAGDIVALDGKVSLDDNASEVRHPAH FT EELEDKGAADPLEAKAKAAGLNYVKLDGEVGIIGNGAGLVMSTLDVVAYAGENHGSVKP FT ANFLDIGGGASAEVMANGLDVILNDPQVKSVFVNVFGGITACDAVANGIVGALNTLGDA FT ANKPLVVRLDGNNVEEGRAILAQANHPLVTLAATMDEGADKAAELANAAK" FT CDS 632774..633676 FT /transl_table=11 FT /gene="sucD" FT /locus_tag="AARI_05700" FT /product="succinyl-CoA synthetase (ADP-forming) alpha FT subunit" FT /function="2.1.3 TCA cycle" FT /EC_number="6.2.1.5" FT /note="succinyl-CoA synthetase, which is composed of alpha FT and beta subunits, catalyzes the interconversion of FT succinyl-CoA and succinate. Involved in the TCA cycle" FT /db_xref="GOA:E1VT45" FT /db_xref="InterPro:IPR003781" FT /db_xref="InterPro:IPR005810" FT /db_xref="InterPro:IPR005811" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR016102" FT /db_xref="InterPro:IPR017440" FT /db_xref="UniProtKB/TrEMBL:E1VT45" FT /protein_id="CBT74798.1" FT /translation="MSIYLNKDSKVIVQGITGGEGTKHTALMLKAGTNIVGGVNARKAG FT TTVTHGEQDIKVYGTVAEAKAETGADVSIVFVPPKFTKDAVVEAIEAEVGLVVVITEGV FT PVQDSAEFWALAQSKVDADGNQITRIIGPNCPGIITPGEALVGITPNNITGKGPIGLVS FT KSGTLTYQMMYELRDLGFSTAIGIGGDPVIGTTHIDALAAFEADPETKAIVMIGEIGGD FT AEERAADYIKANVTKPVVGYVAGFTAPEGKTMGHAGAIVSGSAGTAQAKKEALEAAGVK FT VGKTPSETAVLLREVFAAL" FT CDS 633957..634460 FT /transl_table=11 FT /locus_tag="AARI_05710" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT46" FT /protein_id="CBT74799.1" FT /translation="MPLNPDSASSCDRPYIASEGELRGAPQLLRVDQFYDQDMRHTLVD FT ASVGSSVTFSPRPDWNNVNEVLTAAGAVSETTVVERPYDASEGLESLIRSSEQSAGLVG FT YAAARPVTYTYSVQCLNDQQNDYRLVFDTWSETEFGILDCELRLDAKAQWAAQATYDSY FT CQAS" FT CDS complement(634550..636082) FT /transl_table=11 FT /gene="proP" FT /locus_tag="AARI_05720" FT /product="proline/betaine transporter" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="identified by similarity to protein SP:P0C0L7 FT (Escherichia coli). Proton symporter that senses osmotic FT shifts and responds by importing osmolytes such as proline, FT glycine betaine, stachydrine, pipecolic acid, ectoine and FT taurine. It is both an osmosensor and an osmoregulator FT which is available to participate early in the bacterial FT osmoregulatory response. Metabolite:H+ symporter (MHS) FT family, (Poline/glycine-betaine):(H+/Na+) symporter (also FT transports taurine, ectoine, pipecolate, proline-betaine, FT N,N-dimethylglycine, carnitine, and 1- FT carboxymethyl-pyridinium) (subject to osmotic activation) FT (TC 2.A.1.6.4)" FT /db_xref="GOA:E1VT47" FT /db_xref="InterPro:IPR005828" FT /db_xref="InterPro:IPR005829" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VT47" FT /protein_id="CBT74800.1" FT /translation="MEARNSRKQRFLRKRRLKVEDVTVVDDSMLKKAIGGTVVGNLMEW FT YDVGVYGYLAVIIGKLFMPDTVEPAIQTLFSLGVFAVTFVARPLGGVILGQLGDRVGRQ FT KILVFTLLMMALATFGIGILPDYSTWGVAAPILLVALKLVQGFSTGGEYAGATTFITEY FT APDKRRGFYASLLDLGSYMGFALGAAFVSILQLTLSADVMEGFAWRIPFLVALPLGVIA FT LWFRSKIEDTPAFKEAQEAANRASEDARNSADAPKGVIDLVKSYWRELLTGFVLVSAAN FT TAGYALTSYMPTYLTETLEYDPVHGNLLTLPILVGMSLCIPLAGKLSDSVGRRKVLFIG FT SISSVVLAVPAFLLMMHGQIWSTLAGLALLAVPVTFYVANLASSLPALFPTASRYGGMG FT ISYNFAVAIFGGFAPFIMQALVTMTKSSLAPAFWVMGTSVAGFIAVCYLRESARKPLPG FT SLPSVASEAEAIELVETQEENPDLDVEELFEQVPALEENYQQEIADAKAAQS" FT CDS complement(636661..636945) FT /transl_table=11 FT /locus_tag="AARI_05730" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT48" FT /protein_id="CBT74801.1" FT /translation="MSLIKSETLSTPDDDWMSASVSIDKDRVVIQTEQESLSLENDRLL FT EKIRRVLASPLEEIFYNPKHRMLLIPGAFAAIGSSFLRVDTEAAVGLRG" FT CDS complement(637108..640455) FT /transl_table=11 FT /locus_tag="AARI_05740" FT /product="putative ATP-dependent helicase" FT /function="3 Information pathways" FT /note="possible DNA or RNA helicase" FT /db_xref="GOA:E1VT49" 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:E1VT49" FT /protein_id="CBT74802.1" FT /translation="MSESVPPTIDARHLLAFLGNAPFFYGKTLAAEENSVVDVEFDEDA FT QQIEGTVTESGEEYAPMIQVRLDNEEWKIDSCECTCDAPGICSHIAALAIISNKIASQP FT RTLPAQEEKLNTVWSQQIDSWFEESEPGPADGLLGSQHDAVVPMALQFLLFDSKDTTQQ FT QQWMPTGTIPHPTRNKRFRLGVRPMVRNTEGRWVRGQLRWTTLGFKTYGWNLLRAQHHW FT FTRFASMARSDTQLQFKVDEDWLFLDEYASDLLWPLLEQADELGIPLITTRNEQRVRIV FT DPASFSMRASLNEQHLQLDGVLHIANQDLVLEPEAPSGVIAEHGFYAQLAQPDEIWLAP FT SLEPIPDAHRRWYVDRRPVTVPKSEINNFFESSYPRLARRFELRSTSEELELPVLNPPY FT VQVTVAYKREFNEKDEPNDTASVDFEIRYPGIPSDQEVYDFEAEELLRSAVHEVFEAHE FT EGGNPSLSPKFYARDDTIDFVTEILPELEQLPGIKLLEKGSRPTFRQLRELPQLKINAV FT NHERTDWLDLGLLITVGNHEVPFAQIVEAMSNGRMKLRLPDNTWFSLNHPMFAKLKALV FT DEAQAMNDKPKEGDLKLTVFQISLFEELDEMAEGIDGADLFIARMRSLLKVAEAHHAEV FT PDTLNAQLRPYQVEGFHWLSRLYEGGFGGILADDMGLGKTLQTIALILHAHKLWADPQA FT CAQLPATQRTQLPFLVVAPSSVVSNWEMEINKFAPSLRVVSVEGTLPSARKLQELAENY FT DVILTTYTLLRLNDEIYEAQRFAGLILDEAQFVKNKSTKAHRTAVNLQTNFKLAVTGTP FT MENNLSELGALLSLVAPALFLNTTRFNRQFARPIEVLGDRDVLALLQRRIKPFMLRRTK FT ESVVLDLPAKQEQQVLVRLSEEHQHVYDTHLNRERQKILHLVEDLDRNRFTIFQSLTHL FT RMLALEPSLVDPELSDVTGSKLEALFDQLDDVVGEGHRALIFSQFTSYLKVLADKLTER FT GVKFVYLDGNTRNRAKVIEQFKEGEAPLFLISLKAGGFGLNLTEADYCFLLDPWWNPAV FT EAQAIDRTHRIGQTRQVMVYRMISQGTIEEKVVALQESKRKLISTVMDEADGFSKALTA FT QDIRGLLE" FT CDS 640542..641732 FT /transl_table=11 FT /locus_tag="AARI_05750" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR005269" FT /db_xref="UniProtKB/TrEMBL:E1VT50" FT /protein_id="CBT74803.1" FT /translation="MSQVWPYLPARAVNITSLVEFDRLAAEALASHRARGKNWRVHRVD FT LRERDTVLKSLDLSEALFIDCQYSSQGQQIVQATGGLCMSSGSELPFETGARDLYSADE FT LYSGIRTQTYEHVPDAKIYAYSQQHVAVNGNSDDSALSKTLHDHHIGQALVSAVYEGMF FT QDTPIIGVMGGHAMNRGTVEYARAVELGRMITRAGYAVATGGGPGAMEAANAGAWLADY FT EPEDITTALRMLAEAPDAIHQRTGWARTALMVKERFPSQRQSLGVPTWFYGHEPPNLFA FT TGIAKFFTNSIREAILLEQSNGGLVVLPGAAGTVQEIFQDACENYYATGARVVPMVLIG FT KDYWTKDLPAWPLLQALAKERVMEQKIALVDTAEEAMAFIESMTTLRRRTRHPQGS" FT CDS complement(641795..642898) FT /transl_table=11 FT /locus_tag="AARI_05760" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="5 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR008217" FT /db_xref="UniProtKB/TrEMBL:E1VT51" FT /protein_id="CBT74804.1" FT /translation="MSQHSASEPSKTQIKRWRQYLADEIAEGAIYRALAEKKTGQERQI FT LLGLAEAETRHEEHWRTKLGGHVKDVRPSLRRTMLRFLALHLGSVFVLAMAQRSESSSP FT YRDDKDATAQMAADEQVHEEVVRALATAGRARLSGNFRAAVFGANDGLVSNLALIMGIG FT ATGVSATFVLFSGVAGLLAGALSMAAGEYVSVRSQRELLTASRPTQVTLTAAPNLDLDA FT NELLLIYKARGMSDEDAEHRAAERMGMFTCDCNPGFSLNPEGRSAELEKEHEELGSATG FT AATTSFFLFASGAIVPILPYIFGLSGLSAVIISVVLVGIALMITGGIVGLLSGASPFKR FT GLRQLAIGWGAAAVTYCLGLIFDVSVS" FT CDS complement(642954..643220) FT /transl_table=11 FT /locus_tag="AARI_05770" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT52" FT /protein_id="CBT74805.1" FT /translation="MTYPILPIIDRQTGQVQFKAEGHWHIRYVADPLRLERLLARGVRR FT PIFDPETSNLLLVVPAIADPAGKKFAFSLAKFPSNGALTKLGS" FT CDS 643296..643478 FT /transl_table=11 FT /locus_tag="AARI_05780" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT53" FT /protein_id="CBT74806.1" FT /translation="MNLGLVCGQSELGAASREATILMLLPGWGLEEVMGRNMTAASLLE FT PDAVGTPGHRAVHDS" FT CDS 643633..644196 FT /transl_table=11 FT /locus_tag="AARI_05790" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domain PF01381: helix-turn-helix" FT /db_xref="GOA:E1VT54" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010982" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR013096" FT /db_xref="InterPro:IPR014710" FT /db_xref="UniProtKB/TrEMBL:E1VT54" FT /protein_id="CBT74807.1" FT /translation="MKTLPVEPTGAAINIGARLRGVRQTQRMTIDQVAELSGLTKGFLS FT RVERDLTSPSVSTLLRLCEVLSIEVGTLFEVPETKLVRLEQAPRVSLGGDGITEQLVTP FT RSEKRVQMIRAEIAPKGTGEAELYSVDCELEVLHVIGGRFVLVLPDQRVELEAGDTITF FT PGREPHSWENESDQTAVVTWTLIL" FT CDS 644334..644750 FT /transl_table=11 FT /locus_tag="AARI_05800" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VT55" FT /protein_id="CBT74808.1" FT /translation="MKTREPTTTHDQLRSISWWASILFGVLVGTTLTWIRTQRNFFFIG FT AAILAIVIVTIGVRTIRRRARFPLMAQAHTSWVYMLWTGVLLILAGPVQLVYVADDLSE FT LTIKSLIMSAGFCLGIHEVDRALVKASKKHSDES" FT CDS 645052..646038 FT /transl_table=11 FT /gene="gbh" FT /locus_tag="AARI_05810" FT /product="guanidinobutyrase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="3.5.3.7" FT /note="catalyses the following reaction: 4- FT guanidinobutanoate + H(2)O <=> 4-aminobutanoate + urea. The FT ortholog found in Arthrobacter sp. KUJ 8602 also acts on FT D-arginine, 3-guanidinopropionate and L-arginine" FT /db_xref="GOA:E1VT56" FT /db_xref="InterPro:IPR005925" FT /db_xref="InterPro:IPR006035" FT /db_xref="InterPro:IPR020855" FT /db_xref="InterPro:IPR023696" FT /db_xref="UniProtKB/TrEMBL:E1VT56" FT /protein_id="CBT74809.1" FT /translation="MKEIRIEENGRLGPINAAMIPRYAGGGTYARLPRLDQVEKADIKI FT VGVPFDTGVSYRPGARFGANHVRESSRLIRPYNPATDTSPFAQSQVADAGDMAVNPFNI FT NEAIETIEHEALELTSDGSTLVTVGGDHTIALPLLRAASQRAGAPVAMLHFDAHLDTWD FT TYFGAEYTHGTPFRRAVEEGILDTEAICHVGTRGPLYGKKDLEDDKRFGFGIVTSSDVY FT YQGVREIVDKLRDRIGNRPLYISVDIDVLDPAHAPGTGTPEAGGITSRELLEILRGLRG FT LNIVGADIVEVAPAYDHAELTGVAASHVTYDLISLISDFRASKGMNS" FT CDS 646038..647681 FT /transl_table=11 FT /locus_tag="AARI_05820" FT /product="thiamine pyrophosphate binding domain-containing FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="domain present in thiamine pyrophosphate-requiring FT enzymes (acetolactate synthase, pyruvate dehydrogenase FT (cytochrome), glyoxylate carboligase, phosphonopyruvate FT decarboxylase)" FT /db_xref="GOA:E1VT57" FT /db_xref="InterPro:IPR011766" FT /db_xref="InterPro:IPR012000" FT /db_xref="InterPro:IPR012001" FT /db_xref="UniProtKB/TrEMBL:E1VT57" FT /protein_id="CBT74810.1" FT /translation="MNEQPQRNGGDLVIETLTALGAKTVFGIPGQHALGLFDALSRSSL FT DFISSRVENNSAFAADGYSRATGEVGVLFLSTGPGALTSLAGLQEAYATGVPMVVIASQ FT IPLDGLGARRKGMLHQLDDQKASAANVTKFQQTVHHASGIPSAIQDAWARAITVPMGPV FT WVEVPQDVLLAPVMVPPVQDALAEAYPHPPREELIREAMRWLADAKRPAIIAGGGVRRA FT GAQAELLAVAEELQAPVLCSPGGNGAFSWDHELSLQSWAEDRFVSEVMEDADVLMVIGS FT ALGEVTSNYFTLEPRGKMIQIDAEPRVLESNTPALGIRADAREALKFLDEEMRATGFKA FT QASWHGQTPQQVVAQTLAKVQGRLDAQDLAKERKFMADIRAAVPSEMQTFWDMTIAAYW FT GWSCWDAKDGEFHSAQGAGGLGFGFPAAIGGAIGSKQRVLAVSGDGSSMYSIAELATAK FT QHQAPVTWLIVDDGGYGILREYMEGAFGKATATELARPDFVALAQSFGIPAQAVEPEDI FT GTALAEALKSDGPNVIVVRTLLKMFAPTHL" FT CDS complement(647775..647927) FT /transl_table=11 FT /locus_tag="AARI_05830" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VT58" FT /protein_id="CBT74811.1" FT /translation="MILGGIGAVLLFVSFAVMLAAQSLDWEPLLIGISLGVSTVLFGVV FT FHFTH" FT CDS complement(648064..648924) FT /transl_table=11 FT /gene="suhB" FT /locus_tag="AARI_05840" FT /product="putative inositol-phosphate phosphatase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="3.1.3.25" FT /note="catalyzes the following reaction: myo-inositol FT phosphate + H(2)O <=> myo-inositol + phosphate. Acts on FT five of the six isomers of myo-inositol phosphate, all FT except myo-inositol 2-phosphate, but does not act on myo- FT inositol bearing more than one phosphate group" FT /db_xref="GOA:E1VT59" FT /db_xref="InterPro:IPR000760" FT /db_xref="InterPro:IPR020583" FT /db_xref="UniProtKB/TrEMBL:E1VT59" FT /protein_id="CBT74812.1" FT /translation="MNDRQVQTSPHFAEELRLAALKAARQAAVLLRESFRANVQAEHKS FT NAHDLVTDIDRRSQQLITASLLSAQPDSWVLGEEQVSGDQGLPASGKVQWIVDPIDGTS FT NFVHGVAFFCISIAAAVDGQLLAAVVLDPISGEEFTANSTAAFLNERRLEPSARPEQSR FT ANLMTDYPGAESMLKDGELSMKIFGQWIQDFATVRRKVCAALELAHVAAGWCDASIGFD FT TKVWDVAAGAHLIRMAKGTFRGLSYGQPGLADHQCPGFIAQGPGANYPSLAAAAEQIHQ FT LRASI" FT CDS 649027..649539 FT /transl_table=11 FT /locus_tag="AARI_05850" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VT60" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VT60" FT /protein_id="CBT74813.1" FT /translation="MDKSSNTQADSQIKGLLDELARSSRILRVFSHMDQTDPEVSNASH FT HVLKTLNSREPTHAADLAQFLGIGTAAMSRHLAELEDSGLVAKRSSKIDARRHVLWVTE FT AGRAKLEFRDRLRLERMRGLLPDWDPERLTQISQALSELNDTMMRGIHSQRTEQFGTAG FT EAEHGQE" FT CDS 649526..651085 FT /transl_table=11 FT /locus_tag="AARI_05860" FT /product="putative EmrB/QacA subfamily drug resistance FT transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily, drug:H+ antiporter-2 FT (14 spanner) (DHA2) family (TC 2.A.1.3.z)" FT /db_xref="GOA:E1VT61" FT /db_xref="InterPro:IPR001411" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VT61" FT /protein_id="CBT74814.1" FT /translation="MDKNKPDGERPIDLTEVAADRPQMKQQEVLKSIVGVLASFFAAML FT AATIVSIALPTIMDVLGGTQTDFNWVLSTTLLANAATTPIWGKMADLFDKKKLLQVGIL FT VFVLGSLLAGLSWSIPVLLFARVIQGIGMGGLTAMGMAVIGTVIPPRERGRYSGYFGAV FT MAVSTAAGPLLGGFIVDSPLGWRWCFFFGIPISLLSMVLIHRTLHLKHVKRPVHIDWVG FT AVLLTSAVSILLIWVSYVGKSDYFGWNSWQTYTMVSSVLLLTTILLMVESRVREPIIPL FT KIICTRTTSLAIMASIAIGVGMFGTGAFIGQYFQIAREATPTMAGLMTLPMIAGNYFGS FT VFSGQMITRFGRWKIYLLIGSILNVAGLGLLGMMRHDTEYWLLACGMFLNGVGMGFMLQ FT NLVLSVQNTVKVTDIGAASSSVAFFRSVGGSAGVAVLGALLSRNVAELIAKSPLVSGQP FT SSPLANEDSLNLSGMPDALRQVVEAAYGEATGIVFVVSAAVAVVAFVCILLIKEVPLRQ FT TI" FT CDS 651131..651850 FT /transl_table=11 FT /locus_tag="AARI_05870" FT /product="GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF00392. This FT family of regulatory proteins consists of the N-terminal FT HTH region of GntR-like bacterial transcription factors. At FT the C-terminus there is usually an effector- FT binding/oligomerisation domain. The GntR-like proteins can FT be divided into six sub-families: MocR, YtrR, FadR, AraR, FT HutC and PlmA. Many of these proteins have been shown FT experimentally to be autoregulatory, enabling the FT prediction of operator sites and the discovery of cis/trans FT relationships" FT /db_xref="GOA:E1VT62" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VT62" FT /protein_id="CBT74815.1" FT /translation="MSSMQPIKQKVSLTEQVTTMIRAAIVAGEMTPGEHYSAIGISEKL FT GVSRTPVREALQLLEKEGIVTVAKNRGVRVNQISLEDIVEVFQLRLAIEPPAAARGVRN FT ATDADIEHLKSLHARMLEIGETGDGRATLEADKAFHLHLLGLAGNSKLDSVVGELRNLV FT LAHGQTTVPFARSSQDLAGDREEIMEAIVAKDAQGAAAAVRDHVLRTAQMLIASVCSRT FT PGLDPEPFLERLDALIS" FT CDS 651994..653139 FT /transl_table=11 FT /locus_tag="AARI_05880" FT /product="putative CoA-transferase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.8.3.-" FT /note="CoA-transferases catalyse reversible transfer FT reactions of coenzyme A groups from CoA-thioesters to free FT acids" FT /db_xref="GOA:E1VT63" FT /db_xref="InterPro:IPR003673" FT /db_xref="InterPro:IPR023606" FT /db_xref="UniProtKB/TrEMBL:E1VT63" FT /protein_id="CBT74816.1" FT /translation="MSQPLEGVKVIDLSRILAGPLCTMTLADFGAEVLKVENGAGDETR FT SWKPPVNAQGVSTYYWSVNRNKQAVIADFADAADLQALRELICEADVLVENFRPGVLAK FT FGLDYCSLHELNPKLVYCSISGFGEKQGAALPGFDLLVQAVGGLMSITGEPEGTPSKVG FT VALVDVLAAQNAVTGILLALRERDASGQGQRVSVNLLHSLLAGLTNQSSSTLATGKSPA FT RMGNAHPSIAPYETFAVQDGVVAIAVGNDRQFAALARELGQPELADDPRFSSNSARVAH FT RQDLKAIIEAATAQDTAVHWAQTLMSAGVPAGKVNSIAEAIEFSKELGLDPVAIITDPA FT TGETTEQIASPIGLSRTSAQYRSIPPAHGQHQELLNTLANQ" FT CDS 653167..654345 FT /transl_table=11 FT /locus_tag="AARI_05890" FT /product="putative acyl-CoA dehydrogenase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.3.99.-" FT /note="possibly involved in the metabolism of lipids. Match FT to protein domains PF08028, PF02771 and PF02770. Acyl-CoA FT dehydrogenases catalyze the alpha,beta- dehydrogenation of FT acyl-CoA thioesters to the corresponding trans 2,3-enoyl FT CoA-products with concommitant reduction of enzyme-bound FT FAD" FT /db_xref="GOA:E1VT64" 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:E1VT64" FT /protein_id="CBT74817.1" FT /translation="MSTAERLLDPADLINFDSLLSAEELALRGTVRGFVKEHIKPNIAK FT WYNDAVFPLEIVPEMAKLGLLGMHLDGYGCGGRSAVEYGIAGAELEAGDSGLRTFVSVQ FT GSLAMSAIYKHGSEEQKQQWLPKMAAGEAIGCFGLTEPTAGSDPSSMTTFARRDGDDWV FT INGSKRWIGLANVAQVAVIWAQTEEGIRGFVVPTNTPGFTATPIEQKLSMRASIQCEIE FT MVDMRLPGSAVLPNVVGLKGPFSCLNEARYGILWGSMGAARDAFEDALAYSQERLQFDK FT PLAGYQMTQQKLVDMALEINKGFLLALHIGRLKDAGKLDLHMISVGKLNNCREAIAICR FT EARTILGGNGITLDYSPLRHANNLESVRTYEGTDEVHTLILGNKLTGVPAFR" FT CDS 654377..655834 FT /transl_table=11 FT /locus_tag="AARI_05900" FT /product="aldehyde dehydrogenase (NAD(+))" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.2.1.3" FT /note="catalyses the following reaction: an aldehyde + FT NAD(+) + H(2)O <=> an acid + NADH" FT /db_xref="GOA:E1VT65" 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:E1VT65" FT /protein_id="CBT74818.1" FT /translation="MKHNGTIVALQQYLNGNWVPGQGSGISTQAAVDGTTVLAEGLAAS FT HEQVAAAFDAAHQAKKSWASTPMAARGAILAKAAGYLKEHSESFGAELAAEEGKTRAEG FT TGEVLRAAQILTYYSGEAERAAGTVFQSPRAGEQILVTHKPLGVVGVITPFNFPIGIPA FT WKIAPALVFGNTVVFKPASLVPLLALRFVQALEYAGLPAGVLNLIIGPGALGDAIIANE FT YLNGLTFTGSTGVGRKLCAAGAARGIPVQAEMGGKNASVVLADADLDLASEQVLFGAFR FT STGQKCTATSRLILDETIADEFLDKLTVRLDQWVTGDPLDPSVHMGPLVDAKSARSAAL FT GVAQALEQGATLHYRGQAPETPSFLAPTILELPAGKAGRANCAWRDEFFAPILSVQRAK FT GPQEAFEAAEDSEFGLSLALFTSNLALALEAQQTLDVGILHVNSESAGADPHVPFGGAK FT ASGYGPKEQGAAAREFYTHTTTTYLRG" FT CDS 655872..656729 FT /transl_table=11 FT /gene="hbd" FT /locus_tag="AARI_05910" FT /product="3-hydroxybutyryl-CoA dehydrogenase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.1.1.157" FT /note="identified by similarity to protein SP:P52041 FT (Clostridium acetobutylicum). Reduces 3-hydroxybutanoyl- FT CoA to acetoacetyl-CoA" FT /db_xref="GOA:E1VT66" 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:E1VT66" FT /protein_id="CBT74819.1" FT /translation="MTIENILVIGAGTMGRQIAMSCALGGYTTVLQDISAEALSAARTE FT LEGWAASRLAKGKLEEATVAQALARLSQSTDLAQSASNADLVIEAAVERLDIKEQIFAQ FT LGQHAPAHAILATNSSTLPSSKVAEASGRPQQVCNMHFFNPALVMKCVEVVRNEQTSDA FT TIAAVTAVADQLGKNPVLVNKEIPGFIANRMMGAINAEALNLAHAGIASIEDIDTTAKT FT ALGHPMGPFELMDMVGLDVIDFIAQATYAETGDEADQPHPMITDKVAAGKLGRKSGEGF FT YPYS" FT CDS complement(656818..657252) FT /transl_table=11 FT /locus_tag="AARI_05920" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VT67" FT /db_xref="InterPro:IPR009002" FT /db_xref="InterPro:IPR012349" FT /db_xref="InterPro:IPR024747" FT /db_xref="UniProtKB/TrEMBL:E1VT67" FT /protein_id="CBT74820.1" FT /translation="MKFEHELNSPVLVLDEDQSWQLLSHSAHGRVATVAAGLIDIVPVN FT YAVHNGKLFLRTSPGNKLAAMSINEKIAFEVDGILSDEAWSVVVHGSAEVLDHEADIQE FT ARESGVTPWIPTQKDFWIRVNVDSISGRHFELGEQPEVAE" FT CDS 657350..658435 FT /transl_table=11 FT /locus_tag="AARI_05930" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR019236" FT /db_xref="UniProtKB/TrEMBL:E1VT68" FT /protein_id="CBT74821.1" FT /translation="MSHISTDGDVRHVASRIEDGVHRWRARRALASGHETVILPYVGYG FT STGPNGSWIRVLARVVLARPGAFEAGQHQAQVIADGIRGFRNFISPILPGGKVRIDVGN FT QHFEVEADRGGVIDVKLMVDLPAGWNEIRLQAHDGDDAQAKILVIDQAQKFGVISDVDD FT TVVVTALPRPLLAAWNSFVLSEHARVATPGMAVMLQKVLLEHPGSPTIYLSTGAWNVAQ FT TLQRFISRNLFPRGPLLLTDWGPTDRSWFRSGMQHKVDQLRRLAEEFPDMSWVLIGDDG FT QHDPAIYAEFARRYPELVRAIVIRQLTPSEAVLAGGRSHELRRTTPEVPWVYEPDGARI FT LKQLAKLGIVSTESVNLLKDD" FT CDS 658438..658905 FT /transl_table=11 FT /locus_tag="AARI_05940" FT /product="thioesterase family domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF03061: thioesterase FT superfamily" FT /db_xref="InterPro:IPR006683" FT /db_xref="UniProtKB/TrEMBL:E1VT69" FT /protein_id="CBT74822.1" FT /translation="MAEATLRVQIPMRWGDMDAYGHVNNVNLIRLMEEARIAGFGVPGG FT TGAPGVTPQAEIFSAVPQGTQILVVEHRVRYSRPLEYRNIPVNVDLWVANIKPASFDIC FT YEFRDPVADYLCVKASTTLAYFDPATSRVQRLSPEQRAGLSAYEGAGTFSK" FT CDS 658969..659823 FT /transl_table=11 FT /locus_tag="AARI_05950" FT /product="putative siderophore-interacting protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="identified by match to protein family PF04954. Match FT to protein domain PF08021. Possibly involved in removal of FT iron from iron-siderophore complexes" FT /db_xref="GOA:E1VT70" FT /db_xref="InterPro:IPR007037" FT /db_xref="InterPro:IPR013113" FT /db_xref="InterPro:IPR017927" FT /db_xref="InterPro:IPR017938" FT /db_xref="UniProtKB/TrEMBL:E1VT70" FT /protein_id="CBT74823.1" FT /translation="MSQPTGGGPQAGGRPARPQVVLQVLKREEIAPHLVRLTLGGPGMS FT DFVDKPVTDRYVKFLFAKPELELELPYDMEALRAQLAPEDMPVRRTYTVRRSDLQASTI FT EVDFVVHGDEGLAGPWARDAQIGSSICFSGPGGMFVPRDEFDFHFFAGDETAIPAIAAS FT LEAMSAQMTGLVIIEVADQADEMQLQAPAGVEVRWIHRNAAFTPETTILDSSVRQIPWP FT GGRVQVFAHGEREVMKKLRAYFYDERGVDRRDMSLSAYWAFGRAEDAFQAEKRTEVGKI FT FAD" FT CDS complement(660154..660996) FT /transl_table=11 FT /gene="alkA" FT /locus_tag="AARI_05960" FT /product="putative DNA-3-methyladenine glycosylase II" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.2.2.21" FT /note="DNA repair enzyme that hydrolyzes the deoxyribose N- FT glycosidic bond to excise various alkylated bases from a FT damaged DNA polymer" FT /db_xref="GOA:E1VT71" FT /db_xref="InterPro:IPR003265" FT /db_xref="InterPro:IPR011257" FT /db_xref="UniProtKB/TrEMBL:E1VT71" FT /protein_id="CBT74824.1" FT /translation="MMDMHLPATGTLDVSHALAVLKLHSLPVQERLDEPAARLQRVLQV FT KGRLVEVTLELTPSGIRLSHDAPTEFSLHISEVINYWFGVQQDTSDSYEALNAISCYRS FT LAAAFPSLRLISYPDHFEALATTVIGQQISLAAARTLGSRYVGALGQLHSSGLRAFPTA FT SATAACTPEELREIIRCPLARATTLHTVAAWFQAHGQLLLSNGPEFLDELQGLRGVGPW FT TRNYVALRGLRDPEIFLESDLVVRRALRKLHDSGLAVSPPPVGTGSLATLLLWSFDAS" FT CDS complement(660998..661591) FT /transl_table=11 FT /gene="tagA" FT /locus_tag="AARI_05970" FT /product="putative DNA-3-methyladenine glycosylase I" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.2.2.20" FT /note="DNA repair enzyme that hydrolyzes the deoxyribose N- FT glycosidic bond to excise various alkylated bases from a FT damaged DNA polymer" FT /db_xref="GOA:E1VT72" FT /db_xref="InterPro:IPR005019" FT /db_xref="InterPro:IPR011257" FT /db_xref="UniProtKB/TrEMBL:E1VT72" FT /protein_id="CBT74825.1" FT /translation="MTEDLIVGKDGLARPRWAASNDMLRTYYDQEWGMPITSEAGLFER FT LSLECFQSGLSWAIILSKRESFRQAFAGFAPEQVALFTEDDFERLMNDAGIVRNRLKIR FT ATIANAEATLMLREEGGLPDFVWSFKPEQTPAPHSFSEVPTQSPESKALAKELKKRGFK FT FVGPTTMYALMEAIGMVDTHLVGSHRRGSSGIWA" FT CDS 661673..662044 FT /transl_table=11 FT /locus_tag="AARI_05980" FT /product="putative ArsR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF01022: bacterial regulatory FT protein, ArsR family. ArsR-family transcriptional FT regulators include several proteins that appear to FT dissociate from DNA in the presence of metal ions" FT /db_xref="GOA:E1VT73" FT /db_xref="InterPro:IPR001845" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VT73" FT /protein_id="CBT74826.1" FT /translation="MAIIESNVDVLEVRSSKLQLAALFHALADPTRLLILEHLHTGEHK FT VKELTEHLGLAQSTVSAHLACLKDTGLVNVRSQGRSSIYSLSQGEALDALTDSAMALIA FT KDLAPHHWHEAHSTDEAGG" FT CDS 662047..662973 FT /transl_table=11 FT /gene="czcD" FT /locus_tag="AARI_05990" FT /product="cobalt-zinc-cadmium resistance protein CzcD" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="identified by similarity to protein SP:P13512 FT (Ralstonia metallidurans). Cation diffusion facilitator FT (CDF) family, Cd2+, Zn2+, Co2+ efflux permease (TC 2.A.4.1. FT 1). Also binds Cu2+ and Ni2+. Increase tolerance to FT divalent metal ions such as cadmium, zinc, and cobalt (is FT considered to be an efflux pump that remove these ions from FT cells)" FT /db_xref="GOA:E1VT75" FT /db_xref="InterPro:IPR002524" FT /db_xref="UniProtKB/TrEMBL:E1VT75" FT /protein_id="CBT74827.1" FT /translation="MGHNHSHGHSHDHSAANRTRLAWAFAITALILIAEVIGAIITNSL FT ALLVDAAHMLTDTLGLLLALTAANLIMRKPTTNRTWGFRRAEVLSATFQSALLLAVGVY FT AAIDAVRRLFTPAEVQPAGLLLFGIIGLLGNVISMWIISAGRDSNLNMRAAFLEVVNDA FT LGSVAVIIAAVVISFTGWMRADSIAALVISALIVPRAVKLLGETTHILLESTPRGLDLL FT AVREHLEALPGVIAVHDLHASQIASNLPVLTAHVVVEDSFFSAGVAGGLLRDLQQCVAS FT HFTVSIEHSTFQIEPASHRSTEHEHGC" FT CDS 663094..663843 FT /transl_table=11 FT /locus_tag="AARI_06000" FT /product="putative ABC transporter, ATP-binding subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT lipoprotein translocase (LPT) family (TC 3.A.1.125.z). FT ABCISSE: ABC transporter, ATP-binding protein (ABC), o228 FT family (members of this family might be involved in a more FT general lipoprotein releasing mechanism common to all FT prokaryotes)" FT /db_xref="GOA:E1VT74" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VT74" FT /protein_id="CBT74828.1" FT /translation="MTSETLSKTEYAVAARGLTKTYGHGTTRVEALRDVNVSFERSRFT FT AIMGPSGSGKSTLMHCLAGLDSADSGEIIIGGKNLLDLSDDQLTEMRREQIGFVFQSFN FT LVPTISAKDNILLPMSLAGKKHDRNWFNTVIDALGLGDRLNHKPHELSGGQQQRVAVAR FT ALLTRPEVVFGDEPTGNLDSRTGAEVLSLMRTSTREMGQTIIMVTHDPVAASYADTVLL FT MKDGIIVGSIQEPTVATVTEALASLAE" FT CDS 663847..666342 FT /transl_table=11 FT /locus_tag="AARI_06010" FT /product="putative ABC transporter, inner membrane subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT lipoprotein translocase (LPT) family (TC 3.A.1.125.z). FT ABCISSE: ABC transporter, permease (IM2: 2 IM domains fused FT into a single polypeptide chain), o228 family (members of FT this family might be involved in a more general lipoprotein FT releasing mechanism common to all prokaryotes)" FT /db_xref="GOA:E1VT76" FT /db_xref="InterPro:IPR003838" FT /db_xref="UniProtKB/TrEMBL:E1VT76" FT /protein_id="CBT74829.1" FT /translation="MLHVALSNIKTYARRYIAVILAVAIGTAFLAATLSVNSSTQATLK FT NSLGDAYKNADLVAYPDWDLASDGQDPTALSLKDVKEVQNLSAVTTAYGLGYVDGLLRT FT ADDSYGVSMQPVDPDQGLGGMELLEGRAPQGSNEIIIDAAHAKDMGTSIGDVVALENGA FT ASAENYTIVGIQRSTTNPRTSAYALAGMSEQAWKHFAGEQPLISEIVVNTDGSEAALQE FT QLEKLFADKKMTDIAVMSADEKVLNEVAQLTGGTDQLSVILLVFALIALVVTGLVVVNT FT FAVVIAQRTRELALLRILGAKRKQIRSSVLIEALVIGILASILGVLLAVVLMFGLIQLL FT HVLVPEMSYATLALTPQGLAIPILVGVLMTVIAASLPARRAMKLAPLAALRPFDAASVK FT NRAGKARIIFGILFLLAGASLLAYGAFKGDLIIAFLGGLVSFPGILMLASLFVPSSVSG FT IGKAVAGKSTAGKLAALNAVRNPGRTTATATALLIGVTLVSMIMVGGQTAKASLNNAVA FT AEFPVDMMVSFYDRKVSDSEIKSMLEKIGEVEGITAGSSFTSAYADVDMGTGEMYNSEI FT MSVDPEGFAEVALDPDIVPADGEIVYVLSNPENPTVKIGDQTLKVKKTEAMLSGNIVTE FT QTFDKLEVEEANQYTGILLKVDSDVRASAVNDLVTKISAITGVESSMINGGLVMKSMFS FT QIIDVLLMIVSALLAVAVLIALIGVANTLSLSILERTRENSLLRALGLKKKQLRGMLAT FT EAVLIGGVAALLGLVLGVVYGLLGARSALASMGEMTYEIPWLQLALVLLISIVAALLAS FT VTPGRRAAKLSPVEGLAVE" FT CDS 666437..666781 FT /transl_table=11 FT /locus_tag="AARI_06020" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VT77" FT /protein_id="CBT74830.1" FT /translation="MNIELTRFRVLPGKISVVNEWLDFLNSNMPAVLETLEGEKMYVET FT IFSETLDGVDYLYWYSIQGEGGIAVQGSAHEIDKVHLQYWKQCIDPDFAPQELAPRVVM FT IPERVQHSMA" FT CDS complement(666857..670183) FT /transl_table=11 FT /locus_tag="AARI_06030" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VT78" FT /protein_id="CBT74831.1" FT /translation="MSIEMTLPLGGALNPGQHRLSRVQIVNWGTFHGLHDLAVDRAGTL FT VTGHPGVGKSTLFDAMGHLFFATPRLNESANDAATREDRRTTFSYMRGRKFKTSAGTVY FT QRPGATWSAIVLSYDDGMGNTVTAGAVFDLPDAGLEGQVSKHYLLCEGKIDISELENHG FT PRRFTVTSLSKALAPSEAFDTHKAFIERLRRRLGVESDKAFALLRTLQNGKGLAKGVNQ FT FFRYEVLEEPATLKAAAAAVEDFAHLRGIYRQLDTARAQRDVLAQVPQQDQAYRSLAEQ FT INSVQQLLESEVHTLEAQVRQLVLRNDLDSHESNLAKFKADEASLRQRKDELDDQLQSL FT EAAHDSAGSASLMLLEREADVARKSLSEKENIIRTLQQQATDAGLAFDFSATGLDELRA FT NAARTLQQLSSITHDAQTVEYEAMASLVNLRKRAETLAEQIRSYQRRASNIDDRSIAAR FT RAIASACALKEDQLPFAGELMDVSAEAGMWRLAAEKALHSLARTLLVPGEFLAQVTHAI FT DQLDGLGRVRWSDISQKPRDAEAGPADLVTKLDFAPGEAGSWLKAKITADYPLACVEND FT AAMHVHPKAITPAGTIKTGAGSFERDTRTLPASEYLLGFTNESKIAELQSKATRLDEKI FT VQAQQAADERSAAKNKIVAKAQLLQALISDERTFAQLDASKALEALRRSEQKLGDALAL FT SGDSSRVRQQIEAAKAEAETLVGELALVRSRISDLELQVQRAQQVLSNSDDLASGWEEN FT IPNALRQHQLLGPVLQQVVSGNCPASEEISEAFAEVKLQLGSQVNSLQSQRQEIGGTLS FT DTFRRFAREFGTSHAQTHGTTAEAAGHYAQLHDQIVADGLPHHEAQFREYFANRSYERF FT SDLLQLLDEERRMISERIKPLNQILSEVTFEHGSVLRLEATQSIPVEAGTFRKELKDAL FT QEAYTTKDESTLASSYQALESLVTALSDPAMASWRSTVLDVRQHVMISCNEHKSNGEVE FT TGLEPGTLSGGEGQRFTSFIMGAALAYQLGFASAGFTSYGTVMIDEAFIQANSEYAAAG FT IRALQEFGFHLVLAAPEDKIDLSRHLGSITDIIKHPGSNISGFVTTGRSPAMATTITLR FT S" FT CDS complement(670187..670873) FT /transl_table=11 FT /locus_tag="AARI_06040" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VT79" FT /protein_id="CBT74832.1" FT /translation="MTKSDSYAAPITEPLFDGDTGTFTLPLRQLLVRLLRGPYLDGSVD FT AAAWQLLLDQQQSISDYFAEIFLALSLDMDRKIAMLTPVQIEQVHTSPIAPRRPLKRDE FT TLLALRLRLLLEQHSGSGSDAVISRAGMHEVLAEHRQATDRDDKRFAESCDAAITRLQA FT LRLLTGTELENEFRISPALAMALPITNIQDIPRYIAAIDANDPAFNLSGDDAEGLAEQT FT PELVQE" FT CDS complement(670870..672330) FT /transl_table=11 FT /locus_tag="AARI_06050" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021804" FT /db_xref="UniProtKB/TrEMBL:E1VT80" FT /protein_id="CBT74833.1" FT /translation="MQPSHRANSLWLQSQQFKSSAAYRLLTAQPWALAFIRAEFTADRS FT RVALELFHASLDSFLKQARKSDDQIPSSYSAQDFAETWVKQGILARPLIDGRFIYEPSA FT QTLRTLRFLADFSTDDSHLNSSRLNTLLSSLESLAHETDPDPEARIRALESQIALRQAQ FT IDQLRSGDDPAVLSRTTALSATRSVLDLASSLPADFRRMRDGVQDMLHSLREGILDAST FT AKGVAVGQVLEADRQLRSTAEGETFSGFTEFLNSPDAQQRFRAALAEVLERDFVDDLET FT PERQILTNLLRELRRQAAEVHASYGKLSESLHAFVQSEDYKQAELLRQAVREAELAISK FT SASLKPRSGLTPMELFAPQFVTLTGLGIYDPSEHVAPPPLAQAPEFSEADIVRNPSTPQ FT ADLPLLRESITRNLNCSGSGAIRLDAVFETLDAEHRHLNTIRALVEIGRTNGESLNESE FT LLNIDFQQLDGSMRTAILPALSFTKEPL" FT CDS 672557..673813 FT /transl_table=11 FT /locus_tag="AARI_06060" FT /product="conserved hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.748 FT between position 22 and 23" FT /db_xref="GOA:E1VT81" FT /db_xref="InterPro:IPR002509" FT /db_xref="InterPro:IPR011330" FT /db_xref="UniProtKB/TrEMBL:E1VT81" FT /protein_id="CBT74834.1" FT /translation="MRNLRLAIALGLTLSVAGCSAAEDSSNPAPDPAAVQKAEQEKARV FT ENVKAEINRLADGYDYDGAIRLAKKDSSKALNQMVGGLEDEKEQVSAWEDPDQIPHLFF FT HSLVVDPERAFDDGSSSQGYANYMVTQKEFTAILESLYARDYVLVNPEDFASVDDDGKM FT EYRDIMLPKDKKPLVLSVDDLSYYEYMENDGFASKLVLDGDGTVRNEYVDAQGETQIGA FT FDVTTMVDDFIAEHPDFTYRDARGLIAMTGYNGVFGYRTSASQYPESKTLKADQKDAKE FT IAEAMKDSGWVFASHSWGHIATGTVSMGRLERDTKLWKDEVQPLVGKTMHYIYPFGSDI FT AQTQSYSGARYEFFKDQGFKYFYGIDGTIRSWMQQGDNYQRQMRINVDGLQMAKEQRGD FT RPVLETFFNVQDVIDPARK" FT CDS complement(673835..677290) FT /transl_table=11 FT /locus_tag="AARI_06070" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR019993" FT /db_xref="UniProtKB/TrEMBL:E1VT82" FT /protein_id="CBT74835.1" FT /translation="MFFLEDKFIFSASDLSISVDCNYQSLYLLDVKLGRRPRPDGVRDE FT MLERTAALGDAHEQNVLKGLIATYGEYDPIAGTGVKQFTDRPKMSQAGLRAAHEETMKV FT LRSGADVIFQATFFDGKFLGFADFLVRDQDGTWAVWDTKLARHARVSALLQIAAYADQM FT LAEGLPVSSSATLVLGDGTHSVHRVDEVLPVFRAQRERFLKMVRNHLAGDQPAQWNSDA FT LRLCGRCDFCEEQSLATRDLLLVAGMSMVQREKLRTRGIYTIDQLAQLEAEPGTSLQRV FT TEQAKMQLGLAKTDGSVQGVSYRVKNEKPISSLPRPDQGDIFFDFEGDPLYQDPSDGSW FT GLEYLFGVIEYDTNEPVFKPFWAHSRSEERQAFLDFIAYVEERRQRFPHMKVYHYAPYE FT KTALRKLSQVHIAGEDEVDQWLRENLLVDLYETVRNALVVSTRSYSIKKLEPLYMGEHL FT RSGDVTDAGASVVAYAQYMQARNSPDPAAAEAILESIADYNEYDCLSTLRLRDWLLSLS FT DEAPGTLADMPEPPAAGEEYEPTPEELRLQNYLADLPHGQALSDDDRAIAMVAAATGYN FT RREKKQFWWEHFDRLSVPMDDWSDVRGVFIVDTGEILEDWHKATARARTYTRVTRLNGT FT LAEGSLLSPGSSVFAMFDAPLPEGMEVDDSVRGGAFNATVVELGEGWITIAEKSSAKIP FT EYGALPCALTPDKPLATMSIDAALKEIAQRVGATVPVLPERSGIDILRRIPPRLKTLSA FT PVEPSLVDGQAQIYPAVVQTLKDLDNSYLAVQGPPGTGKTFVASHVIRELIEHGWKIGV FT VAQSHAVVENVLRKAVEAGVDPDVVAKEVKHDDPVPWSGTSKDSLSEVLGSADGALIGG FT TAWTLTGSKVPEGSLDLLVIDEAGQFSLANTLAVSRAARNLLLLGDPQQLPQVTQGTHP FT QPVDESALGWLSGGEPVLPGELGYFLAASWRMHPALCAKVSALSYDHQLFSADAAGLRL FT LEGTPAGVETVFVEHRGNTVSSPQEAETIVRLVREHLGMMWSPGAGKPARPLTVADILV FT VAAYNAQVNLVREVLEAEGLSSVKVGTVDKFQGQEAPIVLVTMACSSAADASRGIEFLL FT NRNRVNVAISRGQWKAIIVRSEALTDYLPSNPSTLSQLGAFMAL" FT CDS complement(677368..677688) FT /transl_table=11 FT /locus_tag="AARI_06080" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VT83" FT /protein_id="CBT74836.1" FT /translation="MSRIASTALAVTGLLGGYATGRATKKRPLAAVVLGTAGTGAFLLW FT KKDAGTTKAIALISAYLGGFGASHPLAKKIGAWPAVNSVTAGVAILSLLLGGSDKNQEE FT LS" FT CDS 677847..678566 FT /transl_table=11 FT /locus_tag="AARI_06090" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VT84" FT /protein_id="CBT74837.1" FT /translation="MNLDIAQAWERLSQPVNVALTQWQWLIVALVILLLVVPRPMWRIT FT GLYSTLVHELGHIVAALFTGRYVAGLRLGWDHSGEVRSVGRGKLSVIISGVFGYPAPLW FT VSAVMFWGIASGYAGRALGIYALLFLVALIFVRNWPAFVVCIISAVVALSVVFYAPVEA FT YLYLALLIAGFLLLAGLKDFVKLLSVHIWRRRDLAQSDAYLIAEATGTFATLWLLAISS FT LGAGGLLWAMLSLFRLF" FT CDS complement(678549..679727) FT /transl_table=11 FT /locus_tag="AARI_06100" FT /product="ribonuclease BN-like protein" FT /function="3.6 RNA modification" FT /note="PF03631 (ribonuclease_BN, ribonuclease BN-like FT family): this family contains integral membrane proteins FT with 5 to 6 predicted transmembrane spans. The family FT includes ribonuclease BN, which is involved in tRNA FT maturation" FT /db_xref="GOA:E1VT85" FT /db_xref="InterPro:IPR017039" FT /db_xref="UniProtKB/TrEMBL:E1VT85" FT /protein_id="CBT74838.1" FT /translation="MPNQNGKTKDRFKESLNCYPRALREFFRNDGLDVAASLSYFMVLA FT MFPGLLALISLLALAGASESGTKWIMELLEQSLGASGQSSGGDSQQLLDTAEQLLEGLA FT SQAGGTFWTILAGSLGALWSTSGYVTAFSRALNRLYGAPEGRPQWKRRPQMFLITVLIM FT LVAVVTLVLVLASGSVARGIGNIFGLGDGFVLMLNIAKPPILLIMLLLVLALLYYFTPN FT VKPRKFRWFSPGTLTALVILGLSVFGFGIYVSQFASYSATYGTIGGVIILVLACWISNI FT ALLLGASVDIEFIRLRQLRTGAQAVDDVLLPLRDDTLIAKQELAAYKDLVHAQEVRINH FT GGDPLEDMEMDPVSGPKRKTKLLPMGLVAVAAWTAGRLNGKRVLRRNSEESK" FT CDS 680351..681097 FT /transl_table=11 FT /locus_tag="AARI_06110" FT /product="resuscitation-promoting factor precursor" FT /function="4.6 Miscellaneous" FT /note="identified by similarity to protein SP:O86308 FT (Micrococcus luteus). Bacterial growth factor or cytokine FT involved in resuscitation of dormant bacteria and FT stimulation of bacterial growth. Signal peptide predicted FT by SignalP 3.0 HMM (probability: 1.000) with cleavage site FT probability 0.996 between position 36 and 37" FT /db_xref="GOA:E1VT86" FT /db_xref="InterPro:IPR002482" FT /db_xref="InterPro:IPR010618" FT /db_xref="InterPro:IPR018392" FT /db_xref="UniProtKB/TrEMBL:E1VT86" FT /protein_id="CBT74839.1" FT /translation="MIQQKTKNLIRRGGASLAAVAVAGTAIVAASAPANAASTWDKLAQ FT CESGGNWSINTGNGYYGGLQFSLATWKGFGGSGMPHQASKAEQIRIATKVQASQGWGAW FT PACTAKLGISGSPSGSSTPQKQAPKQQAAPKQQAAPKQAAPKQAAPKQAAPKQAAPKQQ FT APVQKQAPKQQAAPKHAAPAPKAPVFNIDVTDSGKDYTVKSGDTLAKIADQLGVKDWRG FT LFVLNDDQLANPDLIMVGQTLNVPSN" FT CDS 681210..682580 FT /transl_table=11 FT /locus_tag="AARI_06120" FT /product="putative CoA-transferase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.8.3.-" FT /note="CoA-transferases catalyse reversible transfer FT reactions of coenzyme A groups from CoA-thioesters to free FT acids" FT /db_xref="GOA:E1VT88" FT /db_xref="InterPro:IPR003673" FT /db_xref="InterPro:IPR023606" FT /db_xref="UniProtKB/TrEMBL:E1VT88" FT /protein_id="CBT74840.1" FT /translation="MFSADDERQSVESILGTGFYDHQLLGMGDLDSVSGPPVWWGGPLN FT VERLAAGSVSLVCAALDALAGAELKLASSTPSIGAAFGSSSHLRIEGQRTQGFAQYSGF FT YRCMDGWIRTHANYPHHERALLTALGMASGSGIEDVLRHLGAREAQERIVSAGGIAAVV FT RSRQQWLNSAEGSESGRGPWAQFSLREASSTSSWTYGQRTEMPLQGLKILDLTRVIAGP FT TASRTLAAFGAQVLRLDAPQLPELAWQHVDTGFGKRSTLLDLKSAPGQARLHELLGEAD FT ALILGYRPGALARAGLGLDELRERYPDLIVAELSAWGFEGSWAQRRGFDSIVQAATGIS FT QACSDAGHRPGALPVQALDHATGYGLAAAVIALVRARRVQRQTGSVRFSLARTADALFA FT FDAPHPPVQSLGEVQLRRMSSSYGELEYVGPPFSVAGRELDFAKPPPVYGQDEPVWN" FT CDS complement(682577..683416) FT /transl_table=11 FT /locus_tag="AARI_06130" FT /product="PaaX-like transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF08223: PaaX-like protein C-terminal FT domain. This family contains proteins that are similar to FT the product of the paaX gene of Escherichia coli. This FT protein is involved in the regulation of expression of a FT group of proteins known to participate in the metabolism of FT phenylacetic acid" FT /db_xref="InterPro:IPR013225" FT /db_xref="UniProtKB/TrEMBL:E1VT87" FT /protein_id="CBT74841.1" FT /translation="MASNTSLSALSLDDFEARTGSATSIIRTITGLYVRHEAAGVARTQ FT IVELAHAAGVSVPAAQTAISRLIDRQVLEASQASSLHVPHAAQQMFERGARRIFTPRQM FT SGTDPWCLVAYSLPEALRSLRHQIRKHFLQLGGGMASAGLWIFPEYLRAEVTAVLSALG FT ARDHATLFTAQQPHFPGTPQQAAGAWWDLQRLAALHEAFLENTAAVDAQDIAPPNAYRG FT YVTMIDSWRALPYLDPGLPEFMLPAQWPGAESRERFMALSEALQEPASAFARSLLDS" FT CDS complement(683406..684272) FT /transl_table=11 FT /gene="kynA" FT /locus_tag="AARI_06140" FT /product="tryptophan 2,3-dioxygenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.13.11.11" FT /note="catalyses the formation of N-formylkynurenine from FT L-tryptophan, the first step in the kynurenine pathway FT (major pathway of tryptophan metabolism)" FT /db_xref="GOA:E1VT89" FT /db_xref="InterPro:IPR004981" FT /db_xref="InterPro:IPR017485" FT /db_xref="UniProtKB/TrEMBL:E1VT89" FT /protein_id="CBT74842.1" FT /translation="MSNHQPQTENQRDIEDGVRTDFKNTMSYGSYLDLDRILSAQHPVS FT VPEHHDEMLFIIQHQTSELWLKLMLHELLEARRLLEVDDFGKALKCLARVKHIQKTLTE FT QWSVLATLTPREYAQFRDFLGSSSGFQSFQYRAVEFILGNKHEGMLKVHEADPKAHEVL FT TKLLHEPGLYDVFLAALARHGYAIPEEVLSRDVTKPWAFQEALVPVFKDIYESEDTRWG FT FYQACEDLVDVEDNFQAWRFRHMRVVQRTIGFKRGTGGSSGVDFLKRALDLTFFPELFA FT VRTEIGK" FT CDS 684423..685106 FT /transl_table=11 FT /locus_tag="AARI_06150" FT /product="putative FMN reductase" FT /function="2 Intermediary metabolism" FT /EC_number="1.5.1.29" FT /note="identified by match to PF03358. FMN reductase FT reductase catalyses the following reaction: NAD(P)H + FMN = FT NAD(P)(+) + FMNH(2)" FT /db_xref="GOA:E1VT90" FT /db_xref="InterPro:IPR005025" FT /db_xref="InterPro:IPR023932" FT /db_xref="UniProtKB/TrEMBL:E1VT90" FT /protein_id="CBT74843.1" FT /translation="MGKSIVVISGGLGTPSSSSLLGSRIGQDIADQLASAGVQTHVRNV FT ELREHASDIANNMLTGFAAPGLQDVIDAVTEADVLVAVTPVFTASVSGLFKSFLDVLDP FT KSLSGKPVVLAATAGTQRHQLAIDYAMRPIFSYLRAHIMSTTIFAASEDFGGQGLSGTL FT SDRARRVAREVVLALSLSDGTSSTGTQLSDTRSIAPSVSEFADPDDELSSLPFESLLAN FT LKSGS" FT CDS 685347..686132 FT /transl_table=11 FT /gene="hpcG" FT /locus_tag="AARI_06160" FT /product="2-oxo-hepta-3-ene-1,7-dioic acid hydratase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.-.-" FT /note="identified by similarity to protein SP:P42270 FT (Escherichia coli). Also named OHED hydratase. Involved in FT the homoprotocatechuic acid pathway. Catalyses the FT conversion of 2-oxohept-3-ene-1,7-dioc acid into 2,4- FT dihydroxyhept-2-ene-1,7-dioic acid" FT /db_xref="GOA:E1VT91" FT /db_xref="InterPro:IPR002529" FT /db_xref="InterPro:IPR011234" FT /db_xref="InterPro:IPR012690" FT /db_xref="UniProtKB/TrEMBL:E1VT91" FT /protein_id="CBT74844.1" FT /translation="MLSEETITAIADELVQAGQTRTPVPRLTARYPEMTVEDSYRVQNL FT WRQRSEAAGRELVGRKIGLTSRAMQMATGITEPDYGIIFDDMVYDSGAKLKWEDFTGAR FT VEMELAFKLKKDIEGPRANIFDVLEATEYVIPALEILDARVEMEGRTIVDTISDNAAMG FT AMVIGGNPVKPENIDLRWVSGILFKNQTVEETGVAAGVLNHPAAGVYWLANKIAPHGDK FT LKAGEIILAGSFTRPMWVNAGDTVFADYGPLGTVTCHFE" FT CDS 686117..686926 FT /transl_table=11 FT /gene="hpcH" FT /locus_tag="AARI_06170" FT /product="2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.1.2.-" FT /note="identified by similarity to protein SP:Q47098 FT (Escherichia coli). Involved in the homoprotocatechuic acid FT pathway. Catalyses the conversion of 2,4- FT dihydroxyhept-2-ene-1,7-dioic acid into succinic FT semialdehyde and pyruvic acid" FT /db_xref="GOA:E1VT92" FT /db_xref="InterPro:IPR005000" FT /db_xref="InterPro:IPR015813" FT /db_xref="UniProtKB/TrEMBL:E1VT92" FT /protein_id="CBT74845.1" FT /translation="MSFRVEPDSSLKDALKDADHSLAGVWVCSASPLIAEICAGAGFDW FT LFIDAEHSPNDLQNVLAQLQAVRSYPVVPVVRPAVNDPVLIKQYLDLGVQSLIIPMVND FT AQQAAAAVAACQYPPKGVRGVGSALARSARWNRIPEYLTRADETITIMVQIEADEAVRN FT VEEIVATPGVDGIFIGPSDLAASMGVIGQQSHPDVVAAVLKSINAAKAAGKYAGVNAFD FT QKSAREYMDAGADYVGVGADVALLARATEALAASFSSEAQSKAPQSY" FT CDS 687032..688321 FT /transl_table=11 FT /locus_tag="AARI_06180" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="8 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VT93" FT /protein_id="CBT74846.1" FT /translation="MKTVMLRLRNGWPMPLALQGVFEILQSVVFCLALIALPLIAVYFS FT GGFLEDSFETILQFAGFIWLLIHGVPVEILNLGPEADPSSVTGWATLIPLGLSLLPFLF FT CLRAGRRIARASYTDQLWQGLLGAFVAYGAIGTGIGFLANNAYAQVNILAAAFIPLIIA FT LVGLIIGARREAGSWARLFGVDTAAYIQRVSPHRRWAGSYVWHVIVAGFLGYVAAVGIS FT GLLLTINLGVHWTDVANVSQELRPGPIGSATLTLVQLSYVPNAVFWVLSWISGGGFSIG FT TGSTLSTLETTVGPLPSIPMLASLPSGEVAHQWLFLLIPVAAGIVAGWYFLRVGENHLE FT DWFARRIPFNSLSLAASTACLAVFTGIVTGLLSLIGSWMSSGSLAIGRLVEIGPNMWAT FT AGALALQIGVGTAIGYLIAPLFETDPVLEG" FT CDS complement(688340..688981) FT /transl_table=11 FT /locus_tag="AARI_06190" FT /product="hypothetical secreted protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.998) with cleavage site probability 0.256 FT between position 28 and 29" FT /db_xref="UniProtKB/TrEMBL:E1VT94" FT /protein_id="CBT74847.1" FT /translation="MMPKAHLGKIAALTLTGLLSLNACSASAPQTEESSLPVPSAEEFL FT PLLAQTQSDGDKLPEGFEDTDSYDAQTRHLLATSDFGKHYVAVGNEGQLCMVTIPKPEQ FT KDGDFEIAGTTCPTMDYVVENGVPLKVDGGENSLEVVTYLLPAGISSVTVENSMTGLRA FT EHPDIKAEDIQVISENDAVLLVMEEATAKELGTITINRSEADPLVLASLT" FT CDS complement(689083..689613) FT /transl_table=11 FT /locus_tag="AARI_06200" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VT95" FT /db_xref="InterPro:IPR024344" FT /db_xref="UniProtKB/TrEMBL:E1VT95" FT /protein_id="CBT74848.1" FT /translation="MSQIVPDQKNWTVVLETVCQQCAYDVRNISLSDVIVQLPAYVDRY FT IQVLARPDAQTRTNPARWSDQEYVAHVAEMLQVMVGRFNLMLEQEDPTFPNWDQDQAAD FT EGNYNSLTAGEVAERLREGATQYVAKLSAIDPTQYSRRGLRSNGAAFTVETLNQYAWHD FT IVHHLWDLTAETS" FT CDS 689764..690333 FT /transl_table=11 FT /gene="purN" FT /locus_tag="AARI_06210" FT /product="phosphoribosylglycinamide formyltransferase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.1.2.2" FT /note="catalyses the NADP-dependent decarboxylative FT reduction of 10-formyltetrahydrofolate into FT tetrahydrofolate. Involved in DNA synthesis and in de novo FT purine biosynthesis pathway" FT /db_xref="GOA:E1VT96" FT /db_xref="InterPro:IPR002376" FT /db_xref="InterPro:IPR004607" FT /db_xref="UniProtKB/TrEMBL:E1VT96" FT /protein_id="CBT74849.1" FT /translation="MRIVVLVSGTGSNLQAVIDAVAQGQLQDVEIAAVGADKHDTYGVQ FT RSAEAGIETFVVNFKDFADRGDWNHALTEKCLSYAPDYVVSSGFMRIVGEEFINAFDGT FT YINTHPALLPSFPGAHGVRDALAYGVKVTGCTVHIADAGVDTGPILRQEAVAIEADDTE FT ESLHERIKVVERRLLIATLADLAQGK" FT CDS 690366..691880 FT /transl_table=11 FT /locus_tag="AARI_06220" FT /product="short-chain dehydrogenases/reductases family FT protein" FT /function="2 Intermediary metabolism" FT /note="identified by match to PF00106. The short-chain FT dehydrogenases/reductases family (SDR) is a very large FT family of enzymes, most of which are known to be NAD- or FT NADP-dependent oxidoreductases" FT /db_xref="GOA:E1VT97" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VT97" FT /protein_id="CBT74850.1" FT /translation="MTEKTPSPELAAESELFSEAELATTLKVLSVVHQLDSEDERHIAV FT RRATSNMFKAAKRYRKSQKRAEISAADRSVIERTATGSPQRLDDETLGLDLSTSTEGES FT AGEFRKPRGCYICKKRYTTVDAFHHYLCPECAAEGRERRDARADLRGKRALLTGGRAKI FT GMHIALRLLRDGAHTTITTRFPKDAARRFTALEDSAEWIHRLRIVGIDLRDPAQVIDLA FT DKMAAAGPLDILINNAAQTVRRSANSYQHLIESEQQPLPAELLSRSEGLELWGEANPPA FT EHPRALASAFQLQDSALLASPAERSYDAQQLAELAMTAGSASMERIAQGRAIDAGGLVP FT DVVSENSWTQRLGDVDALEMLEVQLCNVTAPFLLASRLRPALAASKARRKYIVNVSAME FT GQFSRRYKGAGHPHTNMAKASLNMLTRTSAEEMLNSDRILMTAVDTGWITDERPHEAKI FT RKVAAGWHAPLDLIDGAARVYQPIVDGERGIDLYGCFLKDYEPSPW" FT CDS complement(692048..695068) FT /transl_table=11 FT /locus_tag="AARI_06230" FT /product="putative alpha-mannosidase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="3.2.1.24" FT /note="EC 3.2.1.24 hydrolyses terminal, non-reducing alpha- FT D-mannose residues in alpha-D-mannosides. Also hydrolyzes FT alpha-D-lyxosides and heptopyranosides with the same FT configuration at C-2, C-3 and C-4 as mannose" FT /db_xref="GOA:E1VT98" FT /db_xref="InterPro:IPR000602" FT /db_xref="InterPro:IPR011013" FT /db_xref="InterPro:IPR011330" FT /db_xref="InterPro:IPR011682" FT /db_xref="InterPro:IPR015341" FT /db_xref="UniProtKB/TrEMBL:E1VT98" FT /protein_id="CBT74851.1" FT /translation="MHDDNSLTIGRVRRVLTERILPAIYSETMPLELSWHELPGEPITP FT AEGLALDYQPTQVGTAWGVAWGTTWFHLQGRVPAQWAGRRVEAVIDLGFDVNMTGFQCE FT GLVYRPDGITIKAINPRNQWVPIAAEATGDEVIDLYLEAASNPVLLDYHPFLPTEQGDI FT LTSSSRRLYTTRRMDLAVFEPAVHELSLDLDVLLDLQEQLPAGPRKMQILQAMDNALDV FT LDLQRITETAQAARDQLAGVLAAPAEHSAHQISAIGHSHIDSAWLWPLRETIRKVSRTC FT SSMVELLGDEEDFLYGMSSAQQYKWLKTHRPEVWDRVKTAVAEERFLPLGGMWVESDTV FT MPSGESLVRQFLYGQKFFRDEFGITSKGVWLPDSFGYSPALPQLMRRAGFEWFFTQKIS FT WNQQNKFPHHTFDWEGIDGSRMFSHFPSMDTYNSQLSGEEVAKAARQFREARVTNNSIA FT PVGWGDGGGGTTREMTGKAKRLADLEGSAKVRWEHPNDFFDRAKSELPNPPVWVGELYL FT ELHRATLTSQHQTKAGNRRTEQLLVEAELWAATASVYAGAAYPYEQLDELWETVLLHQF FT HDILPGTSIAWVHREVVARYAQIIEQAQALILAAQQQLAGAGSTPIAFNGAAFTRNALA FT FGQAKPVQAPAGTAVQAIAADGGYVLDNSVVRVRVNAQGLITSAVDLATGRETIAAGQE FT ANLLQLHQDFPNMWDAWDVDKYYRNQVTDLRGLESLELSAREDGSQVITIARSFSNSTL FT VQELSLSPGSRTVQISQSTDWHEAEKFLKVAFPLDIRAEHAIAETQFGYHKRVTHVNTS FT WEAAKFETSMHRFVLAEEPGFGAALINDSIYGFDVTRDAKDAQVTTTMRLSLLRAPRFP FT DPETDQGVQTHRYGLVIGADVAAATEAGALLNSAEQVIEGAQGVDPLVSLSGEGLVISS FT VKLAADRSGDLVVRVYESLGRRAHGSLMVNAQLGSAATVSLLEDELAGQSVELDDGAVP FT LKLGAFEVRTLRFALAK" FT CDS complement(695177..695845) FT /transl_table=11 FT /locus_tag="AARI_06240" FT /product="phosphoglycerate mutase family protein" FT /function="2 Intermediary metabolism" FT /note="identified by match to protein domain PF00300" FT /db_xref="GOA:E1VT99" FT /db_xref="InterPro:IPR001345" FT /db_xref="InterPro:IPR013078" FT /db_xref="UniProtKB/TrEMBL:E1VT99" FT /protein_id="CBT74852.1" FT /translation="MRFQLIRHGQTPSNVAGQLDTAYPGAGLTPLGHRQARALPQVFAE FT GQLQSIYASRLNRTQLTARPLSESSGQRLQVIDGLEEISAGTLEMLADEPSHHAYATCL FT YTWMHGGWEQKMPGGPSGYDFIERYSKALETIARAQDYSGTAAVFSHGAAIRVFSAWAT FT RMAPADASELFIENTGGALLELGIGGKWSLDRWNPKPLGGDFVRDVLTEDVTGGEEGAS FT " FT CDS 696055..696624 FT /transl_table=11 FT /locus_tag="AARI_06250" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00440: bacterial regulatory proteins, FT tetR family" FT /db_xref="GOA:E1VTA0" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:E1VTA0" FT /protein_id="CBT74853.1" FT /translation="MRSDALRRRENILRVARELFAEHGAQIAMETIAEASGVGIGTLYR FT NFADRTSLVEEVTLGTLKDVQIASQLAVEGLEADDTGAWDVLLDTLIHQNLGALSEALG FT LQLPKKISARVLEVQASAALSLNAALELAKNADLVRQDISGIDLIATIGAMTRPLSRSF FT SKSAPGLEERIVQIMRDGLRPQAAQQ" FT CDS complement(696629..697966) FT /transl_table=11 FT /locus_tag="AARI_06260" FT /product="putative aromatic acid transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (MFS), aromatic FT acid:H+ symporter (AAHS) family (TC 2.A.1.15.z). Members of FT this family transport compounds such as benzoate, FT hydroxybenzoate, niacin ..." FT /db_xref="GOA:E1VTA1" FT /db_xref="InterPro:IPR005828" FT /db_xref="InterPro:IPR005829" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VTA1" FT /protein_id="CBT74854.1" FT /translation="MSSAPLPSGTSIVQELPFKWKVQGTIFIIGGLGFMFDAWDVTLNG FT ALIPLVAEQWGLDRPTAALLGTSNLVGMALGAFLWGGIADRYGRKNAFSLTLLMFSLFT FT ILGALSPNFGFFVAFRFLAGVGLGGCIPVDYALVGEFTPSKLRGRVLTAMDGWWPVGAA FT LSFFVSGWVMATADNWRLILAVMILPAFMVYLVRRSMPESPLFLAAKGRDAEARAVIDQ FT LVERTGADKRDYVIEPVQLPKAPRWWEQVASLWKYSWKITATSWLLFMTILLVYYLALT FT WLPSILTEAGMAQSTSFFATAVMALMGLVGVVIAALLVERVGRKWLLAISAPISGIVLI FT VVAQNLQVPATAIAWVLVFGVVVQVAIPVLYAYVSELYPTELRASGFGWASTMSRFAAG FT FGPLLFAALWPVVGLGWLFAGATVLVLLAVLFMSRFAPETRGMRLD" FT CDS 698115..698891 FT /transl_table=11 FT /locus_tag="AARI_06270" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTA2" FT /protein_id="CBT74855.1" FT /translation="MGVDWTALEEAIRVTALRHAAEVIAGHPDQDFYAIALHGVSTEES FT ESIGMPLLALNSVQALERDRLSESREQLVERGEDTDEPADYEDRPDAEGEGGLEPEAVT FT LEADSMVITETDDEDEESFDDESADGEDLDEVLASLEADLEEDDAESFYSDKWEPSDWH FT WSSIDLCEDPAATLWSEAMTKQAAREGWEPTVKRYYHTLVAVARSLREELNERTKADLV FT VYVADEEHAEKLLQLCLTDKQLSTYFPQLSSLPEGA" FT CDS 698989..700659 FT /transl_table=11 FT /gene="purH" FT /locus_tag="AARI_06280" FT /product="bifunctional purine biosynthesis protein PurH" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.1.2.3" FT /EC_number="3.5.4.10" FT /note="catalyses the last two steps in de novo purine FT biosynthesis. Phosphoribosylaminoimidazolecarboxamide FT formyltransferase (EC 2.1.2.3) catalyses the formylation of FT AICAR with 10-formyl-tetrahydrofolate to yield FAICAR FT (5-formylaminoimidazole-4-carboxamide ribonucleotide) and FT tetrahydrofolate. IMP cyclohydrolase (EC 3.5.4.10) FT catalyses the formation of IMP from FAICAR" FT /db_xref="GOA:E1VTA3" FT /db_xref="InterPro:IPR002695" FT /db_xref="InterPro:IPR011607" FT /db_xref="InterPro:IPR016193" FT /db_xref="InterPro:IPR024051" FT /db_xref="UniProtKB/TrEMBL:E1VTA3" FT /protein_id="CBT74856.1" FT /translation="MSKTVLDKVAIRRALISVYDKTGLEELAAGLHAAGVQLVSTGSTA FT KKIAAAGIPVTEVEQVTGSPEMLDGRVKTLHPRIHGGILADRRVTEHMDTLSSMEIEQI FT DLVVVNLYPFVQTVASGASQDEVVEQIDIGGPAMVRSAAKNHAAVSIVVDPGFYPQVIS FT AAAEGGFDLKTRQRLAAKAYAHTAAYDTAVASWTASQFLDEDGDGVIDWPAYAGVALQR FT SNVLRYGENPHQQAALYVDEAAPAGIAQADQLHGKPMSYNNYVDADAALRAAFDFEKPA FT VAVVKHANPCGVAVASDDAADPIADAHRKAHSTDPVSAFGGVIAANRTVTKEMAETVKD FT IFTEVVIAPDFEDEAVQILSAKKNIRLLALPEGYGRNKNEFRQVTGGMLVQVGDKIDAQ FT GDNPANWTLAAGEAADAATLADLQFAWSAVRAAKSNAILLAKDGAAVGIGMGQVNRIDS FT CKLAVERANTLGVKVESGADAAGGAENADSAASEQRAQGAVASSDAFFPFADGLQILID FT AGVKAVVQPGGSVRDEEVIAAANEAGITMYFTGARHFFH" FT CDS complement(700814..700918) FT /transl_table=11 FT /locus_tag="AARI_06290" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTA4" FT /protein_id="CBT74857.1" FT /translation="MQGPETELGQSAAKIWAVITTCAIHLALEDCAEE" FT CDS 701018..701149 FT /transl_table=11 FT /locus_tag="AARI_06300" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTA5" FT /protein_id="CBT74858.1" FT /translation="MPAPGQGYGSPDSVAEVVALLASEKGLFTTGTETGSEDGTQSK" FT CDS complement(701254..704163) FT /transl_table=11 FT /locus_tag="AARI_06310" FT /product="putative permease" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="match to PF02687: this is a family of predicted FT permeases and hypothetical transmembrane proteins" FT /db_xref="GOA:E1VTA6" FT /db_xref="InterPro:IPR003838" FT /db_xref="UniProtKB/TrEMBL:E1VTA6" FT /protein_id="CBT74859.1" FT /translation="MPLNLEPQHGDKKQQLKLALRIAWLDIRRNRGRSALIAALIAVPI FT LMISAALVAGFSKMPSTEETIRTELGQSAGRISLQYSDLASLTQGPKGDLSSVMSDSEA FT EPEQRNGTLDDFKDLVVSDYDVLPLSSSPLATERGDATLSFNAVIGDVLNPAFDGKYNL FT LEGRAATGNREALGTPGFMQRFDLQLGDQFSNNAGDFTMVGTVRDSSTNDSIPTFFAAE FT SDMPENFAPGPNETMYYLLGQKPATWALATELNQHGAILTSAELLRNPPTAEQIGAPED FT RFADAPSGNGLDLIATGALIATLAMVEVALLAGAAFAVGTRKQRHDLALLAATGAEAGT FT LKSVVTASGLWLGLIGGVAGALAGTGVGIAWVLLKLRSGENQLWLHIPWPLMLGVILLA FT PIAGLVSAYVPARAVAKQALNDALRSGRTTSNHSRRNLRRGILWLALSILLLALSASLS FT VFGIIQDFELRSYLALVLVIAGSIGLISAFILLSAPLLRLVAAKSAWLPLPLRLATRDS FT ARNTGRTVPAVAAVLAAATLSSALLIYWSSASHSENENYQWSYNLNQMALPLSVQEYSP FT SAVGSVKMASADPFTTRRINAEDVSNAAVKALGPRTSAQTIPGAIDQGECTRLDPDSVE FT LDGILHSPHCSTWALMEPSGHQCFVAPDGKPVDLQDWRCHGSMASDSGFSSLPTIVVGG FT EEILEALLGRKPSSEALQTLRAGGAVISNPVYLNEDETTTLISYDADADPQESADASQQ FT WSSQRASFSPQSSFPLLATVEEPAKPIPYYAVISPETASRIGMPYDERLVLLSLGELPS FT DAVNDTLLVALAEAAGENYGPEKLETGPNSSVATALWQLVGLSALVTFSATGITAGLAL FT ADGREDHSVLASIGADPRLRKSLSAAQLFLTSIFGTLFGIMAGIVAAGTLQLLFRDMAL FT IIPWTQLAIMLLVVPCAGSAMAWLLTKGRLHVLRHRTLA" FT CDS complement(704166..704891) FT /transl_table=11 FT /locus_tag="AARI_06320" FT /product="putative ABC transporter, ATP-binding subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT lipoprotein translocase (LPT) family (TC 3.A.1.125.z). FT ABCISSE: ABC transporter, ATP-binding protein (ABC), o228 FT family (members of this family might be involved in a more FT general lipoprotein releasing mechanism common to all FT prokaryotes)" FT /db_xref="GOA:E1VTA7" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VTA7" FT /protein_id="CBT74860.1" FT /translation="MSNQVLQLRKICMTYGSGATSVGALRDIDLDVSAGEFVAVMGPSG FT SGKSSLLTLAGGLDKATSGEIYVENTPLGALNINDLARLRRRAIGYVFQDFNLVPSLTA FT VENVALPRELDGVPFRKARRQAMDALRSVGIDKLADRFMDQISGGQRQRVAIARAIVGE FT RRLILADEPTGALDTASGDGIMEVLRQRADAGCAVVLVTHEARHAGWADRVHFLKDGKI FT VDQAAQSYDPTVLLELPAN" FT CDS complement(704888..705442) FT /transl_table=11 FT /locus_tag="AARI_06330" FT /product="PadR-like family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF03551" FT /db_xref="InterPro:IPR005149" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR018309" FT /db_xref="UniProtKB/TrEMBL:E1VTA8" FT /protein_id="CBT74861.1" FT /translation="MYGYQLRSEFEERTGSTWPLNIGQVYTTLDRLERDGLALKDGDDG FT EGHVFYRITTAGKAEVSQWFADPVVATNPPRNELAIKLSLAMTLDSVDVEKLLQAQRTA FT SMRNLQTYTRQRREATKFDSNDSHDVAWILVLDSLVFAAEAEIRWLDHCEGWLRKHRFR FT TSKNPAVHAAKALNDSKEVTR" FT CDS 705713..706930 FT /transl_table=11 FT /locus_tag="AARI_06340" FT /product="putative divalent metal ion transporter" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="metal ion (Mn2+-iron) transporter (Nramp) family FT protein (TC 2.A.55.y.z). The generalized transport reaction FT catalyzed by Nramp family proteins is: Me2+ (out) + H+ FT (out) → Me2+ (in) + H+ (in)" FT /db_xref="GOA:E1VTA9" FT /db_xref="InterPro:IPR001046" FT /db_xref="UniProtKB/TrEMBL:E1VTA9" FT /protein_id="CBT74862.1" FT /translation="MALPESTSQSSKARRTALLGAMFLMATSAIGPGFITQTTEFTVKI FT GAAFAFAIVVSILVDIAVQLNVWRVIGVSGMRAQELGNKVLPGIGWVLAALVFIGGMVF FT NIGNIAGTGLGLNAMLGLDAKIGGALSAVVAILIFLSKKAGMALDRIVVMLGAIMILLM FT LYVAIVAAPPVGDAIRNVVLPEKIDFLIITTLIGGTVGGYITYAGAHRMIDSGTSGVEH FT VKSISNISTLAIIVTGVMRVLLFLAILGVVAGGVALTSDNKAAEAFGHAAGPIGIRAFG FT VILWAAALTSVIGAAYTSVSFITKRTTPERTRNLITLAFILVCGIIFMFLGKAPATLLI FT FAGAFNGLILPVGFAVLLWVAWRRRDLLNGYKYPKGLLVIGALTWVLSVYLGWNSLSGL FT AALWNG" FT CDS 706944..707753 FT /transl_table=11 FT /locus_tag="AARI_06350" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR009906" FT /db_xref="InterPro:IPR016938" FT /db_xref="UniProtKB/TrEMBL:E1VTB0" FT /protein_id="CBT74863.1" FT /translation="MKNFKDMELAERAAMSPREARELFRAGQVLPTAGISAGYAQANLM FT IVPQELAFDVLLFAQRNPKSCPILGVLEAGQTSSELLAGGDIRTDVPKYLVYENGIKVA FT EPTDLGDYWRDDLVTFIVGCSFTFEAALMESGISVAHIDQGVNVPMYKTNRRSATAGAI FT SGPMVVSMRPIPASQVADAVRITSRYPAVHGAPVHIGNPGELGIEDLAAPDFGDAVQIP FT EGSIPVFWACGVTPQAAVMESRPALAIGHAPGHMLITDIRDTEYQVP" FT gene complement(707893..708873) FT /pseudo FT /locus_tag="AARI_34560" FT /product="partial transposase of ISAar28, IS481 family" FT /function="4.5 Transposon and IS" FT /note="deletion of 400 bp in IS sequence at position 311. FT Protein is truncated (AA 1-54 and 182-451)" FT CDS complement(709022..710014) FT /transl_table=11 FT /gene="add" FT /locus_tag="AARI_06360" FT /product="adenosine deaminase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.5.4.4" FT /note="catalyzes the irreversible hydrolytic deamination of FT adenosine to ammonia and inosine, or of desoxyadenosine to FT ammonia and desoxyinosine" FT /db_xref="GOA:E1VTB1" FT /db_xref="InterPro:IPR001365" FT /db_xref="InterPro:IPR006330" FT /db_xref="UniProtKB/TrEMBL:E1VTB1" FT /protein_id="CBT74864.1" FT /translation="MKLPVAELHVHLEGTLEPEMIMALAKKNSIELPYASIEELRAQYQ FT FTNLQSFLDLFYANMAVLRTAQDFREITVAYLQRAHDSGVRHVELFFDPQAHIGGALDL FT REVIAGIRAGLADGLERWELSSKLIACFWRHAPASEAMELMKVLVEQKHDIDGIGLDSS FT EVGFPPELFTEVFDYARAHGLHVVAHAGEEGPAEYIWQALDLLKVQRVDHGIRSLDDPQ FT LVQRLVDEQMPLTVCPLSNIRLRAVDTMAEHPLPQMLAKGLKVSVHSDDPAYFGGYMDA FT NFDALMEQFSFSSEQLATLAKNSFESSFLDEQSKQALVAEVQAWAEQQK" FT CDS complement(710393..711070) FT /transl_table=11 FT /locus_tag="AARI_06370" FT /product="GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF00392. This FT family of regulatory proteins consists of the N-terminal FT HTH region of GntR-like bacterial transcription factors. At FT the C-terminus there is usually an effector- FT binding/oligomerisation domain. The GntR-like proteins can FT be divided into six sub-families: MocR, YtrR, FadR, AraR, FT HutC and PlmA. Many of these proteins have been shown FT experimentally to be autoregulatory, enabling the FT prediction of operator sites and the discovery of cis/trans FT relationships" FT /db_xref="GOA:E1VTB2" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VTB2" FT /protein_id="CBT74865.1" FT /translation="MDATSTTAARPAKAPHAHSGVWAADELRRRIAEGELLPGDKLSEQ FT ALAESLGLSRNTLRESFTLLNSELIITRIPNRGVFVASPDADDVREIYAVRRTIEPACL FT AWGPELDLEALERIIAQARAGLAAGDVARMASANQDFHKQLVRSSHSALLQELMGRVLA FT RMRLVFHAMSDAPDFHSHYVERNATLLALLRDGKRMEAAETLRSYLDTAEAELLSHIHQ FT RSS" FT CDS complement(711123..712862) FT /transl_table=11 FT /locus_tag="AARI_06380" FT /product="acetyl-/propionyl-coenzyme A carboxylase alpha FT chain" FT /function="2.4 Metabolism of lipids" FT /EC_number="6.4.1.2" FT /EC_number="6.4.1.3" FT /note="enzymes named acetyl-coenzyme A carboxylase (EC 6.4. FT 1.2), propionyl-coenzyme A carboxylase (EC 6.4.1.3) and FT acyl-coenzyme A carboxylase are constituted by several FT types of subunits. Alpha subunits contains the biotin FT carboxylase (BC, EC 6.3.4.14) and biotin carboxyl carrier FT protein (BCCP) domains, beta subunits contain the FT carboxyltransferase (CT) domain. An epsilon subunit is FT present in some microorganisms" FT /db_xref="GOA:E1VTB3" FT /db_xref="InterPro:IPR000089" FT /db_xref="InterPro:IPR001882" 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:E1VTB3" FT /protein_id="CBT74866.1" FT /translation="MKKVLIANRGEIAVRIARAATDANIASVAIYSDPDADALHVRRAD FT EAYPLHGSTGADTYLNIEKIIQIAKHSGADAVHPGYGFLSENASFAQAVIDAGMSWIGP FT SPEAIEALGNKVTARQIAVRAGAPLAPGTDGPVKDAAEVRAFAEEYGVPVAIKAAFGGG FT GRGIKIAHSMDDIAESFESATREATVAFGRGECFVERFLSKPRHVEAQVLADTHGNVVV FT IGTRDCSLQRRHQKLVEEAPAPFLSDEQRTRIHESARAICKEAGYVGAGTVEYLVAQDG FT LISFLEVNTRLQVEHPITEETAGVDLVAEQFRIADGLPLSLSEDPKPTGHAFEFRINAE FT DPARGFLPAPGTIERFEAPTGAGVRVDTGVRSGSIIPPFYDSMIAKLIVRGADRDQALR FT RARLALEEINIAGVPTVLPFHRSIINHEAFTGQSLGVYTTWIEDEFLNEVEGSDDMDLD FT QRDTSRETITIELDGKAVQLGLPAAMTNALRNSSGAGAAAAAQGEEAGEQDASAVQSSM FT DGNLVRFTVEDGQSVEAGQSVAIIEAMKMESPVTAHRAGIFTAASISVGTGVRRGDTLG FT TIN" FT CDS complement(712871..714475) FT /transl_table=11 FT /locus_tag="AARI_06390" FT /product="putative allophanate hydrolase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="3.5.1.54" FT /note="identified by match to PF02626 and PF02682. EC 3.5. FT 1.24 may be involved in the degradation of urea, together FT with EC 6.3.4.6, or in cyanuric acid metabolism" FT /db_xref="GOA:E1VTB4" FT /db_xref="InterPro:IPR002130" FT /db_xref="InterPro:IPR003778" FT /db_xref="InterPro:IPR003833" FT /db_xref="UniProtKB/TrEMBL:E1VTB4" FT /protein_id="CBT74867.1" FT /translation="MSIRAIHHAGSHDLLVDLDSLDAVLALNAALEASPLEGQRDLLAA FT AQTVLLKFSNAEQAQRARTLLPTLAFGTAAETIGKVVDVPVHYDGEDLAAVAELTGLSI FT DAVITAHSTQAWRAVFDGFAPGFAYLLGQNQQLNVPRRETPRTKVPAGAVALAGEYSAV FT YPRQSPGGWQLIGHTDVQMWDLERENPALIRPQDTVKFTPAMQKIAVRETPASAPAQPA FT ADGSSALRIIDSGLQSLLQDAGRIGYGNLGVGVAGAADPAAFHQANRLVGNPVNHAVIE FT NLGSRITLEAEQDQVLAHTGAEADLWITPAADDEVRTERQVAGNTPFALLHGERLTVTS FT GGRGLRSYLAVRGQIGLEPVLGSLSTDTLSGVGPAPLASGGVLPVQRPRIGHIVGNSLP FT STLPVPDAQGVYTLRVLAGPRADWFGPAGLAQLTGQVWEATSESNRVGVRLGTGAQPLQ FT RIRAGELASEGVARGSLQVPPSGLPVLFLADHPVTGGYPVIATVIAEDLSAAAQLPPGS FT SIRFLLHPAAGQPAAEA" FT CDS complement(714472..715230) FT /transl_table=11 FT /locus_tag="AARI_06400" FT /product="LamB/YcsF family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF03746. This FT family includes LamB. The lam locus of Aspergillus nidulans FT consists of two divergently transcribed genes, lamA and FT lamB, involved in the utilisation of lactams such as FT 2-pyrrolidinone" FT /db_xref="GOA:E1VTB5" FT /db_xref="InterPro:IPR005501" FT /db_xref="InterPro:IPR011330" FT /db_xref="UniProtKB/TrEMBL:E1VTB5" FT /protein_id="CBT74868.1" FT /translation="MAFIDLNSDVGESFGNWKMGDDAAIFTSVSSANVACGFHAGDPST FT IAQTCRDAVSANVTIGAHVGYRDLAGFGRRFLDCSATELADDVLYQLGALQALARAAGS FT EIKYVKPHGALYNTIVHHQVHAQAVIDAIKAFGADLPVLLLPGSVALQKAEAAGLRGVA FT EAFADRNYTPEGTLVSRRESNAVLHDPAQVTENMVRLATEGTIVAVDGSTIKMEAESIC FT LHGDTAGAVAMASAVRAGLEHAGVQIRSFA" FT CDS complement(715438..715584) FT /transl_table=11 FT /locus_tag="AARI_06410" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTB6" FT /protein_id="CBT74869.1" FT /translation="MAAEHHDETTGPDKSPNPHGKNTEVPDPDEAQNAPIPFGHEEDGD FT NED" FT CDS complement(715746..717428) FT /transl_table=11 FT /gene="fhs" FT /locus_tag="AARI_06420" FT /product="formate--tetrahydrofolate ligase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="6.3.4.3" FT /note="catalyses the following reaction: ATP + formate + FT tetrahydrofolate => ADP + phosphate + 10- FT formyltetrahydrofolate" FT /db_xref="GOA:E1VTB7" FT /db_xref="InterPro:IPR000559" FT /db_xref="InterPro:IPR020628" FT /db_xref="UniProtKB/TrEMBL:E1VTB7" FT /protein_id="CBT74870.1" FT /translation="MAMTPESDMSDLAIAARATLQPISRIAAAAGICEEAVEPYGKYKA FT KIDPALLDSSAPMGKVVLVSGMSPTPAGEGKSTMVVGLGDALAAAGTKTMIALREPSVG FT PSFGMKGGATGGGQSQVLPMDEINLHFTGDFHAITSANNLLMALIDNHLQQGNALGIDP FT RRITFKRVMDMNDRSLRNIVIGLGGPADGMPRDAGFEITAASEVMAVFCLATGLADLRA FT RLGRMTLGYTYAKEPVTVDDLGAAGAMTLLLKDALKPNLVQSIGGTPALIHGGPFANIA FT HGCNSAIATNTARTLADVVVTEAGFGTDLGAEKFMDIKARYAECPPATVVVVATIRALK FT MHGGLPKDQLDQQNTEAVNAGLANLARHVGIVRKFGVEPVIGVNRFTADTEAELQVVTQ FT WAAANGIACAVADVWGQGGAGAQELARVVLRAIEAPNNFAPLYALELPVEQKILMLVQE FT IYGGAGVDYSPRAKLMLEQIHANGWEDLPVCIAKTQYSFSDDPQLLGSAEGFTLQIREI FT IPKTGAGFIVAITGALTTMPGLPKLPAAMHMDVDEQGNAVGLS" FT CDS complement(717764..719224) FT /transl_table=11 FT /locus_tag="AARI_06430" FT /product="putative EmrB/QacA subfamily drug resistance FT transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily, drug:H+ antiporter-2 FT (14 spanner) (DHA2) family (TC 2.A.1.3.z). Identified by FT match to protein family TIGR00711" FT /db_xref="GOA:E1VTB8" FT /db_xref="InterPro:IPR001411" FT /db_xref="InterPro:IPR004638" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VTB8" FT /protein_id="CBT74871.1" FT /translation="MTTKPAATSAKPGAAPAGQPTGKALTGIIASLALAAFMMILNETV FT LTVALPGIMQDLSISASTGQWLTTGFLLTLSVVIPTTGYLLQRFAHRSLFFFAILSFIL FT GTAIAVLAPSFAFLLLARIIQAVGTAIILPLLMTTTLALVPVRQRGTVMGLNSIVIGVG FT PAIGPTASGAVVHALDWHYIFILMLPIAVAVLVLGAIFFKIPSTARKIKVDSASVLLSA FT LAFGFLVYGISSIEHAADNSAMMIASFAIGLVALALFIIRQVKLAASGRELLNLAPFAS FT RSFSFAIAMIMIAFGTLLGSLMIVPILLESGQGIDSLQIGIMLLPGGLAQAIASPIFGR FT IYDKRGPRPVLIPGAVFLAAGQWMYTTVTAQTELWMFMLCHIVFSIGLALLMTGLMSSA FT MASVDPRLFGHGSAIFNTAQQLGGAIGTTVFVTVMSLLSKVQLDAGSELAEALFSGAHI FT SFIVGAVLATIGIVFAFMIKGENSHANH" FT CDS 719373..719966 FT /transl_table=11 FT /locus_tag="AARI_06440" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00440: bacterial regulatory proteins, FT tetR family" FT /db_xref="GOA:E1VTB9" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR015893" FT /db_xref="UniProtKB/TrEMBL:E1VTB9" FT /protein_id="CBT74872.1" FT /translation="MGIREDRKAATLQAIHAAALELVESHGLDSVTVGQIAARAGISER FT TFFRYCDSREAAIVPAQHELIDAVAGCEIAPGSTSAQIFRLLAGECRRILVAEIRASEY FT RRISRLIVIEPKLLLAITRQEQAFSAATAQELRRRGLLPAMPALMIGETLAVLWRVAWQ FT CFGQAERAGQPADPVELFDAAMSELSGLAVAVSE" FT CDS 720180..722402 FT /transl_table=11 FT /gene="icd" FT /locus_tag="AARI_06450" FT /product="isocitrate dehydrogenase (NADP+)" FT /function="2.1.3 TCA cycle" FT /EC_number="1.1.1.42" FT /note="involved in the TCA cycle. Catalyses the FT interconversion of isocitrate and 2-oxoglutarate. FT Oxalosuccinate can also be used as a substrate" FT /db_xref="GOA:E1VTC0" FT /db_xref="InterPro:IPR004436" FT /db_xref="InterPro:IPR024084" FT /db_xref="UniProtKB/TrEMBL:E1VTC0" FT /protein_id="CBT74873.1" FT /translation="MAKIIYTHTDEAPMLATHSFLPIVEAFASTAGVELETRDISLAGR FT IIATFPDYVTEEQRISDALAELGELAKTPEANIIKLPNISASIPQLKAAIAELQAAGYA FT LPDYPDNPSSDEETDIRARYDKIKGSAVNPVLREGNSDRRAPLSVKNYARKYPHSMGEW FT SADSKTNVATMGVDDFAANEKSVVIDADKKISIRFVGEDGEVKVLKKPFDVLAGEVIDG FT TVMHAAALSEFLKNSVARAKEEGVLFSAHLKATMMKVSDPIIFGHVVKAYFSELFDTYG FT DELAAAGLNPNNGLAAIIGGLDELSDEVRAGVEKLIAKGLEEGPEVAMVDSDKGITNLH FT VPSDVIVDASMPAMIRLGGKMWDAKGNTADTLAVLPDSSYAGIYQVAIDDCRANGAYDP FT TTMGTVPNVGLMAQKAEEYGSHDKTFEIAGNGHVQIVDENDTVLIEHQVFAGDIWRACQ FT TKDVAIRDWVKLAVNRARASATPAVFWLDENRAHDAVLIGKVNEYLKEHDTEGLTIKIL FT SPVEATQYSIDRIRKGEDTISVTGNVLRDYLTDLFPILELGTSAKMLSIVPLLAGGGLF FT ETGAGGSAPKHVQQLVNENHLRWDSLGEFMALGASFEHLAVNNDNARAQVLADTLDAAT FT GTFLLEDKSPKRKVGELDNRGSHFYLAKFWAEELAKQDKDAQLAQAFSAVAKALDENEE FT AIVSELAAVQGQAVDIAGYYRPDEAKTAAIMRPSASLNKALELLTK" FT CDS 722536..722811 FT /transl_table=11 FT /locus_tag="AARI_06460" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="InterPro:IPR006442" FT /db_xref="UniProtKB/TrEMBL:E1VTC1" FT /protein_id="CBT74874.1" FT /translation="MATTHPLRISSTVAARKGIGFITTQAQERPVTLTSHGKPVAVVMS FT AAERDEQRRLLREVELKVLSMAANLVADRSAMLTTDQAREKLFASD" FT CDS 722798..723535 FT /transl_table=11 FT /locus_tag="AARI_06470" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTC2" FT /protein_id="CBT74875.1" FT /translation="MPPIDELPQQQAEVVFTEESIDWLIENVVAPQRENVMDTIVSLFA FT APQGKHPLSHQNKTNLVGFNTVEAAQREFRIIYRVSVREGVGLIEVITIGHRRDDEVYV FT YAHDLIQSGKLSEAEQTQIWDALTLIDDTKARVGLEDWDYKEEPAPEGLIKSAVAAGAL FT DEDFARILSKDEIVVAMSAAWVNGEVNHEAAIAAALGRIATSTRPDRILASRREPRCGA FT IMPKLKTPCIRVKGHAGAHRGHR" FT CDS complement(723758..724252) FT /transl_table=11 FT /locus_tag="AARI_06480" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTC3" FT /protein_id="CBT74876.1" FT /translation="MPAKPEKRDEHYVLEPCSDTLGLPCIGQQSFDWLRGDPSLKNDKR FT KTLPIDGYFEELGLVVEYHERQHSEAVPFFDSKVTSTAMLRGPQRSLYDARKAALIPQH FT GMALLVIDYRDFANKKGKIVHDPARDRQIVAALLARTAQCTEHGVVTNFPVPLAETPAE FT P" FT CDS complement(724268..724726) FT /transl_table=11 FT /locus_tag="AARI_06490" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTC4" FT /protein_id="CBT74877.1" FT /translation="MEAVGLLHRLGYLGLRILPGINASGTAWRIVIHNVTDWNPEDEFG FT DPFNSEESCVYSTAGANVFNNDVQMPEDVSRVSVAEAILEAMPSLQRSTPGETGNLDYV FT RWYAQLLSQVTRLDELPVAYADYFDDSEGWELGWGSHRRFPAPPTYRP" FT CDS 724762..724911 FT /transl_table=11 FT /locus_tag="AARI_06500" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTC5" FT /protein_id="CBT74878.1" FT /translation="MPWDDVVTLIMPWRTDISAWRSGGRETELAVTPALRMPDARRSDA FT QTRG" FT CDS 724972..725997 FT /transl_table=11 FT /locus_tag="AARI_06510" FT /product="possible reverse transcriptase" FT /function="4.4 Phage-related function" FT /note="match to protein domain PF00075 (RNase H). This FT domain is often associated with reverse transcriptases FT (important enzyme in retroviral replication cycle)" FT /db_xref="GOA:E1VTC6" FT /db_xref="InterPro:IPR002156" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VTC6" FT /protein_id="CBT74879.1" FT /translation="MLVSVPGPQMPVALEPDGVRRLAGAQRQPPPSRLIAVLERSAFIR FT DAHGKKQQYVPFAERIVEEKHLAQRSTHGLHFDFSLTLCDFVNRPLLTLTGTAVNGELD FT QAILQAIAEFSGTCKISQPSSIDLLVPDHDDLGLAELSLNPVFCLNPSWQFGLNLGVDN FT EANSQALAPLVQDYTANLPVIAYTDGSVPRNRKFRSAGAMVTSQGHWACAISPKHYVQD FT TLLAETTGALLALTHAPLESDLTIFSDSRALMKAVNDLVQGRQRTVKVHHELRESLELR FT TGRTRARWVRGHDGNRHNEAANRMAILMSRHFSARINPHLTQSMMTQIVREELSQQALA FT A" FT CDS complement(726071..727603) FT /transl_table=11 FT /gene="dgt" FT /locus_tag="AARI_06520" FT /product="putative dGTPase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.1.5.1" FT /note="dGTPase catalyses the formation of deoxyguanosine FT from dGTP. It is involved in purine metabolism" FT /db_xref="GOA:E1VTC7" FT /db_xref="InterPro:IPR003607" FT /db_xref="InterPro:IPR006261" FT /db_xref="InterPro:IPR006674" FT /db_xref="InterPro:IPR023279" FT /db_xref="InterPro:IPR023293" FT /db_xref="UniProtKB/TrEMBL:E1VTC7" FT /protein_id="CBT74880.1" FT /translation="METRAQTHQTGGRDRAIVERNRTGEDEFRIDIERIRFSPYFSRLS FT SVTQVIPQAGSGTLVHNRLTHSLKVSAVARSIAISLRRSDEPTRRLISDLGGCDPVVVQ FT AAAAAHDLGHPPFGHLGEQELDRVARDTLGLPDGFEGNAQTFRILTALDSCDATPRGMN FT LTRAVRAAVLKYPWTRNEWRSQAPVAPELLPRGVGANPAAGAMKYSAYDIEAEEMDDVL FT SVFPGIGKYQQTLESSVMDIADDIAYAVHDLDDFYRAGILQYTSVSAELRAWLDNSVRF FT QALKAPELDQRQPGHALEITWRHVLAKDPWIAKSEAFRASVQRVGHDLVDGLLAVPYDG FT GLQADRAVTAFTRRWIDRLQESITVERTPNVRSGHIRLSDEAWHDVVVLKFVHSRFVLD FT RSDLAVYQRGQTRIIRSLAEGFNTWLNDPEDAGRAPRRLLDSVEATTEEYRQLRESTPE FT LFSQSGPHEIQRLGQARAIVDYIASFTDAQAVSLNSLLTGTSDNLWEAGRGL" FT CDS complement(727738..728766) FT /transl_table=11 FT /locus_tag="AARI_06530" FT /product="D-isomer specific 2-hydroxyacid dehydrogenase FT family protein" FT /function="2 Intermediary metabolism" FT /EC_number="1.1.1.-" FT /db_xref="GOA:E1VTC8" FT /db_xref="InterPro:IPR006140" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VTC8" FT /protein_id="CBT74881.1" FT /translation="MIRLLNQVGRGTDHFIQRLGTVEFKARATPGNISSHDWIHGLRVL FT VPWQSLVDSMQIPGVEPVLWNINDGEPPAADVLVTERPLDPSHRMRVGRIAGLKHVHLL FT SIGYEWVLDHLPEDVALSNSKGAVEDSTAEHCLALILASLRELPRAYQLQTEESWSRLW FT TSSLHGSNVVVLGVGGVGTAIIERLKPFKPAQITGVASTARTINGGIDVVSIENVHQLL FT PSAEIVICALPHTPQTQGLIGKEFMDRMRDGALLVNVGRGPIIATAALIKELETGRLRA FT ALDVTDPEPLPVGHALWNAPGCIITPHMAGDTGQFVELVSELATRQVQLLSSGQTPLNL FT VR" FT CDS 728816..729019 FT /transl_table=11 FT /locus_tag="AARI_06540" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTC9" FT /protein_id="CBT74882.1" FT /translation="MTQSVKKPQQAGLGMTTGAMFIAWTLGLVGVVMLILGGATAAALV FT ILAAAILQAGAMIAEAIYRSRS" FT CDS complement(729063..729632) FT /transl_table=11 FT /locus_tag="AARI_06550" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTD0" FT /protein_id="CBT74883.1" FT /translation="MDPQDTLILPDVTAWRAWLDEHEETSDGVWLVVAKKGTTSPTSLA FT VAQALPEALCSGWIDAIRRKRDDTTFLQRYTPRRKNSVWSQKNTEFAQELIDQGRMRPR FT GFAEIQKAKEDGRWERAYQGQATAQVPPDLQEALDRSSVAAKNFAALKSQPRYHILHQL FT MIARTEKTRTARLARFVAELEQGPEG" FT CDS complement(729916..731214) FT /transl_table=11 FT /locus_tag="AARI_06560" FT /product="helix-turn-helix domain-containing protein" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00196: bacterial regulatory proteins, FT luxR family. This domain is a DNA-binding, helix-turn- FT helix (HTH) domain of about 65 amino acids, present in FT transcription regulators of the LuxR/FixJ family of FT response regulators" FT /db_xref="GOA:E1VTD1" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:E1VTD1" FT /protein_id="CBT74884.1" FT /translation="MSILDSSFAPGLQAAEPAPGVLESIALLATVALPQIAVRLRDALA FT PEIRCAALAIFTEECTDRPRKLAGDQRITDLVGIAELDRIRGSHPGENRWSERAEIGGA FT PRDILALRYPPSNALLVLIEPRPAGGQPELVEYLWNLAANRIREKVADAPPSYLRESRA FT VSAERVRVTGELVEQYATSLDILLATLRSTQLDDAAARVAAIDLAAKTLVGLKTVDDRT FT NSIVEEPVASAFTRLRDDLRPLTTLSGVDLQFVEPPKNGRALPGEVAHAARAIVRGLAL FT AMMEQEDIQRIRVQWDCDGENLLINVRDDARGGIDPSAAALDRLVRRVEALNGLIEIEV FT MGGWGTEVSVRLPLDAPPSDAADIAEWSLGGREFEVLQLLAAGQRNRAISQALGISENT FT VKFHVRNLFKKMGVGSRAQAVALAHSHGVASST" FT CDS 731376..731972 FT /transl_table=11 FT /gene="rmpB" FT /locus_tag="AARI_06570" FT /product="3-hexulose-6-phosphate isomerase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="5.3.-.-" FT /note="identified by similarity to protein SP:Q9LBW5 FT (Mycobacterium gastri). Catalyzes the isomerization of the FT D-arabino-3-hexulose 6-phosphate into fructose 6-phosphate FT in microorganisms that can use formaldehyde as a carbon FT source (ribulose monophosphate pathway of formaldehyde FT fixation)" FT /db_xref="GOA:E1VTD2" FT /db_xref="InterPro:IPR001347" FT /db_xref="InterPro:IPR017552" FT /db_xref="UniProtKB/TrEMBL:E1VTD2" FT /protein_id="CBT74885.1" FT /translation="MNTMAEPLTEAISQQDVLDTMDLVHSEIEATVRGVKPQQVIELAA FT QLRAAPRVFVAGAGRSGLALRMAAMRLMHLGLAVHVAGDATTPAIAEGDLLLVASGSGT FT TAGVVQNVRTAQRVGARIAAITTDPSSPIGSAAHVLVEVPAAGKTDHGSSITRQYSGSL FT FEQALFLITEIVFHTLWSADDATAQQLWQRHANLE" FT CDS 732030..732653 FT /transl_table=11 FT /gene="rmpA" FT /locus_tag="AARI_06580" FT /product="3-hexulose-6-phosphate synthase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="4.1.2.-" FT /note="identified by similarity to protein SP:Q9LBW4 FT (Mycobacterium gastri). Catalyzes the formation of D- FT arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate FT and formaldehyde in microorganisms that can use FT formaldehyde as a carbon source (ribulose monophosphate FT pathway of formaldehyde fixation)" FT /db_xref="GOA:E1VTD3" FT /db_xref="InterPro:IPR001754" FT /db_xref="InterPro:IPR011060" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR017553" FT /db_xref="UniProtKB/TrEMBL:E1VTD3" FT /protein_id="CBT74886.1" FT /translation="MKIQVAIDLLSTAEALELAGKVAPYVDIIELGTPLIKAEGLSVIT FT AIKQAHPDKTVFADMKTMDAGELEADIAFAAGADLVSILGAADNSTIAGAVKAATERGK FT GIVVDLIGIADKPARAREVAALGVQFVEFHAGLDEQAQPGYDLDVLLSAGAASQVPFSV FT AGGVSISTIADVQKSGAQVAVAGGAIYSAEDPAQAAKELQAALV" FT gene complement(732965..733168) FT /pseudo FT /locus_tag="AARI_06590" FT /product="truncated short-chain dehydrogenase/reductase" FT gene 733271..733567 FT /pseudo FT /locus_tag="AARI_06600" FT /product="truncated protein" FT /note="similar to the N-terminal part of a protein of FT unknown function from Arthrobacter arilaitensis" FT gene 733567..733683 FT /pseudo FT /locus_tag="AARI_06610" FT /product="truncated protein" FT /note="similar to the C-terminal part of a protein of FT unknown function from Arthrobacter arilaitensis" FT gene 733767..733922 FT /pseudo FT /locus_tag="AARI_06620" FT /product="truncated protein" FT /note="similar to the C-terminal part of a protein of FT unknown function from Arthrobacter arilaitensis" FT gene 734293..734742 FT /pseudo FT /locus_tag="AARI_06630" FT /product="truncated protein" FT /note="C-terminal section of a conserved protein" FT CDS complement(734827..735510) FT /transl_table=11 FT /locus_tag="AARI_06640" FT /product="putative Crp/Fnr-family transcriptional FT regulator" FT /function="3.5.2 Transcription regulation" FT /note="cd00038: effector domain of the CAP family of FT transcription factors; members include CAP (or cAMP FT receptor protein (CRP)), which binds cAMP, FNR (fumarate FT and nitrate reduction), which uses an iron-sulfur cluster FT to sense oxygen) and CooA, a heme containing CO sensor. In FT all cases binding of the effector leads to conformational FT changes and the ability to activate transcription" FT /db_xref="GOA:E1VTD4" 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:E1VTD4" FT /protein_id="CBT74887.1" FT /translation="MPVDDLCVSRVPIFQGLTREEQLRVAEFVRPVHVAKGETVYSPGQ FT SVSRLLVMHSGQLKVSHAAANGQEQILRTVTDGDVVGERAFLTGHLPNDLVVALEDSRM FT CVFDHTDLSALLRDYPDVGLRMMRTLSDRLASVERLLAAITSSDVSARIAAYLLDLPGS FT IRDGVPTVWLPLAKYEIASYLGTTPETLSRRLAALSASGVIELHGRRDVTILDIDGLER FT VATPR" FT CDS 735681..735920 FT /transl_table=11 FT /gene="copZ" FT /locus_tag="AARI_06650" FT /product="copper chaperone CopZ" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="chaperone that serves for the intracellular FT sequestration and transport of Cu(+). Delivers Cu(+) to the FT copper-transporting ATPase CopA. Identified by similarity FT to protein SP:O32221 (Bacillus subtilis)" FT /db_xref="GOA:E1VTD5" FT /db_xref="InterPro:IPR006121" FT /db_xref="UniProtKB/TrEMBL:E1VTD5" FT /protein_id="CBT74888.1" FT /translation="MATPTTPTTHTVLRAEGFSCPSCVAKIEKQVGRLKGVENVKVHFA FT SARIEVDHDAERISVDDLVAAIAKAGYRAAPSAF" FT CDS 736015..738018 FT /transl_table=11 FT /gene="copA" FT /locus_tag="AARI_06660" FT /product="copper-exporting ATPase CopA" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.4" FT /note="involved in copper export. Forms an heterodimer with FT CopZ during the transfer of Cu(+). TCDB: P-type ATPase FT (P-ATPase) superfamily (TC 3.A.3.y.z). Identified by FT similarity to protein SP:O32220 (Bacillus subtilis)" FT /db_xref="GOA:E1VTD6" FT /db_xref="InterPro:IPR000150" FT /db_xref="InterPro:IPR001757" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006404" FT /db_xref="InterPro:IPR006416" FT /db_xref="InterPro:IPR008250" 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:E1VTD6" FT /protein_id="CBT74889.1" FT /translation="MNRLQKWVYGNWSVPVVSGVLIIISFAIQRLAGGVANLTVSPQWW FT LDAGAHATHASAAFTLGDVFMIAAAVVAGYGIVAKAVRALIAKVVGIDLLVSVAAIGAV FT IIGNFWEAAAVTFLFAIGHALEAATLNKTRSALAELVAVAPDSAIVVRDGEQQEIPAGQ FT VRMGEIVLVKNGAKVPVDGQVVSGTGAIDEASITGESIPVEKTKGGQVFAGTVSRGGFL FT QVLATGIGADTTLARIIHRVEEAQDAKAKTQAFIDRFSTWYTPAVMVLALVAGLISGDV FT VLALTLLVIGCPGALVISIPVAIVAGIGRAARNGILIKGGEFLETSAKITAVAVDKTGT FT LTEGKPQLTDVIILDSTLDRTEVLRWAAAAEAGSEHPLARPILETAREEGVAPQGIPGA FT VTPVPGKGIVANVNGRQVLIGNPPLLEQYGIASGIAEAAQAAQDLAAAGKTPMIVAVDG FT RVIGVVAVADQIRQDAPEMVARLHRAGVEKVVMLTGDTRPVAEAVGKATGIDEIHASLL FT PEDKLDAVTELQRQGHTIAMVGDGVNDAPALATANIGVAMGAAGSAVAVETADIALMGD FT NLLKLPEAIGLAKRTVNVMKQNIAIALITVVLLLAGVFAGGVTMSIGMLVHEASVLVVI FT ANAMRLLRNTRDSTTMPKSERTIGTAAEQVAA" FT CDS 738124..738549 FT /transl_table=11 FT /locus_tag="AARI_06670" FT /product="conserved barrel domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="presence of one conserved barrel domain of the cupin FT superfamily (PF07883)" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR013096" FT /db_xref="InterPro:IPR014710" FT /db_xref="UniProtKB/TrEMBL:E1VTD7" FT /protein_id="CBT74890.1" FT /translation="MSEKNFTLGDNVEHFTIEDVARDNPDFRKVLWTGEHTQIVAMTIP FT PGGEIGDEVHEHTDQILTFVSGTGEADLNGHTHPIDAGDQCAVPAGAQHNFRNTGDEPL FT VLYTIYSPPEHATGAVFATREEADAAEAAGEDEPPRS" FT CDS complement(739016..739891) FT /transl_table=11 FT /locus_tag="AARI_06680" FT /product="BNR/Asp-box repeat-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="PF02012: BNR/Asp-box repeats. These repeats are FT found in a variety of non-homologous proteins, including FT bacterial ribonucleases, sulphite oxidases, reelin, FT netrins, sialidases, neuraminidases, some lipoprotein FT receptors, and a variety of glycosyl hydrolases. Similar to FT protein SP:Q6SK52 (Arthrobacter aurescens plasmid)" FT /db_xref="InterPro:IPR002860" FT /db_xref="UniProtKB/TrEMBL:E1VTD8" FT /protein_id="CBT74891.1" FT /translation="MLTQNSLLRARKRAVLSVAALSMVLLTGCTQSISEGPAAQEAASV FT AVFSHVHGMSVDPDSGRILLATHEGLFDATADEPQKIGPTIDLMGFATAGKDEYYASGH FT PSAETGLPDPAGLIRSTDGGSTWEPLSLQGKSDFHALAVTGESVIGFDGTLRVTDDTVT FT WNTIDAGIQPYHLAGSPLSQVVLATTEQGVHRSEDGGKTWTLPQDAPVLLLTAFASKSV FT AVGVEPDGAVQLSRDAGRTWQKTGGVVTGQPAAIAATGDDGGQVRIWVATSTGISHSTD FT DGATFTEKTP" FT CDS complement(739976..740581) FT /transl_table=11 FT /locus_tag="AARI_06690" FT /product="conserved hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.999) with cleavage site probability 0.520 FT between position 25 and 26. Similar to protein SP:A1RCQ1 FT (Arthrobacter aurescens plasmid)" FT /db_xref="InterPro:IPR005183" FT /db_xref="InterPro:IPR012347" FT /db_xref="UniProtKB/TrEMBL:E1VTD9" FT /protein_id="CBT74892.1" FT /translation="MKRLTSISATALAAALVLSGCSTDAGTTEPESTMSGMDHGSMPPS FT ASDAAADHNSADAMFAQMMTPHHEQAVQMSDIMLAKKNLDPRVTELAQDIKAAQGPEIK FT KMNDWLQTWGEPMKMSGSHEMDGMMTPEDLSNLEATQGTEASRLFLTQMIAHHEGAITM FT AEDEVANGSNPAAVELAKDVVSSQGTEIQAMKTLLADL" FT CDS complement(740703..741176) FT /transl_table=11 FT /locus_tag="AARI_06700" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0. FT Similar to protein SP:A1RCQ0 (Arthrobacter aurescens FT plasmid)" FT /db_xref="UniProtKB/TrEMBL:E1VTE0" FT /protein_id="CBT74893.1" FT /translation="MNQVMTPRRFLSLLVPASGNPAGRRPVILMLGLAGIILGILGMHV FT LGASHQAPDTAGLSAASAHQAVSHDHGPAVMATDGTVGGEADSTCYGPCNGEHHLMAAM FT CVLIVIVLAVLWFLPKRWFIIPGKGLRAPPVMPAPANRLPWTPSLIELSISRT" FT CDS complement(741276..743447) FT /transl_table=11 FT /locus_tag="AARI_06710" FT /product="cation-transporting ATPase" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.1.-" FT /note="P-type ATPase (P-ATPase) superfamily (TC 3.A.3.y.z). FT Involved in export of cations" FT /db_xref="GOA:E1VTE1" FT /db_xref="InterPro:IPR001757" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006403" FT /db_xref="InterPro:IPR006416" FT /db_xref="InterPro:IPR008250" 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:E1VTE1" FT /protein_id="CBT74894.1" FT /translation="MNHAPENREHGHSVSPGHGGRTLASKDSHTGHPMSEQPTHGQATP FT AGHAHSAVDDEHAVHSHGEHAGHSTAMFKNKFWLSLALSIPVVIFSPMFAHLFGYQIPD FT FPGAVWIAPVLGSVIFFYGGLPFLKGGWKELRSKQPGMMLLITLAITIAFLSSWITTLG FT IGNFNLDFWWELALLVVIMLLGHWIEMRALGSARGALDALAELLPDEAERVTAEGTDTV FT RISDLSVGDIVLVRSGSRLPADGEITEGQAELDESMITGESKTVPRGPGDSVVAGTVAT FT DSSLRIKVAAVGSDTALAGIQRLVSEAQASSSKAQALADRAAAFLFYFALSAGIITFLT FT WVLLGSPNEAVIRTVTVLVIACPHALGLAIPLVIAISTERAARAGVLIKNRMALERMRT FT IDVVLFDKTGTLTLGQPALTGISTAPGLSDNDLLALAAAVEADSEHPSARAIVAAARAR FT DIRIPTATEFTSLTGRGVTANVGGADIMIGGPNLLDSQALTIPRELQEQTQPWVERGAS FT VLHVVRAGQVIGALSLEDEIRADSRQAVAALQSRGLKVAMITGDAQQVAEAVAGKLGID FT EVFAQVLPQDKDKKVAELQARGLKVAMVGDGVNDSPALARAEVGIAIGAGTDVAIESAG FT VVLAGNDPRAVMSMLELSRASYRKMIQNLAWATGYNVIAVPLAAGALAFAGVSISPAIA FT AILMSLSTIVVALNAQLLRRINLDPDTIH" FT CDS 743608..744036 FT /transl_table=11 FT /locus_tag="AARI_06720" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTE2" FT /protein_id="CBT74895.1" FT /translation="MPNNRRLADGRQQQGTSFFAPAASFSADLAMLVHASMLLAFGGTL FT LAGCPAGFKHCLDCRWVLAGLASQNVDGGVADIGAVEIGPDAETQLGDHVFGQARVGTR FT GTALGAFETGGDTVRKLLKDRVIGFVGVGFQHGDDVTH" FT gene 744369..744635 FT /pseudo FT /locus_tag="AARI_06730" FT /product="truncated restriction-modification system FT endonuclease" FT /note="C-terminal section of a type I restriction- FT modification system endonuclease" FT CDS complement(744871..746811) FT /transl_table=11 FT /locus_tag="AARI_06740" FT /product="putative cation-transporting ATPase" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.-" FT /note="TCDB: P-type ATPase (P-ATPase) superfamily (TC 3.A. FT 3.y.z). Possibly involved in export of cations" FT /db_xref="GOA:E1VTE3" FT /db_xref="InterPro:IPR001757" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006404" FT /db_xref="InterPro:IPR006416" FT /db_xref="InterPro:IPR008250" 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:E1VTE3" FT /protein_id="CBT74896.1" FT /translation="MSSACGCDSPEPTEEFEEELPWWRDWHVLVPIASGVFFLAGLVLE FT WSTHGESAAIVALVLFWIGLLLGAFTFVPGALQKLFTKRKLGIGLLMAISATGAVILGY FT VEEAAALAFLYSIAEALEDKAMDRARSGLRSLLKLVPETATVIRDGIPVTVSAAEIKIG FT DALRVKPGERLATDGVVSQGSSSLDTSAITGESIPVEVTVGDQVAAGSINSSGALVVTA FT TANGTDNSLTTLVSLVEQAQSERGERARLADRIARPLVPGVIVLAVLVAVLGAIFGDPE FT TWITRALIVLVAASPCAMAIAVPVTVVSAIGAASKFGVIIKSGAAFERLGSLRRIAVDK FT TGTLTRNQPVVTQVQTVDDATREEVLAVAAALEQHSTHPLATAITAAVPAIPEAAAVNE FT EPGHGITGVLDGVQVGVGSPRWIAPGSLASAVESMEASGQTCVMVTRAEQVIGVIGVRD FT ELRPEAAEAIRDLHNQGIDVVMLTGDNSRTAHALASIAGIDTVHAELRPEDKAREIASS FT VQQVPTGMIGDGINDAPALASATVGIAMGATGADAAIESADVAFTGHDLRLIPQALSHA FT RRGRAIMNQNIVLSMAIIVVLLPLAITGVLGLAAVVLVHEVAEVIVIANGLRAARIHRK FT QLTQQPGNVLH" FT CDS complement(746808..747176) FT /transl_table=11 FT /locus_tag="AARI_06750" FT /product="putative ArsR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF01022: bacterial regulatory FT protein, ArsR family. ArsR-family transcriptional FT regulators include several proteins that appear to FT dissociate from DNA in the presence of metal ions" FT /db_xref="GOA:E1VTE4" FT /db_xref="InterPro:IPR001845" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VTE4" FT /protein_id="CBT74897.1" FT /translation="MMNIESRIAAMNRLGRAMADPTRSRILLSLLHEPGYPAELAQILG FT LSRANVSNHLTCLRGCGIVVAKMEGRKTRYEITDPHLTTALSALVDVTLAVDDQVPCLD FT SSCPDCATSADREHEEQA" FT CDS 747392..747637 FT /transl_table=11 FT /locus_tag="AARI_06760" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VTE5" FT /protein_id="CBT74898.1" FT /translation="MAEKFDIEERWPELFAQLDANQRNAVRQSLAAAWHEGWVPNREDV FT ENLTDEARGVIDEAEYLRRVDAAAERHRSGAHVVAK" FT CDS 747634..748434 FT /transl_table=11 FT /locus_tag="AARI_06770" FT /product="Fic family protein" FT /function="1.7 Cell division" FT /note="identified by match to PF02661: Fic protein family. FT cAMP may be a regulation factor in cell division of some FT bacteria. The Fic (filamentation induced by cAMP) protein FT is involved in the synthesis of PAB or folate. It would FT appear that the Fic protein and cAMP are involved in a FT regulatory mechanism of cell division via folate metabolism FT and in these organisms cell division could be controlled by FT coordination of cAMP, Fic and Fts proteins" FT /db_xref="InterPro:IPR003812" FT /db_xref="UniProtKB/TrEMBL:E1VTE6" FT /protein_id="CBT74899.1" FT /translation="MTEFDTWESYFYPPPDHTTMRNLLGERDPAVLAQKEYGRTAWRQR FT QLNADPSLVAHSYDAEHLRAIHRHLFQDVYEWAGEYRTQNMLKSGTMRGFADVYSGEID FT RYLADAQRLVAQTDWGRLDREQFGVAAANVFAHVNQAHPFREGNGRSSKVFLEHVAQQS FT GFTLDYARVSPQVWNQASEFSRPDIGQYDVVPDSLVPVFRHIAVERTATATPGVDPAAL FT AHSPLSASYPKTPSRSAPTGQQSPPRGTARPGRGYGTNGPGVGR" FT CDS 748431..749105 FT /transl_table=11 FT /locus_tag="AARI_06780" FT /product="putative resolvase" FT /function="3.3 DNA recombination, and repair" FT /note="match to PF00239 and PF02796. Possibly involved in FT site-specific recombination of DNA" FT /db_xref="GOA:E1VTE7" FT /db_xref="InterPro:IPR006118" FT /db_xref="InterPro:IPR006119" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="UniProtKB/TrEMBL:E1VTE7" FT /protein_id="CBT74900.1" FT /translation="MSHVIGYARVSTREQNPEAQEAELRAAGAARVYVDHGESSRFEDR FT PQWIACLDHLMDGDTLIIRALDRIAGSELMAIEIIRDLGRRGVHIKSLTEPFLDVDTST FT PMGEAIVGIMAVLAQLRISTIRENTRRGLAHARAQGRVGGRPSVMTVERTEAAVKMRAE FT GQSIAHIAKVLGVGSSSVSRALARIEDERAAFTSIVDGVLSDHVPDGAPLDGSDQTSAS FT PR" FT CDS complement(749402..749797) FT /transl_table=11 FT /locus_tag="AARI_06790" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTE8" FT /protein_id="CBT74901.1" FT /translation="MAKEPSIEEAVERARRAQEDRISAIRLVGEARQSLADVREETARE FT LAELQAQIAKRVGDAEREDVKAFNAAITAGWSVEELRKIGYAEPDKKVRARRRSTRKTG FT QKSAAQTDSVSDEKDAPQGVEESSSGS" FT CDS 750004..750459 FT /transl_table=11 FT /locus_tag="AARI_06800" FT /product="putative mobilisation protein" FT /function="3.1 DNA replication" FT /note="identified by match to protein family PF05713: FT bacterial mobilisation protein (MobC). This family consists FT of several bacterial MobC-like, mobilisation proteins. MobC FT proteins belong to the group of relaxases. Together with FT MobA and MobB they bind to a single cis- active site of a FT mobilising plasmid, the origin of transfer (oriT) region" FT /db_xref="InterPro:IPR008687" FT /db_xref="UniProtKB/TrEMBL:E1VTE9" FT /protein_id="CBT74902.1" FT /translation="MVPAQGGVAALGRKKVIGLGDEQTPAGRLFARRRRANVEGGRQHH FT HKVKVTPEEEGMLLRLAEAQHVTIPRLLVESALASEASETPTERKQAMAELFALHRLLA FT AISNNVNQIARHANATGEVQPATVSTLAKVREVAERIDAAIDGLSLS" FT CDS 750456..752171 FT /transl_table=11 FT /locus_tag="AARI_06810" FT /product="putative mobilisation protein" FT /function="3.1 DNA replication" FT /note="identified by match to protein family PF03432: FT Relaxase/Mobilisation nuclease domain. FT Relaxases/mobilisation proteins are required for the FT horizontal transfer of genetic information contained on FT plasmids that occurs during bacterial conjugation" FT /db_xref="InterPro:IPR005094" FT /db_xref="UniProtKB/TrEMBL:E1VTF0" FT /protein_id="CBT74903.1" FT /translation="MMPNIVRGDRMAGLMTYLAGPGRSNEHTEPHLVAGDPAVMAWHDD FT AELSRDAALAIARHLDRPRKAYEVEVNGGHVWHCSLSLRADEGALSDEKWNEIASDFVK FT AMGFDDNEGTKAPCRWVAVHHGVSKNGNDHIHLAVNLVREDGTKASVHNDFRRAQAAAR FT ALEVEHGLEPLESAQAQRATRGYDPAEREAQARSRARAKYERTRAKQGTKSPSWENLSG FT ADRKAHIAAELRTDQPRFLLSLKVRAASTASNSEAEFVRRMRRDGLLVRARFADGRSDV FT VTGYSVAERPEAGERPIWYGGGHLGRDLTLPRLRDGWPDTPTGATEAAAEWNAAKRGRR FT VVAPGREAHEPNPELWDQRNAELRELVDRLRAVPVDDRDTWATVARQTSGALAAWSNAT FT ESTPGDLAAAAEALSRSAQTYERTVSPQKAGTVALSGTAMLLASAAHGGQGTVAQAAMV FT RQLLRLTQAVHDACVAGKQARQAKLLAEDTRARLVRVRDAMPQVPTTAKGNGGATATIE FT RPRTLDPEAQAMLDRLHAGQGKPASAAASPIPNKIEPAKTHQTTKPGTDRGPER" FT CDS 752187..753047 FT /transl_table=11 FT /locus_tag="AARI_06820" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="similar to Arthrobacter plasmidic proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTF1" FT /protein_id="CBT74904.1" FT /translation="MAEESDGIEEAFEGQLRVLVTAAGQIGERMARAREDALRRAQAAS FT EQEARELQSRFAAEQRAARVEMSNVHRAEWWDRATPEQIGHTYQVARAWSKEEPEAVRA FT EQRMRDELRTRYSVDVDNAGADPEAVRQAVQRELARSEHDRAAAAAEQSRSEQERAEAQ FT RLMTMADQDERRAEESRAAAVHEPDPEERVRAAAEAEQREAQADRAREDGRTVYDSAER FT RAGTAQSLEAQGIDREVVATRMRADVSQGKPATEAVKGAGKAKAPKARKTRGHGTQVQR FT SGLDR" FT CDS 753359..754717 FT /transl_table=11 FT /locus_tag="AARI_06830" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.990 FT between position 30 and 31" FT /db_xref="InterPro:IPR021631" FT /db_xref="UniProtKB/TrEMBL:E1VTF2" FT /protein_id="CBT74905.1" FT /translation="MNSSVHRTKTVVWGVTMSLMLGAIAGPAFGAERLVAPSTATDSDQ FT NALNSVIPGIGVGTPAPLPFNFSDLGAMTVAKSSISLKDPAGQNIALKKIDGDGSGEDF FT YEGLTKNGKKVEVQVLSETQTAPLADPETLGSPDDPIDEVPVSGESDGYEVEATSKVVS FT AADFKPVLAIASTATTVTIAAPAGTAVKDVISYDSSGIVVAMPASKSENSNGSITLPRA FT EAAAMFGVETEQGDETTQLTIPIATPAAAKKNQWTEFYYTTFIPEKYVDVPAACKVTSN FT SWNVTKHNGNNRSWKNLKNGAAYESYKTVAGIKVDWSRGKVYNVAQVSISKGYDKSGNL FT KKKKQASARGIKTEQMQRSSSYVYWRMRHQVSNPLCPGAGAIRYTGAVKMYRSGTMKVS FT FNRVQVPNHEMYARTNLRGNWTNIHRLKRKSFACLAIPCGNNAYGRTVKLKIN" FT CDS 754792..755199 FT /transl_table=11 FT /locus_tag="AARI_06840" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTF3" FT /protein_id="CBT74906.1" FT /translation="MLSLPIFILIAFTVDLISYMSEATPLGYTTLWAGVLVPFTAILIF FT ATVPTLIKKTRSVVRDLIGVFLGATLFGVIASLPIWSSTAGQSDVARGDYASGVMLSPI FT LGLIVVAIFAVSSGFFEYLLHRRIRTRSTKR" FT CDS complement(755360..755722) FT /transl_table=11 FT /locus_tag="AARI_06850" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTF4" FT /protein_id="CBT74907.1" FT /translation="MNEAVQVAGYALWWSLLTTSLTALWCLGRNTFKHVMPSENVPAGS FT AKALVASLPAAVVALAIISTPSILISAMYPHAQTNAWLWLWTVPAGLGALFIDFLALGL FT LVKLVRRLEPMPSPST" FT CDS complement(755757..756506) FT /transl_table=11 FT /locus_tag="AARI_06860" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTF5" FT /protein_id="CBT74908.1" FT /translation="MSDWGEDEYTENEGQPSAAADTPRSPGRVFGLDIGGLAGEYVDAA FT VKASVRKQVNNVATAAVDEALTEKLLESLRERAGQAAEAAVTEQVEANEAADEAQDDDG FT EAEPEETLYYGSVDEFVREYLRNVYRRAINGRSRVWAARWWEYDEAVIRLEALWRSWEH FT LRMDPSTGMSVWWRDHADHHMAVLLDPDGPFSSAADADENKSKKGQPLPYAAPPEGLFP FT DQRQVHEPKDDVSREEEPEPPAEEWQG" FT gene complement(756503..758059) FT /pseudo FT /locus_tag="AARI_06870" FT /product="truncated traG-family protein" FT /note="fragment of a protein that may be involved in FT bacterial conjugation" FT gene complement(757989..758363) FT /pseudo FT /locus_tag="AARI_06880" FT /product="truncated GNAT-family acetyltransferase" FT CDS complement(758702..759310) FT /transl_table=11 FT /locus_tag="AARI_06890" FT /product="acyl-CoA acyltransferase domain-containing FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VTF6" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VTF6" FT /protein_id="CBT74909.1" FT /translation="MTRIAPITLHGKYVTLEPLSEDHHDGLVEAASDGELWNLWYTSVP FT RPEEMYDEIQRRLAMQSEGSMVPFTTRLNDPTTGEPGKIIGMTTYCDINAELPRLEIGY FT TWNAASAQGTGTNPDSKRLLLGHAFETLNCVAVEFSTHWMNMQSRQAIARLGAKQDGVL FT RATSRMADGSLRDTVIFSIIASEWPQIRSGLDLRLAKKR" FT CDS complement(759511..760632) FT /transl_table=11 FT /locus_tag="AARI_06900" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTF7" FT /protein_id="CBT74910.1" FT /translation="MTDLMSALPRTTIGTTTFYIDEARPVALVRREAMPDLFLTWPDLD FT TGILAPDVSVCAATDALWVLYQSGPDGQEIDYPALHSPTVVVAVRIGVDGSLGFVRTEE FT TTVVGATSAGLWTSTSIVEQTDDNYRGGELPADWAAPSTLQILLPGQVQRTLEVDRYVN FT AVREDEHGHVLFVNPSPPVAHHDSDTISYEYRCTAMVIGTVDEIPEHVKFREFVPQGWG FT TLVASEQLGLDYDSYGPRHDSARVDLSEIAGTHWKRVSLTDAQKTQAVKALTDQFADAD FT AYWRAADGTTAPLADGVQETHVETIGEWPESEVHVTCRHPYFPAGWIRRRIRVFDDAGR FT IKFDRYASLEFMEDLDTHALPDIREAKDGILEV" FT CDS complement(761249..761773) FT /transl_table=11 FT /locus_tag="AARI_06910" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTF8" FT /protein_id="CBT74911.1" FT /translation="MIKFERWSGRFPNKYQSAGLGVVGLVLCAGVLTGCSVFRDYSGDT FT CDGRKPVGSLEQAGKGLVSAAYAADRDGVCRVTAPFPGGVLDDSMVAKTREILAERGIT FT PQNVTVVIGEQMGSGVAVQLTDGSNNVSRAIDINGTFVRDDGFTVGLPPELYPEVPEHP FT ASQPASTDPAP" FT CDS complement(762001..762849) FT /transl_table=11 FT /locus_tag="AARI_06920" FT /product="PDZ domain-containing protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="IPR001478; PDZ domains are found in diverse FT signaling proteins in bacteria, yeasts, plants, insects and FT vertebrates" FT /db_xref="UniProtKB/TrEMBL:E1VTF9" FT /protein_id="CBT74912.1" FT /translation="MSVRHESASGLIWNNKVGKVRMSQNSDARLRFAIIRQLPETGLFA FT DEVVAIAPDVQVVSINLDDGGNIDLAGIENLPLLSSLIIHQCDGILTYGGSGNEVMALT FT RLIMPYAQGVTEQLVASPHLQDLEIEGGTPDLLRHMAKTVRKVLLQRVKGAADLMAWDR FT LTQLDEVEINQSGSIEVVAPAGGWPEVVSFTVIGSLKGIVLASKARPFQYLYLEGVRLF FT DPDASFWDLQAKRVTVGYSTKPPKWLVEAWPHRPDDWDERFCIASHRLLPGSEERYFDE FT L" FT CDS 763759..765096 FT /transl_table=11 FT /gene="trt" FT /locus_tag="AARI_06930" FT /product="reverse transcriptase/maturase" FT /function="3.6 RNA modification" FT /note="identified by similarity to protein SP:Q6DKY2 FT (Bacillus stearothermophilus). Heat-stable reverse FT transcriptase. Possible group II intron associated protein" FT /db_xref="GOA:E1VTG0" FT /db_xref="InterPro:IPR000123" FT /db_xref="InterPro:IPR000477" FT /db_xref="InterPro:IPR013597" FT /db_xref="UniProtKB/TrEMBL:E1VTG0" FT /protein_id="CBT74913.1" FT /translation="MNPGEYFLACSVEPAADGKDIRDQQVDLWEQVFSRGNLLIALKRV FT ERNKGSAGVDGLEAHELRDWCREHWIETRKSLDAGTYAPLPVRQVMIPKPDGGERMLGV FT PSVLDRLIQQALAQVLSPIFDEGFAPMSYGFRPGKSAHDAASMARKVIEQGYRWVVEVD FT LDAFFDRVNHDVLMSRVARKVKDKRVLKLVRKYLTAGIMAQGVRRETVEGTPQGSPLSP FT LLSNIILDDFDQEFWSRDHRFVRYADDIRIFVKSKRAAERVLGQATKVLEQRLKLKVNR FT QKSVINPASVATLLGFGFYFVKGSKVRIRVAPKAWIRMKERIRRLTSRRWSVSMDYRIE FT QLNRFVRGWMGYFRLSMTADKFATLDQWFRRRLRQIRWVEWKRPRTRVANLRRLGIVKD FT KAYQWGNSSRAYWRVAKSPILHRALPTSYWEELGVLFFRRAWDRFQ" FT CDS 765331..766038 FT /transl_table=11 FT /locus_tag="AARI_06940" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTG1" FT /protein_id="CBT74914.1" FT /translation="MTESAASAESDATSELTDEVSKSAKATDEASEARVEDSNEAPASE FT PASEATEPTPARVQEESKSVNPEVKSVATVLPESPKQSSNSFGLVSSDDRWDEINALLP FT EGSEDWSDEQWEVFVETEAGEEYFRQLNELLEEEYPVEDDFELSEEEQAFWDLILDTLP FT QDSLEWDDSEWEEYFRSDAGLEFIEQLLPIIADSVETDEDAADLQAFLEEVFADDPELR FT AYYLEMYLGITGS" FT CDS complement(766062..767339) FT /transl_table=11 FT /locus_tag="AARI_34570" FT /product="transposase of ISAar15, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTG2" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VTG2" FT /protein_id="CBT74915.1" FT /translation="MIKDTGRIDAASILLNLTDYRVITVTQELAGRQVLVEPIETEAAC FT PSCGVLTTRIQARPVHQVKDLPAGGDDLQVLVRKRRMACQEPACERRSFVQTTEQLPFR FT ARITTRLSQRLVDEMSCELRAVSRVAAAHGVSWPTVMARLTTVGELVGNVDRMFIRRLG FT IDEHRFRKVRYALGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRGTAVKKWLKNRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKVSVDHFHVIARANLMITQVRRRRSHEVHERR FT GRATDPAYKYRKLLTCNLENLSIKQVERLKLILESDPELGVIYGIKEHVRQLLKTADIH FT EFQSRWAVLEKSVKATKMTEAKTLFRTLTAWRRELLVFVRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRLRILLYTAGLRPC" FT mobile_element complement(767404..768799) FT /mobile_element_type="insertion sequence:ISAar16" FT /rpt_family="IS110" FT CDS complement(767420..768499) FT /transl_table=11 FT /locus_tag="AARI_34580" FT /product="transposase of ISAar16, IS110 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTG3" FT /db_xref="InterPro:IPR002525" FT /db_xref="InterPro:IPR003346" FT /db_xref="UniProtKB/TrEMBL:E1VTG3" FT /protein_id="CBT74916.1" FT /translation="MTILPQTVAKTYSYIIGVDTHARKHVYSIITYTGEHVETRDFPAT FT SSSIKRAIAWVGRRTGADASTLWIIEGTASYGAVVTGAVTDAGYTVAEAPSGYQKAGRG FT VGKTDPLDAQRMAAAALPIEVQKLRVPRLNDGARAALRVLVTARDMLAVERTKYVNALT FT ALLRVTSLGIDARKPLSSTQFLEVAGWRSREETIESQVARAEAVRLARRVGELDTHIKE FT NTTQMTELVKLSEGKELLELTGIGPVVAAVCVAAWSHQGRLRSEAAFASLAGVNPIPAS FT SGNTVRHRLNRRGDRRLNKALHTAAMVRMTHDEETRAYVVKRTAEGKTLKEIRRCIKRF FT LARRIYKILESAEVLPLTA" FT CDS 768891..769151 FT /transl_table=11 FT /locus_tag="AARI_06950" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="InterPro:IPR019931" FT /db_xref="UniProtKB/TrEMBL:E1VTG4" FT /protein_id="CBT74917.1" FT /translation="MDEPEVSESERPVADAEIKPVGSIGKTIVTKAQKASKSTEPVAVV FT EASAPALANTGFDGFWAAGVGILLAIGGVVFIARSRKASAK" FT CDS complement(769232..769774) FT /transl_table=11 FT /locus_tag="AARI_06960" FT /product="flavin reductase-like domain protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF01613" FT /db_xref="GOA:E1VTG5" FT /db_xref="InterPro:IPR002563" FT /db_xref="InterPro:IPR009002" FT /db_xref="InterPro:IPR012349" FT /db_xref="UniProtKB/TrEMBL:E1VTG5" FT /protein_id="CBT74918.1" FT /translation="MSKVSIDATDSLPAEDFKAVFRGHPGGVSVITADAGQGPVALTAT FT SVASISVDPPLLVFSISALSSASDGLSRAQTVVVHSLDVHDIELAKLGATSGVDRFAQD FT QTWTRLSTGETVFDNVRAWVRCEVVERIQAGTSTVIVARGLQSHIARDSQPGELGDALV FT YHNRSWHHLNSGSHLGH" FT CDS complement(769767..770807) FT /transl_table=11 FT /gene="metE" FT /locus_tag="AARI_06970" FT /product="5-methyltetrahydropteroyltriglutamate--homocysteine FT S-methyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.1.1.14" FT /note="final step in methionine synthesis" FT /db_xref="GOA:E1VTG6" FT /db_xref="InterPro:IPR002629" FT /db_xref="InterPro:IPR016456" FT /db_xref="UniProtKB/TrEMBL:E1VTG6" FT /protein_id="CBT74919.1" FT /translation="MTSPLIPTSIVGSLPKPSWLAEPEKLWSPWKLEGEQLREGQQDAM FT RAAVLEQTQRGIDIISDGEQTRQHFVTTFIEHLSGVDFEKRETVRIRNRYDASVPTVVS FT AVEREKPVFVEDAKALRTFTDKPIKWTLPGPMTMVDTLYDAHYQSREKLAWEFATILNQ FT EARELEAAGVDVIQFDEPAFNVFFDEVADWGIAALERACEGLKAETVAHICFGYGIKAN FT NDWKATLGAQWRHYEKSFPLLQASTIDTVSLESHHSNVPLEVVEMVRGKKVMLGAIDVA FT NVAIETPQEVAQTLRKALEFVDADKLIASTNCGMAPFPRDVSLAKLSALNAGAGILREE FT LVGASV" FT CDS complement(770826..771818) FT /transl_table=11 FT /locus_tag="AARI_06980" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR015004" FT /db_xref="UniProtKB/TrEMBL:E1VTG7" FT /protein_id="CBT74920.1" FT /translation="MADALNFSISTTRFDENYSPSTNSRTTTNFANLARGERREENLRN FT ALTMINRRFNSLAHWDNPQGDRYSLELEIISANVHFSADNTDKQFPLLEVLETTIVDKL FT TGTRSQGMVGNNFSSYVRDYDFSVVLPASCNDSGAPVLPEDFGDLHGQLFQHFLNSQAY FT RERFAQLPVICISVSTSKTYFRTGNSHPVLGLEYHQDENSLTDAYFGKMGLSVRYFMPP FT GAVAPLAFYFRGDLLNDYTNLQLISLISTMETFQKIYRPEIYNANSAAPSVYHPSLGAE FT DFSPTRVFYDREERTQLGKIQGKFTEEHFIIPNRQLLDQWSSSYPTPVA" FT CDS 771941..773071 FT /transl_table=11 FT /locus_tag="AARI_06990" FT /product="LysR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00126: bacterial regulatory FT helix-turn-helix protein, lysR family. 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 /db_xref="GOA:E1VTG8" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VTG8" FT /protein_id="CBT74921.1" FT /translation="MVQGTNGLTLQQLRYFVAVASEGSISAAADLIYVAQPSMSSAMKE FT LESRVGRTLLMRSARGVTLTAEGAEFLGYARQVLEQVELLEHRYLGRPSARRLLGVSTQ FT HYSFSVDAFVRMVQASGAEEYQFSLRETRTEQIIEDVRTLRSDIGILYRNDFNRKVIDK FT LLRESRLVFHPLFLADPHIFISRSNPLATRTQVTLEDLEDLPRLTFDQGANNSFYFAEE FT VLSTRSSQREIQVSDRATIFNLMIGLGGYTISTGIISDELDPLHRGHPAGHRGAHRNRL FT DRPRRHPAHRPGPALPARSAHRGRQLRGRSARLSRQWRNSRSPSTGTSSQTSSKTSTSR FT RFISKLRVIKCCRSPRHHDNEKSYEAWRPCMKPAAR" FT CDS 773295..774608 FT /transl_table=11 FT /locus_tag="AARI_07000" FT /product="O-acetylhomoserine aminocarboxypropyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.5.1.49" FT /note="catalyses several reactions, including the formation FT of L-homocysteine from O-acetyl-L-homoserine and H2S, and FT the formation of L-methionine from O-acetyl-L- homoserine FT and methanethiol" FT /db_xref="GOA:E1VTG9" 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:E1VTG9" FT /protein_id="CBT74922.1" FT /translation="MSQETDAVHAGYRPSGDFRPMLPPLHNSAAYQFASHAEAIEKFAL FT RQAGFTYSRTGNPTVSILEQRVAALEGGAHAVATATGQAAVALSLLALTQGPKHIVASS FT SLYGGTVDLFTDTFADFGIRVSFVDQADPSAWAAAIESDTRAFFLESVSNPLCTVADIP FT AIAAIAHERNIPVVVDNTLATPLNVRPLELGADIVVHSATKGLAGHGSVLGGVVVDSGT FT FDFSDSSRWPQIAAPRVRLNGTSLLERHGPAAYAMLVRSKFLHDLGPTLAPASAQGILA FT GIETLPVRAAHVQRSVTRLIDALAEYPGIAAIHHPSLPEHPSHELARALAPKGTGCVLA FT IELAHPSLVSPVIDGLKLISLAANVGDTRTMVSHPATMTHCRLSEQQLADAGLNTSTLR FT LSVGLEDPADLLADITQSLDLALAATQATAGTKEVSFA" FT CDS 774605..775828 FT /transl_table=11 FT /gene="metB" FT /locus_tag="AARI_07010" FT /product="cystathionine gamma-synthase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.5.1.48" FT /note="catalyzes the conversion of cysteine and succinyl- FT homoserine into cystathionine and succinate. Several other FT reactions may also be catalysed in some organisms" FT /db_xref="GOA:E1VTH0" FT /db_xref="InterPro:IPR000277" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:E1VTH0" FT /protein_id="CBT74923.1" FT /translation="MSGFNTLAVHAGQHKDPHTGAVIPPIYQTSTFIQDGINVLRAGHE FT YSRGSNPTRNGFESQLAALEGGAAGFSFASGIAAEDALLRAVLEPGDHIILGADGYGGT FT NRLISKLHGKWGITSSAVDITNLDAVRAAVRPNTALLWVETPSNPLLGIADLAGWAAIA FT AEHGALLVVDNTFATPYLQRPLDFGAHAVVHSTTKYIGGHSDVLGGAVIVADHLHRGQS FT LAEAVGYQQFAGGAVSGPQDSYLAARGLKTLGLRMERHGATASTLARWLDDQPEVTRVY FT YPGLERHPGHELAKSQSAAGRGFGGILSLQLSDEAAARAFAQSMEYFQLSVSLGGVESL FT VCYPREMTHASLIGTPLEIPANLVRLSVGIEEADDLIADLERGLAAARATQPVHKPAVV FT REKALENA" FT gene 776192..776350 FT /pseudo FT /locus_tag="AARI_07020" FT /product="truncated protein" FT /note="similar to the C-terminal part of a protein from FT Arthrobacter arilaitensis" FT CDS complement(776416..777030) FT /transl_table=11 FT /locus_tag="AARI_07030" FT /product="putative transferase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00132: Bacterial transferase hexapeptide FT repeat. A number of different transferase protein families FT contain this repeat, such as galactoside acetyltransferase- FT like proteins, the gamma-class of carbonic anhydrases, and FT tetrahydrodipicolinate-N-succinlytransferases" FT /db_xref="GOA:E1VTH1" FT /db_xref="InterPro:IPR001451" FT /db_xref="InterPro:IPR011004" FT /db_xref="UniProtKB/TrEMBL:E1VTH1" FT /protein_id="CBT74924.1" FT /translation="MAARATGRGPHADLRSSVANSPLQCLAITVGEMTHIITIDGATPK FT VGQDVFVAPTATLSGDVELADRASAFYGVSVRGDSAPIRVGEGTNLQDNVVLHADEGFP FT CTLGAGISVGHSAVVHGATVGDGCLVGMSATIMNGAVIGEQSLVAAGALVLEGTQVPPR FT SLVAGVPSKVRRELSDEEVAGLKTNADHYLVLAAKHLEANA" FT CDS complement(777083..777448) FT /transl_table=11 FT /locus_tag="AARI_07040" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTH2" FT /protein_id="CBT74925.1" FT /translation="MDYAAIAVVALLIAASACWPLLRASGKRRKALKAQAPQLPEHHRP FT RYRQSLAGDPLAYPLAMSSSYALCRDSDTARSFWRAQPDSALDGAHDAHRTQVFTGAEG FT LLRRWLSPHRYRLASCC" FT CDS complement(777451..778293) FT /transl_table=11 FT /gene="purU" FT /locus_tag="AARI_07050" FT /product="formyltetrahydrofolate deformylase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="3.5.1.10" FT /note="catalyses the following reaction: 10- FT formyltetrahydrofolate + H(2)O <=> formate + FT tetrahydrofolate" FT /db_xref="GOA:E1VTH3" FT /db_xref="InterPro:IPR002376" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR004810" FT /db_xref="UniProtKB/TrEMBL:E1VTH3" FT /protein_id="CBT74926.1" FT /translation="MNQYIVTLSCIDRPGIVHAISGGLLGAGCNITESQQFLSPETGTF FT FMRIEVATEQSLAQIRAGLAPIRDDFHMSLRVDDGAKRTRTMIMCSKAGHALNDLLFAQ FT RAGTLAIDVPVIVSNHLDLKPMADFYGVDFVHLPVTKENKSQAEAELLKLAEDYGIELV FT VLARYMQILSDSLCERMEGRVINIHHSFLPSFKGAKPYHQAYARGVKLIGATAHYVTAD FT LDEGPIIDQEVTHVSHTRTAEQLVELGRSVEGRTLTRAVQWHAEHRVMLDGQRTIVFS" FT gene complement(778469..779371) FT /pseudo FT /locus_tag="AARI_07060" FT /product="truncated FAD-dependent pyridine FT nucleotide-disulphide oxidoreductase" FT /note="N-terminal section of a FAD-dependent pyridine FT nucleotide-disulphide oxidoreductase" FT CDS 779557..780420 FT /transl_table=11 FT /gene="folD" FT /locus_tag="AARI_07070" FT /product="bifunctional methylenetetrahydrofolate FT dehydrogenase/cyclohydrolase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="3.5.4.9" FT /EC_number="1.5.1.5" FT /note="methylenetetrahydrofolate dehydrogenase (EC 1.5.1. FT 5) catalyses the following reaction: 5,10- FT methylenetetrahydrofolate + NADP(+) <=> 5,10- FT methenyltetrahydrofolate + NADPH. Methylenetetrahydrofolate FT cyclohydrolase (EC 3.5.4.9) catalyses the following FT reaction: 5,10- methenyltetrahydrofolate + H(2)O <=> 10- FT formyltetrahydrofolate methenyltetrahydrofolate FT cyclohydrolase" FT /db_xref="GOA:E1VTH4" FT /db_xref="InterPro:IPR000672" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020630" FT /db_xref="InterPro:IPR020631" FT /db_xref="UniProtKB/TrEMBL:E1VTH4" FT /protein_id="CBT74927.1" FT /translation="MSARILDGKATAAAIKQELAERVAKLKAAGHTTGLGTILVGNDPG FT SAWYVGGKHKDCAEVGIESIRVDLPEETTQDELLAKVRELNENPDCTGYIVQLPLPKHI FT DTDVILEAMDPAKDADGLHPMNLGRLVANVNRPMASPLPCTPLGCVELLARHDIDLNGK FT HVLVLGRGVTIGRPVGLLLTRRDVNATVTLAHTGTTNLPELLAQADVVIAAAGVPHIIK FT ADAIKEGAIVLDVGVSRVDGKVTGDVDPAAAEVASWISPNPGGVGPMTRAMLLNNVVEA FT AERNAK" FT CDS complement(780559..781944) FT /transl_table=11 FT /locus_tag="AARI_07080" FT /product="MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (MFS), metabolite:H+ FT symporter (MHS) family (TC 2.A.1.6.z)" FT /db_xref="GOA:E1VTH5" FT /db_xref="InterPro:IPR005828" FT /db_xref="InterPro:IPR005829" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VTH5" FT /protein_id="CBT74928.1" FT /translation="MTQPKAAKANQRRVAFATVIGTTVEWYDFFIYATAAGLVFSQLFF FT EPAGQDIALLISFASVGLSFLFRPLGAFLAGHFGDKIGRRAMLVLTLALMGAATTLIGV FT LPTYETAGIWAPIMLLLLRILQGISAGGEWGGAVLMAVEHASDGHRGRAGSYPQVGVPL FT GMLLASGTMALMTGVISPGDAFLEWGWRVPFLVSIVLIAVGYFVRRSVDESPVFEEISE FT NKAQTAVPILVLFKKHWPLVLIAALVFAGNNAAGYMTTGGFFQAYTTNPEGPVGLERTD FT VLIAVAFGAAVWLVMTLVAGYLADRIGRKRTYQLGFIILAASLFPVFALVNSGSLVLLY FT AAFGLFSIGLGLTYGPQAALYSELFPASVRFSGVSNSYAIGAIVGGAFAPTIAQALVQA FT TGGTTAVAVYLLIVVAISFTAVSMIRDRSGIDLSFRNQAEQEVGALVFDKRRADAVKAT FT QDV" FT CDS 782072..782971 FT /transl_table=11 FT /locus_tag="AARI_07090" FT /product="LysR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00126: bacterial regulatory FT helix-turn-helix protein, lysR family. 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 /db_xref="GOA:E1VTH6" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VTH6" FT /protein_id="CBT74929.1" FT /translation="MYSMRHLEIMAELPVHSTLGSAASELRISESALSQAITAIEKHAG FT ETLCLRRKAHGIRLTASGQHFAAMARKILSDVGELRATFPQTEGALRGPVRFGCFASLS FT PHLIPATLEGFDHPEVQLDVRVGTHEDLLPALREGEIDVAFVYDLQLPADIDKQQIYQT FT EMQVVLHPEHRLAKLARPLELADLVDESLIIYESDPSTEHQQQLFASQGLQPRIAASVP FT QMILVSAMVGRGLGYGLLMRRPNNAEVSIEGRPLAFRELKAPNYPNAVVAITPRGVRIP FT ARVQALIDHCTCAMAESW" FT CDS 783004..783360 FT /transl_table=11 FT /locus_tag="AARI_07100" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTH7" FT /protein_id="CBT74930.1" FT /translation="MIGTWQAMVIDCEDPDALAGFYEQLLGMVRIDNEPDWVSIGDAPD FT HPALAFQAVSPYVAPQWPGHVHPQQAHIDVKVKDLDLAEEQVLHLGARWTGEGSKTFRV FT YLDPQDHPFCLVSW" FT CDS complement(783308..783970) FT /transl_table=11 FT /locus_tag="AARI_07110" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VTH8" 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:E1VTH8" FT /protein_id="CBT74931.1" FT /translation="MKVLIVDDHATVRMGIRLVLQAAEDLEVVGEAADGRSAISMARAL FT SPDVILMDLRMPVLDGIEATKALHGSCRVVVLTTFDDDQYLFGALQAGAHGFLLKSAEP FT QAIIMGVRAAGRGESVLDPQVTSRILARALAPEPGTAKLPDGLTGREREVLDGLAEGLS FT NPQLAQRLGIGQSTVKTHVSQVLAKLGVSTRLQAAKIAYAATSSPGRTGGPADPDRP" FT CDS complement(783967..785130) FT /transl_table=11 FT /locus_tag="AARI_07120" FT /product="putative signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VTH9" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR011712" FT /db_xref="UniProtKB/TrEMBL:E1VTH9" FT /protein_id="CBT74932.1" FT /translation="MNFIRRMGSGDKEPEVVGTYLVLTAILHLSGLANPPWFAIRGYEW FT IVLLLIGLAAVLVRRRFLVASSVAMLLAGAGLLAVGSIGGYFLVFECVFGLFLLGSVRT FT RTVALALLCLAAISLAIATWLGTRNPQEVVLALLMAGFILFTPMLWAENVRTAKELANA FT EAQRAQAVQSAADAREDQLVAEHDFSRVQERTALAREMHDVLSARFSSIALLSGALLPA FT APQEVRAPLQSIRDESVSGLEDMAAMVRMLHAGGPALQARIEDLPELVAGFGSPVRWEY FT RVAHPQRFGPAVHTAAHRTVCELLVNHAKHAPGTTLELSVVQEKGLAITASNGLRQDAG FT RAPGAGTGLENIRTRVAALDGRFEVRTGPDFAVHVEFPGPAEAMEKP" FT CDS 785240..786022 FT /transl_table=11 FT /locus_tag="AARI_07130" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR021315" FT /db_xref="UniProtKB/TrEMBL:E1VTI0" FT /protein_id="CBT74933.1" FT /translation="MDIMTSNPELSLLILALIDSTSIGTLVIPLWLLLRGRHEAIAKVL FT AYLLVIAGFYWVIGVLLRSGLLLIDPGIFEHRFFRLAGMAVGALMIIWALTYRTDAQKE FT ASARKKAIAHSGAALEGPAPSPADATGQVPRRLRSRLGTALDTRTGLIALALFAGLLEL FT PTMLPYLAAVGVMQGAGWGTGLQLLALIGYCLVMIVPALVLVGARALAGPRIEAWLQKM FT GTKASAYAQETLGWVVGIGGYLLIRACLSGQDLHSLLS" FT CDS 786092..786589 FT /transl_table=11 FT /locus_tag="AARI_07140" FT /product="hypothetical membrane protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTI1" FT /protein_id="CBT74934.1" FT /translation="MEPLGSSAKQGRKVTLNASTLAMSVMVIVLLVAVVFAANSNEIVG FT WFVVVISAGWLLLAAFMMFGLKRGADKINNSLREATAAATPRAQPGTVVVDESTSQRDM FT KLDHSFKIVQVQARVIAEQREAKGEDYEGMIDRALETIQMTATNARDMIKPAKPMDGEI FT ID" FT CDS 786692..787531 FT /transl_table=11 FT /locus_tag="AARI_07150" FT /product="exodeoxyribonuclease III" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.1.11.2" FT /note="removes the damaged DNA at cytosines and guanines by FT cleaving on the 3 -side of the apurinic/apyrimidinic sites" FT /db_xref="GOA:E1VTI2" FT /db_xref="InterPro:IPR004808" FT /db_xref="InterPro:IPR005135" FT /db_xref="UniProtKB/TrEMBL:E1VTI2" FT /protein_id="CBT74935.1" FT /translation="MIPTSVEILNKDAGALRVASVNVNGIRAAYKRNMADWIAARDVDI FT LCLQEVRAPDKILRDLIGEGWHILHAEAKDKGRAGVAVLSRTAPVAVREHIGEDYFAES FT GRWVEADFEVNGEVFTVVSAYVHSGELGTQKQEDKYRFLQRMNVRLVELKNEKDHVLVV FT GDLNVVHTQKDIKNWKPNHNKRAGVMDEEIAYFDGFFGPQIGYKDVARELAGDVQGPYT FT WWSFRGQAFDNDAGWRIDYHMATPALAAKAIKSHVDRASAYDLRFSDHAPLVVDYQF" FT CDS 787540..788556 FT /transl_table=11 FT /gene="trpS" FT /locus_tag="AARI_07160" FT /product="tryptophan--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.2" FT /note="activates tryptophan and transfers it to tRNA(Trp) FT as the first step in protein biosynthesis" FT /db_xref="GOA:E1VTI3" FT /db_xref="InterPro:IPR001412" FT /db_xref="InterPro:IPR002305" FT /db_xref="InterPro:IPR002306" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR024109" FT /db_xref="UniProtKB/TrEMBL:E1VTI3" FT /protein_id="CBT74936.1" FT /translation="METTRPRVLSGMQPSGDSLHLGNYLGALVNWVKTQDDHEAFFFIP FT DMHAITTPQDPAELRARTRKTAAQFIAGGIDLDKSTLFVQSQVPEHAQLAWVFNCITGF FT GEASRMTQFKDKSSKGGADAASVGLFTYPVLMAADILLYQPEGVPVGDDQRQHVELARD FT LAKRFNHRFGQTFTVPEAFIPKEGARIYDLQNPTSKMSKSAESPAGLINVLDEPKLIAK FT RIKSAVTDAGSVVAYDKAEKPGVSNLLDILAAVTGKHVPELVNEFEGKMYGHLKVAVAE FT AVVERLTPIRTRTLELLDDPAELDRLLLVGATKAREVASKTVADVYQKVGFLPPLGI" FT CDS 788556..789068 FT /transl_table=11 FT /locus_tag="AARI_07170" FT /product="2',5' RNA ligase family protein" FT /function="3 Information pathways" FT /note="match to PF02834. Corresponds to a number of known FT and predicted phosphoesterases, including bacterial and FT archaeal 2 ,5 RNA ligases. The physiological substrate(s) FT in prokaryotes may include small 2 ,5 -link-containing FT oligonucleotides, perhaps with regulatory or biosynthetic FT roles" FT /db_xref="GOA:E1VTI4" FT /db_xref="InterPro:IPR009097" FT /db_xref="UniProtKB/TrEMBL:E1VTI4" FT /protein_id="CBT74937.1" FT /translation="MAFEYTLGVVIPVPQPHRETLRAWRQEYGGEATGPIAPHITLVSG FT SYLNSWEKAAAQVRRVAATVEPFSIQLGPARTFRPASDVVFLPLETGADECWALHRALL FT GDALRHESAFAYHPHLTIAQNVPAEQLDAAQAALGGTRLSFTADRIQLFDTRGGEWNFS FT EEIALGT" FT CDS complement(789114..790568) FT /transl_table=11 FT /locus_tag="AARI_07180" FT /product="catalase" FT /function="4.2 Detoxification" FT /EC_number="1.11.1.6" FT /note="decomposes hydrogen peroxide to molecular oxygen and FT water. Its main function is to protect cells from the toxic FT effects of hydrogen peroxide" FT /db_xref="GOA:E1VTI5" FT /db_xref="InterPro:IPR002226" FT /db_xref="InterPro:IPR010582" FT /db_xref="InterPro:IPR011614" FT /db_xref="InterPro:IPR018028" FT /db_xref="InterPro:IPR020835" FT /db_xref="InterPro:IPR024708" FT /db_xref="InterPro:IPR024711" FT /db_xref="UniProtKB/TrEMBL:E1VTI5" FT /protein_id="CBT74938.1" FT /translation="MASNEPRSTTQAGIPAVSDRNSLTVGANGPIVLHDHHLAETLQHF FT NRMNVPERRPHAKGSGAFGEFETTEDISRYTKAALFQPGVKTETLMRFSTVAGELGSPD FT TWRDVRGFSMKFYTTEGNFDLVGNNTPVFFLRDPMKFPHFIRSQKRLPDSGLRDGTMQW FT DFWTQNPESAHQVTYIMGQRGLPKTWREMNGYGSHTYMWVNAAGEKFWVKYHFLNQQSD FT KFETMSGDQAQALAGSDAEFHRRDLFDAIKAGNFPKWDLYVQIMPYEEAKTYRYNPFDL FT TKVWSKKDYPRIKVGTLTLNRNPENFFAQIEQAAFSPGNMVPGMGMSPDKMLLGRNFAY FT ADAQRYRIGTNFQQLPVNKPKCPVHSYNFEGNMTFDHTGDRCVYAPNSFEDSWSDETGP FT VDNSFESDGELVREAYTLREDDGDFVQPGILVREVMDDAQRAELVNTVTGALDGVIEPV FT LSNAIDYWKNIDADTGAKIEAIVRAK" FT CDS complement(791662..792939) FT /transl_table=11 FT /locus_tag="AARI_34590" FT /product="transposase of ISAar15, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTG2" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VTG2" FT /protein_id="CBT74939.1" FT /translation="MIKDTGRIDAASILLNLTDYRVITVTQELAGRQVLVEPIETEAAC FT PSCGVLTTRIQARPVHQVKDLPAGGDDLQVLVRKRRMACQEPACERRSFVQTTEQLPFR FT ARITTRLSQRLVDEMSCELRAVSRVAAAHGVSWPTVMARLTTVGELVGNVDRMFIRRLG FT IDEHRFRKVRYALGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRGTAVKKWLKNRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKVSVDHFHVIARANLMITQVRRRRSHEVHERR FT GRATDPAYKYRKLLTCNLENLSIKQVERLKLILESDPELGVIYGIKEHVRQLLKTADIH FT EFQSRWAVLEKSVKATKMTEAKTLFRTLTAWRRELLVFVRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRLRILLYTAGLRPC" FT mobile_element complement(793004..794399) FT /mobile_element_type="insertion sequence:ISAar16" FT /rpt_family="IS110" FT CDS complement(793020..794099) FT /transl_table=11 FT /locus_tag="AARI_34600" FT /product="transposase of ISAar16, IS110 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTG3" FT /db_xref="InterPro:IPR002525" FT /db_xref="InterPro:IPR003346" FT /db_xref="UniProtKB/TrEMBL:E1VTG3" FT /protein_id="CBT74940.1" FT /translation="MTILPQTVAKTYSYIIGVDTHARKHVYSIITYTGEHVETRDFPAT FT SSSIKRAIAWVGRRTGADASTLWIIEGTASYGAVVTGAVTDAGYTVAEAPSGYQKAGRG FT VGKTDPLDAQRMAAAALPIEVQKLRVPRLNDGARAALRVLVTARDMLAVERTKYVNALT FT ALLRVTSLGIDARKPLSSTQFLEVAGWRSREETIESQVARAEAVRLARRVGELDTHIKE FT NTTQMTELVKLSEGKELLELTGIGPVVAAVCVAAWSHQGRLRSEAAFASLAGVNPIPAS FT SGNTVRHRLNRRGDRRLNKALHTAAMVRMTHDEETRAYVVKRTAEGKTLKEIRRCIKRF FT LARRIYKILESAEVLPLTA" FT repeat_region complement(795597..795604) FT /rpt_type=DIRECT FT mobile_element complement(795605..797053) FT /mobile_element_type="insertion sequence:ISAar19" FT /rpt_family="ISL3" FT repeat_region complement(795605..795628) FT /rpt_type=INVERTED FT CDS complement(795611..796918) FT /transl_table=11 FT /locus_tag="AARI_34610" FT /product="transposase of ISAar19, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRG4" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VRG4" FT /protein_id="CBT74941.1" FT /translation="MLNPTFTAPDLTTFTNLDGLGLTAIGQHLSAAKAEILCHVTNPIP FT WCQTCGAAGIPRDTVTRRLAHEPLGWRPTVLVIKHRRYRCANCQRVWREELSQAVAPRQ FT KISRTGLRWALVGLVCHHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFDGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLIDMVPGRSKAVFKTWLADQEEQW FT KQGIEVVAMDGFTGFKTAAVEELPHAVEVLDPFHVVKLGSEALDQTRQRIQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKTKLEDLFKEPEYEPVQLVWSVYQKMVDAYRQPKP FT EVGRWALEQLINEVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRRRLHPQS" FT repeat_region complement(797030..797053) FT /rpt_type=INVERTED FT repeat_region complement(797054..797061) FT /rpt_type=DIRECT FT CDS 798815..799813 FT /transl_table=11 FT /locus_tag="AARI_07190" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="9 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR016196" FT /db_xref="UniProtKB/TrEMBL:E1VTI9" FT /protein_id="CBT74942.1" FT /translation="MVAALIVYLAFVSILPLLVDLAEEFYLNDLGQVDSTAAIRGNTMI FT AVGTIICGAVVGKSLGALTATQGIIIGVTVNIVLSICAVVLRTASRSQFEPEHEVENMS FT HKESLNAALRNHFFPTRAKVLVDGGILSPWVSGVATIASAVTGIYVLLWISGSGQAGPT FT RLSLLFVLVGSLSAVLPLISGRIMKGPSQRVMRYLRILSVLGILGYGSTLIVALLYSQL FT GIDRLWAAPGIIVATATGGAITFTVSTLRQMSLERARFKAMIGWVFSIAALCGLAASWV FT AYALNAVGNPVLVLVLATLSSTCLALIFSAGKLPAKPDEEAETMVDEERSN" FT CDS complement(799879..800661) FT /transl_table=11 FT /gene="sdhB" FT /locus_tag="AARI_07200" FT /product="succinate dehydrogenase iron-sulfur subunit" FT /function="2.1.3 TCA cycle" FT /EC_number="1.3.99.1" FT /note="the succinate dehydrogenase complex catalyses the FT interconversion of fumarate and succinate. It contains FT several subunits: a flavoprotein (SdhA), an iron-sulfur FT protein (SdhB), and membrane anchor proteins (SdhC and FT SdhD). Involved in the TCA cycle" FT /db_xref="GOA:E1VTJ0" FT /db_xref="InterPro:IPR001041" FT /db_xref="InterPro:IPR004489" FT /db_xref="InterPro:IPR009051" FT /db_xref="InterPro:IPR012285" FT /db_xref="InterPro:IPR012675" FT /db_xref="InterPro:IPR017896" FT /db_xref="InterPro:IPR017900" FT /db_xref="UniProtKB/TrEMBL:E1VTJ0" FT /protein_id="CBT74943.1" FT /translation="MSTELPEPPSKIDLKPGVGGGGEIPSFDITLRVRRYLPEATADAY FT WEDFKLTMYGTDRVLDALHKVKWEQDGTLSFRRSCAHGVCGSDAMRINGRNRLACKTLL FT KDLDTTKPITVEAIKGLPLEKDLIVDMEPFFQSYREIMPFLISKGHEPTKERYQSAEDR FT EIFDDTTKCILCAACTSSCPVFWTDGQYFGPAAIVNAHRFIFDSRDDAGDMRLEILNDK FT EGVWRCRTTFNCTEACPRGIQVTKAIAEVKQAILARTV" FT CDS complement(800661..802448) FT /transl_table=11 FT /gene="sdhA" FT /locus_tag="AARI_07210" FT /product="succinate dehydrogenase flavoprotein subunit" FT /function="2.1.3 TCA cycle" FT /EC_number="1.3.99.1" FT /note="the succinate dehydrogenase complex catalyses the FT interconversion of fumarate and succinate. It contains FT several subunits: a flavoprotein (SdhA), an iron-sulfur FT protein (SdhB), and membrane anchor proteins (SdhC and FT SdhD). Involved in the TCA cycle" FT /db_xref="GOA:E1VTJ1" FT /db_xref="InterPro:IPR003952" FT /db_xref="InterPro:IPR003953" FT /db_xref="InterPro:IPR004112" FT /db_xref="InterPro:IPR011281" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR014006" FT /db_xref="InterPro:IPR015939" FT /db_xref="UniProtKB/TrEMBL:E1VTJ1" FT /protein_id="CBT74944.1" FT /translation="MQVHKYDVVIVGAGGAGMRAAIESGQRARTAVLTKLYPTRSHTGA FT AQGGMCAALANVEEDNWEWHTFDTIKGGDYLVDQDAAEVMAKEAIDAVLDLEKMGLPFN FT RTPEGKIDQRRFGGHTRDHGKAAVRRACYAADRTGHMILQTLYQNCVKHNVEFYNEYYV FT LDLLMVEEDAYREDGTAYKQKRVAGVVSYDLATGELHVFQAKSVIFASGGAGKVFKTTS FT NAHTLTGDGMSIAFRSGLPLEDMEFFQFHPTGLAGLGILLTEGARGEGAILRNSDGERF FT MERYAPTIKDLAPRDIVARAMANEVREGRGCGPNKDYVLLDLTHLEPEHIESKLPDITE FT FARTYLGVEPFTDPVPVYPTAHYAMGGVPTNINTEVLQDNDTVIPGLFAAGEVACVSVH FT GSNRLGTNSLLDINVFGKRAGVAAAEYSKTADFVELPQNPEAFVTAQIEGVLSGNGTER FT VSDLRSTLQETMDANVQVFRDERSLKEARDVIEDLRIRYKNISIQDKGKRFNLDLLEAI FT ELGFLLDLAEVITVAALHRKESRGGHYREDFPDRDDENFMKHSMSYRDADAVTEDIKGI FT RMETKPVVFTRYQPMERKY" FT CDS complement(802506..802949) FT /transl_table=11 FT /gene="sdhD" FT /locus_tag="AARI_07220" FT /product="succinate dehydrogenase membrane subunit" FT /function="2.1.3 TCA cycle" FT /EC_number="1.3.99.1" FT /note="the succinate dehydrogenase complex catalyses the FT interconversion of fumarate and succinate. It contains FT several subunits: a flavoprotein (SdhA), an iron-sulfur FT protein (SdhB), and membrane anchor proteins (SdhC and FT SdhD). Involved in the TCA cycle" FT /db_xref="GOA:E1VTJ2" FT /db_xref="InterPro:IPR000701" FT /db_xref="UniProtKB/TrEMBL:E1VTJ2" FT /protein_id="CBT74945.1" FT /translation="MSVSIPAPRSQRIDPKYKRGPKSRGSFEMLAWLFMRLSGVVLVIL FT IFGHLFSNLMVGEGISGIGFGFVAGKWASPLWQFWDLAMLWLAMLHGTNGVRTIINDYA FT EKHATRAWLKGILYVATIFIIVLGSLVIFTFDPCVAGSTLPQC" FT CDS complement(802953..803333) FT /transl_table=11 FT /gene="sdhC" FT /locus_tag="AARI_07230" FT /product="succinate dehydrogenase membrane subunit" FT /function="2.1.3 TCA cycle" FT /EC_number="1.3.99.1" FT /note="the succinate dehydrogenase complex catalyses the FT interconversion of fumarate and succinate. It contains FT several subunits: a flavoprotein (SdhA), an iron-sulfur FT protein (SdhB), and membrane anchor proteins (SdhC and FT SdhD). Involved in the TCA cycle" FT /db_xref="GOA:E1VTJ3" FT /db_xref="InterPro:IPR000701" FT /db_xref="InterPro:IPR014314" FT /db_xref="UniProtKB/TrEMBL:E1VTJ3" FT /protein_id="CBT74946.1" FT /translation="MSKTSSGTLYRGHEGMWSWVGHRVTGVVIFLYLLVHVLDTAMVRV FT DAGAYDAIISTYQTPWMALGETGLVAAILFHAFNGLRLILVDFWKQGTKYQRQMLWGVL FT ILWVIVFAGFAIRHLSIAFGGH" FT CDS 803613..804728 FT /transl_table=11 FT /gene="manC" FT /locus_tag="AARI_07240" FT /product="putative mannose-1-phosphate guanylyltransferase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="2.7.7.13" FT /note="catalyses the following reaction: GDP + alpha-D- FT mannose 1-phosphate <=> phosphate + GDP-mannose. FT Participates in fructose and mannose metabolism" FT /db_xref="GOA:E1VTJ4" FT /db_xref="InterPro:IPR001538" FT /db_xref="InterPro:IPR005835" FT /db_xref="UniProtKB/TrEMBL:E1VTJ4" FT /protein_id="CBT74947.1" FT /translation="MNADLLARFHGVIPAGGVGTRLWPLSRASAPKFLHDLTGSGSTLI FT RATYDRLVPLAGERIMVVTGRAHRGAVVSQLPELCDEDLVLEPEPRDSAAAIGLAAAIL FT YRRDPSIIMGSFAADQVIEPVEVFQAALSEAIHTAATGKIVTIGIHPTHPSTGFGYIQT FT GQPLDVPNAPSARGVVQFVEKPDEDTARKYLASGGFLWNAGMFVAPVSLMLQHLEANEP FT ALYAGLMKIADAWETDQRETVMREVWADLPKIAIDYAVAEPAAEAGDVAVIPGVFNWDD FT VGDFAAIGRLNKASAEEGIINLGGESVRVYADSATGVVYSDRPRVVALVGIEDVVVVDT FT ADALLVTTKEHAQKVKQTVEALKADGATEVL" FT CDS 804878..807022 FT /transl_table=11 FT /gene="betT" FT /locus_tag="AARI_07250" FT /product="high-affinity choline transport protein" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="identified by similarity to protein SP:P0ABC9 FT (Escherichia coli). Betaine/carnitine/choline fransporter FT (BCCT) family, choline:H+ symporter (TC 2.A.15.3.1). FT Involved in the osmoregulatory choline-glycine betaine FT pathway (choline uptake)" FT /db_xref="GOA:E1VTJ5" FT /db_xref="InterPro:IPR000060" FT /db_xref="InterPro:IPR018093" FT /db_xref="UniProtKB/TrEMBL:E1VTJ5" FT /protein_id="CBT74948.1" FT /translation="MTTAKISSEPSESAKPAPPGSLPPPGKTRINKAVFYGSALLVLAI FT ALWAIIDRDSANLAISAAVTWIGRNFGWYYTLVVVAVLVFVIGVAISKVGKTRLGPDHS FT RPSFNIFTWAAMLFAAGIGIDLMFFSVAEPVTQYLAPPAMEGSTVEAARQALVWTLFHY FT GLLGWGLYALVGLALGYFAYRHNLPLSIRSALYPILGKRTEGWVGHSVDIAAMLGTIFG FT IATSLGIGVAQLNYGLNYMFGIPENRSWQIILIVAAVVMATISVLTGVEKGIRRLSELN FT VLLCVALMLFVLIAGSTAYLFDGIVNNIGDSLAMFPSMALDTFAYDRPDEWLNGWTLFF FT WAWWIAWAPFVGLFLARISRGRTIRQFVTGVLVVPFAFILLWISIFGNSALAIVRSGNQ FT AFGEVAMNTPERAFYSLLDQMPGAPITAAIATFTGLLFYVTSADSGALVMANFTSHLKD FT PQSDGSKPVRLFWSLATGLLTLGMLFVDGISTLQGATVIMGLPFSFVLLLIMLGLFKSL FT RMESALADRYRNNMHKVLTSRMGSGAEKRNWKQRLSRAMSYPGHRSAKRYLGQVALPAL FT QEVSEEFTARGATVALDIEQVANLELNSLDLVVENGAERPFKYQIYPVQLPVPTYARVS FT AGTDVYYRMEVFSQEGSHGYDLMGLTKEQLICDVLDQYEAHLEFLEAQTESAAPSQINS FT DGASKTDWESDFETTLKEEA" FT CDS 807019..808545 FT /transl_table=11 FT /gene="betB" FT /locus_tag="AARI_07260" FT /product="betaine-aldehyde dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.2.1.8" FT /note="involved in the synthesis of the osmoprotectant FT betaine" FT /db_xref="GOA:E1VTJ6" 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:E1VTJ6" FT /protein_id="CBT74949.1" FT /translation="MSSPSNQNPLLHHGATLFIDGAFTPAASGETRTINCPANGEAVAT FT VSEAGEADSIKAIEAARRSFDSGIWSSVPAAQRGDFLLKAAEQLVARKAEFALAETLDT FT GKRLVESELDMDDIISCFRYFGKLAGQEAGRVVDANDPNVISRIDYEPVGVAAMITPWN FT YPLLQAAWKIAPALAAGCSFVLKPAELTPSTAILMMEVLKDLGLPAGVANLVTGAGAQA FT GAVLSEHKDVDLVSFTGGLVTGRKVAAAAAGTVKKVALELGGKNPNVVFADADFDAALD FT NALNGAFVHSGQVCSAGARLVIHESIAEKFVDELVRRAQQITLGGPFDQKAETGALISA FT AHLEKVDAYVQAGIAEGARVRCGGRRATEQDGAGLGSGHFYLPTVIDQVTGSMSVAQDE FT AFGPTITVETFSTEDQAVAIANDTIYGLAGAVWSQDAGKAARVAKRLRHGTIWINDYHP FT YLPQAEWGGFGQSGVGRELGPTGLGEYQEAKHVYQNLNPQVTGWFAQKQS" FT CDS 808563..810134 FT /transl_table=11 FT /gene="codA" FT /locus_tag="AARI_07270" FT /product="choline oxidase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.1.3.17" FT /note="catalyzes the following reaction: choline + O2 <=> FT betaine aldehyde + H2O2. Involved in the synthesis of the FT osmoprotectant betaine" FT /db_xref="GOA:E1VTJ7" FT /db_xref="InterPro:IPR000172" FT /db_xref="InterPro:IPR007867" FT /db_xref="InterPro:IPR012132" FT /db_xref="UniProtKB/TrEMBL:E1VTJ7" FT /protein_id="CBT74950.1" FT /translation="MSMHKKDFDYIVIGGGSAGAAAASRLSEDPSVTVALVEAGPDDRG FT YDEVLQLDRWMELLESGLDWDYPIEEQENGNSFMRHARAKVMGGCSSHNSCIAFWAPRE FT DIDEWESKFGATGWNSQMAYRLYKKLETNEDAGPQAPHHGDSGPVKLMNVPANDPCGVA FT ILDAAEQAGIPRAKFNNDQTVVNGANFFQINRLPDGTRSSSSVSYIHPITGRENFFLLT FT GLQARKLNFDASKRCTGVDVVDGAFGRTSTLNAAREVVVSAGAIDSPKLLMLSGIGPAE FT HLEEVGVQVLVDSPGVGEHLQDHPEGVIQWEAKKPMVESSTQWWEIGIFTPTREGLDRP FT DLMMHYGQVPFDMHTLRQGYPTGENTFCLTPNVTHAKSRGTVRLRSCDFRDKPKVDPRY FT FTDPEGHDARVMTFGIRKAREIVAQSPMADWAGEEQFPGKDVQTDDQIFDYLRRTHNTV FT YHPAGSVRMGAEDDAMSPLDPQLRVKGVSGLRVADASVMPELVTVNPNITVMMIGERCA FT ELIQQD" FT CDS 810281..811477 FT /transl_table=11 FT /locus_tag="AARI_07280" FT /product="putative metal-dependent FT amidase/aminoacylase/carboxypeptidase" FT /function="3.10 Protein degradation" FT /db_xref="GOA:E1VTJ8" FT /db_xref="InterPro:IPR002933" FT /db_xref="InterPro:IPR011650" FT /db_xref="InterPro:IPR017439" FT /db_xref="UniProtKB/TrEMBL:E1VTJ8" FT /protein_id="CBT74951.1" FT /translation="MNENGNVASVAEVTEPLAEQLIGFRRELHRNPELSFAEHQTTERI FT LETLRAAGLSPQKMAETGAFVDIGQGPIRIAFRADIDALPVVEETNLEFASMTPGVAHA FT CGHDIHTTVMLGVALALGQLDAAGKLEGRVRVIFQPAEEKLPGGALSVIEQGLLDGVPR FT VLALHCDPRIDAGHIGTRIGAITSASDTIRIEVNGRGGHTSRPHLTEDIVFAMSQIATQ FT VPAVLGRKVDVRSAVSVVWGQIHAGSVPNAIPATGYLAGTMRCLDGDIWYEAGELLDSA FT VRQIAAPYGVEIKLQHTRGVPPVVNAPAETALIEDAARREFGAEAIELTPQSMGGEDFA FT WMTQKVSGAMLRLGTRTPGGKTYDLHRGDYIPDESCIGVGVRIMTAAALQAVSEANAK" FT CDS 811766..812854 FT /transl_table=11 FT /locus_tag="AARI_07290" FT /product="putative sugar ABC transporter, substrate-binding FT protein" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-2 (CUT2) family (TC 3.A.1. FT 2.z). ABCISSE: ABCISSE: ABC transporter, binding protein FT (BP), MOS-family (monosaccharides: pentoses and hexoses)" FT /db_xref="GOA:E1VTJ9" FT /db_xref="InterPro:IPR003760" FT /db_xref="UniProtKB/TrEMBL:E1VTJ9" FT /protein_id="CBT74952.1" FT /translation="MRFVSRKTGVAAAMLGISALALSACGAAPEESSSDGQFKDFVGCI FT VSDSGGFDDQSFNESSHRGLMNAKEDLGIQVKTAESKSNADFTTNLNGMVTAGCDLTVT FT IGFLLGDATAEAAAANPDKNFAIVDFQYEKPIENVKPIIYDTAQAAYLAGYAAAAASKT FT GTVATFGGIQIPTVTIFMDGFADGVDKFNEDKGKDVKLLGWNKDKQNGTFSGDFEKQDK FT GKQITKNFIASGADVIMPVAGPVGKGAGAAVVEANKSGKEAKLVWVDSDGFLTAPDYKD FT VMLTSVIKTMDTAVEDVLRTDAEGNFDSTPYVGTLENEGVALAPFHNFDEEIGEETKSE FT IEALKQQIVSGELKIDSASSPK" FT CDS 812992..814590 FT /transl_table=11 FT /locus_tag="AARI_07300" FT /product="putative sugar ABC transporter, ATP-binding FT subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-2 (CUT2) family (TC 3.A.1. FT 2.z). ABCISSE: ABCISSE: ABC transporter, fused ATP- binding FT protein (ABC2), MOS-family (monosaccharides: pentoses and FT hexoses)" FT /db_xref="GOA:E1VTK0" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VTK0" FT /protein_id="CBT74953.1" FT /translation="MKLELRGISKAFGSFYANKDIDLVVDDAQIHCLLGENGAGKSTLM FT NVLYGLYQPTEGQILLDGKPVEFSGPGDAMAAGIGMVHQHFMLVPVFTVAENIALGAET FT TKAGGMLDLQVTRKKIREISDRYGFDVDPDAVVEDLPVGVQQRVEIIKALVRDARILIL FT DEPTAVLTPQETDELLDIMRQLKANGTSIVFISHKLREVRAVSDVITVIRRGEVIDSVS FT PESSTTELANLMVGRAVELNLHKEAATPGAAALEVSNLSVVNAAGSTTLDSVSFTIHEG FT EILAVAGVQGNGQTELTEAILGTQPVTGGSVKLAGKELVGKSVKQILRSGLGFVPEDRS FT VHGLVTQFSIEENLVLDLYDRPPFGKGISMNLAAIKKNATQQIEGFDVRTDNPLNPASS FT LSGGNQQKVVMARELSRDLKLFIASQPTRGVDVGSIEFLHRRIVAERDKGTPVMIVSTE FT LDEVMELADRIAVLYKGKINGIVPGDTSREVLGLMMAGVSQEEALAQADFTKADNEPVE FT AKPVSEQDNQEGEAQ" FT CDS 814587..815792 FT /transl_table=11 FT /locus_tag="AARI_07310" FT /product="putative sugar ABC transporter, inner membrane FT subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-2 (CUT2) family (TC 3.A.1. FT 2.z). ABCISSE: ABCISSE: ABC transporter, permease (IM), FT MOS-family (monosaccharides: pentoses and hexoses)" FT /db_xref="GOA:E1VTK1" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:E1VTK1" FT /protein_id="CBT74954.1" FT /translation="MSEKAPVVPESGKQGNDLLRQITQGPGLVSILGVIVALVIGGLLI FT AVTDEKVGETAGYLFAQPSAFFSEFWRAATESYVALFNGSIYNSSQGFKPFLETLTVST FT PLICAGLGVAVAFRAGLFNIGAQGQIIIGSVLAAYIGFAWHLPLVLHLLLVIVFGLLGG FT AIWGGLVGLLKAKTGAHEVILTIMFNYVAVYLIEFLMNTQAFRRPGETNPISPILDPSA FT VFPAIPGSRLHLGFVMAVLLVILISWMFKRSTVGFEFRAVGHNPEAAQTAGINVARTTI FT LAMALAGALAGAAGVAQVAGTEKVLTAGIAGSLGFDAITVALLGRSTPWGTFFAGLLFG FT AFQAGAVNMQITTGTPIDIVSVVQSLIVLFIAAPPLVKALFGMNRKKKRSSKLEPTKAG FT AK" FT CDS 815789..817060 FT /transl_table=11 FT /locus_tag="AARI_07320" FT /product="putative sugar ABC transporter, inner membrane FT subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-2 (CUT2) family (TC 3.A.1. FT 2.z). ABCISSE: ABCISSE: ABC transporter, permease (IM), FT MOS-family (monosaccharides: pentoses and hexoses)" FT /db_xref="GOA:E1VTK2" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:E1VTK2" FT /protein_id="CBT74955.1" FT /translation="MTTSTLQPAINVLPSKKTPIILSMIAVIVFFSFGLLGNDQSAHFT FT LDSAGDAFTLPELVFPGRITNIVFGVLLLALAAYSWMQRKQGKMLATWMVAVAAVLFVL FT GFLIWVVSGANINSISLASLLAGGVVLAVPLVFGSLSGVLCERAGVVNIAIEGQLLGGA FT FTAALVASLTKNAFAGLIAAGLAGALVSLVLAIFSIKYLVNQIIVGVVLNVLVSGITGF FT LFTTVMQEDPERFNSPAHLPVIDIPLLSSIPVIGPILFKQSVIGYLMYLAVFLVWFGLF FT KTKWGLRVRAVGEHPKAADTLGIKVNSIRFWNVTLGGIVAGIGGSFFTLVAIDSFTKEI FT SGGRGFIALAAVIFGRWNPIGAFLAALLFGFADNLQVILTIIGTPVPSQFMAMMPYLVT FT IFAVAGLVGRSRGPAAAGEPYVKE" FT CDS 817070..817480 FT /transl_table=11 FT /gene="cdd" FT /locus_tag="AARI_07330" FT /product="cytidine deaminase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.5.4.5" FT /note="catalyzes the hydrolysis of cytidine into uridine FT and ammonia" FT /db_xref="GOA:E1VTK3" FT /db_xref="InterPro:IPR002125" FT /db_xref="InterPro:IPR006262" FT /db_xref="InterPro:IPR016192" FT /db_xref="InterPro:IPR016193" FT /db_xref="UniProtKB/TrEMBL:E1VTK3" FT /protein_id="CBT74956.1" FT /translation="MNANNAPWPQLEAAAAAALSQAYAPYSNFRVGSAALTSDGRLISG FT CNVENAAYGVTLCAECAMIGQLFATGGGTLEHFVCFGQLEDGAMELITPCGRCRQLLFE FT HRGAALQIKTARGIVGINDLLPDAFGPQNLNA" FT CDS 817524..818837 FT /transl_table=11 FT /gene="deoA" FT /locus_tag="AARI_07340" FT /product="thymidine phosphorylase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.4.2.4" FT /note="catalyzes the reversible phosphorolysis of FT thymidine, deoxyuridine and their analogues to their FT respective bases and 2-deoxyribose 1-phosphate. This enzyme FT regulates the availability of thymidine and is therefore FT essential to nucleic acid metabolism" FT /db_xref="GOA:E1VTK4" FT /db_xref="InterPro:IPR000053" FT /db_xref="InterPro:IPR000312" FT /db_xref="InterPro:IPR013102" FT /db_xref="InterPro:IPR017459" FT /db_xref="InterPro:IPR017872" FT /db_xref="InterPro:IPR018090" FT /db_xref="InterPro:IPR020072" FT /db_xref="UniProtKB/TrEMBL:E1VTK4" FT /protein_id="CBT74957.1" FT /translation="MATEQFSAVEVIRAKRDGQVLGNEMIDWTIDAYTRGAIAEEQMSA FT LNMAIYFQGMNRSEISRWTNAMINSGERMDFSTLADPSGKHLATTDKHSTGGVGDKITL FT PLAPLVASFGVAVPQLSGRGLGHTGGTLDKLEAIPGWKAELSNEALFDQLSTVGAVICA FT AGTGLAPADKKLYALRDVTATVEAIPLIASSIMSKKIAEGTGTLVLDVKVGSGAFMKDE FT AMSRELAETMVNLGTDAGVNTVALLTNMETPLGLTAGNAIEVEESVEVLAGGGPQDVIE FT LTVALATEMLAGAGIKDVDVAGALKNGQAMDVWRKMIAAQGGDPDAKLPVAKESHTVVA FT PAEGVLLKLDAMDIGLAAWTLGAGRARKEDSVQAGAGVRMHVKPGALVRRGEPIATLLT FT DTPEKMERAIELVQRAIMVGSADDRPDTRLILDRIAAK" FT CDS 819121..819795 FT /transl_table=11 FT /locus_tag="AARI_07350" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR015414" FT /db_xref="UniProtKB/TrEMBL:E1VTK5" FT /protein_id="CBT74958.1" FT /translation="MELVNEAITQAASAWWILPLLFLFCMIDAIFPVVPSESFLVSLAA FT VGVHTGVPNLVLIGLLGAGGALLGDQITFAIGRKIGSRGFKWMRGKRAQRVLKYAEKKL FT ATSGALLIFTARYIPIGRVAVNLTAGATGFSHKRFTIFDTIGVLTWAAYSISIGAMAGN FT WMHDNKLLGIIVSIVIAVVLGFIIDRIVSWVLGRMHRHADARKEHTGELLRQTVPPAPQ FT ER" FT CDS 819887..821080 FT /transl_table=11 FT /gene="add" FT /locus_tag="AARI_07360" FT /product="adenosine deaminase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.5.4.4" FT /note="catalyzes the irreversible hydrolytic deamination of FT adenosine to ammonia and inosine, or of desoxyadenosine to FT ammonia and desoxyinosine" FT /db_xref="GOA:E1VTK6" FT /db_xref="InterPro:IPR001365" FT /db_xref="InterPro:IPR006330" FT /db_xref="UniProtKB/TrEMBL:E1VTK6" FT /protein_id="CBT74959.1" FT /translation="MTEEMIHTAYDPEFDFRDLPKVSLHDHLDGGLRPQTIIDLAAEIG FT HELPETEAEALGEWFRESADSGSLTRYLETFEHTVAVMQTRDALIRVAREFVEDLAEDG FT VIYGEVRYAPEQHRREGLSLDDVVDAIQEGLDQACEKLNAEGHPMQIGQIVSAMRHSDQ FT SVEIAKLALRHRGRGVVGFDIAGAEDGFPPSKMKEAFDLLAENLFPTTVHAGEAAGLES FT IKEAILIGRAQRLGHGVRVAEDIEIEFGAIDENGEELSDDTGLVSLGPVANWVRERGIP FT LEVCPSSNLQTGATAKFGEGITNHPIDLLVQTGFNVTISPDNRLMSQTTISDEFELLVE FT AFDYDLEDLLDLTLNAAEAAFVPLEMRELLVEYINDYYDNLLDDEDYDEDEYENVAD" FT CDS complement(821165..822655) FT /transl_table=11 FT /locus_tag="AARI_07370" FT /product="aldehyde dehydrogenase family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /EC_number="1.2.1.-" FT /note="identified by match to protein family PF00171" FT /db_xref="GOA:E1VTK7" 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:E1VTK7" FT /protein_id="CBT74960.1" FT /translation="MTVQSTAKLRFLEQLPATLFIGGQWVEGRSDATLRTTNPFDDSLL FT AEIRQASTEDVDAAYQAAATSQPGWASFSPAKRSKVLNQAADYLQGNFDGILALLIAES FT GSTHLKANIELGGTIAAIREAATFPTRVHGKILPSNAEGKENRVYREPVGVVAVISPWN FT FPMLLSARSVAPALALGNAVVLKPASDTPLVGALVLAKAFAEAGLPEGVLNALVGSGSE FT IGDYFVAHQTPSLVSFTGSTPVGKNVGKIAVSGEHMKRVALELGGNAPFVVLEDADLEE FT AAKAATLGKFLHQGQICMAINRIIVQAPVYEEFIEKFIEQVNKLGYGDAADPANLVGPI FT INDTQLESVSTKIKTARSQGAREVLAGSINGRVVSPHVFADVTSQMELFREEIFGPVVG FT IAKAESQAHALELANDTEFGLSSAVFTQNLEKGVAFARGIKAGMTHINDITVNDEPHVM FT FGGEKNSGLGRFNGEWAIEEFTTDHWIGVQSTKKQYPF" FT CDS 822766..823464 FT /transl_table=11 FT /locus_tag="AARI_07380" FT /product="MazG nucleotide pyrophosphohydrolase FT domain-containing protein" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /note="match to protein domain PF03819. In Escherichia FT coli, MazG was characterized as a nucleoside triphosphate FT pyrophosphohydrolase which can hydrolyze all eight of the FT canonical ribo- and deoxynucleoside triphosphates to their FT respective monophosphates and PPi, with a preference for FT deoxynucleotides" FT /db_xref="GOA:E1VTK9" FT /db_xref="InterPro:IPR004518" FT /db_xref="UniProtKB/TrEMBL:E1VTK9" FT /protein_id="CBT74961.1" FT /translation="MHENRTQLEQLNATVRTLRSKCAWTNALTHESLRTYLIEESYEVL FT DAIAEQNPSLLKEELGDLYFQILLHSLIAEEHGQFGLDDVAETLNAKLLRRNRHIFDEQ FT GQVRQEIITDVDEIIRVWDAAKQAERAGQPRKRKNAGLPAGLPALALAQKLLDRHARAG FT SEQAATGLVSQQVRERVTDERSLAAELTALSARAEELGLDAESVLRAALGQQYGAETDA FT TTSRKSPLKR" FT CDS 823557..824837 FT /transl_table=11 FT /gene="eno" FT /locus_tag="AARI_07390" FT /product="enolase" FT /function="2.1.2 Main glycolytic pathways" FT /EC_number="4.2.1.11" FT /note="other names: 2-phosphoglycerate dehydratase, 2- FT phospho-D-glycerate hydro-lyase. Catalyzes the reversible FT conversion of 2-phosphoglycerate into phosphoenolpyruvate" FT /db_xref="GOA:E1VTK8" FT /db_xref="InterPro:IPR000941" FT /db_xref="InterPro:IPR020809" FT /db_xref="InterPro:IPR020810" FT /db_xref="InterPro:IPR020811" FT /db_xref="UniProtKB/TrEMBL:E1VTK8" FT /protein_id="CBT74962.1" FT /translation="MALIDAIHAREILDSRGNPTVEVEVLLSDGSHGRAAVPSGASTGA FT FEAAERRDGDQDRYLGKGVLGAVESVIEEIADELEGLDATDQRAIDAAMIELDGTANKS FT KLGANAILGVSLAVANAAAVSANLPLYKYLGGPNAHVLPVPLMNILNGGSHADSDVDIQ FT EFMIAPIGAPSFSEGLRWGVEVYHNLKSVLKEKNLSTGLGDEGGFAPNLPSNRAALELI FT TEAIKRAGYTPGEDIALALDVASSEFYENGAYQFEGKALSAQEMSDYYAGLVADFPLVS FT IEDPLDEDDWDGWKTLTDAIGDKVQLVGDDLFVTNPQRLADGIAKGTANSLLVKVNQIG FT TLTETIDAVTMAQRAGYTTITSHRSGETEDVTIADICVATNAGQIKTGAPARSERVAKY FT NQLLRIEEDLGASALYAGRSAFPRFNS" FT CDS 824962..825801 FT /transl_table=11 FT /locus_tag="AARI_07400" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="GOA:E1VTL0" FT /db_xref="InterPro:IPR007060" FT /db_xref="UniProtKB/TrEMBL:E1VTL0" FT /protein_id="CBT74963.1" FT /translation="MAQRPPRMPRRNTPDPAEQSAVTPVDQAKPVNAGNEAEPATDALH FT IVDPQKPVKKAPRTARPETPAAGAPKPRSASVKPKTTTRSTSDASRGPKKFEGNYTQKP FT KAPLRERAKEKQNERRRDDRVKFSAAVRRKPGQKPVDNKQVPEGEPIAAHRFSGRIAAL FT IVVLAFFAVMLVPTVNFYRTQMAELNELHASIEALETQRDELKAEIARWDDPLYIKQQA FT RERINLVMPGEKLYMVVGERPQDEETSTEGNGSTFEVRQELPWVDALLDSVRRSATD" FT CDS 825831..826532 FT /transl_table=11 FT /locus_tag="AARI_07410" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007511" FT /db_xref="UniProtKB/TrEMBL:E1VTL1" FT /protein_id="CBT74964.1" FT /translation="MTEQPIREALDAAGRVPSEADLDTLSRQLNRPVRDVVEIGARCVC FT GNPLVATTAPRLSSGIPFPTTYYLAHPVITAAVSRLEAAGLMNEMNENLGEDPQLAQAY FT VAAHESFLANRDAIGARSGTGAVPEIAGVSAGGMPTRVKCLHVLVGHSLAAGEGVNPLG FT DQALEAISQWWTKDKCYCVGAWDTESAAPSRDRSRHVKTQEMQDPAAKRADRARKRAQR FT EAAQGSDQDDA" FT CDS 826532..827458 FT /transl_table=11 FT /locus_tag="AARI_07420" FT /product="Ppx/GppA phosphatase family protein" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.6.1.-" FT /note="identified by match to protein family PF02541. FT Similar to exopolyphosphatase (Ppx, EC 3.6.1.11) and FT guanosine pentaphosphate phospho-hydrolase (GppA, EC 3.6.1. FT 40) proteins" FT /db_xref="GOA:E1VTL2" FT /db_xref="InterPro:IPR003695" FT /db_xref="UniProtKB/TrEMBL:E1VTL2" FT /protein_id="CBT74965.1" FT /translation="MRVAGIDCGTNSIRLLIADVDAEGQLVDVLRTMRIVRLGQGVDAT FT GAFAPEALERTFAATREYKKLCDEHQVQAIRFAATSAARDASNRELFSAQITKILGVAP FT EVISGEEEASLSFTGAASVRAGQSGKSLVIDLGGGSTEFVLGDETGPLAAKSLDMGCVR FT VTERFHQAGLRSDAALDFMDSTLETLTGAVDVSQVDAVIMVAGTFTTLTAQALGLKAYE FT SEKIHGAQLSFAQMRQATDSMLSYTREERASLGFMHPGRVDVIQAGAAIVQRILHYLEK FT TSANREMLLIASEHDILDGIAASAAVA" FT CDS 827493..828998 FT /transl_table=11 FT /locus_tag="AARI_07430" FT /product="membrane-associated subtilase family protease" FT /function="3.10 Protein degradation" FT /EC_number="3.4.21.-" FT /note="identified by match to PF00082. Subtilases are a FT family of serine proteases. The vast majority of the family FT are endopeptidases. Signal peptide predicted by SignalP 3.0 FT HMM (probability: 1.000) with cleavage site probability FT 0.974 between position 38 and 39. 1 transmembrane helice FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="GOA:E1VTL3" FT /db_xref="InterPro:IPR000209" FT /db_xref="InterPro:IPR015500" FT /db_xref="InterPro:IPR023827" FT /db_xref="InterPro:IPR023828" FT /db_xref="UniProtKB/TrEMBL:E1VTL3" FT /protein_id="CBT74966.1" FT /translation="MSSALRARKKTSIFKFSTVLVVALLAFTSLSIGAPAHADNMRESE FT YWLDSLGVTEAHKTTKGEGVKVAIIDTGIDTSHPDLKGAIVGGTDMSGSGGEKGNKPIG FT VMSEHGTLVATLLAGRGNNKSEINRVKSENERLKTAWEKAKKTAEDDDKDIPEEPEYEK FT VPKLTRGSDGVLGVAPAADLLSVSLWMGEGNPSKIPVETQIPRAVKWAVDSGAKVINMS FT LGSTSPAWPESWDDAFKYAEDHDVVIVAAAGNRSGGMSQVGAPATIPGVLTVAGVDASG FT KASQDSSTEGISIGVAAPAEQLVGGLPGDGYARWSGTSGAAPLVAGVAALIRSEYPDMK FT APEVINRILKTAKDTGAAGVDNLYGYGIIDANAALTAKVPAVTKNPLGTIEEWIRVHRR FT NTVSQTETPAPGVSMEKSDLKQVAAPKPVLPDGKAPVLQPVLIIGGGVLLLLVLVAGGT FT QTMVRRRRERATENLASASLSSLEVPKQAEGRDLFDEIPEEEK" FT CDS 829189..830556 FT /transl_table=11 FT /gene="ndh" FT /locus_tag="AARI_07440" FT /product="putative NADH dehydrogenase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="1.6.99.3" FT /note="NADH dehydrogenase catalyzes the following reaction: FT NADH + acceptor <=> NAD(+) + reduced acceptor" FT /db_xref="GOA:E1VTL4" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:E1VTL4" FT /protein_id="CBT74967.1" FT /translation="MSIIESSQKRPRILIVGGGYVGLYVAMKLQKKVKAHGGIVTVVDP FT NPYMTYQPFLPEVAGGQIEPRHVVVSHRQHLKHSELVNGSVLSIDHASKKAVIAPVNGE FT QFELEYTDIVMSAGAITRTFPITGLAETGIGLKTIEEAVALRNKVAERIESASNMTDPV FT ARKRALTFVVVGGGFAGIETIAELEDMARHLIELNDRIDAKEARFVLVEAMGRIMPEVT FT AEQAEWVVEHLRSRGIEVLLNTSLNSAEEGNLELINMADKSPAGSFGADTLIWCAGVMA FT NPMVRSTDFPIEQRGRIETRTDLRIKDANGDPLEGAWAAGDISAVKDVTGGLPDGTCVP FT NAQHAVRQAKLLAKNLYAARYGVGTIKEYKHSNLGAVAGFGRNKGVAKVMGLKLKGWPA FT WMAHRGYHGMAMPTFERKFRVVGDWLVALFFKRDALQLNNLEAPRTAFEESAKPKK" FT tRNA 830672..830753 FT /locus_tag="AARI_36640" FT /product="transfer RNA-Leu" FT /anticodon=(pos:830706..830708,aa:Leu) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 831054..831860 FT /transl_table=11 FT /locus_tag="AARI_07450" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR010539" FT /db_xref="UniProtKB/TrEMBL:E1VTL5" FT /protein_id="CBT74968.1" FT /translation="MGNPIFGSSSRSDAWGTKPGSPVGFRDTANMSADQLQQMYQQPTA FT TSADTGRMTIGGTINKTAICLALVVIGAAIGWTIPALMLPGALVGFVLGLVNAFKKRPS FT PVLILLYAAAQGLFLGGLSGFLESQPNLKGIAVQAVLATLCVAGVTLALYRSGKYRMTP FT KLNKMFMIGMIGLIAFSLLNMVLMLTGVIDGMFGMRGGVLGLVIGVVAVLLATYALVAD FT FTMIEELSNQGAPAIMAWRGAFGLTMTLIWLYTEILRILAILRGDE" FT CDS 832073..833512 FT /transl_table=11 FT /locus_tag="AARI_07460" FT /product="putative amino acid transporter" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="amino acid-polyamine-organocation (APC) superfamily FT (TC 2.A.3.y.z)" FT /db_xref="GOA:E1VTL6" FT /db_xref="InterPro:IPR002293" FT /db_xref="InterPro:IPR004841" FT /db_xref="UniProtKB/TrEMBL:E1VTL6" FT /protein_id="CBT74969.1" FT /translation="MSIDESTGKSPGLVKSLGNLDALALGFGAMIGFGWVVLTGGWLSN FT AGTMGAMLAMLVGGGIMAVVGLTYAELTAAMPKAGGEHNFILRALGARPSFIGSWAITG FT GYVTIVAFEAVALPRTVEYIFPGMSQIPLWTVAGFEVNLTWALVGVLAAVLITWINIRG FT VKQAGVLQTFVVLFLLAIGALLIFGSFSGGEVQNMQPLFTPGISGFFAVLVAVPFLFIG FT FDVIPQSAEEVNIPAKQIGKLVVVSVIMATLWYVMVVLTTASAMPAGELAGADIATADA FT FGAMFNSDLMAKVLIAGGIAGILTSWNSLLLGASRLVYSLARSGMLPSWFGQLHPKYST FT PANALLFIGGISVLAPFFGAEMLGWLVDSGAPSIIVAYFLVSVTFLVLRKREPQMDRPL FT RVGGNNNGGVIIGWVSVLLTAALFSLYMPGMPASLSWEPWAIFGVWWLLGAAFYFKVPA FT GIKPGEDAEHRVLEVVRRRRK" FT CDS 833692..835023 FT /transl_table=11 FT /locus_tag="AARI_07470" FT /product="putative permease" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="match to protein family PF01594" FT /db_xref="InterPro:IPR002549" FT /db_xref="UniProtKB/TrEMBL:E1VTL7" FT /protein_id="CBT74970.1" FT /translation="MKSSRFDRLRRLRVSLPSKPANALDVPRADSTDFQSAEDMPYAVR FT MAAAWAWRFLIVVAALGVLVWALSKISLLVIPVLVSALLAGLLSPVVNAMNSRLAVPRG FT LAVGITLIGFFALVTAGLSLAGQRLTAGFNALWTQALAGIEQVQNWLFNGPLKLTNDDL FT QSVLDDTLAQLRGNATNILSEAISWTSAIGQILTGTLLAIFALIFLLLDGRKIGLFLIN FT LLPRRARPAMDGALTRGWASLVSYVRVQMVVAMIDAIGIGLGAFFLGVPLAMPLGVLVF FT IGSFIPIVGALITGALAVLLALVANGWINALIMLAVVLLVQQAESNILQPLIMGKAVSL FT HPLAVVLAVAGGTMLAGIPGALFAVPLLAVLNAVIRYLSHRSWETDAHVIKLYGEQIIK FT AGSAKNPPVKNPAPAVPPADIASPAATPQTSPELRHPETKADEE" FT CDS 835027..836298 FT /transl_table=11 FT /gene="ilvA" FT /locus_tag="AARI_07480" FT /product="threonine ammonia-lyase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.3.1.19" FT /note="catalyzes the conversion of threonine into 2- FT oxobutanoate. Involved in isoleucine biosynthesis. The FT enzyme from a number of sources also acts on L-serine" FT /db_xref="GOA:E1VTL8" FT /db_xref="InterPro:IPR001926" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR005789" FT /db_xref="UniProtKB/TrEMBL:E1VTL8" FT /protein_id="CBT74971.1" FT /translation="MSTETTLPVTLADIEAAAKVLKPVIARTPVEHSRVLSQHLGSEVF FT LKCENMQRAGSFKVRGAYVRMSKLSDEEKARGVVAASAGNHAQGVAQAASHLGIKARIY FT MPRGVALPKLTATRDHGAEVVLFGDTVDEALAEAQRFADESGAVFVHPFDHPDIIAGQG FT TIGLELLEQLPEVDTVLMGVGGGGLLAGVAIALKEKARELGREIKVVGVQAENAAAYPP FT SLAADALVPLDTVHTIADGIAVGKPGQLPFAIIKELVDDVVTVSEDALARALVVLLERN FT KLVVEPAGAVGVAALLENRLEEHGINPATTAVILSGGNIDPLLMLKVIQRGLAAAGRFL FT TVRMMLPDRPGALAQISSIIAESDANVTRLDHTRIGGSLSMGDVAITIDLETKGHEHSK FT QVLNNLRAEGFDPQITNNAGGSVA" FT CDS complement(836371..836868) FT /transl_table=11 FT /gene="greA" FT /locus_tag="AARI_07490" FT /product="transcription elongation factor GreA" FT /function="3.5.3 Transcription elongation" FT /note="necessary for efficient RNA polymerase transcription FT elongation past template-encoded arresting sites" FT /db_xref="GOA:E1VTL9" FT /db_xref="InterPro:IPR001437" FT /db_xref="InterPro:IPR018151" FT /db_xref="InterPro:IPR022691" FT /db_xref="InterPro:IPR023459" FT /db_xref="UniProtKB/TrEMBL:E1VTL9" FT /protein_id="CBT74972.1" FT /translation="MSTNSNEPVVWLTQEAYDRLQDELTFLSGPGRAEIVARIEQARSE FT GDLKENGGYHAAREEQGKAEARILYLKDLLRRADVGDAPADDGIVEPGMLVVANIAGDE FT TTFLFGSREVAGDTDLEVYSEQSPIGVAVHGAKVGDKLSYLAPNGRDIKVEIISAKPYE FT AK" FT CDS complement(837158..837634) FT /transl_table=11 FT /locus_tag="AARI_07500" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTM0" FT /protein_id="CBT74973.1" FT /translation="MFGISSSNAARQESGARQIMSDPSLTARYNNPKKRNLSKKSRNWL FT IAAALSLGVAGAAYIGFSNYSSIGSQDLEFEVISATQAKAVVAVEYNTKLRVQCDIRAM FT NESKAIVGYKTVLLDPGEATGHITQILEIDLHTDNLATTAGVEDCYEVPQEYKG" FT CDS 837768..838685 FT /transl_table=11 FT /locus_tag="AARI_07510" FT /product="LmbE-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF02585. Members of this FT family have been characterised as a probable N- FT acetylglucosaminyl-phosphatidylinositol de-N-acetylase (EC FT 3.5.1.89) that catalyses the second step in FT glycosylphosphatidylinositol biosynthesis in eukaryotes" FT /db_xref="InterPro:IPR003737" FT /db_xref="InterPro:IPR017811" FT /db_xref="InterPro:IPR024078" FT /db_xref="UniProtKB/TrEMBL:E1VTM1" FT /protein_id="CBT74974.1" FT /translation="MEIHDVKKIAPSQGLRLMAIHAHPDDESSKGAATMAAYVDAGAEV FT MVVSCTGGERGDILNAAAGELAHAHRDLAGVRRTEMAEAAAVLGVKHRWLGYVDSGLPE FT GDPLPELPFGAFALQPVEIAAAGIIKLIREFRPHVITTYDENGGYPHPDHIHCHKVSTF FT AFEHAANPEMYPELGAPWSVSKLYYDRAFAPDRFRTLHYAMLEAGYESPYTERVAMWEE FT DQDNQMFKWVSPHTTTTQIDCADFFSQRDQALLAHRTQIDPEGFFFAVPEHVYAEHWPW FT EDYTLISSKVSTELPETDLFAGLR" FT CDS 838729..839010 FT /transl_table=11 FT /locus_tag="AARI_07520" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTM2" FT /protein_id="CBT74975.1" FT /translation="MNTIFESLALTSSTLGVGTETSSEYGPGFLGFIFTAAMVVAVIFL FT IRDMVRRVRRVRYTSEAESKQQGLVDKGEARNLQEPDAPHDPKTDEQQ" FT CDS 839043..841157 FT /transl_table=11 FT /locus_tag="AARI_07530" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VTM3" FT /db_xref="InterPro:IPR004879" FT /db_xref="InterPro:IPR008928" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR012341" FT /db_xref="InterPro:IPR024705" FT /db_xref="UniProtKB/TrEMBL:E1VTM3" FT /protein_id="CBT74976.1" FT /translation="MAQRLAGSSSQYLRQHSHQLVDWFPYGDEAFEQARLRDVPVMLSI FT GYAACHWCHVMSHESFDDSEIAALLNENFVAIKVDREEHPLVDDTYMLATQALTGAGGW FT PMTIFTLPDGRTVHAGTYYPKEPRGKTPSFRQVLNAVHEAWETKRAGLVEQAQMLAEHL FT AELGSRQSALLSLQSQQPADQAFSTALDRWMAAGKPEGGFTPAPKFPPTWALKTLSRAV FT ITEPQRAEEAFEAAATHLEAIFLGGLQDHVDGGFARYCVDANWSVPHFEKMLYDNAGLL FT SLAARTSVLAAEMALKGQGDTAQRAQKLAGLAQRSAQGIITFLEEELLTNSSSTPALAA FT SLDADSSRDGHQVEGAYYTLNREEIAQVTDPLIQRLPKGLLRFGPVAEDPQNFCFSLLR FT TPEASELEVLQELREQMRTLRRSRIMPIRDEKVIAGWNGLAIEALCEAALLLEAPDALK FT LAAQAAESVWQMQWDQQNKRLARVSFAGAATHANEGTLQDYSALALGFLALHQATGQQQ FT WAQRAKDLLGRAADFVDPESGVPRDTVQSDARITAQRSSIAAVTVLDDAMPASGALYAK FT ALAVQALQSMAAGEYTDADAAALESARGLSAHALALASEAPTQVATALEVQCIISSPVH FT YLAISQWDSDQAKRVRSVAMSLGINVRHDPSLPHADQGLQIQPCREELCQIPVLGIEGL FT FSLFSAPKNA" FT CDS 841275..842036 FT /transl_table=11 FT /gene="uppS1" FT /locus_tag="AARI_07540" FT /product="di-trans,poly-cis-decaprenylcistransferase" FT /function="1.1 Cell wall" FT /EC_number="2.5.1.31" FT /note="generates undecaprenyl pyrophosphate (UPP) from FT isopentenyl pyrophosphate (IPP). UPP is the precursor of FT glycosyl carrier lipid in the biosynthesis of bacterial FT cell wall polysaccharide components such as peptidoglycan FT and lipopolysaccharide" FT /db_xref="GOA:E1VTM4" FT /db_xref="InterPro:IPR001441" FT /db_xref="InterPro:IPR018520" FT /db_xref="UniProtKB/TrEMBL:E1VTM4" FT /protein_id="CBT74977.1" FT /translation="MQLPNLAYRYYERRLAKSLPADKLPHHIGVMVDGNRRWAKLAGTP FT TMAGHQAGADKILEFLDWCEDLNIQMVTLYMLSTDNLNREASELRDLLEVIGSTLDRLG FT ETNRVKVQQVGAKDLLPEDLAQKLAALETITANRDGVHVNVAIGYGGRREILDAFKALL FT CDAAKDGRTLEELASSLSTDDIESALYTKGQPDPDLVIRTSGEQRLSGFLTWQSAYSEF FT YFCEALWPDFRRVDFLRALRDFADRQRRFGT" FT CDS 842293..843609 FT /transl_table=11 FT /locus_tag="AARI_07550" FT /product="PhoH-like protein" FT /function="1.3 Sensors (signal transduction)" FT /note="identified by match to protein family PF02562: PhoH, FT PhoH-like protein. PhoH is a cytoplasmic protein and FT predicted ATPase that is induced by phosphate starvation" FT /db_xref="GOA:E1VTM5" FT /db_xref="InterPro:IPR003714" FT /db_xref="InterPro:IPR006596" FT /db_xref="UniProtKB/TrEMBL:E1VTM5" FT /protein_id="CBT74978.1" FT /translation="MNRTAEQGVRTYVIDTSVLLSDPKAMFRFDEHHVVIPLTVVIELE FT NKRKDPDLGFFARQALRLLDDLIASHGGLAQAVPVSKTGGTLRIELNNIAPDVLPVGMR FT SGDNDARILAVAKHLLDEGLDVALVTKDLPMRIKASAMGIHAEVYRNDQIASTGWSGIQ FT GLELDEETMAKLYEHEQLLNHPAVAEHPINTGFVITSPRGSALGRKIDANTVKLVRGDQ FT QAFGLHGRSAEQRIALDLLMDPSVGIVSLGGNAGTGKSALALCAGMEAVLERREHRKIT FT VFRPLYAVGGQELGYLPGSEGEKMGPWAQAVFDTLGSIVSKNAIDEVVERGMLEVLPLT FT HIRGRSLHDSFVIVDEAQSLERNVLLTVLSRIGQNSKVVLTHDVAQRDNLHVGRYDGVA FT AVVEQLKGHSLFGHVTLTRSERSAIAALVTDLLDSPTRP" FT CDS complement(843606..844424) FT /transl_table=11 FT /locus_tag="AARI_07560" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTM6" FT /protein_id="CBT74979.1" FT /translation="MDVPTAPVLFPGQPAPDSAARRRFRALARSAPWLSTSLQFRIQVP FT EPYAKPDEGLEGELTAILRQREAISVRSADGQLVYQKEKFTADRSHGYVAATNSSWKLP FT ASLTSPVYTSDQLILRRPQISGFNGLLPLEHWEAMLDPVELAGTEPASHDLAFGHPTYI FT HELAEITHDDRPALAAVLSAGHNYQPTVASCPLVPHGTRTLVVLDRATGLCVNRRVLLA FT EAQVPPAPELSLQLLAHNQYYIDSLFTAPAPTLTDVRAPIPWELRSERPA" FT CDS 844508..845011 FT /transl_table=11 FT /locus_tag="AARI_07570" FT /product="putative leader peptidase" FT /function="1.6 Protein secretion" FT /EC_number="3.4.23.-" FT /note="match to PF01478: Type IV leader peptidase family. FT This group of aspartic endopeptidases belong to MEROPS FT peptidase family A24 (type IV prepilin peptidase family, FT clan AD), subfamily A24A. Possibly involved in protein FT secretion" FT /db_xref="GOA:E1VTM7" FT /db_xref="InterPro:IPR000045" FT /db_xref="UniProtKB/TrEMBL:E1VTM7" FT /protein_id="CBT74980.1" FT /translation="MSEIWSVAQESPVSAALVLLQLACFLGFGVLLAKQDMATHRLPNR FT LVASWLAASLAVIALLGIFRSDLHGVLIGLLGLLLLGGGYLLLTLASGGAMGMGDVKLA FT GVLGLNLGYYSLPSLFFATLLAFVLATLWVIGGVVARKLTLKSAVPFGPFMLIGSFIAL FT LMAR" FT CDS 845016..845483 FT /transl_table=11 FT /locus_tag="AARI_07580" FT /product="NUDIX domain-containing protein" FT /function="4.6 Miscellaneous" FT /note="identified by match to PF00293. Members of the Nudix FT hydrolase superfamily catalyze the hydrolysis of nucleoside FT diphosphates linked to other moieties. Substrates of nudix FT hydrolases include intact and oxidatively damaged FT nucleoside triphosphates, dinucleoside polyphosphates, FT nucleotide-sugars and dinucleotide enzymes. These FT substrates are metabolites or cell signaling molecules that FT require regulation during different stages of the cell FT cycle or during periods of stress. In general, the role of FT the nudix hydrolase is to sanitize the nucleotide pools and FT to maintain cell viability, thereby serving as surveillance FT and house- cleaning enzymes" FT /db_xref="GOA:E1VTM8" 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:E1VTM8" FT /protein_id="CBT74981.1" FT /translation="MATPEFVTNLRTRIGHELLWLSGVKVVVLHEDKVLLVRRADNGQW FT TLPAGIIDPGEEPSHTAVREVLEETGVECEITDLLGVGVTAPTVYPNGDHAQYLDVVFK FT ARHLSGEANVNDDENLEVGYYALADRPELPPLHERALQWALNPRPGGYFAS" FT gene complement(845496..846473) FT /pseudo FT /locus_tag="AARI_07590" FT /product="truncated renal dipeptidase family protein" FT /note="C-terminal section of a renal dipeptidase family FT protein" FT gene complement(846473..846616) FT /pseudo FT /locus_tag="AARI_07600" FT /product="truncated renal dipeptidase family protein" FT /note="N-terminal section of a renal dipeptidase family FT protein" FT CDS complement(846808..848220) FT /transl_table=11 FT /gene="fumC" FT /locus_tag="AARI_07610" FT /product="fumarate hydratase class II" FT /function="2.1.3 TCA cycle" FT /EC_number="4.2.1.2" FT /note="catalyzes the reversible hydration of fumarate to L- FT malate. Involved in the TCA cycle" FT /db_xref="GOA:E1VTM9" FT /db_xref="InterPro:IPR000362" 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:E1VTM9" FT /protein_id="CBT74982.1" FT /translation="MTNSDDFRIEHDTMGEVRVPAQALYRAQTQRAVENFPISGKTLES FT SHIKALAQVKKAAAQANLALGVLDEERAAAIVSAADQVATGQYDEHFPIDVFQTGSGTS FT SNMNTNEVLAELATRALKAQNSDTEVHPNDHVNASQSSNDVFPTSVHVAATGALINDLI FT PALGTLASALEAKSAEFKDVVKSGRTHLMDATPVTLGQEFGGYAAQVRYGIERIEAALP FT RVAEVPLGGTAVGTGINTPEGFPQRVIEFLREDTTLPIIEARNHFEAQANRDGLVEASA FT ALRTIAISLIKIANDLRWMGSGPNTGLGEISIPDLQPGSSIMPGKVNPVISEATIQVAA FT QVIGNDTAIAWAGTNGAFELNVGIPVMASNLLESIRLLSNTSTVMSEKMIQGISANVER FT ARFLAEASPSIVTPLNKLIGYENAAKIAKKAVAEGLTVREATIALGFVERGELTEEQLD FT QLLDVSTMVGKY" FT CDS complement(848351..848980) FT /transl_table=11 FT /locus_tag="AARI_07620" FT /product="carbonate dehydratase" FT /function="2 Intermediary metabolism" FT /EC_number="4.2.1.1" FT /note="carbonate dehydratases are zinc-containing enzymes FT that catalyze the reversible hydration of carbon dioxide. FT They are ubiquitous enzymes involved in fundamental FT processes like respiration, pH homeostasis and ion FT transport" FT /db_xref="GOA:E1VTN0" FT /db_xref="InterPro:IPR001765" FT /db_xref="InterPro:IPR015892" FT /db_xref="UniProtKB/TrEMBL:E1VTN0" FT /protein_id="CBT74983.1" FT /translation="MLPESTQQSLTPKEAWEKLSSGNLRFVSEDTQHPNQDSARRQKLI FT SGQEPFAVIFGCSDSRLAAEIIFDVGLGDMFVVRTAGHVLDPASLGSLEFAVDILNVPL FT IVILGHNSCGAVTSAIKAKETGEMPKGFVRDLVEHITPSVHAAERKGITDVNGTVVEHV FT KQTTDRLVDLSSIIALAIEEGRTAVAGVAYHLHDGRAQLVSSLGLD" FT CDS 849072..849488 FT /transl_table=11 FT /locus_tag="AARI_07630" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTN1" FT /protein_id="CBT74984.1" FT /translation="MSTVGVTREEIRDYVHQYNLQPHGTRTAWLQQQPFSRATFYRWNQ FT LVFEGDLDRNLVPRDHGQMNTTPSQRSAFEQARAKEQAEHEDELKALRERVRQLEGTNE FT ALGKAIGLLHALNEQEPATSTTDERKNSSPRKTN" FT gene 849740..850504 FT /pseudo FT /locus_tag="AARI_34620" FT /product="partial transposase of IS3 family" FT /function="4.5 Transposon and IS" FT CDS complement(850571..851245) FT /transl_table=11 FT /locus_tag="AARI_07640" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTN2" FT /protein_id="CBT74985.1" FT /translation="MHPENNTENNAPATENAASGSGLPVASPRSLDDPNATFEDLPFKP FT QLTEKQAKRANQTFKGMVLSIGFTVAILIPVLMLNPAPKDDAFESDVNLQATAEQTEQI FT SGFEIFAPELGEKEYANFARWQANTAQGVPYWEFGLVSEDKNFVWVRQAAESNPTWIAL FT ITDAATPTEKRTIGGTEWEVRVKDQSTYLIADFADSTVVLSSDTSVEQLNSVAEQVAND FT LK" FT CDS 851402..852436 FT /transl_table=11 FT /gene="glpX" FT /locus_tag="AARI_07650" FT /product="fructose-bisphosphatase, class II" FT /function="2.1.2 Main glycolytic pathways" FT /EC_number="3.1.3.11" FT /note="catalyzes the hydrolysis of fructose 1,6- FT bisphosphate to fructose 6-phosphate. Involved in FT gluconeogenesis" FT /db_xref="GOA:E1VTN3" FT /db_xref="InterPro:IPR004464" FT /db_xref="UniProtKB/TrEMBL:E1VTN3" FT /protein_id="CBT74986.1" FT /translation="MGSFVTEKNNYAHLSSRLSVSDAEPDRNLALELVRATEAAAIASS FT PWVGFGDKNAADGAAVDAMRGLLSTVNFNGVVVIGEGEKDEAPMLFNGEQVGNGSGAEC FT DVAVDPIDGTRLTALGLNNALSVLAVADRGSMFDPSAVFYMEKLVTGPEAAELVDLRLP FT VKQNLHLIAKAKGKKISQVTVTILDRPRHAGLIEEIRAAGARTKLIMDGDVAGAIAATR FT EGTGVDALMGVGGTPEGIVTACAIKALGGVIQGRLWPTDDDEKQQAIDAGHELGRVLTT FT NDLVTSDNCYFAATGITDGDLLRGARYKDNRIHTQSIVMRAKSGTIRFVDGEHQQDKWE FT AYTR" FT CDS complement(852541..853749) FT /transl_table=11 FT /gene="manA" FT /locus_tag="AARI_07660" FT /product="class I mannose-6-phosphate isomerase" FT /function="1.1 Cell wall" FT /EC_number="5.3.1.8" FT /note="catalyzes the interconversion of mannose-6- FT phosphate and fructose-6-phosphate. In prokaryotes, it is FT involved in a variety of pathways including capsular FT polysaccharide biosynthesis and D-mannose metabolism" FT /db_xref="GOA:E1VTN4" FT /db_xref="InterPro:IPR001250" FT /db_xref="InterPro:IPR011051" FT /db_xref="InterPro:IPR014710" FT /db_xref="InterPro:IPR016305" FT /db_xref="InterPro:IPR018050" FT /db_xref="UniProtKB/TrEMBL:E1VTN4" FT /protein_id="CBT74987.1" FT /translation="MFELKNAIRDYHWGSASQISDLLDLPADTTPQAEMWLGAHPGCPS FT RISTDGTALNDFIAQDPEHILGAGVAQRYGRLPYLFKVLSATSPLSIQTHPTLQQAKER FT FAQETASGKALDAADRNYRDDNHKPEMLFALTDFVALSGFRQPAQIVEDLQVLEPHLPE FT QSHRIVGELVALLQGSDPLASTFKHVLTAGEEISQLAQQISHAVSASTELQRNVQFAEL FT VSINKVYPGDPGVLVALLLNLVFLEPGQAISLGAGNVHAYLRGLGIEVMANSDNVLRGG FT LTSKHIDVPELLDVTIAQPSPAPILEPVALDTHDRLYKPDFEEFQLQVLDPTEPGLAAD FT LQLHGAAVVLCTAGEFMVATREGERSISRGQSLFITAAELPATATLQGTVPGQLFATSA FT QID" FT CDS complement(853817..855424) FT /transl_table=11 FT /locus_tag="AARI_07670" FT /product="putative cell envelope-related transcriptional FT attenuator" FT /function="3.5.2 Transcription regulation" FT /db_xref="InterPro:IPR004474" FT /db_xref="UniProtKB/TrEMBL:E1VTN5" FT /protein_id="CBT74988.1" FT /translation="MGSASHRAPSPLRQPETISSPQRSKRAMILVLLTIFFPGSAQLIA FT GNRKLGRIAVSITMLCWLAIIALAALYFIDRSIILGRVAHPNFQLFLIIVLGTLALGWL FT VMFINTLVIIRPKLLAPGMRAIVSVFTLAAVVATSGVFVYGASLLNTGRETITAVFDKG FT PAFDPIDGRYNIAVFGADSGDNREGVRTDVAALLSVDAKTGKSLLISVPRNFQSARFAA FT GSPMEKIWPNGYNCGDECIFNSIYRNAETEHADAFPDTVKNIGAQAAMDALEGTTGLPV FT QGYVMINMAGFEQFVDALGGVTINSGGWVPYNGKYYPNSTVRTHWFAPGTHTFTGKQAL FT WFARSRDFTDDYHRIKRQQCLQQAIIKQVKPQTILSNFTSIMSAGEQLVETDIPAGQLG FT SFVSLAEKVSNEPMTRLTLGAPDFERSFSTYPKFDELQERIQSLIAKQNKPKEDKPKKS FT KDSSKSAESEETTKASEESEDSTDVNNAPKLSNSDDKEFTKPDGSPITEEYLVNLEMAG FT YRTLISEIAANNDECSVP" FT CDS complement(855442..855972) FT /transl_table=11 FT /gene="purE" FT /locus_tag="AARI_07680" FT /product="phosphoribosylaminoimidazole carboxylase FT catalytic subunit" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="4.1.1.21" FT /note="phosphoribosylaminoimidazole carboxylase catalyses FT the sixth step of de novo purine biosynthesis, the FT decarboxylation of 1-(5-phosphoribosyl)-5-amino-4- FT imidazole-carboxylate (AIR)" FT /db_xref="GOA:E1VTN6" FT /db_xref="InterPro:IPR000031" FT /db_xref="InterPro:IPR024694" FT /db_xref="UniProtKB/TrEMBL:E1VTN6" FT /protein_id="CBT74989.1" FT /translation="MSEAPLVGLVMGSDSDWPVMRLAAQALAEFGIPFEADVVSAHRMP FT TEMIDYGKKAHERGIRVIIAGAGGAAHLPGMLAAVTPLPVIGVPVPLAKLDGMDSLLSI FT VQMPAGVPVATVSIGGARNAGLLAVRMLSAGTDELAESLQVKLLQFADSLREQAHAKGA FT ALRAEVANENFAS" FT CDS complement(856046..857158) FT /transl_table=11 FT /gene="purK" FT /locus_tag="AARI_07690" FT /product="phosphoribosylaminoimidazole carboxylase ATPase FT subunit" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="4.1.1.21" FT /note="phosphoribosylaminoimidazole carboxylase catalyses FT the sixth step of de novo purine biosynthesis, the FT decarboxylation of 1-(5-phosphoribosyl)-5-amino-4- FT imidazole-carboxylate (AIR)" FT /db_xref="GOA:E1VTN7" FT /db_xref="InterPro:IPR003135" FT /db_xref="InterPro:IPR005875" FT /db_xref="InterPro:IPR011054" 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/TrEMBL:E1VTN7" FT /protein_id="CBT74990.1" FT /translation="MMAPEALNLGFELHILAEGPDVSAARCVPDAPVGDYKDLETLREF FT AKGKDVVTFDHEHVPNDFLTTLINEGVNIQPRPAALIHAQDKLVMREAIERLGLPNPLW FT AKVEDVEALIAFGEKAGWPIVLKTPRGGYDGKGVRMLDNAQDAKDAADWFANGPLLAED FT KVDFSRELSALVARTPSGEAKAWPVVHTIQVDGVCDEVIAPAQDIDDATAATAANAALR FT IAEEFGVTGVMAAELFETPGVGAGFVINELAMRPHNTGHWTMNGSVTSQFEQHLRAVLD FT LPLGETSALGVTVMKNYLGGANQDLYSAFQAALAAAPEVKVHAYGKSVRPGRKIGHVNI FT VANAGQSVDELRSQANKVAALIRDGADATV" FT CDS 857383..857952 FT /transl_table=11 FT /locus_tag="AARI_07700" FT /product="GtrA-like protein" FT /function="1.1 Cell wall" FT /note="identified by match to protein family PF04138. FT Members of this family are predicted to be integral FT membrane proteins with three or four transmembrane spans. FT They are involved in the synthesis of cell surface FT polysaccharides" FT /db_xref="GOA:E1VTN8" FT /db_xref="InterPro:IPR007267" FT /db_xref="UniProtKB/TrEMBL:E1VTN8" FT /protein_id="CBT74991.1" FT /translation="MLERIKLKIAGLISLLWREVAKFGVVGGIAFIIDSGIYVWLLHGP FT MSDSQVKAKIIAGIVATMFSWVANRYWTFRHRRQANVLRELVMFIIMNAIGLGIAAACV FT WVTKYWLGLTDPTSVFIAGSVVGLVLGTIFRFFAYRFWVFGKEMDQEEKFAHDHEILDK FT NRADTGTGTMESTAQADTGTLPTVVR" FT CDS complement(857949..858677) FT /transl_table=11 FT /locus_tag="AARI_07710" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTN9" FT /protein_id="CBT74992.1" FT /translation="MSNSLQSGTFVENLLSPRRGSASPWLTWYSVIGERIELSGRVFDN FT WVAKSANLLGEVFDLDEDSVVVLDLPAHWKSLVLALAALHHGATLVDAEQADAQQASVW FT VTAQPNDPRIPNSSEILAVNPAALALSFGSDLGPVAEDFNASVRTYGDQFYPSPVSGDT FT SAIATNGDAPIGLAALFDAAAKAQGTILVRAQQPVLTLLPYAIGQWKAGDGIVLVEDGL FT EVTERLREGERITSDYQPAG" FT CDS 858976..859500 FT /transl_table=11 FT /locus_tag="AARI_07720" FT /product="WhiB-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF02467. WhiB FT is a putative transcription factor in Actinobacteria, FT required for differentiation and sporulation" FT /db_xref="InterPro:IPR003482" FT /db_xref="UniProtKB/TrEMBL:E1VTP0" FT /protein_id="CBT74993.1" FT /translation="MANLEHGYSEFSTSAVASAQYGLEDAPSDWFVDPQAGESARVAVA FT ADLETAADNFLKVHDASSEPEEISSVGSWAPELDEDDEVRETIKAVWLGVGGEVDEGEL FT GWQARALCAQTDPEAFFPEKGGSTRDAKRVCGACVVRSECLEYALSNDERFGIWGGLSE FT RERRRLRKRAI" FT CDS 859569..862970 FT /transl_table=11 FT /locus_tag="AARI_07730" FT /product="putative group 2 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="3.4.-.-" FT /note="match to PF00535: glycosyl transferase family 2. FT This domain is found in a diverse family of glycosyl FT transferases that transfer the sugar from UDP-glucose, UDP- FT N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to a FT range of substrates including cellulose, dolichol phosphate FT and teichoic acids" FT /db_xref="GOA:E1VTP2" FT /db_xref="UniProtKB/TrEMBL:E1VTP2" FT /protein_id="CBT74994.1" FT /translation="MAALRNQSRPIERFVGVDASSSDASLEVLQANLPSNAALLVADEG FT SLGLSLEVAVSQLPEARLDRDEWLWIIHDDSMPAPDALEQLTRAVEASESVSIAGCKLL FT DIDNPRHLAEVGLSVDRKAQRLTLIDIDEVDQGQYDGRSDYFAVSSAGMFIRREVFEHL FT GGFDPAIPGRGDDVDLCWRNRLAGHRVVVVPSAKMYHQVEVVDSLAGPREAKRAEVFQR FT LKFASPLALPFLWIGLLLGGIGHFLVALLAKDPGHGFSHLGSVLRGLFTPGKLAASRRN FT VAQIREIPRRQVRKLMATGAQVREYRRNVTTGRGDGEVYGDGSGADAMVEPSGDNFSDF FT VRIARPPRTTAVLSLILALLFSGAASMIAWRSLLGSSALSGGALRPFSNTNQEIGANAL FT SWWQNTTTGLSAPPDNSDLLFWLFSLLTFDHANEASVYLFFAAMPLAALSAWWGIGAVS FT RSRAVRFFAALIWALLPSLVSSLASGRVGSVLIHILLPLFFLAIIRAMNAHVAIDGAKP FT KTAKQQSVSAWTASASAALLLWVISAGSVSFFLTASILIYVLAIFSVRRARSLWWIPLP FT ALVWNLPLLFAGLGDLRLLFTEPGAAQAFSPAAPWQMLLGFPEYFNANASLVGWDFLPT FT GPWALVAALLVGAPIIGLAVFGTLSSSFSHNASMRRNSRRLLWGAVLSLAAGWAVGFVP FT YTLDSHTGVSAYTGPFVSFAMFAMLAAAANALAALRHEDQLRSVRKQAARPVMGLMAVF FT SVLTILASGSFLLGAQLNPAAESETLSAMNSAQQVRSSQPRTLPATAADAGRSEFQKRT FT LVLSPRSSGEIDSHLVVGSGETLDGISRYSLVKQLSGSLLDPERNEASATAQVQSKAVA FT MLLSGSALDSRESLRDLGVGYIVLNETGESVPATVRTLDAATGLASVGQTDSGWLWRVD FT YESTEDSQSAGFARIVSENGDVTILPTQRGKITNIEIPAADSQRTLVLATASDPQLRAS FT LNGESLRSVAYPQDSETRWAQAYELPAEGGKLALTHKDSMAIPVLVLSAIVLLITVLLA FT IPVPSSRRFANYRNTEYRFREPRGETEEVADGSQVLAAAEVQSPATGTMPQSRREARER FT ASEIRENLTPKLSDRISDAEAEQEKK" FT CDS 862970..865567 FT /transl_table=11 FT /locus_tag="AARI_07740" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTP1" FT /protein_id="CBT74995.1" FT /translation="MSDEKNVNSADSADQPAEQTPVPQPAAAQPEPKDSAPVSAALSRA FT EEKAAKAKAKVDAKLDKIRAKEAQARAKAEAKNSAKAAKSEAKASKQQEAKDQPKPVAQ FT PAAKDASSPAADSSSAAKPDAKKTEDQSAPKPEAAGSVTAKSSEAQEKTAAGLPAAASK FT DDAVAKPVAKSAEPAKDPDSAKAKSLPESAIGKAPEQAADDPVTKPVAGDSAGSATKPS FT DAKDSSARHSTVAPVAATAAPSAAMSSAEAETEPKPSAESKSEDAPKAAEAEDPKAAKR FT RQKLEKVRARNAAKEEAAKTSAVAAPAAAAEPSAAEPADGKVSQRRLKLDKARAAASKD FT AASATTRKKTGAVLLSLAAVLAAGAVVGAGSIFAPAPAEKSLPAAVTNLPAGDSSSVCS FT ATPKLLRGVEGTDAQFAPGAKEISSNLRSVVVSDLAKRIPGSSLSKLDGSDVHELTERI FT DDAEAAEARGADDEGLTGFISKISTLKDIDDAQVYSLQPLGELASKGSTLRSYQAKDGD FT LAGLAAGTCQAPASNWRFTGLQTSTGSTSVMHLSNPTHTTAQVSLRLRGPEGLIDTSTL FT QNIVLAAGESRAIVLGGYAQDLNSISAEVTSIGGKITASVQQAALRGLTPSGVELVGAN FT ASASNSQVIPGVWIESKENLSKLSKDNKSLVPQLHVSATGASGAGFKVKVLGEDGEVAA FT SFEDNLAVESDATKSIDLSQLAGGYYTVVVESDAPVTAAVKMVRGSDPKDSSDTAWAAS FT SNVLSGTQAMPLSANGTGKFAIAAVASDSEVEAVVVNKDGKLEKPKNLQIDAGQSIVFD FT PKSVSEDAQAVIFSTDANAYLAQLVLGSERSIAWAAMPQANAGRDGMVVNIGG" FT CDS 865594..866523 FT /transl_table=11 FT /locus_tag="AARI_07750" FT /product="putative cytochrome oxidase assembly protein" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /note="identified by match to protein family PF02628. One FT member of this family, CtaA, is required for cytochrome aa3 FT biosynthesis in Bacillus subtilis" FT /db_xref="GOA:E1VTP3" FT /db_xref="InterPro:IPR003780" FT /db_xref="UniProtKB/TrEMBL:E1VTP3" FT /protein_id="CBT74996.1" FT /translation="MVTPFAWLAQRVALERKSLKAASLSAMIAAILIIVGGGVVRVTGS FT GLGCPDWPTCTGASIAPTAEMGIHATIEFVNRLLTFVLCAAVGWVIIAARLQREAVPQI FT TRWAWFQFWLVVLNAVIGGVTVWVKLNPYVVAAHFLAATLLLTAAAATWDKVQNLGRTE FT PQFSTESVRKLGSALVVLSAVLVILGTGVTGSGPHAGDSAEVPRMGFDWLLITVVHASV FT AFGALSVASVLWNRARRDQITEVERKAKLYVYVFAAQGLIGVIQSVTSLPELLVVAHLV FT GSALVWIGAVRVGIATHAPCREVQSPAR" FT CDS complement(866536..866994) FT /transl_table=11 FT /locus_tag="AARI_07760" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR010428" FT /db_xref="UniProtKB/TrEMBL:E1VTP4" FT /protein_id="CBT74997.1" FT /translation="MNSKLPDRPSGPRRNRHGRGRRGPLIPMHLPAYRSRPERFDDAVM FT ASAQRLAQRWPGKIEKIEFLIDPVPSDKLLDQASALGERVPLASSVPAGARSPARIIIY FT RLPIEQIAENTGELLDLVHQCVVHEVAQLWMKPISEVDPSYFPEDPDF" FT CDS 867027..867254 FT /transl_table=11 FT /locus_tag="AARI_07770" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTP5" FT /protein_id="CBT74998.1" FT /translation="MVISPQKAQDPKEVRASRVEWQTWKVFVFVLAQLAVKRLVQLLPT FT YTLIQQQFLGPWRLTRSRTAMTCVPVMPIA" FT CDS 867251..867487 FT /transl_table=11 FT /locus_tag="AARI_07780" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="InterPro:IPR021888" FT /db_xref="UniProtKB/TrEMBL:E1VTP6" FT /protein_id="CBT74999.1" FT /translation="MTVPSGWNLIRGAIPEVLEPEDELNALVNAVRDREPKVREPRHAS FT ESPTDSVRARDNRTQRFDSRVRLAVLPAGDDET" FT CDS 867698..869299 FT /transl_table=11 FT /locus_tag="AARI_07790" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR010178" FT /db_xref="UniProtKB/TrEMBL:E1VTP7" FT /protein_id="CBT75000.1" FT /translation="MAEAAKNPTGGQGPTGQPAAAATGNAPRSQASLSQKAEELAARLE FT EHKNQAQANAAAEREAARKEAIRRAMSGKTEAEAQAAAASKTSPAAAKPAEATKPAAAA FT AKPAAAAAKPAAAAAKPAAAKTPAAKAPAVKQPVKPAAAKPAAAKPAAAKPAAAAKPAT FT AKPAAAKPGTAKPAAAAKPAAKASAAKPTAKEPVEDVIRAIKLPHEIEAEKQAQSKGKE FT AGAKSAQPAAKADTTSTAEQSVPPVSVAPKTGSLPTTKAAVAQARNRVFGSYEPEPERS FT EAAVKRRVARERALNSKPALGRTAQVIVALVFPLLTLIAAIRLIATPAFLALSYGRPGF FT PSDSFGFTDPERLTYGSYGVDYLNNFAGPEYLSGLKLPTGSSMFTDGEVQHMVDVKNLI FT GFAYILGVVLAIILVIGVWYLAKRYAGGVRRALFAGAILTLAGIAALVVLAIMGWDAFF FT TQFHALFFSEGTWTFSVSDTLIRLYPEQFWLDSAIGIAVLVLAAIIAVLISCWPTGRRR FT EAARLRQEARAFGIGN" FT CDS complement(869369..871210) FT /transl_table=11 FT /locus_tag="AARI_07800" FT /product="putative fatty-acid--CoA ligase" FT /function="2.4 Metabolism of lipids" FT /EC_number="6.2.1.-" FT /note="activates fatty acids by binding to coenzyme A. FT Possibly involved in the synthesis of cellular lipids or FT their degradation via beta-oxidation" FT /db_xref="GOA:E1VTP8" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR020845" FT /db_xref="UniProtKB/TrEMBL:E1VTP8" FT /protein_id="CBT75001.1" FT /translation="MQEVTVELLTALAPEVNTTNLLLDRVARGAQRPLFSVQRDGVWHE FT LSACAFLTDVKRLAMTLINDGLQPGDKVAIISRTRYEWALAEEAIWFAGGVTVPIYETS FT SAFQIEWILRDSGARVVFAENHELRANVRQAAAQLGESVRTHIFEGSDTADKSLIPSAG FT LHQLMVPASQVDEQLIESRRASMALEDVATMVYTSGTTGRPKGCNMTHSNFAMVAHNLA FT EHMLEVLGEERRTLMFLPLAHVLARAVQQTCIHGGSVIAHSSSMANLVEDLAAVKPGFL FT LAVPRVFEKIRTTALATAERGGKAELFLKAEQTAIEVSKIRDARSRGIKARMPLGLRAR FT HALFNKVLYPKLRSVFGGQCAYAISGASALSQDLAHFFRGAGIDLLEGYGLTETTAPAT FT VNQASRNRVGTVGRPLPGTSIKIAEDGEILVKGIGVFASYHNSPEATAAVFDQDGYFKT FT GDTGVLDDGGFLQVTGRKKELIVTAGGKNVSPGPLEEMVRAGRIAAQCVLVGEQRPFIS FT AIVTLDREELVLWAKANGLGTMTLAEAAINPAVIAEIQSYVDTANLTVSKAESIRKFVV FT LEDEFTEASGHLTNSLKLKRQSVLDQFEDRIEAFYRK" FT CDS complement(871289..872899) FT /transl_table=11 FT /locus_tag="AARI_07810" FT /product="putative dolichyl-phosphate-mannose-protein FT mannosyltransferase" FT /function="1.1 Cell wall" FT /EC_number="2.4.1.109" FT /note="identified by match to protein family PF02366. FT Transfers mannosyl residues to the hydroxy of serine or FT threonine residues, producing cell-wall mannoproteins" FT /db_xref="GOA:E1VTP9" FT /db_xref="InterPro:IPR003342" FT /db_xref="UniProtKB/TrEMBL:E1VTP9" FT /protein_id="CBT75002.1" FT /translation="MGTSVLNTPDTGHVRSARQAFTFESLKQRLLPVVAPRGPLIWIVP FT LLVTLIAGLLRFINLAHPHLLIFDETYYVKDAFAMLQSGYEREWADESDEQFIAGDPQL FT QDESSFVVHPPLGKWMIGVGMLLFGDFNGFGWRFSTALLGTLSVLLVTLCARLLFGSHI FT LAAIAGLLMAVDGHSIVMSRTALLDIFLMFFVIAAFYALLKDRAQGRTALARKLAVPEG FT NRPDEFLLIHGPMLWWRPWRLVAAIMLGGAVGIKWSALSFVAVFCLMAVLWDFAARRTA FT GIHKWQSAAFTRDGLYSFITMMPLVLLTYLSTWTGWLITQGGRYRNWAQENPGEGISWL FT PGPLRSLWNYHQAGYEFHTGLNSEHGWQSSPWTWPFAGRPVLFYFEGYDKGVNGCELQR FT CTEVITDLPNPLMWWACTISMFLLILWWIGARDWRAGAILSSVAAGFLPWLMYPERTMF FT FFYTLPLVPFMVLALTYMIGRFIPRDPHSGAVYRSRVIIVTIFMALLLVTSAFFWPIWS FT GEMIADDYWRLHVWLPSWG" FT CDS 872968..873828 FT /transl_table=11 FT /locus_tag="AARI_07820" FT /product="putative tetrapyrrole methylase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="identified by match to protein domain PF00590. This FT entry represents several tetrapyrrole methylases. These FT enzymes catalyse the methylation of their substrates using FT S-adenosyl-L-methionine as a methyl source. Enzymes in this FT family include: uroporphyrinogen III methyltransferase FT (EC:2.1.1.107), precorrin-2 C20- methyltransferase FT CobI/CbiL (EC:2.1.1.130), precorrin-4 C11-methyltransferase FT CobM/CbiF (EC:2.1.1.133), sirohaem synthase CysG FT (EC:2.1.1.107) domains 4 and 5, and diphthine synthase FT (EC:2.1.1.98)" FT /db_xref="GOA:E1VTQ0" FT /db_xref="InterPro:IPR000878" FT /db_xref="InterPro:IPR008189" FT /db_xref="InterPro:IPR014776" FT /db_xref="InterPro:IPR014777" FT /db_xref="InterPro:IPR018063" FT /db_xref="UniProtKB/TrEMBL:E1VTQ0" FT /protein_id="CBT75003.1" FT /translation="MQNSDNEGVIVLGATPIGNLSDASPRLREIMATADIIAAEDTRNF FT HHLAHALGIKINAKVMSLHEHNEAHKLTEVLELATEGATVLVVSDAGMPAVSDPGYPLV FT AAAMSAGIRVTAVPGPSAVLTALALSGLPTGRFTFEGFLPRKTGERRKRLDSLLNEDRT FT MVFFEAPHRLNDFLDAAIEAFGPEREAAVARELTKKFEEVRRDSLSGLRAWAEDGVRGE FT IVVVVHGAPEADAASIEDLLPKVASLVDEGVRMKQAVADVAEKFGAKKRELYEAVLASR FT HEAEK" FT CDS 873967..875454 FT /transl_table=11 FT /gene="gabD" FT /locus_tag="AARI_07830" FT /product="putative succinate-semialdehyde dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.2.1.16" FT /note="succinate-semialdehyde dehydrogenase (NAD(P)(+)) FT reduces succinate semialdehyde into succinate. Involved in FT the degradation of gamma-aminobutyrate" FT /db_xref="GOA:E1VTQ1" 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:E1VTQ1" FT /protein_id="CBT75004.1" FT /translation="MSITAQREAELLAKVPTGLLINGEWRDASDGGTFDVLDPATGEKL FT LTLASATSEDAMAALDAADAVQAEWALTAPRERAEILRRAFDLVTARKDDFALLMSLEM FT GKPLAEAYGEVTYGAEFLRWFSEETVRHYGRYVTTPEGKNKVLVHHKPVGPCLLITPWN FT FPLAMATRKVGPAIAAGCTMVLKPAKLTPLTSQLFAATMMEAGLPAGVLNVVSGSSASK FT ISGPLMADDRLRKVSFTGSTPVGKQLMKDAADKVLRTSMELGGNAPFLVFEDADLDAAV FT EGAMAAKMRNMGEACTAANRFLVHEDVAEEFTAKFASAMKALKPGRGTDPDTTVGPLVE FT EKARDEVHALVEAAVAAGATAVTGGAPVDGPGYFYQPTVLANVANDATILTQEIFGPVA FT PVTTFKNEAEAIKLANASEYGLASYIYSQDFNRMFRVSEQIEFGLVGFNAGVISNAAAP FT FGGVKQSGLGREGGAEGLAEYTTVQYIGIADPYAAKK" FT CDS complement(875523..877940) FT /transl_table=11 FT /locus_tag="AARI_07840" FT /product="putative transglutaminase-like protease" FT /function="3.10 Protein degradation" FT /note="identified by match to protein domain PF01841: FT Transglutaminase-like superfamily. Most microbial FT homologues of the transglutaminases are probably proteases. FT 8 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VTQ2" FT /db_xref="InterPro:IPR002931" FT /db_xref="UniProtKB/TrEMBL:E1VTQ2" FT /protein_id="CBT75005.1" FT /translation="MSADLAARLAQIANPPAPTPEPGYKRALRWLLVPIAAACCLAVAV FT LAGSASLSGVVEGARWFPALVVPILALHLSAAVLRAIPRLRWAAFPAAAIVALLAVAFS FT EARTLNLGNLPFTQWVWAMLSEAGMQLATQVPPVATSLPVAFSVLCFTLAISLAVELLA FT GSRRLAMLSIIPITLAPIIASLFKQEGAGIGYLALILLGMLGYIALIPYLFAPVSAKHA FT RVPLPKPRTLGILGITAMACISVLLAASSWMPGFRNGMFSEGQRPSGDLLASNVDPLIN FT LGRDLRSNSGVPILTYYTTAEKAPYLRTQVIKDLSADRWEPSEDMLTSTLNGTTAVPKN FT FNELNSTNELLQMNWPGGISTSVLPLPNRAHFVQGIAGDWNWTYETSVAGLSSEARAST FT NDISVTYADLFINTEMVRNIGQLGISAAAQLPEYLKLPQDPDNGLEPLLQQTLNEVFGQ FT GGIPANDIDAAIALQHFFRSGDFVYSERTPLREGYDGANSRVVEAFLSRRQGYCVHFAS FT AMALLARKAGIPSRIVVGYAPGEATGESINFNDDMSRGMLDRSIEDGTELTGYSVSGKQ FT SHAWPELYLNGMGWVSFEPTPGRGYSPSYAPEPTPTSTPQESTAPEVPTERSVPSASAS FT ATPTAQADAVGNEAQDSFVAWLVPVLLVAACFALSVSPWIRHRQRQERLERVRRGGDSA FT ARALLAELQAIGADYREPAGHHESAGDYTTRLSENHPQVADELQTLKTVVQESFYANRH FT LGAEDSTILLDALRAVQENLRSELSFIQRCSAFLFPNSVRPARPGKRPRINA" FT CDS complement(877930..879255) FT /transl_table=11 FT /locus_tag="AARI_07850" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR002881" FT /db_xref="UniProtKB/TrEMBL:E1VTQ3" FT /protein_id="CBT75006.1" FT /translation="MEKIPRYDSRDALSWTRTETTPPALRRWHLDLFTVRGWCTAAAGG FT LLVFVSYLLGRHEMMALGLALLTLALASWALAFNLRGRTNLHRELLSVVPSVGEVSRFR FT LTCAEPATIQEQLPEDFGPGPRFQAPGSVEYELVFRTRGIHLLGPAQQIVGDPLGLIRG FT MVRTGDDLEVPVRSQLHALDRLASLGERTLTGDAKFSRSTTADYYDVATRDYQQGDSIR FT QVHWKASARHGKLMVRQENHVATAQALLALDTSLDRWIHSGSDLKLSLPQARAEALTSS FT RRFENALSLASSIGLRYANSGYQLAFRNLDGMPLAERDQQSISELGALDSFEDFHAATS FT ELALVNDAMPANGAEIFGSSLHKELLGYRDEPVIMILGELDTAQAAWLATLARTVRHGE FT LFLLVSNPERYLRVHQELARTGWKIHILPGNMSIDSMWNDER" FT CDS complement(879266..880228) FT /transl_table=11 FT /locus_tag="AARI_07860" FT /product="putative AAA-type ATPase enzymatic complex FT assembly chaperone" FT /function="3.9 Protein folding" FT /note="identified by match to protein family PIRSF002849. FT AAA family proteins often perform chaperone-like functions FT that assist in the assembly, operation, or disassembly of FT protein complexes" FT /db_xref="GOA:E1VTQ4" FT /db_xref="InterPro:IPR011703" FT /db_xref="InterPro:IPR016366" FT /db_xref="UniProtKB/TrEMBL:E1VTQ4" FT /protein_id="CBT75007.1" FT /translation="MSANQTVPSLDSAFQSNCQRIFDAVQSVITGKPEAVTSALTVLLA FT QGHLLIEDVPGVGKTMLAKSMARSVNGSVHRIQFTPDLLPSDVTGVSVYSPQTHEFTFH FT PGPIFANIVIADEINRANAKTQSALLECMEEQQVTVDSITHRLEQPFMVVATQNPVDSE FT GTFALPEAQRDRFMARLSLGYPQRDAEISMLAGRHQFDPLEALRAVVELAELRHMIEQV FT KTVIVTERLGSYVVDLGRATREHPQVALGASPRALIQWVRAAKARAAIQGRDHVLPEDV FT RSVAQMVLNHRLILTRRAVADGMDTSAVIQELVASTPVN" FT CDS 880437..881393 FT /transl_table=11 FT /locus_tag="AARI_07870" FT /product="putative TatD-related deoxyribonuclease" FT /function="3 Information pathways" FT /EC_number="3.1.21.-" FT /note="identified by match to protein family PF01026" FT /db_xref="GOA:E1VTQ5" FT /db_xref="InterPro:IPR001130" FT /db_xref="InterPro:IPR012278" FT /db_xref="InterPro:IPR015991" FT /db_xref="UniProtKB/TrEMBL:E1VTQ5" FT /protein_id="CBT75008.1" FT /translation="MSKKKHTDLTLVPAAYRPVDEAPQAQQGERARAADSEEGGSKRNL FT HYPEAPEALPVPVVDNHTHLDFLDGTVKVSASEALAAAAAVGVKGLIQVGCDVQSSEYA FT VQVANEHANILAAVAIHPNDAARLAERAQLDQAIGRIEELASDPRVRAIGETGLDYYRT FT GEEGRGAQEHSFREHLRIAVEQGKALQIHDRDAHDDVVRVLQDAQLPKKVVFHCFSGDA FT QLARICNDNGWYMSFSGTVTFKNSHDLREALELADPKLLLVETDAPFLTPHPFRGRPNA FT SYMIPYTTRFLAETKGIELAEFCTQIDANTREVYGGF" FT CDS 881652..882815 FT /transl_table=11 FT /locus_tag="AARI_07880" FT /product="possible cell wall function protein" FT /function="1.1 Cell wall" FT /note="match to protein domains PF03990 (DUF348 domain of FT unknown function), PF07501 (G5 domain) and PF06737 FT (transglycosylase-like domain). The PF07501 domain is also FT found in proteins involved in metabolism of bacterial cell FT walls suggesting this domain may have an adhesive function" FT /db_xref="GOA:E1VTQ6" FT /db_xref="InterPro:IPR007137" FT /db_xref="InterPro:IPR010618" FT /db_xref="InterPro:IPR011098" FT /db_xref="UniProtKB/TrEMBL:E1VTQ6" FT /protein_id="CBT75009.1" FT /translation="MTHLLKKTWVKYLAQALAVAVVIAGAVFYISGQMSVVVSVDGQRE FT EITTRAATVGALLEQQDINLAKRDEISAALDSDLADEQLVDIKRNKSIDVTVDGTERVV FT HTTGMTVADVVAQLDIDKDSEISLDGDMELAALSDELEVVTPKDMTLIVKDKKKKIAST FT ALTVKELLAEQKIEVDGNDEINVKIKGETDKNAKDSVKLAADATVEVIDVTVKTWDETR FT DIDFETKKVKDSSLDKGETKVKTEGEKGERDLTLRQESRNGKKGEEEVLKSKITKKPVA FT EVIKVGTKEEEKETTSKKTPTPSNISSTWAALAKCESGGNWSINTGNGYYGGLQFSASS FT WRAAGGAQYAPLPHQASPAEQIATAEKLRANGGWGHWPHCSAKLGLR" FT CDS 882913..883800 FT /transl_table=11 FT /gene="ksgA" FT /locus_tag="AARI_07890" FT /product="dimethyladenosine transferase" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.-" FT /note="specifically dimethylates two adjacent adenosines in FT the loop of a conserved hairpin near the 3 prime-end of 16S FT rRNA in the 30S particle. Its inactivation leads to FT kasugamycin resistance" FT /db_xref="GOA:E1VTQ7" FT /db_xref="InterPro:IPR001737" FT /db_xref="InterPro:IPR011530" FT /db_xref="InterPro:IPR020596" FT /db_xref="InterPro:IPR020598" FT /db_xref="InterPro:IPR023165" FT /db_xref="UniProtKB/TrEMBL:E1VTQ7" FT /protein_id="CBT75010.1" FT /translation="MMSKESLPLLGATEIRRLAEELGIRPTKTLGQNFVIDGNTIRRIV FT AAAKVDPSETVLEVGPGLGSLTLGIMDAAAKVVAVEIDPPLAKRLPQTMAEFRPGREDD FT LTVILSDAMKVTELPGEPTSLVANLPYNVAVPVVLHLLEHFPSIRNGLVMVQDEVADRM FT AATPGNKIYGVPSVKGAWYGTMRKAGVIGMNVFWPAPKIHSGLVGFTRDKDRSDAPDRR FT EVFAIIDAAFAQRRKTLRAALSGWAGSGARAEQILVAAGIDPKERGEKLDIEQYIDIAR FT AAQAVPAQAPSSEA" FT CDS 883803..884735 FT /transl_table=11 FT /gene="ispE" FT /locus_tag="AARI_07900" FT /product="4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol FT kinase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.7.1.148" FT /note="forms part of the non-mevalonate pathway for FT terpenoid biosynthesis" FT /db_xref="GOA:E1VTQ8" 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/TrEMBL:E1VTQ8" FT /protein_id="CBT75011.1" FT /translation="MSKQHVIATAPGKINCYFKVGPPREDGYHEVASLYVAVSLTEQIE FT ATLRTDGELLLSLEPDSPVVSEPENFPLGSNNLVHQAAELLREHTGCTLGADLHITKRV FT PIAGGMGGGSADAAATLVACNELWGTGLDREELGRLGARLGADVPFALMGGAAIGLGIG FT DKLAPLLTRGKTHWVLIPASYGLSTPRVYGMLDRLRSGTEVEVPQEIDPAVIEALMASD FT APALSQVLANDLTQASLALAPELGTMRDMAEGAGALRAMVSGSGPTLALLVKDGEHAQE FT VMAQLGDEVGVATIPVTAPAAGAHIILSE" FT CDS 884890..886260 FT /transl_table=11 FT /locus_tag="AARI_07910" FT /product="FAD-dependent oxidoreductase" FT /function="4.6 Miscellaneous" FT /note="identified by match to protein family PF01266. This FT family includes various FAD dependent oxidoreductases: FT glycerol-3-phosphate dehydrogenase (EC 1.1.5.3), sarcosine FT oxidase beta subunit (EC 1.5.3.1), D-alanine oxidase (EC 1. FT 4.99.1) and D-aspartate oxidase (EC 1.4.3.1)" FT /db_xref="GOA:E1VTR0" FT /db_xref="InterPro:IPR006076" FT /db_xref="UniProtKB/TrEMBL:E1VTR0" FT /protein_id="CBT75012.1" FT /translation="MLNGRVSHWWEEIGLPAPREQLRGHSTADVAIVGAGFTGLWTAYY FT LAKANPKLDITILEARHVGYGASGRNGGWLTNTITAGRDRYLASHGRQAVNDFQLAMNQ FT TVAEVIAVCSAEGIDAELKQGGELEVAYTAAQEQRLRDDAMTDARWEHSDTVLLEAGAT FT QAKINVANARAGLFHPHAARIHPAKLVRGLAEVVERLGVKIHEDTRATALQPHHVDFEA FT GTLKAQSVIRATEGFTAGLAGHKRLWLPMNSSLIATEPLPSSIWDELNWKHGEVLGDYA FT HVYMYAQRTADDRIAIGGRGVPYKYGSRTDTDGVTPQKTVQGLQEILHRMFPQTRGARI FT EHAWSGVLGVPRDWAATVGLDPDTGLGWAGGYVGTGVGAANLAGRTLRDLILGAETELT FT NLPWVNHRVRKWEPEPLRWLATKGLYAAYGAADRSELKGRTSTSALAVLADRITGKP" FT CDS 886292..886471 FT /transl_table=11 FT /locus_tag="AARI_07920" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTQ9" FT /protein_id="CBT75013.1" FT /translation="MGRKTRGFYLWAAALVLIISGVLMITLMQVGILGWLLQGAGIILS FT AFAIGARSRPQTHA" FT CDS 886464..886988 FT /transl_table=11 FT /locus_tag="AARI_07930" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VTR1" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VTR1" FT /protein_id="CBT75014.1" FT /translation="MPEGGKMLLNDGKLSVQGRNYLVREARIEDLEQVIALMEQDEIRR FT AEHSGAAGGPEHYLEAFGEIDADPAHALIVLEGEGGKIVGTMQLTTLPSLARRAAKRMQ FT IEAVRVASESRRSGLGTQMIRWAICDAEHKGISLIQLTSDAQRQDAHRFYQRLGFIPSH FT VGFKMRLATRP" FT CDS complement(886975..887253) FT /transl_table=11 FT /locus_tag="AARI_07940" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007138" FT /db_xref="InterPro:IPR011008" FT /db_xref="UniProtKB/TrEMBL:E1VTR2" FT /protein_id="CBT75015.1" FT /translation="MGTVILEGKLLCKDAAEVELVKKLLPEHIRLTKAEPGCISFTVTQ FT SQDPWVWLVNEEFADGAAFEAHQQRATASTWGRRTSGLQRSYEVTGV" FT CDS complement(887363..889153) FT /transl_table=11 FT /locus_tag="AARI_07950" FT /product="putative drug resistance ATP-binding protein" FT /function="4.2 Detoxification" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT (putative) drug resistance ATPase-2 (Drug RA2) family (TC FT 3.A.1.121.z). ABCISSE: fused ATP-binding protein (ABC2), FT ART-family, ARE-subfamily (antibiotic resistance)" FT /db_xref="GOA:E1VTR3" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VTR3" FT /protein_id="CBT75016.1" FT /translation="MAHLLGGEALHLEYPTHVVFDSVTIGISDGDRIGLVGRNGEGKSS FT LLGMLSDKIEPNSGRVTKRNGLRVGVLDQSDTLDPEATVHFSVVGEMDDHQWAGEARIR FT DIISGLVADLDWEAKIGTLSGGQRRRVALAALLVQDWDVIILDEPTNHLDVEGISWLAE FT HIDKRWSKSSGGLMVVTHDRWFLDAVCTTTWEVHDRLVEPFEGGYAAYVLQRVERDRIA FT AVTENKRQNMMKKELAWLRRGAPARTSKPKFRIEAANQLIADVPPARNPLELQKMATSR FT LGKDVIDLLDTEVSFGAKQVLKPFTWRIGPGERTGLLGANGAGKSTLLGLIAGTVEPTG FT GKIKRGQTVKLAVLDQQFRELEQIGQDKVREVLARYRTTFNVDGKDLTPAQLLERLGFS FT SAHLSTKVAELSGGQRRRLQLLMILMDEPNVMILDEPTNDVDTDMLAALEDLLDSWPGT FT LIVVSHDRYLLERVTDQQYAILNGHFRHVPGGVDEYLKLRSAEGSTGGSNPSQASSAAP FT AKPAGPSGAELRAAQKELNANERKVGQLEEKIAKVHAKMAAHDQSDYEGLGKFTAEINE FT YQSQIDQLEERWLELSELLG" FT tRNA 889351..889425 FT /locus_tag="AARI_36650" FT /product="transfer RNA-Gln" FT /anticodon=(pos:889383..889385,aa:Gln) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 889558..891009 FT /transl_table=11 FT /gene="glmU" FT /locus_tag="AARI_07960" FT /product="bifunctional UDP-N-acetylglucosamine FT diphosphorylase/glucosamine-1-phosphate FT N-acetyltransferase" FT /function="1.1 Cell wall" FT /EC_number="2.3.1.157" FT /EC_number="2.7.7.23" FT /note="glucosamine-1-phosphate N-acetyltransferase (EC 2.3. FT 1.157) and UDP-N-acetylglucosamine diphosphorylase (EC 2.7. FT 7.23) perform the last two steps in the synthesis of FT UDP-N-acetylglucosamine, which is an essential precursor in FT both the peptidoglycan and the lipopolysaccharide metabolic FT pathway" FT /db_xref="GOA:E1VTR4" FT /db_xref="InterPro:IPR001451" FT /db_xref="InterPro:IPR005882" FT /db_xref="InterPro:IPR011004" FT /db_xref="UniProtKB/TrEMBL:E1VTR4" FT /protein_id="CBT75017.1" FT /translation="MSDQVNAPVAVIVLAAGAGTRMKSAKPKIMHEIAGRSMIGHALHA FT ASALQPQNLVAVVRHQRDLVAEHILSQFPSITIADQDEIPGTGRAVQQGLEVVDPALEG FT TVVVTYGDVPLLTSEVLQDLVATHESNGNSVTVLTTELDDPNGYGRILRDDKGEVAGIR FT EQKDASADELLIKEINSGIYAFDAKILRSALTEVTTENAQGEMYLTDVLAIARERGGRV FT ASSQIADRWQIEGANDRVQVSNLARIYNERKTEFWMRQGVTIVDPATTWIDADVMIGQD FT ATIKPGTQLHGETIIGANATVGPDTTLTNVVVGQRATVKRTDATDSRIAEGASVGPFAY FT LRPGTDLGVDGKIGAFYETKNVTIGRGSKLSHLGYAGDAEIGEFTNIGCGNITANYDGE FT KKHRTKIGSHVRTSSNTVFVAPVEIGDGAYTGAGAIVRKNVPAGALALSVAPQRNSEGW FT TLEKRPGTSSADAAFKSSLNSSASE" FT CDS 891082..892062 FT /transl_table=11 FT /gene="prs" FT /locus_tag="AARI_07970" FT /product="ribose-phosphate diphosphokinase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.7.6.1" FT /note="catalyzes the formation of PRPP from ATP and ribose FT 5-phosphate. PRPP is then used in various biosynthetic FT pathways, as for example in the formation of purines, FT pyrimidines, histidine and tryptophan" FT /db_xref="GOA:E1VTR5" FT /db_xref="InterPro:IPR000836" FT /db_xref="InterPro:IPR000842" FT /db_xref="InterPro:IPR005946" FT /db_xref="UniProtKB/TrEMBL:E1VTR5" FT /protein_id="CBT75018.1" FT /translation="MSEISHNVDKKLVLATGRAHPELAAEVAKALDTELLPLNAYDFAN FT GEIYVRSDESVRGKEVFLLQSYPAPLNNWLMEQLIMIDSMKRASARRITVVAPFYPYAR FT QDKKGRGREPISARLVADLFKTAGADRVISCDLHTAQIQGFFDGPVDHLFGFPLLADYI FT KSKVDVNEVTVVSPDTGRVRVAEQWADRLGGTPLAFVHKSRDLTVPNQAESKTVVGQVE FT GRTAILIDDMIDTGGTIAGAVRVLKEAGAKDVIIAATHAVFSDPAAQRLAECGAKEVVV FT TNTLPIPEEKRFENLTVLSIAPTIARAISEVFHEGSVTNLFDGRA" FT CDS 892820..893566 FT /transl_table=11 FT /locus_tag="AARI_07980" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTR6" FT /protein_id="CBT75019.1" FT /translation="MNSRVEFVLDGCGLTDLIGPDALSGYVSIFDASDIKLAAEVLMGR FT TRLTDYFPSEGRIPLLFCSCGDPGEGAMTVRLSITKDTVTWDQWAWEHDSFPIEWLPHL FT PAYHFPFDGYEAALDEAGQMALEIMGTASSIIRIASPGQGIMHWLDKRKRGELACQLDL FT LDIEIIQPAPDLQVTDLRQLINEVQALRTALGASLSNRRYEPTREQSQQVVSSTAKILD FT STEAFRLPGQTQESLEWLRDRFQSGA" FT gene complement(893905..894708) FT /pseudo FT /locus_tag="AARI_34630" FT /product="partial transposase of IS3 family" FT /function="4.5 Transposon and IS" FT CDS complement(894921..895337) FT /transl_table=11 FT /locus_tag="AARI_07990" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTN1" FT /protein_id="CBT75020.1" FT /translation="MSTVGVTREEIRDYVHQYNLQPHGTRTAWLQQQPFSRATFYRWNQ FT LVFEGDLDRNLVPRDHGQMNTTPSQRSAFEQARAKEQAEHEDELKALRERVRQLEGTNE FT ALGKAIGLLHALNEQEPATSTTDERKNSSPRKTN" FT repeat_region 895455..895462 FT /rpt_type=DIRECT FT mobile_element 895463..896911 FT /mobile_element_type="insertion sequence:ISAar19" FT /rpt_family="ISL3" FT repeat_region 895463..895486 FT /rpt_type=INVERTED FT CDS 895598..896905 FT /transl_table=11 FT /locus_tag="AARI_34640" FT /product="transposase of ISAar19, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRG4" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VRG4" FT /protein_id="CBT75021.1" FT /translation="MLNPTFTAPDLTTFTNLDGLGLTAIGQHLSAAKAEILCHVTNPIP FT WCQTCGAAGIPRDTVTRRLAHEPLGWRPTVLVIKHRRYRCANCQRVWREELSQAVAPRQ FT KISRTGLRWALVGLVCHHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFDGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLIDMVPGRSKAVFKTWLADQEEQW FT KQGIEVVAMDGFTGFKTAAVEELPHAVEVLDPFHVVKLGSEALDQTRQRIQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKTKLEDLFKEPEYEPVQLVWSVYQKMVDAYRQPKP FT EVGRWALEQLINEVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRRRLHPQS" FT repeat_region 896888..896911 FT /rpt_type=INVERTED FT repeat_region 896912..896919 FT /rpt_type=DIRECT FT CDS complement(897229..900018) FT /transl_table=11 FT /locus_tag="AARI_08000" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.575 FT between position 36 and 37. 7 transmembrane helices FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="UniProtKB/TrEMBL:E1VTR9" FT /protein_id="CBT75022.1" FT /translation="MKSFLRLMRDTPKLAASIIAIAAITAMFLSQMVVQGNAQEKIAET FT WRGAYDILVLPASASNQELTDEEGRTLLDSNFANVSGDPIPSKLLQSIDKLENVDVAAP FT IGFIARYSGASEVPTLTIPLDIFDQNSKLALRLTQKVVINDGLTDRLATVNTDTMVLDS FT SEYEGGPIMPFGENFMVVGNRDIPYVSVGDGNLRIALNQLPDVSTTLFAVDPVKEKMLL FT GAENSGFLDRLVAFESAVSTLDNTGVATARDLAELDANDPVRQDLSKIGVDYASNPALR FT FGIYGMESLAVPIVQNSDAYPPATLDTKVEKLMGSTSGDAEDILRTMGTADFQNVGTES FT LNLSTAFQPFAGSQLSLPWPGTDEIALNSYAGKYEASTIGPLQWSPSSDSGPDKRLTSI FT GVQPQGFTYATSRMNEQVKLGNAGSATGRSLGDSQTYRSTGPIDQDEDGMLPWGFSGMP FT KGKAAAAPIVTGHFEPHKIIGAGTLPLGAYDSSKVNVLDEEGNTQEALEPTLHGLGLAA FT QASSALTTLNGAHTLGIKDPVNAIRVRVGGLTGEMEQDSEKIDAVAASIAGLGLSAYPV FT AGSSPQSVQAFVPKYAFGTDSDSEAQVVDSLGWVALEYTTLGAGITARDAVSTSGAQVA FT SWSQFLVLGSLIALIIIQYPKRRINNNLLVGQSLSYWHRFRWHLSEDIYLVLAVLVLVA FT TLGQRAHLQNADFTRWDSVVPLVVTGLAALVGASLSARVEGQFSSESRTDMGRRLPRLV FT RVISSRLPMLLTKSVALSLIAVAIAFMVDLVVRSNYLLGTTELGKEIASGIIGPSVVSC FT AAAAGSGILILATATQSDLKRQASDWVVATRSAAVRWRNIRSKQVLEHFVMFLLAASLT FT AFLFVVLLSGASLDASSVPVGLATFPNLEILLIGIASIFVVAGSATLLQLALRMARSR" FT CDS complement(900015..900635) FT /transl_table=11 FT /locus_tag="AARI_08010" FT /product="putative ABC transporter, ATP-binding subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT lipoprotein translocase (LPT) family (TC 3.A.1.125.z). FT ABCISSE: ABC transporter, ATP-binding protein (ABC), o228 FT family (members of this family might be involved in a more FT general lipoprotein releasing mechanism common to all FT prokaryotes)" FT /db_xref="GOA:E1VTS0" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VTS0" FT /protein_id="CBT75023.1" FT /translation="MAEKPISYEFSTGAFTVLRGRSGTGKTTLLHTMAGFQAPESGNVY FT WDEQDYYSFSKSKRESLRQENVGWVDQEYGMISSLTVQENIVLGCSRGQIKTLRPMVCE FT LAEALAITHVLKSRPMNISGGERQRAAIIRALIYQSRSAFILDEPTSALDLHSTELVMD FT LLLRKCHNGATLVIASHDQEVIARAEHIIELDHTLTMSDIANP" FT CDS complement(901049..901534) FT /transl_table=11 FT /locus_tag="AARI_08020" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VTS1" FT /protein_id="CBT75024.1" FT /translation="MMTVISAPADLVVATNIGVGVRFAGIESIADVPIVSDEWLGKEGL FT RLYLQGIRSDETRQRDARFEEQLNQWGALRELSGVEAAGDPPSMPGQLVLGVVGAVISD FT DVGTTYRLSAGQVAGGMSGWESTWVYLPAPPKTARVLTLEFTVNGGPTGKICKIQLD" FT gene 901953..902108 FT /pseudo FT /locus_tag="AARI_08030" FT /product="truncated DNA gyrase subunit" FT /note="N-terminal section of a putative DNA gyrase subunit. FT Disrupted by insertion of ISAar3, IS3 family" FT repeat_region 902083..902086 FT /rpt_type=DIRECT FT repeat_region 902087..902124 FT /rpt_type=INVERTED FT mobile_element 902087..903344 FT /mobile_element_type="insertion sequence:ISAar3" FT /rpt_family="IS3 group IS407" FT CDS 902168..902446 FT /transl_table=11 FT /locus_tag="AARI_34650" FT /product="transposase of ISAar3, IS3 family, IS407 group, FT orfA" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTS2" FT /db_xref="InterPro:IPR002514" FT /db_xref="UniProtKB/TrEMBL:E1VTS2" FT /protein_id="CBT75025.1" FT /translation="MARRHTPDQVIAKVRQGQKMLNDGHPMIEVIKELQITEATWYRWI FT NQYGSEKNAEASKRTKELERENARLKKLLADQMLANDILTEVAKGKF" FT CDS 902476..903315 FT /transl_table=11 FT /locus_tag="AARI_34660" FT /product="transposase of ISAar3, IS3 family, IS407 group, FT orfB" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTS3" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VTS3" FT /protein_id="CBT75026.1" FT /translation="MAMEKFGASERFACHVLGQNRSALRKKKTPMSFDEAQLRADLRAV FT ASKHPTWGWRKARWHLLATERWKDTVLNSKRIRRLWREEGLVCKPKRRKKRRTGPDAGE FT QKRLTAEYPMHVLSFDFQSDVTSCGRHIRFFNVIDEYTRTALAIIPRRSFKAADVVAVL FT EDIIAEIGIQPTFVRCDNGPEFTAGALVDWCNTVGVSTAFIDPGSPWQNGFIESFNAQF FT RREQLSGEIMDTMVEAKYLADEWKDIYNHERPHGSLDGLTPSRFWDEWVRENQLAIA" FT repeat_region 903307..903344 FT /rpt_type=INVERTED FT repeat_region 903345..903348 FT /rpt_type=DIRECT FT repeat_region complement(903750..903755) FT /rpt_type=DIRECT FT repeat_region complement(903756..903782) FT /rpt_type=INVERTED FT mobile_element complement(903756..906738) FT /mobile_element_type="insertion sequence:ISAar7" FT /rpt_family="IS21" FT CDS complement(903909..904241) FT /transl_table=11 FT /locus_tag="AARI_08040" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VTS4" FT /protein_id="CBT75027.1" FT /translation="MSVDHDEPVEEHSGEHVEEGQVMGVQIPGRWHPEGLTLEEDLALL FT ASGEGTGWWDESGRPAPWPQDFLDPAAGWSQDGVLAVDWVQGAQVPEVKPLEQLLDEWD FT GAEPPF" FT CDS complement(904238..904969) FT /transl_table=11 FT /gene="istB" FT /locus_tag="AARI_34670" FT /product="helper of transposition of ISAar7, IS21 family, FT istB" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTS5" FT /db_xref="InterPro:IPR002611" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:E1VTS5" FT /protein_id="CBT75028.1" FT /translation="MNPVSVEELVQAGRAASMTASVISEWAHKGTPKQREFLYELLQAE FT HESRTASRHQRLLKAAKLPALKSLVGYDWTSVTFPTDYGREALSDLDFLDHAQDLVLFG FT DVGTGKTHLATALAAAACLRGIPARFFTTASLVMTLRRAKDEGRLDKELGSIAKNQLLV FT IDEFGYLPIDSDGARLLFQVIADGYEKRSLVLTTNLEFKRWGTVFGDDNMAAAVIDRIV FT HHGRLLQFRGQSYRVKHALMK" FT CDS complement(904966..906429) FT /transl_table=11 FT /gene="istA" FT /locus_tag="AARI_34680" FT /product="transposase of ISAar7, IS21 family, istA" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTS6" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VTS6" FT /protein_id="CBT75029.1" FT /translation="MSVQETIRKLDSEGISGRKIAVQLNLSRATVAKYLSITNYSPAPP FT RTGQRPAGSVITGFEETISTWLEGDRGRPRKQRHTAQRVFDRLVDEENYQGTYSPVQRF FT IKRYKQERQSDNDGFLELDWAPGTIQVDFGEAEVILNGEQKVVHLFVVTFPYSNMRFAQ FT AYGGQTAECVCHGLRTVFEHIGSVPHRMIFDNATGVGRRVKTKVLETKLFAAFKAHYRS FT EAKYCNPYSGNEKGNVENAVGFLRRNLMVPLPVAASLEGLNKVLLERCDRLGDKPHWRR FT KILIKDLFAQDVQAGLALPGVGFDPVRYESRKADKYGHLKVGSNTYAAGPVFARRSLTV FT GIRHDVVEILDEQASVLRRFPRIFGDHPEIIMEPSGVLALLAHRPGAWANSPVRAVVSD FT PVRDWMDTAHTEDRRRLLTALDKASETAGFETAIQAAGQIIEQGDDPGHETLSMLARRL FT AEGTEPETGDVDLSVYDRLFAAQEESVLA" FT repeat_region complement(906712..906738) FT /rpt_type=INVERTED FT repeat_region complement(906739..906744) FT /rpt_type=DIRECT FT gene 906750..906962 FT /pseudo FT /locus_tag="AARI_08050" FT /product="truncated resolvase" FT /note="disrupted by insertion of ISAar17, IS21 family" FT CDS 907397..908152 FT /transl_table=11 FT /locus_tag="AARI_08060" FT /product="hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1) with cleavage site probability 0.973 FT between position 26 and 27" FT /db_xref="UniProtKB/TrEMBL:E1VTS7" FT /protein_id="CBT75030.1" FT /translation="MKKRLAIAGLALSGLLLVTSAIPVSAATESKAIQELAAMSPGLPI FT SELKSSLTTYAKENGLTLSQATNKALAENRQSVAAAAPVASKSSSLTQGAAPANAGGGR FT IYNLGSAKQGGDVFVMPAGYGIINHGHTGIFISKTVLVEAPGRNKKSRSTSSLNYKVSK FT GAVKQQVNHIASVKTNAANRAKGLTGKNYNMNFAVNKSASGRDMNCSQLVWAAFKLVNK FT SIDLDGNGGLGVYPYDIKKSSRTTTYKTF" FT CDS 908235..909416 FT /transl_table=11 FT /locus_tag="AARI_08070" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1) with cleavage site probability 0.751 FT between position 32 and 33" FT /db_xref="InterPro:IPR011047" FT /db_xref="UniProtKB/TrEMBL:E1VTS8" FT /protein_id="CBT75031.1" FT /translation="MTRTRPVAITLGTLLALALSGCTGGVETRAPAESNLQDLGQTKYA FT VYLSPPSTDLDAEKGSQGKVLLFEQDGSYQLVETDGMDNGLFAWNEKALFFSDMNNDYK FT IDDSGLEISPSPKTDSQNGMFSTDNGSSIGVYNDGFIENGYASQVVISSDGKSTLHEAE FT GNYFITSQCGDMIYGASRTTGRYTPPGELEKEPMMFAQLTGTKNGSEHVLGSSNLATEG FT AVVPDAPCVDGSVYYLSDASSQSIGDQPKPVLSAWDTRTGKYTEVPLTNVSNDEPLMRD FT DGTGLPQLGSASIRKGAIEWYGAGNAIFTTDLKTGETTHKFNVEGHTSQASSSQAVFTP FT SEVVQLVDNNDGSDYRIIAYDRDTGREVSRTVLPGLVDEFSNDLILRGFAVRP" FT repeat_region complement(909814..909840) FT /rpt_type=INVERTED FT mobile_element complement(909814..911262) FT /mobile_element_type="insertion sequence:ISAar20" FT /rpt_family="ISL3" FT CDS complement(909820..911127) FT /transl_table=11 FT /locus_tag="AARI_34690" FT /product="transposase of ISAar20, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTS9" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VTS9" FT /protein_id="CBT75032.1" FT /translation="MLNSTFTEPDLTTFTGLDGLGLTAIGQYLGAAKAEILCHVTTPNP FT WCRTCGGEGTPRDTVTRRLAHQPFGWRPTVLVIKHRRYRCGHCQRVWREDLSRAAPERQ FT KISRTGLAWALNGLVCQHLSVSRIAEGLGVTWNTANDAVLAEGQRLLIDDPARFSGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLLDMVPGRSKAVFKTWLAGQDDQW FT KQGIDVVAMDGFTGFKTAAAEELPHAVEVLDPFHVVKLGSEALDQTRQRVQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATDKQKAKLEDLFTAPEYEPVQLVWSVYQKMVDAYRQPKP FT EIGRWALEQLINGVGSKVPKGLPELKKLGGTLRRRKTDILAYFDHVGSSNGPTEALNGR FT LEHLRGIALGFKNLTHYIARSLLETGGFRPWLHSQS" FT repeat_region complement(911236..911262) FT /rpt_type=INVERTED FT repeat_region complement(912336..912343) FT /rpt_type=DIRECT FT repeat_region complement(912344..912367) FT /rpt_type=INVERTED FT mobile_element complement(912344..913759) FT /mobile_element_type="insertion sequence:ISAar13" FT /rpt_family="ISL3" FT CDS complement(912376..913653) FT /transl_table=11 FT /locus_tag="AARI_34700" FT /product="transposase of ISAar13, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTT0" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VTT0" FT /protein_id="CBT75033.1" FT /translation="MFKDTGGNDAASILLNLTDYRVIDATQEPAGRQVLIEPKATEAAC FT PTCGVITTRIHARPVHRVKDLPTGGNDIKVLVRKRRMACQETACERRSFVQTTEQLPLR FT ARITTRLSQKLVDEMSCELRAVSRVASAYQVSWPTVMARVNMVGELVGNVDRMFIRRLG FT IDEHRFRKVRYARGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRCAAVKKWLKSRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKISVDHFHVIQRANLMITQVRRRRSHEVLQRR FT GRAADPAYKYRKLLTCNLENLSIRQVERLKLILEADPELGVIYGIKEHVRELLKTRDIH FT DFQSRWAVLEKSVKATKMVEAKSLFRTLTAWRRELLVFIRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRVRILLYTAGLRPC" FT repeat_region complement(913736..913759) FT /rpt_type=INVERTED FT repeat_region complement(913760..913767) FT /rpt_type=DIRECT FT CDS complement(913958..914374) FT /transl_table=11 FT /locus_tag="AARI_08080" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTT1" FT /protein_id="CBT75034.1" FT /translation="MNSRLSSVVSAALLLTMPILAGCSILDPQRDLTLHTFVNSENEGV FT EDATTQPEDITKTACAPPVDCVEAYSTAEADYFRFESKKRAEEYGATVKDGFVINYIVM FT DFAGKEAPVENQLWAMQELAGTWNDYEGDFPDRR" FT CDS complement(914521..915093) FT /transl_table=11 FT /locus_tag="AARI_08090" FT /product="putative resolvase" FT /function="3.3 DNA recombination, and repair" FT /note="match to PF00239. Possibly involved in site- FT specific recombination of DNA" FT /db_xref="GOA:E1VTT2" FT /db_xref="InterPro:IPR006118" FT /db_xref="InterPro:IPR006119" FT /db_xref="InterPro:IPR006120" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="UniProtKB/TrEMBL:E1VTT2" FT /protein_id="CBT75035.1" FT /translation="MGHLLGYARVSTTDQDAQLQLDALSAAGCYRIFTDTASGALESRP FT ELDKLLDQIRPGDTLVVWRLDRLGRSIRHLINHMDALQQRGIEFKSLQESIDTSSSGGR FT LVFNIFASLAEFERDLIRERTNAGLQAARARGRTGGRPASLSPDKLRTAKRLYEQRDMT FT VTQIGEVLGVSRSTVYRALGKAKKNQL" FT CDS 915253..915783 FT /transl_table=11 FT /locus_tag="AARI_08100" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTT3" FT /protein_id="CBT75036.1" FT /translation="MMDQGPGDDSMEFGIRQVAVGGLERAELMQHLAQSGVQLNGFAKQ FT LLEHQIFDELVPAHNLTLTSRNLQQLGLDAGATLPQIFERAVSVGLKLCPAYAGPYLRL FT DFLDQAASDDSVLSAGKKPDGSLTIASASVGDEDFPRGFYLRVVDEVAWLRGYRCDDTN FT GFALADTFVFRCR" FT CDS 915999..916283 FT /transl_table=11 FT /gene="rplY" FT /locus_tag="AARI_08110" FT /product="50S ribosomal protein L25" FT /function="3.7.1 Ribosomal proteins" FT /note="part of the 50S ribosomal subunit. Contacts the 5S FT rRNA" FT /db_xref="GOA:E1VTT4" FT /db_xref="InterPro:IPR011035" FT /db_xref="InterPro:IPR020055" FT /db_xref="InterPro:IPR020056" FT /db_xref="UniProtKB/TrEMBL:E1VTT4" FT /protein_id="CBT75037.1" FT /translation="MASVNLDAVVRSDFGKGAARQARRDGQIPAVVYGAGSEPQHVLLP FT ARETTLAVRDRGVELVLNIEGKTVKTTIKDIQIHALNRTVDHMDLIIAA" FT CDS 916314..916895 FT /transl_table=11 FT /gene="pth" FT /locus_tag="AARI_08120" FT /product="peptidyl-tRNA hydrolase" FT /function="3.7.4 Translation elongation" FT /EC_number="3.1.1.29" FT /note="cleaves the ester bond linking the nascent peptide FT and tRNA when peptidyl-tRNA is released prematurely from FT the ribosome. This ensures the recycling of peptidyl-tRNAs FT into tRNAs produced through abortion of translation and is FT essential for cell viability" FT /db_xref="GOA:E1VTT5" FT /db_xref="InterPro:IPR001328" FT /db_xref="InterPro:IPR018171" FT /db_xref="UniProtKB/TrEMBL:E1VTT5" FT /protein_id="CBT75038.1" FT /translation="MSDGTWLVAGLGNPGAGYAGNRHNIGQMVLDELAQRVGSKFKTHA FT SRSQIVEGRMGVGGPRIVLAKPTVFMNLSGGPVANAAKFFGIGVDRLIVVHDEIDIPFD FT TIKLKRGGGEGGHNGLRDISKAMGSKDYLRVRAGVGRPPGRMDTAKWVLQDFSKAEKAD FT LPFLIDNCADAVELLMTSGLEAAQAKFHTS" FT CDS 917153..918445 FT /transl_table=11 FT /gene="sufS" FT /locus_tag="AARI_08130" FT /product="cysteine desulfurase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.8.1.7" FT /note="cysteine desulfurase catalyses the following FT reaction: L-cysteine + [enzyme]-cysteine <=> L-alanine + FT [enzyme]-S-sulfanylcysteine. It is involved in the FT biosynthesis of iron-sulfur clusters, thio-nucleosides in FT tRNA, thiamine, biotin, lipoate and pyranopterin FT (molybdopterin) and functions by mobilizing sulfur" FT /db_xref="GOA:E1VTT6" 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="InterPro:IPR020578" FT /db_xref="UniProtKB/TrEMBL:E1VTT6" FT /protein_id="CBT75039.1" FT /translation="MTGHQEALEALTAKEVARIKADFEILDHQVNGVDVVYLDSGATSQ FT KPRCVYEAEQHYYENANAAVHRGAHSLAVEATEIYEEAREKVAKFIGARTNELVWTANA FT TEALNLISYSMSNASLGRGGEAAARFRLGPGDEILTTELEHHANLIPWQELAFRTGATL FT RYVPITEDGALRYDLLDELVNENTKLVAFTHVSNVLGTITDTQKFVDAARKVGALTVLD FT GCQSVPHLPVDVKALDVDFMAFSGHKMLGPTGIGALYGREELLNAMPPFLTGGSMITVV FT DMEHAEYMPSPQRFEAGTQRIAQTHGLATAVSYLDEIGMGRIAAWEEHLGQMLYEGISK FT IEGVRVFGPANAPRIGTVPFEVIGVHPHDVGQYLDSRGIAVRVGHHCAQPLHRALGVNS FT TTRASTYLYNTEADITALLEALGSVREYFGV" FT CDS 918446..918898 FT /transl_table=11 FT /gene="sufU" FT /locus_tag="AARI_08140" FT /product="SUF system FeS assembly protein" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="identified by match to protein family TIGR01994. The FT SUF system is an iron-sulfur cluster assembly system that FT operates under iron starvation and oxidative stress. SufU FT may act as a scaffold on which the Fe-S cluster is built FT and from which it is transferred" FT /db_xref="GOA:E1VTT7" FT /db_xref="InterPro:IPR002871" FT /db_xref="InterPro:IPR011341" FT /db_xref="UniProtKB/TrEMBL:E1VTT7" FT /protein_id="CBT75040.1" FT /translation="MNELDQLYQQVILDHAKRRVGSPLVENTEGLLHGESHQHNPICGD FT QIRVRVELGEDGQFTSMSWEGDGCSISMASASVLSEMLPELSKDEFLDKLEIFREMMRS FT KGTFEPDEEVLEDAAAFVGVSKFPARVKCAMLAWVAAEAAMLGAGK" FT CDS complement(918977..920260) FT /transl_table=11 FT /gene="nhaA" FT /locus_tag="AARI_08150" FT /product="Na+/H+ antiporter NhaA" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="NhaA Na+:H+antiporter (NhaA) family (TC 2.A.33.y.z). FT Na(+)/H(+) antiporter extrudes sodium in exchange for FT external protons. Active at alkaline pH. In E. coli, NhaA FT protein probably functions in the regulation of the FT internal pH when the external pH is alkaline. It also uses FT the H+ gradient to expel Na+ from the cell. Its activity is FT highly pH dependent" FT /db_xref="GOA:E1VTT8" FT /db_xref="InterPro:IPR004670" FT /db_xref="InterPro:IPR023171" FT /db_xref="UniProtKB/TrEMBL:E1VTT8" FT /protein_id="CBT75041.1" FT /translation="MRIGDILRKETVGGMVLIAGALLALVWANTPLRESYFALRDFHFG FT PTLFGVDLNLSIGHWAADALLAVFFFLTGLELKKEFVIGDLRNVKTAAVPVAAAFGGVL FT VPALIFVAIASMSGGGELLRGWAIPTATDIAFAVAVLAVIGSALPTALRIFLLTLAVVD FT DLIAIVIIAFVFTDELNLGYLGLSLIPIILFTVLARYLGKFFAKRRWAAWAILLPLGVI FT TWIFVFGSGIHATIAGVVLGFCVPVKRTDGKEGIGLAERFEHRFRPLSSGFCIPIFAFF FT AAGVTVVSPAPGSGSVLTDPVVWGIVLGLVLGKPIGILGFTWVLTKFTKASLDKDAGWG FT DLFGVTLLAGIGFTVSLLVSELSFGLESPHYEHAKVAILAGSFIAAILGALWLIPRNRR FT YKVLQERETRDADKDGIPDVYQQGDEQI" FT CDS complement(920498..920992) FT /transl_table=11 FT /locus_tag="AARI_08160" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR019639" FT /db_xref="UniProtKB/TrEMBL:E1VTT9" FT /protein_id="CBT75042.1" FT /translation="MALNASTQIAHPAEQVIATLSDRGFAEHLTKVANGTLNDFTVNGD FT TAGAFTLTTVRSVPTDRVPDMARKFVGATIEITQVDKWSAPDAAGNRTANVQITVAGVP FT VTVSGTEQLKAQGENSEFAIDAKVSSSIPFIGGKLASAAEPYLGKALKLQADQVNAWLS FT K" FT CDS 921238..924852 FT /transl_table=11 FT /gene="mfd" FT /locus_tag="AARI_08170" FT /product="transcription-repair-coupling factor" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.6.1.-" FT /note="necessary for strand-specific repair. A lesion in FT the template strand blocks the RNA polymerase complex FT (RNAP). The RNAP-DNA-RNA complex is specifically recognized FT by TRCF which releases RNAP and the truncated transcript; FT the TCRF may replace RNAP at the lesion site and then FT recruit the uvrA/B/C repair system" FT /db_xref="GOA:E1VTU0" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR003711" FT /db_xref="InterPro:IPR004576" FT /db_xref="InterPro:IPR005118" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR014001" FT /db_xref="UniProtKB/TrEMBL:E1VTU0" FT /protein_id="CBT75043.1" FT /translation="MSLTGLHDFLREEPSFRRIRQSATHEYATRSEALEIAAPQGMRSL FT LSAHISQALGESKNPGVTLIVTATGREAEEISTSLGAYLPAEQIAEFPSWETLPHERLS FT PRSDTVGRRLEVLRRLHDRDQALNIIIAPIRAVLQPLVAGLGQLRPVRLELDDEPGFDA FT VIKDLAAAAYARVDMVTHRGEFAVRGGIIDVFPPTLDHPVRIDFFGDQIDSMRYFSIAD FT QRSTAEDGPQRIIATPCREMLITPKVMSRAANLKNHFPAAQEMLTKIAGGIAVEGMESL FT APLLVDQMVPLLSLLPECSIALVMEPERVRARAHDLNATNAEFLAAAWASASDGASAPL FT DLNTADSERKLASGDFASLAETVQHAHQAKVSWWALTSMGADEELELGSSTIRIPAREP FT LGYQGDIEAMMEFIAGRVKDQWRFVVATEGPGPAARLSELFADFKIPAHRVEDISATPT FT AGLIEITQATAGRGFVFEELKLGLLTEADLLGRSSAYPNRKGRKLTVKRKRNAVDPLSL FT QAGDFIVHEQHGIGKFVELMARKVNGSGKDAKREYLVVEYASSKRGAPGDRLFVPMDQL FT HMVTRYVGGEAPTLSKMGGSDWSSTKSKARKAVKEIAGDLIKLYSARMASRGHAFGPDT FT PWQNELEEAFAFIETPDQLTAINEVKSDMEKEIPMDRLISGDVGFGKTEIAVRAAFKAV FT QDSKQVAVLVPTTLLASQHHQTFTERYSGFPVRVKTLSRFQTAKESKEILAGLKDGSVD FT IVIGTHRLLSKNVEFKNLGLVIVDEEQRFGVEHKEELKKMRTNVDVLAMSATPIPRTLE FT MSLTGIRETSTLATPPEERHPVLTYVGPRSDKQISAAIKRELMRDGQVFFVHNRVSSIE FT RVAAELRELAPEARIEVAHGKMSESRLERIIQDFWEKKFDVLVSTTIIETGLDISNANT FT LIVDRANNYGLSQLHQLRGRVGRGRERAYAYFLWDVEKPLGEVALERLKAVAAHNELGS FT GYQLAMKDLELRGAGNLLGGEQSGHIAGVGFDLYLRLVGEAVADYKGEGEEESTEMKID FT LPVNAHLPHNYVPGERLRLEAYRNIAQAETNEALAEVREELEDRYGKLPEPVENLLRVA FT ALRIRARAVGLHDIQQVGNHIKVSPAKIEDLPASRQVRLERLYPGSANKPALNSIFIPK FT PKTSPVGGRDLADEAMLDWAENLVYAIFEPTPVAAAKG" FT CDS complement(925175..925582) FT /transl_table=11 FT /locus_tag="AARI_08180" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTU1" FT /protein_id="CBT75044.1" FT /translation="MNWPSAIAAIFVDSLLIWLPAWGALFLDTGNDLVLAIAWVSLVSI FT VNFASYVKGTSVGSLAAGIRFERNQGQAPGKGYALLLSFLSLFSIPVLAVIILIDYLGN FT DIPSKPLSKYPLIGIRTAKRRVLEACDKLWG" FT CDS complement(925774..926274) FT /transl_table=11 FT /locus_tag="AARI_08190" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VTU2" FT /db_xref="InterPro:IPR011990" FT /db_xref="UniProtKB/TrEMBL:E1VTU2" FT /protein_id="CBT75045.1" FT /translation="MGMDYWQQRIDDFWESAQGKDAAALRAELGILLEPAIPAGHAAFE FT LASLHDYLGEEVQAIPLYKTALDSGTLSRAKRSEASIQLGSSLRNIGEPALAAKALNEV FT DPDDPLYADAQAFLALALFDAGEESAALKTALAALAPTLQQYAGPVRRYAQELEDCRPP FT KNR" FT CDS complement(926276..928174) FT /transl_table=11 FT /locus_tag="AARI_08200" FT /product="cation-transporting ATPase" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.-" FT /note="TCDB: P-type ATPase (P-ATPase) superfamily (TC 3.A. FT 3.y.z). Involved in export of cations" FT /db_xref="GOA:E1VTU3" FT /db_xref="InterPro:IPR000695" FT /db_xref="InterPro:IPR001757" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006404" FT /db_xref="InterPro:IPR006416" FT /db_xref="InterPro:IPR008250" 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:E1VTU3" FT /protein_id="CBT75046.1" FT /translation="MKLGQLIRRYPLLAAAVIALLATGAAALAGMDAASRWIAWIAIAG FT AVLWIGAGMVKDLLRGHYGLDILALVAIIACLLVGEYLASLIIVLMLSGGEALEDFAQR FT RATSELSALLDRSPLQAHLAADESGQDVADVPVEQVEVGDLLLVRPGELVPVDGLMRSE FT AGSFDESSLTGEPLPVIHARGSEVMSGSVNGSQAVYLQALRRSSDSQYQQIIALVRQAQ FT DSKAPVVRLADKFAIPFTLLSLLIAGIAWAVSGDPVRFAQVLVLATPCPLLIAVPVAFL FT GGMSRASKEGVVVKGGAVLEQLAKVRSAAFDKTGTLTAGRPALLGIQTQLDPDELLQLV FT ASAEQFSTHVMAAGLTAALADRGLPLLPAEDAQEVATNGVSALVDGRRVAVGKPSFIAA FT IDPALERVELEPGQSAAYVAVDNSFAGVILMADAPRPEASAVLRWMRDHGVENQVMLTG FT DVEQTALGVAAQVGIGKVEAELRPGQKVQLLKDMQPRPVLMLGDGTNDAPALAAADIGM FT AMGSRGSTAAGQAADAVVLRDSLGPVAQVMAISRYTLSVAHSAIWIGIGLSVGLMLVAT FT TGVIPAVTGALLQEVVDLVVIVYALRTLRGPRPADFHGALPTQSTVALAQHVRSRD" FT CDS complement(928320..928487) FT /transl_table=11 FT /locus_tag="AARI_08210" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTU4" FT /protein_id="CBT75047.1" FT /translation="MNPLIPNAYEVVVFYVLPLVITVVLAIVVYKLIRRSTKETELHRN FT SDDQHPDYDS" FT CDS complement(928702..928959) FT /transl_table=11 FT /locus_tag="AARI_08220" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTU6" FT /protein_id="CBT75048.1" FT /translation="MYSNGKNTAHSGEGRLVGNIVTLVIFFVMFAAGIYVLGYWTLEVA FT WWPTLVGFALMFLAFAIPMHLMGRAEKAEDLVAAANAHQN" FT CDS complement(928995..929681) FT /transl_table=11 FT /gene="deoC" FT /locus_tag="AARI_08230" FT /product="deoxyribose-phosphate aldolase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="4.1.2.4" FT /note="catalyzes a reversible aldol reaction between FT acetaldehyde and glyceraldehyde 3-phosphate to generate 2- FT deoxyribose 5-phosphate" FT /db_xref="GOA:E1VTU5" FT /db_xref="InterPro:IPR002915" FT /db_xref="InterPro:IPR011343" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR022979" FT /db_xref="UniProtKB/TrEMBL:E1VTU5" FT /protein_id="CBT75049.1" FT /translation="MTELSAREIASYIDHTLLAQNASREQIVQICEEAKKYEFKSVCVN FT PLWVSTVSRELEGSEVLTCSVIGFPLGASATDTKVFETKHAVADGANEIDMVIDVAAAL FT RGDRDALVNEIFAIAQAAHEGGAILKVIIETCLLTEEAKVLACEAAKAAGADFVKTSTG FT FSTGGATVEDVALMRKTVGPDMGVKASGGVRSVETARAMIAAGATRLGSSSGVAILEGE FT QSGSSY" FT CDS complement(929741..931471) FT /transl_table=11 FT /locus_tag="AARI_08240" FT /product="alpha-D-phosphohexomutase family protein" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="5.4.2.-" FT /note="this family is composed of four related enzymes, FT each of which catalyses a phosphoryl transfer on their FT sugar substrates: phosphoglucomutase (PGM), FT hosphoglucomutase/phosphomannomutase (PGM/PMM), FT phosphoglucosamine mutase (PNGM), and FT phosphoacetylglucosamine mutase (PAGM). PGM (EC:5.4.2.2) FT converts D-glucose 1-phosphate into D-glucose 6-phosphate, FT and participates in both the breakdown and synthesis of FT glucose. PGM/PMM (EC:5.4.2.2; EC:5.4.2.8) are primarily FT bacterial enzymes that use either glucose or mannose as FT substrate, participating in the biosynthesis of a variety FT of carbohydrates such as lipopolysaccharides and alginate. FT Both PNGM (EC:5.4.2.3) and PAGM (EC:5.4.2.10) are involved FT in the biosynthesis of UDP-N-acetylglucosamine" FT /db_xref="GOA:E1VTU7" FT /db_xref="InterPro:IPR005841" FT /db_xref="InterPro:IPR005843" FT /db_xref="InterPro:IPR005844" FT /db_xref="InterPro:IPR005845" FT /db_xref="InterPro:IPR005846" FT /db_xref="InterPro:IPR016055" FT /db_xref="InterPro:IPR016066" FT /db_xref="UniProtKB/TrEMBL:E1VTU7" FT /protein_id="CBT75050.1" FT /translation="MNHTQKIQLLDAAGKWAAQDPDPQTQEELQLLIQRVTEGDALAFE FT DISERFSGVLEFGTAGLRAELGAGPMRMNRVVVMRTAAGIARFLSEQANGQYTPKVVIG FT FDARFNSDVFAQDSAGVFAAAGFEVLLMPSALPTPVLAWAVREFSAEAGVMVTASHNPP FT RDNGYKVYVGGRITDASGRGAQIVSPIDAQIASLIDHEQPVAQIPRALSGWQVLPAIGT FT EGDIEAAYLASIHPIIDAPNEQDAARKNLRIVVSAMHGVGGHTMRQALLNAGFPDVHMV FT AEQEHPDPIFPTVKFPNPEEPGAIDLSLELARKVGADLVIANDPDADRCAAAILDGDAW FT RMLRGDEVGWLLGDQVSKTLPEGKKLANSIVSSRMLAAIAKDAGREHEETLTGFKWISR FT VEDLGYGYEEALGYCVAPELVRDKDGISAGIVLADLAAQLKADGSTISVRLDELAAKHG FT VHVTDQLSLRFTDLAQIPVLMDKIRKNAPASLGGSDVSEVTDLSEGTEKLPATNAMVLH FT TFAGARVIVRPSGTEPKLKCYLETIEPVDDLADVPEARKRATAQVLAIKDELAAYLNAN FT " FT CDS complement(931525..932334) FT /transl_table=11 FT /gene="deoD" FT /locus_tag="AARI_08250" FT /product="purine-nucleoside phosphorylase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.4.2.1" FT /note="catalyzes the cleavage of guanosine, deoxyguanosine, FT inosine, deoxyinosine, adenosine or deoxyadenosine to FT respective bases and sugar-1-phosphate molecules" FT /db_xref="GOA:E1VTU8" FT /db_xref="InterPro:IPR000845" FT /db_xref="InterPro:IPR001369" FT /db_xref="InterPro:IPR011268" FT /db_xref="InterPro:IPR011269" FT /db_xref="UniProtKB/TrEMBL:E1VTU8" FT /protein_id="CBT75051.1" FT /translation="MTDMHNDPQALAAQAAQAIAEQTGVEKHDIALVLGSGWGQAAELI FT GETTHTLDATSIPGFHAPAVPGHKGSISSILTATGKRVLVLGARTHYYEGRGVRAVVHP FT IRTAAATGCEQLVLTNGCGGLNPDWTPGTPVMISDHINLTATSPLEGATFVDLTDLYSS FT RIRGLAREVDATLDEGVYAQFTGPHYETPAEVQYAKAIGADLVGMSTALEAIAARHAGM FT EIFGMSLVTNLAAGISPVPLSHEEVIEAGQAAGPRISKLLAQIIAKL" FT CDS 932452..933861 FT /transl_table=11 FT /gene="lpdA" FT /locus_tag="AARI_08260" FT /product="dihydrolipoyl dehydrogenase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.8.1.4" FT /note="E3 component of pyruvate dehydrogenase and 2- FT oxoglutarate dehydrogenase complexes" FT /db_xref="GOA:E1VTU9" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR004099" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR016156" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:E1VTU9" FT /protein_id="CBT75052.1" FT /translation="MNVSADRRNEATRLVILGGGPGGYEAAMGAAQLGANVTVVERAGM FT GGSAVLTDVVPSKTLIATADAVRRVKHAETFGVHVDGLDSAVTDFSVVNHRLLDLAKEQ FT SSDIRTTLERAGVRIVIGEGRLLDDHTVAVSHPDGSEQKIEADAMLIAVGAHPRELPTA FT KPDGERIFNWTQIYNMNEVPEHLIVVGSGVTGAEFASAYNLLGAKVTLVSSRDRVLPGE FT DADAAGVLEDAFKENGVNVVSQARAEGVERQGDRVLVTLADGRVLEGSHCLVAVGGIPN FT TANMGLEEAGVQLTDSGHIKVDGVSRTTATNIYATGDCTGVFALASVAAMQGRIAVAHL FT LGDSVKPLNLDLVASNVFTSPEIATVGVTQRAVAEGKYQANIIKVDLNTNARAKMMNVD FT QGFVKIVSRKGSGTVIGGVVVAPRASELIFSLALAVQNSLHVDDVAETFTVYPSLSGSL FT AEAARRLHRHR" FT repeat_region complement(933933..933940) FT /rpt_type=DIRECT FT mobile_element complement(933941..935281) FT /mobile_element_type="insertion sequence:ISAAr5" FT /rpt_family="IS256" FT CDS complement(934010..935209) FT /transl_table=11 FT /locus_tag="AARI_34710" FT /product="transposase of ISAar5, IS256 family" FT /function="4.5 Transposon and IS" FT /db_xref="InterPro:IPR018289" FT /db_xref="UniProtKB/TrEMBL:E1VTV0" FT /protein_id="CBT75053.1" FT /translation="MGIESISVKLTGQSHTCIICHSRLKKNGTTSKGTQRWRCITCNAS FT TVFKREDTTARNQLTGFVSWLMSKHSQAEFGGGTGRTFRHQTAWCWNVHPYLHHTGEVF FT DEIQVDGIYLRQGWCLLIAIAHGRVIGWQWCDREKAEAWTVLVQHFPEPKVVVTDGGSG FT LMKALKEFWPNVKIQRCLVHIQRNVRTYLTLNPRLPAGKSLRRLSLKLTKIRTQEAAAE FT WIAAFAAWHAENHELINERTYAADWSGAWPRGLRRNRKWWYTHDRLRSAYESMNKALRR FT GHLFTYLDKDLNGLGINATTNMIEGAVNSGIRAMIFYHRGMPIEHRRRACEWFCWTHAD FT EGNRPALRTLLRPEHYTPETKKKAQHMVDEAPIGPELYGTGPSAEDGQFIRSGWMRNIY FT " FT repeat_region complement(935282..935289) FT /rpt_type=DIRECT FT CDS 935545..936933 FT /transl_table=11 FT /locus_tag="AARI_08270" FT /product="MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (MFS), metabolite:H+ FT symporter (MHS) family (TC 2.A.1.6.z)" FT /db_xref="GOA:E1VTV1" FT /db_xref="InterPro:IPR005828" FT /db_xref="InterPro:IPR005829" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VTV1" FT /protein_id="CBT75054.1" FT /translation="MSQANQAVAPKENTRGRVLFASMIGTTVEFFDFYAYATASVLVFP FT ALFFPNASTINAILSSFAIFGVAFVARPLGSIIFGHYGDKLGRKGTLVASLLLMGIATF FT LIGFLPPAAGNWTVLAPTALVLLRFAQGLALGGEWSGAALLATENAPKNKRAIYGTFPQ FT LGAPIGFIIANLLFVALQTFCTPEQFMAWGWRVPFYFSAVMVVIGLWVRLKLVESASFK FT KVLDQKKVVKSPFAVTMKKHWRPTLAGTFIMLATYVLFYLMTSFTLTYGTQPATVEQAT FT AAAEAKGKTFDATGFVPGLGIERPTFLTMLIIGVVFFGIFTVVSGPLAEKFGRRKFLIW FT VTAGIFVFGLSWTLFFGPGQGAAMAGLIIGFTLMGLTFGPMAAYLPELFPSNVRYTGSA FT VAYNMSSVIGAAPASFVAVALWKAGAGNTTGVGLYLALGAVLTLVALFMTRDTSDMDME FT EWVE" FT gene 937117..937659 FT /pseudo FT /locus_tag="AARI_08280" FT /product="truncated NAD dependent epimerase/dehydratase FT family protein" FT /note="N-terminal section of NAD dependent FT epimerase/dehydratase family protein" FT gene 937738..937857 FT /pseudo FT /locus_tag="AARI_08290" FT /product="truncated NAD dependent epimerase/dehydratase FT family protein" FT /note="C-terminal section of NAD dependent FT epimerase/dehydratase family protein" FT CDS 938047..938415 FT /transl_table=11 FT /locus_tag="AARI_08300" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTV2" FT /protein_id="CBT75055.1" FT /translation="MRLELSRSRIKDGQDENFGAWMDMLNARYEECEASLSAQRAALEA FT TFRHVEADGSTWIYHLSLVGESGGGLDTQQEIDAAHEAASRQAKMPDWEELEPKFLLMP FT DHLKASMAHWAEHGQVPE" FT CDS complement(938487..940271) FT /transl_table=11 FT /locus_tag="AARI_08310" FT /product="acetyl-/propionyl-coenzyme A carboxylase alpha FT chain" FT /function="2.4 Metabolism of lipids" FT /EC_number="6.4.1.2" FT /EC_number="6.4.1.3" FT /note="enzymes named acetyl-coenzyme A carboxylase (EC 6.4. FT 1.2), propionyl-coenzyme A carboxylase (EC 6.4.1.3) and FT acyl-coenzyme A carboxylase are constituted by several FT types of subunits. Alpha subunits contains the biotin FT carboxylase (BC, EC 6.3.4.14) and biotin carboxyl carrier FT protein (BCCP) domains, beta subunits contain the FT carboxyltransferase (CT) domain. An epsilon subunit is FT present in some microorganisms" FT /db_xref="GOA:E1VTV3" FT /db_xref="InterPro:IPR000089" FT /db_xref="InterPro:IPR001882" 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:E1VTV3" FT /protein_id="CBT75056.1" FT /translation="MMNPLTKVLIANRGEIAVRIIRAARDEGIESVAVYADSDRDALHV FT RLADEAYALGGTTAAESYLRIEKILDAAERSGADAIHPGYGFLSENAEFAQAVIDAGLT FT WIGPSPESIDQLGDKVKARHIAEKVGAPLVPGTKDPVASADEVYAFADEHGLPLAIKAA FT YGGGGRGIKVVRNREEIGEMYDSAVREAVAAFGRGECFIERFLDAPRHVETQCLADIHG FT NVVVVSTRDCSLQRRNQKLVEEAPAPFLSEEQTTRLYEASKAILREAKYNGAGTCEFLV FT GQDGVISFLEVNTRLQVEHPVSEEVTGLDLVREQFRIARGEELGYTDPEIRGHSFEFRI FT NGEDAGRNFMPTPGTISKMNLPSGPGVRVDSGIEQGESVSGNFDSMISKLIVTGSTREV FT AAARARRALEEFQIEGMATVLPFHRAVMSDPSFVPAQGPFKVHTRWIETEFDTAIEPHP FT MPMDGEDAAEDERTSVTVEVGGKRLEVTLPSSLGSVSSNGAEKAAGKKKRKPGRKAASS FT AGANSAELRSPMQGTIVKVAVENGEAVAQGDLIVVLEAMKMEQPITAHRDGVVSGLEVA FT PGETLSSGAVIASIEEAK" FT mobile_element complement(940467..941938) FT /mobile_element_type="insertion sequence:ISAar2" FT /rpt_family="IS110" FT CDS complement(940490..941686) FT /transl_table=11 FT /locus_tag="AARI_34720" FT /product="transposase of ISAar2, IS110 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTV4" FT /db_xref="InterPro:IPR002525" FT /db_xref="InterPro:IPR003346" FT /db_xref="UniProtKB/TrEMBL:E1VTV4" FT /protein_id="CBT75057.1" FT /translation="MITTDIEIFLGLDVGKTDHWACAVTQDGTKIWNKTLPNDEAKLTA FT VYQKLLALGHVLVVVDQPATIGALAVAVAQHLGIPVAYLPGLSMRRIADMYPGTAKTDE FT KDAFIIADAARTMPHTLRSIQVSDEDEATLGMLTGFDLDLARQITQTSNRIRGLFTQIH FT PPLERVIGPWLEHDAVLEVLATWPTPAQLKHAGKARIDAKLKKQGARRHTAWAGAIMDA FT LDEQTVVVVGTDAAGLVLPHLARQMISLHAQRVDVATHLEAMVEAHPLYPVLTSMPGVA FT VRTAAIIIAETSGKTFASAASLSSYAGLAPNTRQSGTSIKSERVSHSGNKRLKRALFLS FT AFASIRFDPTSRAYYDRKRAQGKRHNQALIALAHRRLTVLFAMIRDGSLYDVPELKIA" FT CDS 942018..942377 FT /transl_table=11 FT /locus_tag="AARI_08320" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.973) with cleavage site probability 0.445 FT between position 32 and 33" FT /db_xref="UniProtKB/TrEMBL:E1VTV5" FT /protein_id="CBT75058.1" FT /translation="MENKEAAVGNRGKALCALLAAGMLALAGCSSATGIPALDREPAGT FT DQWPGDRSQLENLGMQSVCFLVMHGNADYYAAASADEQKACLFKFAQGEVSAAGGCGGA FT GDADAIVEVRALLRG" FT CDS complement(942651..943139) FT /transl_table=11 FT /locus_tag="AARI_08330" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR010852" FT /db_xref="InterPro:IPR021005" FT /db_xref="InterPro:IPR023286" FT /db_xref="UniProtKB/TrEMBL:E1VTV6" FT /protein_id="CBT75059.1" FT /translation="MRLAASLANDWPSNRDGIEQRTRDVGMTMPFPRLASDYAQTRCVV FT DDWLDIVDAPSEPERAMLLNLQMARASAYPRLVDHDGEGWHLHYRDDGQSMPQVLRSVI FT CVGTALHLTTRGMHRLRRCEAAPCGHVVVDVTRNGRQRFCSVRCANRAAVRRHRERQA" FT CDS 943195..943398 FT /transl_table=11 FT /locus_tag="AARI_08340" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTV7" FT /protein_id="CBT75060.1" FT /translation="MTTTQHSQATESREATDAHEHCWEVESSHQTSTGLVEYFYCRRCR FT RHVMRQRGFGDEQMLLSKELQA" FT CDS complement(943454..944095) FT /transl_table=11 FT /locus_tag="AARI_08350" FT /product="Maf-like protein" FT /function="1.7 Cell division" FT /note="match to PF02545. Maf is a putative inhibitor of FT septum formation in eukaryotes, bacteria, and archaea" FT /db_xref="GOA:E1VTV8" FT /db_xref="InterPro:IPR003697" FT /db_xref="UniProtKB/TrEMBL:E1VTV8" FT /protein_id="CBT75061.1" FT /translation="MSEQLKTEPSLLLASASWGRKKVLTDAGLKFATQVSNVDEDAVLA FT AAVAADGEQSPAQTALLLARAKAEDVATGGHAAGTVVLGCDSVFELGGVAYGKPHTEEV FT ARERWKQLSGSTGVLHSGHWLIDPAHPNQARGQVSSTVVHFSTVSDAEIEAYVASGEPL FT PCAGAFTIDGLAAAFIESIEGNFQNVVGLDVFVLRSLLAQSGISIVDLWK" FT CDS complement(944092..947595) FT /transl_table=11 FT /locus_tag="AARI_08360" FT /product="putative drug exporter of the RND superfamily" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="Resistance-Nodulation-Cell Division (RND) FT superfamily (TC 2.A.6.y.z). C-terminal part of the protein: FT PS50156 domain (sterol-sensing domain). In bacteria, this FT domain is found in a number of drug resistance protein" FT /db_xref="GOA:E1VTV9" FT /db_xref="InterPro:IPR000731" FT /db_xref="InterPro:IPR004869" FT /db_xref="UniProtKB/TrEMBL:E1VTV9" FT /protein_id="CBT75062.1" FT /translation="MASLLYRLARWAHLHRYRVISMWLAAFIFIGLCASLFMGQLSNTF FT TLPGTETQRTLDRMKEELPDLSGGSGSIVFRESSDRPLNETQQNAIAESLDQLALHSQV FT VEAMSPFELQEQLDKAQPELDKAQQELVDGQAKIDDAQKQIADGKEQLKDGREELTKGW FT AEYFDGQKEIQSAEPQIAAAEKQLADSRAQLEAGQRELASGRAQLEAGEAKYKDGLAQY FT NAGKAQYEAGQKQFEAGEQKLDAADAKLAEGEKEYQAGLDQLLGDSSREEFTATLAESK FT QEATAGVKAADDALATAQAGLEEANTAIETLTTQIAGVKQQLAAAEEAGNQEEIAKYTK FT ALNDLQSGLAEAEAGKAAAESGIEQATAGKQQATAALKQIAKAEAGLSSLDAARKELDA FT GQAQAQAGREELEANRSKLTDSKAQLADAKAQLDAAKTEIASNKEKLNQGQAELDAGKT FT KLEAGQREFDAKKAQFLAGKEQLVEAKKQLDAGEKTIKEKTAELEQGEKDVAQGLKDLE FT SGRAELEFASRQVGASSDMRFVSEDGSTAVSQVTFKVQTDALTPDDREQIKAIAAGPQA FT NGVEVLFSKEIMQDMSQVFGASEIIGVIIAAIVLIAMLGTLVAAGLPLLLAILGVGAGV FT GTTMAFSSLIDMASITPALALMLGLAVGIDYALFIIHRHRSQLLGGMEVGESIARAVGT FT SGNAVVFAGLTVIIALAALAVPGLPFLTILGLSAAFTVFCSVILNITLLPALLSLAGNK FT LVSKRARKKAAAQAANPKIKESFSIRWVRMVTKIAVPVTLLVVVVLGAIALPATQMRTA FT LPDGSAEPADSQAFQAYEQTSDKFGSGYNGPLLVLADLPAGLSERQADEMSLDVADKLR FT EYSGVVAAIPVTMTEDRTLAAIQVIPTDGPSSEATEALVHQLRADYAKFSEATGADIAV FT TGQVAAQIDVSEKVTAALVPYLSIVVGLSLILLLLVFRSVVVPLLATGGFLLSLAAAFG FT ASVMVYQFGWFSSVFDVNVPGPLLSFLPILLTGILFGLAMDYQVFLVSAMRERFAHGEP FT AKEAVRSGFSMAAPVVTAAALIMISVFAGFVFSHLAMIRPLGFALAFGVLFDAFIIRMT FT FIPAVMHLLGDKAWYLPKWLDKILPDVDVEGSKLNEMLESGHDDSDAGFEPNQTKENAA FT V" FT CDS complement(947600..948271) FT /transl_table=11 FT /locus_tag="AARI_08370" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00440: bacterial regulatory proteins, FT tetR family" FT /db_xref="GOA:E1VTW0" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR015893" FT /db_xref="UniProtKB/TrEMBL:E1VTW0" FT /protein_id="CBT75063.1" FT /translation="MTSPSSGTRRELNKRATKQAIVEAVADLLRNGAGTALTATQIAEA FT AGVSRRTLFNYFPSVDAVFSYPLHQVLGSMVDSISDLTDSMPLVEAILESLKSDEVSQL FT LGQVAQFGAFLRTEEAKCGFPAMMGEWQNATAEVIEKVARRYPQADSFSIRVFTHAMLG FT AGQAAFDEWIERLPVDETHGLDISPELISVFHSLITRAMKTLDQGFTALPLTSTSTLKD FT I" FT repeat_region complement(948323..948337) FT /rpt_type=DIRECT FT repeat_region complement(948338..948387) FT /rpt_type=INVERTED FT mobile_element complement(948338..949930) FT /mobile_element_type="insertion sequence:ISAar28" FT /rpt_family="IS481" FT CDS complement(948417..949772) FT /transl_table=11 FT /locus_tag="AARI_34730" FT /product="transposase of ISAar28, IS481 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTW1" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VTW1" FT /protein_id="CBT75064.1" FT /translation="MKNDPVNSTIRLAIARWPQDAPRGAVTAFCTEHEISRKTFYQIRK FT RAQTKGQAAALEPRSRRPKKAPTATNEAVKDQAVAMRKALQASGWDHGPISVHDHMKKL FT GMPTVSISALARIFSERGLVTPAPQKRPRSSYRSFRYPMPNSCWQLDATEYVLEGGRKC FT VIFQLIDDHSRLAVASLAAKTENGQDAVKVFRKGIESCGVPQRLLTDNGDALNPIRRGV FT LSELVAYANGLGIATITGKPHKPTTQGKNERLHSTLFKWLKKQPFATDLAQLQAQLDVF FT DHAYNTQRGHQSLEDRMTPQEAWDATPAAEPLELGQWKELSTKPGPSQAQVALGVQAGS FT ERVARQLAAARTPPEPAKLSATLRSELMGESGSHVLRANKNRCLRVAGVEIYLGKLLRS FT TVVNVVWDPTDLMVLSMEGELVAKFDYPFPQGVKYLSLKHATEKFQNMPDPV" FT repeat_region complement(949881..949930) FT /rpt_type=INVERTED FT repeat_region complement(949931..949945) FT /rpt_type=DIRECT FT gene complement(949991..950857) FT /pseudo FT /locus_tag="AARI_08380" FT /product="truncated dicarboxylate/amino acid transporter" FT /note="C-terminal section of a dicarboxylate/amino acid FT transporter. Disrupted by insertion of ISAar19, ISL3 FT family. Dicarboxylate/Amino Acid:Cation (Na+ or H+) FT symporter (DAACS) family (TC 2.A.23.y.z). The members of FT the DAACS family catalyze Na+ and/or H+ symport together FT with (a) a Krebs cycle dicarboxylate (malate, succinate, or FT fumarate), (b) a dicarboxylic amino acid (glutamate or FT aspartate), (c) a small, semipolar, neutral amino acid FT (Ala, Ser, Cys, Thr), (d) both neutral and acidic amino FT acids or (e) most zwitterionic and dibasic amino acids" FT repeat_region 950856..950863 FT /rpt_type=DIRECT FT repeat_region 950864..950887 FT /rpt_type=INVERTED FT mobile_element 950864..952312 FT /mobile_element_type="insertion sequence:ISAar19" FT /rpt_family="ISL3" FT CDS 950999..952306 FT /transl_table=11 FT /locus_tag="AARI_34740" FT /product="transposase of ISAar19, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRG4" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VRG4" FT /protein_id="CBT75065.1" FT /translation="MLNPTFTAPDLTTFTNLDGLGLTAIGQHLSAAKAEILCHVTNPIP FT WCQTCGAAGIPRDTVTRRLAHEPLGWRPTVLVIKHRRYRCANCQRVWREELSQAVAPRQ FT KISRTGLRWALVGLVCHHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFDGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLIDMVPGRSKAVFKTWLADQEEQW FT KQGIEVVAMDGFTGFKTAAVEELPHAVEVLDPFHVVKLGSEALDQTRQRIQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKTKLEDLFKEPEYEPVQLVWSVYQKMVDAYRQPKP FT EVGRWALEQLINEVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRRRLHPQS" FT repeat_region 952289..952312 FT /rpt_type=INVERTED FT gene complement(952297..952791) FT /pseudo FT /locus_tag="AARI_08390" FT /product="truncated dicarboxylate/amino acid transporter" FT /note="N-terminal section of a dicarboxylate/amino acid FT transporter. Disrupted by insertion of ISAar19, ISL3 FT family. Dicarboxylate/Amino Acid:Cation (Na+ or H+) FT symporter (DAACS) family (TC 2.A.23.y.z). The members of FT the DAACS family catalyze Na+ and/or H+ symport together FT with (a) a Krebs cycle dicarboxylate (malate, succinate, or FT fumarate), (b) a dicarboxylic amino acid (glutamate or FT aspartate), (c) a small, semipolar, neutral amino acid FT (Ala, Ser, Cys, Thr), (d) both neutral and acidic amino FT acids or (e) most zwitterionic and dibasic amino acids" FT repeat_region 952313..952320 FT /rpt_type=DIRECT FT CDS complement(953085..953531) FT /transl_table=11 FT /locus_tag="AARI_08400" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.890) with cleavage site probability 0.644 FT between position 24 and 25. 3 transmembrane helices FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="InterPro:IPR021396" FT /db_xref="UniProtKB/TrEMBL:E1VTW3" FT /protein_id="CBT75066.1" FT /translation="MAIITSRIVLVAAFLGAFLVQLVALPAFIQESLHIHPEVQPLARP FT YQWTVNSGILCFQIAIIATWILLAKFARNHKLMHDALPWISLIIWMAALGTFLVLALGV FT HLLGIYGAGGPGVAFMVFTTVSCGTAATVLLIAKRSQVRAQLRQ" FT CDS 953784..954440 FT /transl_table=11 FT /locus_tag="AARI_08410" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTW4" FT /protein_id="CBT75067.1" FT /translation="MPASALFAVSIESGNARIATSPLRELCKREGPDGVKDLRIVPLLY FT SDGRRDPDRTTRIAVGYCRLLQLNSGALKLSIVLQDSWKLEDIPVFIEGVQNDFQVLRQ FT VHGAGQKQDVQEMESSVQHDLEKLVNENASHGGEYLLPRVAKTLCESSRDVMTAVRDLR FT YEFESGLALSSLEAHASDSYTHIVASLLSDQCPVWTSLGSGKGSQPRGAMGLSVR" FT CDS 954559..954942 FT /transl_table=11 FT /locus_tag="AARI_08420" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTW5" FT /protein_id="CBT75068.1" FT /translation="MQLQQQAEMETIAIQSLISSATGISSSREADAQSRFNLLVALLSI FT GIGIGIPGLFLAMYGASELLPLDSMGKLLLFAPVLVSLLGAAVIAWWKAPRGRLGKLWK FT QCAALTVVICAFMVGCAWYFQRL" FT CDS 955060..955449 FT /transl_table=11 FT /locus_tag="AARI_08430" FT /product="putative glyoxalase family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00903: glyoxalase/bleomycin FT resistance protein/dioxygenase superfamily" FT /db_xref="InterPro:IPR004360" FT /db_xref="UniProtKB/TrEMBL:E1VTW6" FT /protein_id="CBT75069.1" FT /translation="MRIYMTSVFVDDQKLAKNFYTEILGFKVKNDIPMGEFSWLTLVSS FT QEEQGTELLLEPSAHPAVGPYRDALKADGIPAASFAVEDVQAEYERLSELGVQFTQEPM FT DAGPVMVATFDDTCGNLIQISSNKS" FT CDS complement(955505..957172) FT /transl_table=11 FT /locus_tag="AARI_08440" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR010281" FT /db_xref="UniProtKB/TrEMBL:E1VTW7" FT /protein_id="CBT75070.1" FT /translation="MTSSAPHREPSAIDQIAETFFAKSLELTPELGVSLGMPGYETTYS FT DYSPAATTMQINLLRETLGSLANATPVDAIDEVSLDAMTERLSLELEILFTGRTELNNI FT ASPAQDIRAMLDLMPQESSEDFAFIAQRMANIPAAIEGYIASLRDSASNGLIAARRQVS FT IVITQTTDYAKDGGFFDQLAASGSTVDSGLQEQLETGAAAAKQAYRQLASFLEDELLAQ FT APQEDAVGREYYSLMSRRFLGAAVDLEETYAWGVAELDAIIEEQQRVAQQIKPGSTIEE FT AKKLLNEDPARKLSGTDSLREWMQGKADQAISELSRTHFEIPAPMDRIECMIAPTQDGG FT VYYTGPSEDFSRPGRMWWSVPPGEDEFTTWAELTTVYHEGVPGHHLQIGTAQMQAATLN FT SWRRLMCWVSGHGEGWALYSERLMHQLGYLDDPGDYMGMLDAQRIRAARVVFDIGVHLG FT LEVPEQWGTGTWNAENGYEFLEKNLDMSKGQLDFEFNRYLGWPGQAPSYKIGQRLWEQI FT RDDLAAAKGENFSLKDFHTAALKLGSVGLDTLKRALVR" FT CDS 957522..963725 FT /transl_table=11 FT /locus_tag="AARI_08450" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="InterPro:IPR003961" FT /db_xref="InterPro:IPR013783" FT /db_xref="UniProtKB/TrEMBL:E1VTW8" FT /protein_id="CBT75071.1" FT /translation="MAKAASTGWTGLLKSTGFKVTAIPVVAALAVTGAIIYPGFETADV FT ELNDGGVWVVNQSEGKIGHVNYQSRTIDGGVATPLANYDLVQHEENVLVRNLEQASLTT FT IDPSMVQFAGDNNLPANSSFSFGAAVVAVTDAEHGTVHASNLDQIADFKGEGAEPLIES FT KGEVAAVVGADDSIWAADMAAGTLSNFALDDDGAAELTLEIEVPELVGMKEPQLSAVGT FT IGVVFDASSGELITSEGDSASIENPANAKIQSPGPETQKVAIALDQSLATVSLSGKDIN FT YEQLETAGTPIQPVRVGSCTYAAWQTSGEYLRFCDDPGNNQSTKIPEMSEGAELAFRVN FT RDVVVLNDVHSGQVWLANEGMEIVSNWSDLEPPAGEGEAKEEETKEITDAIELPNRTEE FT NKKPIAEDDTYSVRPGRTTLLPVLYNDVDPDGDLLTAKLEGAEPSIGTVQPVHDDTGFQ FT IVVPEDAKGGASFVYTTKDGRGGQDTASVKLNVVDEKTNKAPEQQRTTVLRVQQGESVS FT QNLLTDWTDAEGDDLRLLGGTSEGDDVIRVQPDGTLTFQDDGKKLGQKELAIQVSDGQE FT GTKGRVLVEVLADTTVKPVTAADHVVANINESVSFSPLENDTDPTGDGLRLAGVDDVPG FT LELKTNAQTGTVTARAERAGTYYVEYMATNGPASAPGLARIDIKKTEEKAEDPIAVRDV FT ALLPAGQDVLVNVLGNDTDPAGGVLVVTGVQSASDKPFTTSVERNTFVRVTDVRGLTDP FT TTISYTVSNGSREATGSIRVIPIPAPPRMDPPQANPDTVTVRENDVATVKVLENDIHPN FT GAELILRPELEEADDLGEGSLISVADETIRFRAGDFGGKAKQVSAVYTVAGPDGQETSA FT SITFNVQPEAEANDLEKNSPPNPEPVTGRVFAGSSTNVLIPIDAIDPDGDSVSLVQFGD FT SPRMGTAKISGASIDYTANADASGTDEFSYVVEDRLGARATGTIKIGVAPLAESNNSPV FT AVNDFLTVRPNRPVAVDVMDNDTDPDGDPIALMSEVSTESSADVEVVDGRVTLTSPPED FT GNISVRYMISDGRGGTAAGTLSIKSDPEAQLLAPIARDDRVSLEEIIGDEQVNVDILRN FT DEDPDGSTSELEITLPDNPQTAQVSEDGLAITATEDAQIIAYTLTDPDELTSTAFVHVP FT GTAGARPILRSGLNLQVEAGQELPLDLNDLVLVREGHSPRLTTEESVSSMPQNDGELVK FT SATELSFKAPIDFDGSATVSFEVTDGTGPDDDKGLKSKLTLPINVTPAPRSQETEDRQN FT QNEEGQPEEEEEEEQEEEEEEQPEEENFAPTLQANSLAVGQGEEPAFLDLRMAANDANE FT EDVQNLEFAIASVDIQGVQAELVEGHSLKVSAEASTPKGTTGTVTVTVSDGVNPPVPAA FT MNITVTGSVRELPVAVADNVADAAQGKTEVVDVLANDHNPYADEGPLRLINARAMENTG FT EVKKTGDKIAITPNDDFVGTMRVEYTIGDVTEDVARNVIGTVTLNVKGAPRAPGLPRVQ FT STGDQKVVLQWDPPANNGSSITHYTVSGGGHTQQCATTTCTITPLTNDTVYNFTVTATN FT EIGESPASAQSADARPDVEPEQPAAPTGTDGDQQAAFKWTAPVSRGSAIQSYTLEISPA FT PANGVTQITGITGTSYTWKGLKNGTDYQVRVRAVNKASKPSAYSAYSAAVTPAGKPFKP FT SAPTAVRKESAVDGGVVNVAWNAPGTNGAPITGYTLRVFKSGTLEKTIGSIPANQTSQS FT VTGLSTSGSYTFSIAASNRKGRSEQSSKSVAVTPYGRPKAVSSVSATATGANRMVKLNF FT EAPTANGSKITGYQYSTDGGGWNSFGGPGAVIDTGSNGTAHTWRVRALNAAGAGTASPA FT SNKTSAYGPLRDNAKISSSHGKDWIAFSWNQNAGESNGRTVTQTVKIGGSKTKNDGSEK FT VTGLGYSTSRTIKIVATDTEGQSKSWSKTDKTDPKPARSVILSKGPLYNGYSNSTCPPN FT CYKYHVELYDFTPGTYTYLATCHHSGGQFSQDHYLSFTINGQGRASKDLPCVVEPGYAE FT PYFARIDGTESNRTTF" FT CDS 963778..964788 FT /transl_table=11 FT /locus_tag="AARI_08460" FT /product="putative AAA-type ATPase enzymatic complex FT assembly chaperone" FT /function="3.9 Protein folding" FT /note="identified by match to protein family PIRSF002849. FT AAA family proteins often perform chaperone-like functions FT that assist in the assembly, operation, or disassembly of FT protein complexes" FT /db_xref="GOA:E1VTW9" FT /db_xref="InterPro:IPR011703" FT /db_xref="InterPro:IPR016366" FT /db_xref="UniProtKB/TrEMBL:E1VTW9" FT /protein_id="CBT75072.1" FT /translation="MTMSTEQATWFCDTFAKLVSNVGQSVLGKEQAIKLVLAAMLTEGH FT VLLEDAPGTGKTMLARSLAATVQGSNSRIQFTPDLLPSDVTGITIYDQRSGQFDFHHGP FT IFANLVLADEINRASPKTQSALLEVMEEGRVTVDGTTYPQARPFMVIATQNPIEQAGTY FT RLPEAQLDRFLIKTSIGYPDREATVALLSGSAQRDRSAALKPIITTEAVVEMAQLAATV FT HVDTAVLEYVAALCEATREVSETRLGVSVRGALAMVRAAKVWAASQGRNYVLPDDIKEL FT APHIFTHRLVLDPEAEFTGTTATQVISSVLRKVPAPTRRGSEESSPVAGKDQDER" FT CDS 964788..966107 FT /transl_table=11 FT /locus_tag="AARI_08470" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR002881" FT /db_xref="UniProtKB/TrEMBL:E1VTX0" FT /protein_id="CBT75073.1" FT /translation="MNRRAKRSTRSTKLNRRAEKSLTMAGEVLEVLREYLRPAMSRAKE FT FNSRSLAPITSVLSPLGFVLLGTAVLLWILGASFGWQEALLGAFMASLLLVASVGFILG FT RSEFSVELDLHRTRVAVGDRAVGALQVQNKASRSSAPAMMELPVGHGAAQFRIPRLDSQ FT EIHEDLFTIPTQRRQVLDVGPVRSVRQDPFAILRRQVKWTDSYELFIHPRTTALAGSSA FT GFIRDLEGMPTSDLSNSDVSFHALREYQSGDDRRHIHWKSSARTGELMVRQFEETRRSH FT LALSLSTNLEEYSQQHAEEDFELAVSVAASIGQQAVAEQRKLAILTQQGPVRTESGRMM FT MDGLTRIEAAASLRENLVDVVRHTADTVPGASVIFFLTGTGTSAKALREAWMHVPSGVR FT AIAIRCESGTEPTRSSIGELTVLSLGKLDELGLMLRKAVA" FT gene 966104..968089 FT /pseudo FT /locus_tag="AARI_08480" FT /product="truncated transglutaminase-like protease" FT /note="N-terminal section of a putative transglutaminase- FT like protease" FT gene 968086..968457 FT /pseudo FT /locus_tag="AARI_08490" FT /product="truncated transglutaminase-like protease" FT /note="C-terminal section of a putative transglutaminase- FT like protease" FT CDS 968460..969542 FT /transl_table=11 FT /locus_tag="AARI_08500" FT /product="RDD domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF06271. The molecular function of this FT region is unknown. However it be involved in transport of FT an as yet unknown set of ligands" FT /db_xref="InterPro:IPR000253" FT /db_xref="InterPro:IPR008984" FT /db_xref="InterPro:IPR010432" FT /db_xref="UniProtKB/TrEMBL:E1VTX1" FT /protein_id="CBT75074.1" FT /translation="MDLVDARTTQRLVSWLIDFLPVLILSVIFLPMIASEMMKSLSTDQ FT VVGEVAGTYFLYGALTLAYTIFLWWWEATAGKTLGNALLGLRTTTVAGERPGWGKTIIR FT RLLIAVAGIVPILGSVLVVISNHFDENGKKQGWHDKAAGTLVLDIKAGRDPLTTGGSAG FT PASFAPEQQYAPGRRFVGEPEEQSQSSSVIDSVPGAARTNAPQVQKVARPRPVAKPKPK FT AKIVVVSPSKADADPDADLGHTQIRSEAPEALHLLFDDSQCLEVSNSILLGRNPSYADG FT DIGVHLVAVDDPERTVSKTHLLIQPGVDSVWVTDRDSGNGSSIVDKDGNVRELVPGKPE FT QAMAGHVVYFGDRYFQVERP" FT CDS 969539..970366 FT /transl_table=11 FT /locus_tag="AARI_08510" FT /product="protein phosphatase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00481: protein phosphatase 2C" FT /db_xref="GOA:E1VTX2" FT /db_xref="InterPro:IPR001932" FT /db_xref="InterPro:IPR015655" FT /db_xref="UniProtKB/TrEMBL:E1VTX2" FT /protein_id="CBT75075.1" FT /translation="MTDLSPGVSLGFIHGQATDRGLRRTLNEDSLLASERLLAIADGMG FT GHEAGDIASALCLKILGDGFQQAGAHLDPQSLDTLLIEADRNIVEAGSGRAGTTLTGAL FT LIDASSIEDEPVEQPQLLVFNVGDSRTYLWAQGILQQVSVDHSEVQELMDIGQLDAAQA FT ATHPRRHVITRALGINADNRPDYWMVPLSGCERILVCSDGLSSEIGDSAIQEVLAHFPD FT PQQAAEELVQAALDSGGRDNISVIVADVQYGHPDDVGITVPRITTTSHQEEKS" FT CDS 970363..972156 FT /transl_table=11 FT /locus_tag="AARI_08520" FT /product="FHA domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00498. The forkhead-associated (FHA) FT domain is a phosphopeptide recognition domain found in many FT regulatory proteins" FT /db_xref="InterPro:IPR000253" FT /db_xref="InterPro:IPR008984" FT /db_xref="UniProtKB/TrEMBL:E1VTX3" FT /protein_id="CBT75076.1" FT /translation="MNSLRYLPGDWYALVNDEHIVLLPANTSAEQINGLWTKLAGTTTV FT EALLSELLSMYQMNIAALPNFALVSRDSAPHLVLRGALEFAAQSAAGVEEISGAGVTTW FT TERKLGEATSWTLRTGSANLEVAFALPIGSGIVRVSSLSWGTANGSKAGGPADAASTES FT GAEPQKPTVATPKTAEPDKPAAAPAIAKTAEPAKAPAPAAKPAAVAPAPTAKPAAVAPA FT AKPAEPAKAPAPAAKPAAVAPAAKPAEPAKAPAPAAKPAAVAPAAKPAAAPAPAAKPAA FT APAAKPVVAPATTAAKPAEAPKAPAPATAPEKKAEAPKSASDVLARAAKAAEAANAPSY FT NEDSEITQDPRQYEQEAYSEEFSLAGQLLGARGAAETEYATNDGDDLETIIKPRPAAVA FT AAYPVESADDEHTIIRGSSVPKTDTSSSLDAKDGTENSVSLNEFILARSCSKQHPNPPT FT SSTCRECGERLSGQAQQVRKPSMGRMIVSDHGGAREFAHELNRSVILGRQPNAAALKSD FT KEPRLLQVESPSGDISRSHLCVRVEGWHVQLVDLGATNSTVLLREGQRPRRLSRHQEIM FT LINGDVADLGDGVSIRFEDLP" FT CDS 972153..973712 FT /transl_table=11 FT /locus_tag="AARI_08530" FT /product="putative serine/threonine protein kinase" FT /function="4.6 Miscellaneous" FT /EC_number="2.7.11.1" FT /note="identified by match to protein domain PD000001. FT Match to PS00108 pattern. Protein kinases are a group of FT enzymes that possess a catalytic subunit which transfers FT the gamma phosphate from nucleotide triphosphates (often FT ATP) to one or more amino acid residues in a protein FT substrate side chain, resulting in a conformational change FT affecting protein function. They play a role in a FT mulititude of cellular processes, including division, FT proliferation, apoptosis, and differentiation" FT /db_xref="GOA:E1VTX4" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR008271" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR017441" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:E1VTX4" FT /protein_id="CBT75077.1" FT /translation="MSKRRAPAEAPQIPGFTYVKPLGTGGFSDVYLYEQHRPNRQVAVK FT VLLADVSEEEARQQFETEANLMAQLSTHPYIVTIYQAEITQDGRSYLAMEYCSRPSLDA FT RYRRGVLSIDETLSLAIQLCSAVHTAHLAGIVHRDIKPANVLTTDYNRPALTDFGISGT FT IGSHTAGLSVPWSAPEAFGDGMAPGVRMDVYSLGATIYTVLAGHSPFVRPGQDNSQAVL FT IERICNTPLKPLERLDVPDSLNQALAASMAKNPASRFGSAAELARSLQRIQIELGFSVT FT PFEILEEPSESADEQNGETTRVRSVTSISDAQRPLSGGPLISFVPGQRPQQEQPPLPAP FT QQQVRERFQSASVKENESRDDSASPAEAPATPNTRQSLPKIFIAVGAVLVLLIGGAAIA FT NQYLLEPESTQRSGPPITATNEPKDAIVGGTVPMVDNFAFSTVGETVTFRWSNPEPNQG FT DHYRWAHITATETGKFEQTTSPSATTSIGEGGQTCIEVKLVRDDGRISDGARFCTPAGS FT GK" FT CDS 973722..974423 FT /transl_table=11 FT /locus_tag="AARI_08540" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTX5" FT /protein_id="CBT75078.1" FT /translation="MAEVTIEYCGQHYPVHDAKPFTIGREGDLAIDDNPYLHRRFLTIT FT KQNGLWWLNNVGSRLTATIADRTGGLQAWLSPDSSLPLVLNRVAVVFTAGPTTYELSVH FT VAQPAFRQASPEYDDSGETTIGPVLLTRSQRALVVALAEPMLRRDGTGLSSIPTSAAAA FT ARLGWGITKFNRKLDNVCDKLDKAGVVGLRGGPGNLATNRKARLVEHAVSSHLVTRADL FT AVLDSEVLDED" FT CDS complement(974509..974727) FT /transl_table=11 FT /locus_tag="AARI_08550" FT /product="acetyl-/propionyl-coenzyme A carboxylase epsilon FT chain" FT /function="2.4 Metabolism of lipids" FT /EC_number="6.4.1.2" FT /EC_number="6.4.1.3" FT /note="identified by similarity to protein SP: P96886 FT (Mycobacterium tuberculosis). Enzymes named acetyl- FT coenzyme A carboxylase (EC 6.4.1.2), propionyl-coenzyme A FT carboxylase (EC 6.4.1.3) and acyl-coenzyme A carboxylase FT are constituted by several types of subunits. Alpha FT subunits contains the biotin carboxylase (BC, EC 6.3.4.14) FT and biotin carboxyl carrier protein (BCCP) domains, beta FT subunits contain the carboxyltransferase (CT) domain. An FT epsilon subunit is present in some microorganisms" FT /db_xref="GOA:E1VTX6" FT /db_xref="UniProtKB/TrEMBL:E1VTX6" FT /protein_id="CBT75079.1" FT /translation="MEQNTALPVAPQIRVTKGNPSDEELAVVTALLAAMGNAPAAEPET FT VEPKKRVARIRRRRALAPRLGWTIGRR" FT CDS complement(974777..976387) FT /transl_table=11 FT /locus_tag="AARI_08560" FT /product="acetyl-/propionyl-coenzyme A carboxylase beta FT chain" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="6.4.1.2" FT /EC_number="6.4.1.3" FT /note="enzymes named acetyl-coenzyme A carboxylase (EC 6.4. FT 1.2), propionyl-coenzyme A carboxylase (EC 6.4.1.3) and FT acyl-coenzyme A carboxylase are constituted by several FT types of subunits. Alpha subunits contains the biotin FT carboxylase (BC, EC 6.3.4.14) and biotin carboxyl carrier FT protein (BCCP) domains, beta subunits contain the FT carboxyltransferase (CT) domain. An epsilon subunit is FT present in some microorganisms" FT /db_xref="GOA:E1VTX7" FT /db_xref="InterPro:IPR000022" FT /db_xref="InterPro:IPR000438" FT /db_xref="InterPro:IPR011762" FT /db_xref="InterPro:IPR011763" FT /db_xref="UniProtKB/TrEMBL:E1VTX7" FT /protein_id="CBT75080.1" FT /translation="MTQGRTEAAESIDLSTTAGKLAEFRRRQKLSEAPSGEAAIEKQHS FT RGKHTARERIEMLMDEDSFVEFDALAVHRSTAFGMEKKKPLGDGLVSGYGTVDGRLVAV FT YSQDFTVYGGSLSQVNGEKIVKVQEFALRNGCPVVGILDGGGARIQEGVASLAMFADIF FT RNNVHASGVVPQISLIMGPSAGGAAYSPALTDYVIMVDKTSHMFITGPDVIKTVTGEEI FT DMETLGGARQHNANTGTATYLASDEEDAIDFCKDLLDFLPSSNLADPLIAEFDEELEIT FT ADDLELDTLIPDSANQPYDMRTIIESIVDDAHFFEMQSLYAPNVMIGYARVEGRTVGIV FT ANQPMQFAGTLDIAASEKAARFVRNCDAFNIPILTFVDVPGFLPGKDQEFQGIIRRGAK FT LLYAYAEATVPKLTVITRKAYGGAYIVMGSKKLGADLNLAWPTAQIGVMGAQGAVNILY FT RRDLAAVEAEGGDVEARRKQIIDDYEAELLNPYQAAELGYVDAVIAPSETRFQLVRGLR FT ALREKHATLPPKKHGNIPL" FT CDS 976584..977441 FT /transl_table=11 FT /locus_tag="AARI_08570" FT /product="short-chain dehydrogenases/reductases family FT protein" FT /function="2 Intermediary metabolism" FT /note="identified by match to PF00106. The short-chain FT dehydrogenases/reductases family (SDR) is a very large FT family of enzymes, most of which are known to be NAD- or FT NADP-dependent oxidoreductases" FT /db_xref="GOA:E1VTX8" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VTX8" FT /protein_id="CBT75081.1" FT /translation="MTSESRTHIAPEPGNLKGRTILMSGGSRGIGLAIALAAAKQGANL FT VLLSKTDTPHPTLEGTIHTAVEQINAAGGKGMAVVGDVREDADVQRAVQEAVVKFGGID FT IVVNNASAINLAKTDQVDMKRYDLMQDINVRGTFLLSKTALPYLRDSAHAHILTLSPPL FT NLDPKWAGQHLAYTMAKYGMSLTTLGLAEELKDEGVGVNSLWPETLIDTAAIRNLPGGQ FT QMVQGARDASVVADAAMAILASPPAGVSGNFFTDGQVLTLAGETNLEKYTLNPEVPLVQ FT DIFL" FT CDS 977498..978364 FT /transl_table=11 FT /gene="birA" FT /locus_tag="AARI_08580" FT /product="biotin-(acetyl-CoA carboxylase) ligase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="6.3.4.15" FT /note="acts both as a biotin-operon repressor and as the FT enzyme that synthesizes the corepressor, acetyl-CoA:carbon- FT dioxide ligase. This protein also activates biotin to form FT biotinyl-5-adenylate and transfers the biotin moiety to FT biotin-accepting proteins" FT /db_xref="GOA:E1VTX9" FT /db_xref="InterPro:IPR004143" FT /db_xref="InterPro:IPR004408" FT /db_xref="InterPro:IPR008988" FT /db_xref="UniProtKB/TrEMBL:E1VTX9" FT /protein_id="CBT75082.1" FT /translation="MENPHGTDRAVIDSQLFTKLTAELGLGLVALKKTSGSTNTELAQL FT ASTGEAGHLSVYFTEHQQAGKGRLGREWVTPEGSSLTLSVLVAPGAGFPAQSLSWYTML FT AALAWSRAAENISGVKLGIKWPNDLLAGEQKVCGILAQMVPTGDSYAVVVGTGVNVNQE FT RKELPVPTATSLRLAGAKDLNRTVLLAEYLKQFAALDQSFRQVAGVAQMPLPGNGGKSL FT LELVSEKLVTLGHEVRVEFPDGSTLVGNAVQLGSDGSLVLEYGAGERKHVLAGDVHHVR FT RADGKYA" FT CDS 978451..978999 FT /transl_table=11 FT /locus_tag="AARI_08590" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTY0" FT /protein_id="CBT75083.1" FT /translation="MKLPLHERERVIIKTREHSRVLRQPVGAFLFLTALCAFCLGYLSR FT DDLSEWLAANADVWMIVSVVLWAALVLIWSVIPWARWLRSQIVLTTERIMFRPTYNDGK FT LQSVGLFTVRDLVAHTKAKNAMTRAGTLDIVLNQGYVRLAHVPSVPYFRSLAMDAMTNL FT RSNQHVAYTETTNSEGMGA" FT CDS 978996..980207 FT /transl_table=11 FT /gene="cya" FT /locus_tag="AARI_08600" FT /product="adenylate cyclase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="4.6.1.1" FT /note="identified by similarity to protein SP:P27580 FT (Arthrobacter nicotianae). Plays essential roles in FT regulation of cellular metabolism by catalyzing the FT synthesis of a second messenger, cAMP" FT /db_xref="GOA:E1VTY1" FT /db_xref="InterPro:IPR001054" FT /db_xref="UniProtKB/TrEMBL:E1VTY1" FT /protein_id="CBT75084.1" FT /translation="MSTEHTNTPRADSPQSAAEAVRGARQHPPVATPAESDPILELAQA FT MEGPLRIPAHTPDAVRDTVASLERRLIGGQREFRRREVASEAGVSLHSARKLWRAIGFP FT ELSDDEVFFTQADKEALGTMVGMVREGKLTEETAISLMRSVGQMTDRMVVWQIEALVED FT MIANQNMSDRQARRQLFSLLPEIIPAIEDLLLYSWRRQLNSAVHRMALRVETGVAAYQQ FT DSGESDGGTPLPLARAVGFADLVSYTSLSRRMNERTLAQLVQRFEAKCAEIISVGGGRL FT VKTIGDEVLYVAETPQAGAQIALSLSRELAKDEMFPQTRGAVVWGRLLSRLGDIYGPTV FT NMAARLTSLAEPGSVLTDAITANTLRNDARFVLTAQEITAVRGFGDIQPYELSAGEGEG FT LVID" FT CDS 980207..981163 FT /transl_table=11 FT /locus_tag="AARI_08610" FT /product="protein phosphatase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00481: protein phosphatase 2C" FT /db_xref="GOA:E1VTY2" FT /db_xref="InterPro:IPR001932" FT /db_xref="InterPro:IPR015655" FT /db_xref="UniProtKB/TrEMBL:E1VTY2" FT /protein_id="CBT75085.1" FT /translation="MSKEPAPVPFILAAAGLTDVGRKRTENQDRILMHDIVYAVADGMG FT GHEAGEVASQLAVETMQEICVFANKTSVRKLPTVPDVQRQVQLADDRIREALESRGGTT FT LCALVQIKTPGKSRDSVTAPLAAVPPWTSSFAMTQNTDVISKITPQMLEHHRANLAPAT FT EPITVVTEEIPSLLLVNVGDSRGYRLRDGALQQLTRDHSAVQEMVDAGQITELEARNHP FT HRNLITRALGAGAESQPDVTVLHPRIGDRYMLCSDGLSGELTEDILQTLLVNYKDRADA FT ARVLTGAALEAGGRDNIAVIVIDVLATPSVETDAPEN" FT CDS 981184..983487 FT /transl_table=11 FT /gene="ligA" FT /locus_tag="AARI_08620" FT /product="DNA ligase" FT /function="3.1 DNA replication" FT /EC_number="6.5.1.2" FT /note="catalyzes the formation of phosphodiester linkages FT between 5 prime-phosphoryl and 3 prime-hydroxyl groups in FT double-stranded DNA using NAD as a coenzyme and as the FT energy source for the reaction. It is essential for DNA FT replication and repair of damaged DNA" FT /db_xref="GOA:E1VTY3" FT /db_xref="InterPro:IPR001357" FT /db_xref="InterPro:IPR001679" FT /db_xref="InterPro:IPR004149" FT /db_xref="InterPro:IPR004150" FT /db_xref="InterPro:IPR010994" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR013839" FT /db_xref="InterPro:IPR013840" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR018239" FT /db_xref="UniProtKB/TrEMBL:E1VTY3" FT /protein_id="CBT75086.1" FT /translation="MLRWGTIEYVSEKDVAPVETTNVPPEADKTRYDQLVEQIRAHRDA FT YYQNDAPLVSDVEYDALFHELQLLEATYPILAGQDSPTQEVGGEVSAAFASVTHASRMY FT SLEDVFSLDELEAWLERAQANAERLHPQTPVRWLCEVKIDGLALNLTYRDGKLVRAATR FT GDGTTGEDVTHNALTISDIPQQLEGSGWPAEFEVRGEVFIATEDFNKFNEALIAQGKAP FT LANPRNAAAGSLRQKDPAQTAKRPLRMFVHGLGRSRDFKLTEQSQAYELMRGWGLPVSP FT YGRVVDSRQAAKDYIAEHGEKRHDLIHDIDGIVIKVDDLATQEQLGYTSRVPRWAVAYK FT YPPEEVHTKLLDIQVQVGRTGRVTPFGVMEPVLVAGSTVARATLHNQEVVKAKNVKIGD FT TIILRKAGDVIPEIVGPVLPLREGNDELRDFIMPTECPSCGQPLAPAKEGDVDIRCLNA FT ESCPAQLTERVAYLGGRSALDIEALGYEAAAALTSGPGEDPATLGGIILPAGPGPLKNE FT AELFNLKDKLEELGEVKVWREKRVKGEGTGKFELVPYFYSKATAKKPSAPTKSTMKLLD FT ELEKAKDNPLWRVLVALSIRHVGPNASRAIATRYGSMDALLEVLDSGNAEAELSEIDSV FT GSIIAEALVDWFKVDWHREIVASWQAAGVKMQDEQDENITKNLEGLAIVVTGTLENYSR FT DTAKEAIIVRGGKATGSVSKKTDFLVAGEAAGSKLDKAQSLGVPVLDEAGFGVLLEQGP FT DAAREVALAAPTEG" FT CDS 983490..984290 FT /transl_table=11 FT /gene="suhB" FT /locus_tag="AARI_08630" FT /product="putative inositol-phosphate phosphatase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="3.1.3.25" FT /note="catalyzes the following reaction: myo-inositol FT phosphate + H(2)O <=> myo-inositol + phosphate. Acts on FT five of the six isomers of myo-inositol phosphate, all FT except myo-inositol 2-phosphate, but does not act on myo- FT inositol bearing more than one phosphate group" FT /db_xref="GOA:E1VTY4" FT /db_xref="InterPro:IPR000760" FT /db_xref="InterPro:IPR020583" FT /db_xref="UniProtKB/TrEMBL:E1VTY4" FT /protein_id="CBT75087.1" FT /translation="MERAVTHDPLVLVARRAAAAGAEVLGRRDESQFNLTDKSAAGDWV FT TDFDRASEEAIRATILTSRPNDELTGEEYPSAKPANPSGFRWSIDPLDGTTNFVRNIAY FT YCSSVGVCQRNADGSETWVAAGIVAPALQVEYFAGKGLGAWKQDLRTGKLTQLAGPAES FT EAKILATGFGYDAQRRQFQANVLGQMLEDYVNVRRLGSAALDLCLVAEGSLDAYAEYGT FT QEYDWAAGALIAEEAGCLVGRPSTNPGWQYAGLVDPAKLTEPEA" FT CDS complement(984287..984898) FT /transl_table=11 FT /locus_tag="AARI_08640" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="5 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTY5" FT /protein_id="CBT75088.1" FT /translation="MQQRTAASSTSTVRKIALLVSHLLSPIILATILLLVTPWRDSSVR FT WSESVVAALFTTIIPWLILAGAKLRGKVTDMHVTVRHQRHRIYAYTAGLILCGLLVLQL FT MDAGAGIFIEVLSILLGLAVVAVINFRWKVSVHLAVGTYVILQIAGAQSALMPLILCFI FT AVLSWARIRSFQHTATQVCGGVAVGVVIHYAHQGLATVLG" FT CDS 985105..985461 FT /transl_table=11 FT /locus_tag="AARI_08650" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.959 FT between position 37 and 38" FT /db_xref="UniProtKB/TrEMBL:E1VTY6" FT /protein_id="CBT75089.1" FT /translation="MRSVSSLIIRNSMISAVLVAVAATGILLVIATPKSVADKYCEAEQ FT PQLIYEEGKQGTKATVMAVAPACELDLPEGTEYPLALGPSETVSRHRADLMIPVNSDGS FT FSHELPLDASDLTG" FT CDS complement(985576..986025) FT /transl_table=11 FT /locus_tag="AARI_08660" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTY7" FT /protein_id="CBT75090.1" FT /translation="MAVYFECVTHADAPCAELFEKSLSIDAHTGSMAESGEQAVAGVTS FT GSIGLGEQVTWRAKHFGIPFRMTSRISDLQAPRTFTDQQVRGPFKSFHHVHDFHELEHG FT TLMVDKIHFSAPLGPLGWLAERLVLGWYMPKLIRIRNEYLVKMQG" FT gene complement(986053..986346) FT /pseudo FT /locus_tag="AARI_08670" FT /product="truncated glucosamine-6-phosphate isomerase" FT /note="C-terminal section of a glucosamine-6-phosphate FT isomerase (EC 3.5.99.6. Presence of one or more frame- FT shift mutations which are not the result of sequencing FT errors" FT gene complement(986108..986857) FT /pseudo FT /locus_tag="AARI_08680" FT /product="truncated glucosamine-6-phosphate isomerase" FT /note="N-terminal section of a glucosamine-6-phosphate FT isomerase (EC 3.5.99.6. Presence of one or more frame- FT shift mutations which are not the result of sequencing FT errors" FT CDS complement(986931..988061) FT /transl_table=11 FT /locus_tag="AARI_08690" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00480: ROK family" FT /db_xref="InterPro:IPR000600" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VTY8" FT /protein_id="CBT75091.1" FT /translation="MTSPRKDWNVLSHGSAILPSHGREHNLSLVLQTLADQGALSRADL FT ARATGLTRVTVSELVAELLHRSHVIETGTQEGKRPGKPSTLVDLNRPGLRIIGVDLSGI FT IPFRAAIMDLDGVILQSFSSQGRGATGQDAADQLLELLDTALAQCQVPVLGIGIGSPGV FT VTDKGIVLSAEKFGWRDYDLRSAVEQATGISTHVLNDADCAILAEHTFGQGSGHMILLR FT LGRGVGCGVITHNTLVRGAGFAAGELGHVRLHAQDTAECSCGNIGCLETCISLPAIWKA FT LSEGQPKNQLDQQVAAYLASAVAPLLSVLDIRNVIFTGPRDVVDQALAQALHEALALRS FT HTARASDFRLVLSEDPEHLVLRGSAVNVLFHELGIA" FT CDS 988273..988803 FT /transl_table=11 FT /locus_tag="AARI_08700" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VTY9" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VTY9" FT /protein_id="CBT75092.1" FT /translation="MTDAQTFSFSTGDLSIELAAPEHYQRVGELTAESYFAAGHFDSPD FT NQYLQFVRKVAERAAQTEIYVVRRAGEIIGSMTLIRAGSEYADIARADELEIRMLSVDP FT AVQRSGVGRFMVQASIERARLLPGINAVSLTTGSSWKTARNLYESMGFTHFPERDWVVP FT NTEIKLVVYAYSL" FT CDS 988895..990808 FT /transl_table=11 FT /locus_tag="AARI_08710" FT /product="penicillin-binding protein" FT /function="1.1 Cell wall" FT /note="match to PF00905. The large number of penicillin FT binding proteins, which are represented in this group of FT sequences, are responsible for the final stages of FT peptidoglycan biosynthesis for cell wall formation. The FT proteins synthesise cross-linked peptidoglycan from lipid FT intermediates, and contain a penicillin-sensitive FT transpeptidase carboxy-terminal domain" FT /db_xref="GOA:E1VTZ0" FT /db_xref="InterPro:IPR001460" FT /db_xref="InterPro:IPR002137" FT /db_xref="InterPro:IPR005311" FT /db_xref="InterPro:IPR012338" FT /db_xref="UniProtKB/TrEMBL:E1VTZ0" FT /protein_id="CBT75093.1" FT /translation="MSAIRRSVVALSVASLVMGSLSACSAGAPDPAPSADALASAMNSG FT DFSGVQFAGSNAEEAAKALETAFGSMGEIKHTSTVSSAAEDEEEQDGVKTATVNITTVW FT DVDKSDKDLSYDTQAVWEFDSEAEAWKLRLDPAIFAPEFESGDYLKASFEPAARGNITD FT AEGASIVTNRPVIRVGMDKTHTEKENWESSAKKLAKLVDIDEKAYAQRVMAAGEKAWVE FT AIVLRDDATREVTDAEIKDIPGANFHNDELPLAPTRSFARPLLGSVGKATAENIEKSEG FT KVKAGEQIGQSGLQAAYNDTLAGTAGVSVSQYTAEHDAVAELFTTAAAAGEDVKTTLDV FT KLQDAADDLLAEADSNSAIVVIRPSDGSVLAASSGPVSSGLNTSLQGSYAPGSSFKVVS FT ALAMLRDGATPSTKVKCPATAVVDGKSFKNYDGYPASAVGTIPLAEAIAQSCNTIFVNQ FT GQDIGGKKLAEAAAALGLLAEDGTGTGAVFGSVPEDSEGTTQAANMIGQGVVESSPLGM FT ATVMASIQAKSTVQPKLVLEPAPQAPAKPASTLTEEEAEQLSTMMAEVVDHGTLKDLKS FT AGSGKIIGKSGTAEYDSEKNAHAWAIAAQGDLAIAAFVEDGDGGAQSAGPLVKSMLEEA FT AK" FT CDS complement(990826..991425) FT /transl_table=11 FT /locus_tag="AARI_08720" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VTZ1" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VTZ1" FT /protein_id="CBT75094.1" FT /translation="METSQGWNSIDQAQQYGENLLRDAVIDLRESEQEDFAHMAGWWNA FT PAWAVLQQRTIKPRPEAPLAEMFAQWSRNIPYSGDAGFSIFERGTGTFIGHITLHGGVL FT PHRAAELAVMIGPDFVGQGFGTRAIKLMTGYGFRELGLHRISLCVAVFNPRAIRSYEKA FT GFTLEGRQREVYFHNGQFHDQVLLSLLSHEYFARQG" FT CDS 991511..992062 FT /transl_table=11 FT /locus_tag="AARI_08730" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTZ2" FT /protein_id="CBT75095.1" FT /translation="MGIVYNTTMSPTKVELVTQWLKEQDFYAGQGAPELENIGGFRLED FT PRGEVGIELLIFADHSDTSDVVYHVPLTYRDAPLEGAETYLLGTSDHAILGERFIYDAA FT GDPVFAAQARELLAGKVSAQHRHESFTEDPRITLCADTAGKDAVIIRRPVASKPAQAGV FT LGIWENALGQELSGLVLRTA" FT CDS 992147..992443 FT /transl_table=11 FT /gene="gatC" FT /locus_tag="AARI_08740" FT /product="aspartyl/glutamyl-tRNA amidotransferase subunit FT C" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.3.5.-" FT /note="allows the formation of correctly charged Asn- FT tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of FT misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms FT which lack either or both of asparaginyl-tRNA or FT glutaminyl-tRNA synthetases" FT /db_xref="GOA:E1VTZ3" FT /db_xref="InterPro:IPR003837" FT /db_xref="UniProtKB/TrEMBL:E1VTZ3" FT /protein_id="CBT75096.1" FT /translation="MSAISREDIVHLAHLAHIEMSDAELDKMTGELDAIVGAIASVSEV FT AASDVPATSHPIPLTNVLREDTVGQTLSIEEVLLNAPDSDSDRFKVPAILDGE" FT CDS 992448..993986 FT /transl_table=11 FT /gene="gatA" FT /locus_tag="AARI_08750" FT /product="aspartyl/glutamyl-tRNA amidotransferase subunit FT A" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.3.5.-" FT /note="allows the formation of correctly charged Asn- FT tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of FT misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms FT which lack either or both of asparaginyl-tRNA or FT glutaminyl-tRNA synthetases" FT /db_xref="GOA:E1VTZ4" FT /db_xref="InterPro:IPR000120" FT /db_xref="InterPro:IPR004412" FT /db_xref="InterPro:IPR020556" FT /db_xref="InterPro:IPR023631" FT /db_xref="UniProtKB/TrEMBL:E1VTZ4" FT /protein_id="CBT75097.1" FT /translation="MNELIKLSATELAAKLRAGETTSVEAVQAHLDRITEVDGTLNAFL FT HVNAEEALAVAAEVDAIRAAGGSEAEALHPLAGVPIAIKDLIVTKGQPTTAASKMLEGW FT MSPYDATVIEKIRAAKLPMLGKTNLDEFAMGSSTEHSAYGVTRNPWDLNRIPGGSGGGS FT AAAVASFEAPLALGTDTGGSIRQPGAVTGTVGVKPTYGAVSRYGAIAMASSLDQIGPVS FT RTVLDSAYLQELIGGHDPKDSTSLPKDLEGLVSAAESGAAGDLTGLRIGVVKELQGEGY FT QDGVQARFDESLELLKAAGAQIVEVSCPNLKYALGAYYLIMPSEVSSNLAKFDGVRFGH FT RVLPEEGPMTIERVMGSTRAAGFGDEVKRRIILGTYALSAGYYDAYYGSAQKVRTLIQR FT DFDAAFEQADVLVSPTTPTVAFELGANDNDPLAMYLNDVATIPANLAGIPGITVPGGLS FT ENLPVGIQFLAPAYEDARLYRAGAALETLLEKQWGHSLISQAPAIDTASIAQEA" FT CDS 993992..995500 FT /transl_table=11 FT /gene="gatB" FT /locus_tag="AARI_08760" FT /product="aspartyl/glutamyl-tRNA amidotransferase subunit FT B" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.3.5.-" FT /note="allows the formation of correctly charged Asn- FT tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of FT misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms FT which lack either or both of asparaginyl-tRNA or FT glutaminyl-tRNA synthetases" FT /db_xref="GOA:E1VTZ5" 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/TrEMBL:E1VTZ5" FT /protein_id="CBT75098.1" FT /translation="MSNYTDELVDFDTALDRYDPVLGFEVHVELNTKTKMFSDAPNAFG FT DAPNTNVTPVDLGLPGVLPVVNKTAVEYSILIGLALNCQIAQKCGFARKNYFYPDTPKN FT FQTSQYDDPIAFDGYLDIELEDGEVFRVEIERAHMEEDAGKLTHMGGATGRIQGADYSL FT VDYNRAGVPLVEIVTKPIVGAGKRAPELAKAYVAAVREIVKNLGVSDAKMERGNVRCDA FT NVSLMPKGADKFGTRTETKNVNSLRAVEHAVHFEIERHAAVLDSGAKIVQETRHWHEDT FT RSTTSGRPKSDADDYRYFPEPDLVPIVTTAEWVEELRGRLPEPPAERRKRLKAEWGYAD FT KEFRDVVNAGVLDEIEQTIAAGASAAVARKWWMGEIARLAKAADKDIADLGVTPATIVE FT LNSLIEAKKINDKIARQVLEFVIAGEGTPSEIVEKRSLAVVNDDGALGKAVDDAMAAMP FT DVVEKIKGGKMQAIGALMGPVMKATRGQADAGRVREIVMEKLGL" FT CDS complement(995715..995840) FT /transl_table=11 FT /locus_tag="AARI_08770" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VTZ6" FT /protein_id="CBT75099.1" FT /translation="MGFEALVRYLATPANAVKFVIRRIGIAGAFSCVGGIIGLYI" FT CDS complement(996223..996510) FT /transl_table=11 FT /locus_tag="AARI_08780" FT /product="hypothetical membrane protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VTZ7" FT /protein_id="CBT75100.1" FT /translation="MGRMLTWLGLGNRQNNESLPLWHGVDEKTKWGSLLVCMGIAFVAF FT LITNWLLEGTSSAPTYLALLISAGTLLISTLIAERSLTRVTPDEKSNEGD" FT repeat_region complement(996574..996581) FT /rpt_type=DIRECT FT repeat_region complement(996582..996605) FT /rpt_type=INVERTED FT mobile_element complement(996582..998030) FT /mobile_element_type="insertion sequence:ISAar19" FT /rpt_family="ISL3" FT CDS complement(996588..997895) FT /transl_table=11 FT /locus_tag="AARI_34750" FT /product="transposase of ISAar19, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRG4" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VRG4" FT /protein_id="CBT75101.1" FT /translation="MLNPTFTAPDLTTFTNLDGLGLTAIGQHLSAAKAEILCHVTNPIP FT WCQTCGAAGIPRDTVTRRLAHEPLGWRPTVLVIKHRRYRCANCQRVWREELSQAVAPRQ FT KISRTGLRWALVGLVCHHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFDGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLIDMVPGRSKAVFKTWLADQEEQW FT KQGIEVVAMDGFTGFKTAAVEELPHAVEVLDPFHVVKLGSEALDQTRQRIQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKTKLEDLFKEPEYEPVQLVWSVYQKMVDAYRQPKP FT EVGRWALEQLINEVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRRRLHPQS" FT repeat_region complement(998007..998030) FT /rpt_type=INVERTED FT repeat_region complement(998031..998038) FT /rpt_type=DIRECT FT gene 998371..998517 FT /pseudo FT /locus_tag="AARI_08790" FT /product="truncated protein" FT /note="similarity with part of protein SP:OB0294 FT (Oceanobacillus iheyensis)" FT gene 999741..1000046 FT /pseudo FT /locus_tag="AARI_08800" FT /product="truncated GNAT-family acetyltransferase" FT /note="C-terminal section of a GNAT-family FT acetyltransferase" FT CDS 1000107..1001039 FT /transl_table=11 FT /locus_tag="AARI_08810" FT /product="aminoglycoside phosphotransferase-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF01636. This family consists FT of bacterial antibiotic resistance proteins, which confer FT resistance to various aminoglycosides. It also includes FT homoserine kinase" FT /db_xref="GOA:E1VTZ9" FT /db_xref="InterPro:IPR002575" FT /db_xref="InterPro:IPR011009" FT /db_xref="UniProtKB/TrEMBL:E1VTZ9" FT /protein_id="CBT75102.1" FT /translation="MSRTSANKPAMPEAEIAIGSDLVRDLISTQAPQWASEEITYLATG FT WDNEVFRLGSELIIRLPRRVLGETIGAKERKWLPELASASGLEIGVPLFEGKPTSDYPF FT TFSICPFAHGSSAAEMKRRQRDAYAKEFSGLLKMLHQPAQPDAPASEFRGCPLDTVDAR FT TRLQITQLATELQAPASKLWDEALAAEVYAGQPVWLHGDPHPHNTIVDDSGSQDSTVTL FT VDFGDLCIGDPASDLGMFWMHFSPAGISEAFDQYGAEPYSPIWRRSRGWGLRYAMLTAG FT LGPNDLLGIVGRETLGILLADSDSPAIAG" FT CDS complement(1001461..1001805) FT /transl_table=11 FT /locus_tag="AARI_08820" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VU00" FT /protein_id="CBT75103.1" FT /translation="MIFAVLLLVASYVFLVFVIVRCADGRIGINSIAGIRTPTIMTDEQ FT TWLAGHKAARNPSLAGTIGAIVLTIVAVFLPNLESQSLAIILGCLLLLAGILYGTVKGT FT KAARKILANQ" FT gene 1001914..1002513 FT /pseudo FT /locus_tag="AARI_08830" FT /product="truncated protein" FT /note="similarity with a protein of unknown function, FT absence of the N-terminal part of the protein" FT CDS complement(1002483..1003184) FT /transl_table=11 FT /locus_tag="AARI_08840" FT /product="putative hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /EC_number="3.-.-.-" FT /note="identified by match to protein family TIGR01509: FT HAD-superfamily hydrolase, subfamily IA, variant 3; match FT to protein family PF00702: haloacid dehalogenase-like FT hydrolase" FT /db_xref="GOA:E1VU01" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006402" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:E1VU01" FT /protein_id="CBT75104.1" FT /translation="MIPQEGSNLPRPKFSAVLFDCDGVLVDSESITNAVLREMLIELGW FT DISQEECISIFIGKALKDQWEPILAHTGVRIDEQWITGFRQRRDVALRENLQAVPGALE FT AVKQISAAYCEKIACATGADRAKVEMQLSITRMAPFFGNRVYSGMEYAQSKPAPDVYLA FT AASGLHIDPSQAAVVEDTVTGVTAGVAAGATVFGYCPGGPISSTEEKLLAAGAAEVFTN FT MDQLPGLLTQK" FT CDS complement(1003192..1003638) FT /transl_table=11 FT /locus_tag="AARI_08850" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VU02" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VU02" FT /protein_id="CBT75105.1" FT /translation="MGIADDAVEIRARGWRTLASLHGLIDAALEKDLTSQAGLSVVEYT FT LLDALNRQDGWHMRMAQLARATALSPSATTRLVTRLEDRNLLSRVLCADDRRGIYTELT FT AAGHELYQKAKPIHDATLERVLKQAEEQPELAPLARILHEFSAA" FT CDS 1003753..1004895 FT /transl_table=11 FT /locus_tag="AARI_08860" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VU03" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VU03" FT /protein_id="CBT75106.1" FT /translation="MPLGLIALAIMGLLPDVAADFAVSEAAAGWLISGYALSVVVGALG FT LTAATVRLPRKPVLVGLLVLFILGNSLTAMASTYEVAMIGRVIAALCHGAFFGIGAVVA FT ADLVPANKKAGAIAIMFTGLTAANVLGVPFGTLLGQHSGWRSTFWAISGIGVIALIGIL FT VLVPAIKHAAEGISLRKELGAFTSLQVWLSLAITVLGYGGMFGAFTYIAYTLTEVTGFN FT ETSVPWLLMLFGIGLFAGNWIGGRMADKSIDRTLLFFIAALLAVLIAFAALASNPVATM FT VALFLMGGFGFGTVPGLQSRIMQFAGSAPTLASGANIGAFNLGNALGAWAGGLGIAAGL FT GYTSPIWIGAAITVAALLVVLVAMSLAKKSAKTPELVPAC" FT CDS 1004940..1005770 FT /transl_table=11 FT /gene="dkgA" FT /locus_tag="AARI_08870" FT /product="putative 2,5-didehydrogluconate reductase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.1.1.274" FT /note="catalyzes the reduction of 2,5-diketogluconic acid FT to 2-keto-L-gulonic acid, a key intermediate in the FT production of ascorbic acid. Can also reduce ethyl 2- FT methylacetoacetate stereoselectively to ethyl (2R)-methyl- FT (3S)-hydroxybutanoate and can also accept some other beta- FT keto esters. Identified by similarity to protein SP:Q46857 FT (Escherichia coli)" FT /db_xref="GOA:E1VU04" FT /db_xref="InterPro:IPR001395" FT /db_xref="InterPro:IPR018170" FT /db_xref="InterPro:IPR020471" FT /db_xref="InterPro:IPR023210" FT /db_xref="UniProtKB/TrEMBL:E1VU04" FT /protein_id="CBT75107.1" FT /translation="MTTAIPTITLNNGVEMPQVGFGVFQVPNEETTAAVSAALKAGYRS FT IDTASIYGNEEGVGAALAQSGIAREDLFITSKVWISDMGYEQTLEAFEASLQRLGLDFL FT DLFLIHWPAPEKDLYVETWKAMEKLYTDKKIRAIGVSNFQPAHLAKVIAEGSVIPAVNQ FT VELHPALQNREVIAANAQHGIVTEAWSPLAQGAMLTDETIVGIAQAHEVSAAQVILRWH FT LQQGRVIIPKSVTESRIIANLDLFGFELTSDELASIDALDRDGRTGPNPDAFNG" FT CDS complement(1006160..1006462) FT /transl_table=11 FT /locus_tag="AARI_08880" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VU05" FT /protein_id="CBT75108.1" FT /translation="MSAEKIRATLVDPRYVSQENPNPVYRVDFWDEDRVCYENRIEDAE FT SIVDVLAWTEANRHDRYAVIWVEYTYEGGIGMTRLHGWIPTEAGSSSANDPYFRQ" FT CDS complement(1006662..1007327) FT /transl_table=11 FT /locus_tag="AARI_08890" FT /product="conserved hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="GOA:E1VU06" FT /db_xref="InterPro:IPR005532" FT /db_xref="InterPro:IPR016187" FT /db_xref="UniProtKB/TrEMBL:E1VU06" FT /protein_id="CBT75109.1" FT /translation="MPTFDLRPLTAGQVELHDARRKRRWTVDLEPFEIGAISVTTAQYG FT QLMGTSETGSQAPLVDINWLEAIKFCNAASINEGLAPAYIFEAGEVSWQTNASGYRLPT FT EAEWEYACRAGTVGPHYGSLDAIGWTADDKLENPKEVGQKLPNAFGLHDTLGNVWEWCW FT DLLDPARYDDYRVFRGGGFADKSWSVRASTRRGGAPGMSHPDLGLRMARGAFDEEQAA" FT CDS complement(1007386..1007787) FT /transl_table=11 FT /locus_tag="AARI_08900" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VU07" FT /protein_id="CBT75110.1" FT /translation="MQTIEAAQRWATTWANAWPFKNVDAIVGLQADDGEHWASMFRPLR FT GRSGLRAYLEECFAAETKPAETWFSEPIVNGSSASVEYWVVMFIEDQPMTVSGCTVLSF FT DDSGLVTTARDYSHVKEGHHLRPEHPFSA" FT CDS complement(1008036..1008632) FT /transl_table=11 FT /locus_tag="AARI_08910" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VU08" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VU08" FT /protein_id="CBT75111.1" FT /translation="MDFTDVAVLESPFVRLEPLSETHHDDLVTAVETDELWRTWYTHIP FT SPATMEKEIKRRVSLHTEGRIVPWAIIDPRTSRAVGMTTYLNLEPANRRLEIGSTWIGS FT RAQGTGINAAAKMLLLQRAFEELGCIAVEFRAHWHNHQSRHAIERLGAKQDGVLRNHTI FT FENGTVRDTVVFSIVEAEWPTVKFGLAERLNAYES" FT CDS 1008779..1009531 FT /transl_table=11 FT /locus_tag="AARI_08920" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PS00383 pattern (tyrosine specific protein FT phosphatases active site)" FT /db_xref="GOA:E1VU09" FT /db_xref="InterPro:IPR000387" FT /db_xref="InterPro:IPR016130" FT /db_xref="UniProtKB/TrEMBL:E1VU09" FT /protein_id="CBT75112.1" FT /translation="MSYDVLMTTNMELAWDGYVNARDLGGLPTSLSRTGTTVPGRIARG FT PRRERLTPAGWEAARAWGLTSIVDLRCSYEVGKQDGDPSTLTEILAELAITSAPTEDHS FT DREFQKVCFPILDSPEYWSHNWRLQPHLVRAALEAIASANPGVLVHCSAGRDRTGMISA FT LILGNAGVEPQAVANDYAASVRAMAGIASHAPTVDDQAKWSQKTANEWLNDKLPIVRDV FT AVNAQDILDSLNVSAATRESLRAKLIDC" FT CDS complement(1009791..1010846) FT /transl_table=11 FT /locus_tag="AARI_08930" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VU10" FT /db_xref="InterPro:IPR010290" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR022324" FT /db_xref="UniProtKB/TrEMBL:E1VU10" FT /protein_id="CBT75113.1" FT /translation="MVTSNAVSGAVQVTIAILILTGVAELWMLATSVFLLGVASVFFQP FT ASQGSIVQLVPAELRVAANAVLRLPLNVAKVLGQALGGLVVALVGPGWALAFNALTFLI FT SVFFLASVRLPQPIKNKSSALLDFRIGWKEFSARRWYVIMVVQSAIVVLMWLVGFQLFG FT PVVSHSSLGGAFAWGLISGGFAFGLVGGSLVAVAVRPQRVGITVSLCLAAQALPLVVLA FT FIAPIWLIVVATVLAGIALDISIVSWSAFFQEQIPEGLQSRLSSISTFGQLLPVPIGYL FT LFGLLSRYFSNTVMVSLMSGILVVAALVPLLLPSIRQLRLGQLAYGPSGTGEDSPVPDV FT LAKNTKSEGTA" FT CDS complement(1011351..1011854) FT /transl_table=11 FT /locus_tag="AARI_08940" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VU11" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VU11" FT /protein_id="CBT75114.1" FT /translation="MWQDVGVMELNDELQLAVSLEPHAVRSAALIWARATALRDGLPEP FT ATGEEKMPGIQRRLSLEGSRLLLARQADTYVGFTLFAPQAENLEIFYLAVGPDSWGSGV FT ASALLVGAEEHARSLGRAALELWVINDNDRALGVYERAGFADTKQVKLDEFSDQIERRL FT LKQI" FT CDS complement(1011915..1012457) FT /transl_table=11 FT /locus_tag="AARI_08950" FT /product="conserved hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VU12" FT /protein_id="CBT75115.1" FT /translation="MSNEADVSLSVRLSKLAADLGPSPSDEDSMQSPEAVLRSVAAFGD FT IARVSTQLQSQAVATAQASGLSWAKIGKVLGISRQAAQQRFDTRRTEAIQAMETMRIVG FT PVSRNEEVEQINAAGRQGWKLIRSLHGEHALELDDDTWEVTRVSIFSLRPLPAASDGWE FT AASTRFPDCFFIRKILN" FT CDS complement(1012454..1012642) FT /transl_table=11 FT /locus_tag="AARI_08960" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VU13" FT /protein_id="CBT75116.1" FT /translation="MLGICMVVFAAFVGFGLPGFIISVAGWIALIASLIGFAVVFVQKS FT TAASRANPWRPADKEEL" FT CDS 1013023..1013586 FT /transl_table=11 FT /locus_tag="AARI_08970" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VU14" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VU14" FT /protein_id="CBT75117.1" FT /translation="MRETDQEVGYVRFEHVAPDEIWAEVTSLFVLCFAAHPYNESADEL FT QSIVQWGPEKLASPGGRLVVTRHDGQLVGFALSQRLDQDSSWLQRLNGMPPMLDLDILP FT SRTLVVQELAVNKNFRGRGIAKQCIRELLSNRAEQDAVLGVFGQATQVREMYRHWGFSE FT LGTSPIYGGTVTLHALHHKLPWTA" FT CDS complement(1013760..1014467) FT /transl_table=11 FT /locus_tag="AARI_08980" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VU15" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VU15" FT /protein_id="CBT75118.1" FT /translation="MKLESSTITSIQLAWAQILGVPPEALEIEGNRVYREKDDSALLMF FT VSLFGTGILVGPSWAKEAAQNLTDTELASHAKLMEISAPYGGQALGEAELYYCDTAPPA FT PSLRPTASRQQEHAIALENICLPDDSAEVGLSEMESTFVLLSDCNNGPQPLAGAGYDIW FT EGKLAHLGVLTAPEKRQSGFGSNAVAIAMEQAMNCGLIPQWRARTDNTASIRTALRAGF FT EYVGTQTSVILEA" FT CDS complement(1014770..1015633) FT /transl_table=11 FT /locus_tag="AARI_08990" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VU16" FT /protein_id="CBT75119.1" FT /translation="MSPETVQLRDRSRPSWSTPAQHRLLQARIWPTNGPTPAPVVVLSH FT GTGGAGEDLDWLAKPLNDAGFLVASVDHPGNSYNDEYLVEGFSFAWERARDISLLLDYL FT VAEHDIDVDRIGAAGFSFGGYTVAALLGGRIDVDIMGAMFRGLIPAPEVPEFPDLIKAL FT RSKYSDAELTSLAESGARSMSDTRVRVGILLAPAIGRLLLPRSLQQISVPVLVRWGDDD FT SNTPPEDNAHLYRDLIPHAHGESLGSDVGHYVFLGDREDATGVRPHVAAETVEFFTSHL FT SVRHTD" FT gene complement(1015729..1016307) FT /pseudo FT /locus_tag="AARI_09000" FT /product="truncated peptidase" FT /note="C-terminal section of a metallopeptidase family M24 FT protein" FT CDS complement(1016535..1017287) FT /transl_table=11 FT /locus_tag="AARI_09010" FT /product="putative phosphotransferase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF01636. This family consists of bacterial FT antibiotic resistance proteins, which confer resistance to FT various aminoglycosides. The aminoglycoside FT phosphotransferases inactivate aminoglycoside antibiotics FT via phosphorylation. This family also includes homoserine FT kinase" FT /db_xref="GOA:E1VU17" FT /db_xref="InterPro:IPR002575" FT /db_xref="InterPro:IPR011009" FT /db_xref="UniProtKB/TrEMBL:E1VU17" FT /protein_id="CBT75120.1" FT /translation="MEEVHLAGGNATDGVVRVGSTVRKPWSAATPSVLAYMRAVRNAGV FT DVPAVYGQDAQGRQVTEFVPGCLAMDSGPLSLSELSRVGRLVRTIHDASAAYETDFGST FT WITHIPAPGADLICHNDLAPWNLLIGDRWVFIDWDAAAPSTRLWDLAYAAQSFTLNDAS FT ADPHMAAQALAAFIDGYDADEELRAALPSTMWQRTTAMHELLKNSHARGIEPWGTMFTT FT GHGDHWNTVTQFVRNNESLWLEAIRTVR" FT CDS complement(1018064..1018969) FT /transl_table=11 FT /locus_tag="AARI_09020" FT /product="LysR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00126: bacterial regulatory FT helix-turn-helix protein, lysR family. 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 /db_xref="GOA:E1VU18" FT /db_xref="InterPro:IPR000847" FT /db_xref="InterPro:IPR005119" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VU18" FT /protein_id="CBT75121.1" FT /translation="MELHQLRILRELADLGSVNAVAKALFVSPSAVSQHLAQLQRNFPV FT PLTQKDGRRLVLTTEGKLLASAATSVASTLAEASARIRTQEQERDTPIRIAGFHSIGQT FT IFAPLLTYPEGQLPPLHFSDEDVSQQDFPALTSTYDLVLAHRMPHTDPWPEDRISVIPL FT AFEPLDVAIHRDHPLAKFGELSPEQVIDEPWVVSRSGFSPADVLETIAALAGKAPRIEH FT RVNDYATAGALVEASGCLGILPRFTARKTLDETVTLRPIKGLNSGRQIDLLLRAEHLHR FT ITINDVIEAIRSTVKRLVIN" FT CDS 1019105..1020157 FT /transl_table=11 FT /gene="tdh" FT /locus_tag="AARI_09030" FT /product="L-threonine 3-dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.1.1.103" FT /note="catalyses the conversion of L-threonine to L-2- FT amino-3-oxobutanoate" FT /db_xref="GOA:E1VU19" FT /db_xref="InterPro:IPR002085" FT /db_xref="InterPro:IPR002328" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR013149" FT /db_xref="InterPro:IPR013154" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VU19" FT /protein_id="CBT75122.1" FT /translation="MKALYKSGPHAGLELVDRPEPETGAHEVKIRVMTAGICGTDLHIE FT AYDDAAKAMINTPLVPGHEFYGEVVEIGDFVHGVKVGDRVSGEGHVVCGLCRNCRAGRK FT QMCINVDSVGVQRDGAFAEFVVIPESNVYIHRDERITPLLGAIFDPFGNAVHTALQFPM FT VGEDVLITGAGPIGLMAAAVARHVGARNIAITDVSEQRLELAKTMGIDLAVNVANTRIK FT EAQQKLGMVEGFDYGMEMSGHKTALPEMIENMNHGGKICMLGLPSTSIDINWGKVVTHM FT LTLKGIYGREMFETWYAMSAMLTSSEVMRERISSVVTDFLPATEWQQGFEAARSGHGGK FT VVLDWTVFSG" FT CDS 1020189..1021388 FT /transl_table=11 FT /gene="kbl" FT /locus_tag="AARI_09040" FT /product="glycine C-acetyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.3.1.29" FT /note="catalyzes the addition of acetyl-CoA to glycine to FT form 2-amino-3-oxobutanoate: the second reaction step of FT the main metabolic degradation pathway for threonine" FT /db_xref="GOA:E1VU20" FT /db_xref="InterPro:IPR001917" FT /db_xref="InterPro:IPR004839" FT /db_xref="InterPro:IPR011282" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:E1VU20" FT /protein_id="CBT75123.1" FT /translation="MYTDLKGQLAAELEELKTSGLFKAERHIDSAQSASIMAGSLGDDA FT RQVLNFCANNYLGLADNQQIIDAAKNAMDERGFGMASVRFICGTQDLHLELEAKLSEFL FT GTEDTILFSSCFDANGGVFESLFGKEDAIISDALNHASIIDGIRLSKAARFRYANQDMA FT DLETQLQAAAQLNDGAGARRTIIVTDGVFSMDGYLAPLEAICDLADKYNALVMVDDSHA FT VGFMGATGAGTPEHAGVSDRVDIYTGTFGKALGGASGGYVSGRGEIVAMLRQKARPYLF FT SNSLAPSIVAATLKALDLVVDSGDLREKLFENAAHFRRRMSEEGFELLEGEHAIIPVMF FT GDAVKAAEVAGKMLERGVFVTAFSFPVVPKGAARIRVQLSAAHSAEDIEACVQAFVASR FT " FT CDS 1021477..1022493 FT /transl_table=11 FT /locus_tag="AARI_09050" FT /product="LacI-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domain PF00356. Numerous bacterial FT transcription regulatory proteins bind DNA via a helix- FT turn-helix (HTH) motif. These proteins are very diverse, FT but for convenience may be grouped into subfamilies on the FT basis of sequence similarity. One such family groups FT together a range of proteins, including ascG, ccpA, cytR, FT ebgR, fruR, galR, galS, lacI, malI, opnR, purF, rafR, rbtR FT and scrR. Within this family, the HTH motif is situated FT towards the N-terminus" FT /db_xref="GOA:E1VU21" FT /db_xref="InterPro:IPR000843" FT /db_xref="InterPro:IPR001761" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VU21" FT /protein_id="CBT75124.1" FT /translation="MATRDDVARLAGVSPSTVSYVISGRRTISDATKTRVLAAMRDLNY FT TPNAFAQGLAGARRGILALHFPTSVDGYSSTEFEYVTAAMERARALGYHMLLWSNPMTD FT VMGMESLVAQKLVAGVLLMEVSVSDPRFDVLRRAKIPFASIGRPDDSDDVIYVDNDFAE FT AGRLAIEHLAGLGHRSIMYINVSQQDQAAGNGPAIRTARAITESAQAQNMSIVEMPVEN FT NARGGRQALDGYLKFNPRPSAVVGLKEFATAGFLNAAGMAGLSIPADVSVVALGIGDRS FT AEMVSPALTTVAPSGEVIAHTAVDALVEQIEGRSSDVIQQLFTPVMVIRESSGIAPV" FT CDS 1022564..1023985 FT /transl_table=11 FT /locus_tag="AARI_09060" FT /product="oligosaccharide/polyol ABC transporter, FT substrate-binding protein" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family (TC 3.A.1. FT 1.z). ABCISSE: ABC transporter, binding protein (BP), FT OSP-family (oligosaccharides or polyols)" FT /db_xref="GOA:E1VU22" FT /db_xref="InterPro:IPR006059" FT /db_xref="UniProtKB/TrEMBL:E1VU22" FT /protein_id="CBT75125.1" FT /translation="MEGITRAKLELPAGYNSKVEGIMKKTKRGLKLVPALSVASIGLLL FT AGCSGGADPNDPNAQGGETQVAESDGVVDVYGPVTGTEAELLEKSWADWSEENGIKIRY FT TGDKNFESQLGIKVQGGDTPDLAVFPQPGLLEATVASGKVQKLPEGAQAEVGKNWSEDW FT QNYGKVDGVQYGAPLMASVKGYIWYSPKQFEEWGVSVPKTWDEMTALGTEITKKTDEPA FT WCAGFASGEASGWPGTDWIEDAVLRQSGTEAYDKWVSGELEFTSPEITSAFDSVGEILL FT DPKQVNAGYGDVKSINATAFGDIGTAVAKGTCPLTHQASFLEGFILDAKNADGETPTVA FT PDGDVWAFIAPQFNEGDPTSVVGGGEFVAAFSNDEDTAKVQEYLASADWANSRVKLGGV FT ISANSGLDPENASSDLLRSAVELLQDPSTTFRFDGSDLMPKSVGADSFWKGIVDWIDGK FT PTKEVLENIQAGYDS" FT CDS 1024053..1025192 FT /transl_table=11 FT /locus_tag="AARI_09070" FT /product="oligosaccharide/polyol ABC transporter, inner FT membrane subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family (TC 3.A.1. FT 1.z). ABCISSE: ABC transporter, permease (IM), OSP- family FT (oligosaccharides or polyols)" FT /db_xref="GOA:E1VU23" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VU23" FT /protein_id="CBT75126.1" FT /translation="MSDFFQWLAGLSPLLQIPVTLLSFAVVIGLVLAFVEVSTNRGRGF FT AILRLLASVLVPVVILLLLGLYASVMWVAAVAAVLGLAVYFYDRRSRSGAGTFLQLTGF FT LAPAMILLAIGLIYPTIRTAISAFMTNDGSGFAGLANFAWVFTSPDGLTALLNTLVWVL FT VAPVVSTIIGLAYAAFIDKSRGEKFFKLLVFMPMAISFVGASIIFKFFYDARQGEQIGV FT LNAIITAFGAKPVDWLGLEPWNTLFLVIILIWTQAGFAMVILSAAIKAVPAEQLEAAAL FT DGTTPWQSFMNVTLPGIRSSVIVVLTTISIASLKVYDIVSSMTGGRSETTVLAYEMVRQ FT FQLGSRTGYSSALAVVLFVLVLPIIIYNVRQQKKQGGTR" FT CDS 1025189..1026136 FT /transl_table=11 FT /locus_tag="AARI_09080" FT /product="oligosaccharide/polyol ABC transporter, inner FT membrane subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family (TC 3.A.1. FT 1.z). ABCISSE: ABC transporter, permease (IM), OSP- family FT (oligosaccharides or polyols)" FT /db_xref="GOA:E1VU24" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VU24" FT /protein_id="CBT75127.1" FT /translation="MSTVSDSSRRLLKATEKTGGKLRKASSSRIATAAAFLIAAIWTIP FT TFGLFVSSFREANDIKTTGWWTALSNPSFTLENYAQAFVSGDSLPLSKAFLNSLVITIP FT AAIIPIIIASLAAYAFAWINFKGRNTLFILVFALQIVPIQMALVPLLQMFSDGVKIGEL FT YILPGLGVNGLDGAYAKVWIAHTIFALPLAIFMLHNFISEIPEEVIEAARVDGAGHGTI FT FTRIVLPLATPAIASFGIFQFLWVWNDLLVATVFTSGGELPITKALQDLSGSYGQSWEL FT LTAGAFISMIIPLVVFFALQRFFVRGLLAGASKG" FT CDS 1026273..1027460 FT /transl_table=11 FT /gene="hutI" FT /locus_tag="AARI_09090" FT /product="imidazolonepropionase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="3.5.2.7" FT /note="catalyzes the third step in the histidine FT degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5- FT dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L- FT glutamate" FT /db_xref="GOA:E1VU25" FT /db_xref="InterPro:IPR005920" FT /db_xref="InterPro:IPR006680" FT /db_xref="UniProtKB/TrEMBL:E1VU25" FT /protein_id="CBT75128.1" FT /translation="MATLLLTNIGQLTTVDQNARVLEHAAVLIQDSLIAWVGDMGQAPQ FT ADESIDLGGRAVLPGWVDSHSHLIFGGDRAEEFVARMAGQSYAAGGIAVTTSATSQLSD FT NELSEAVAARRAEALAMGTTWMETKTGYGLAVDEETRHSVLGKPLVDSLTFLGAHLVPA FT GWDADEYTELVTGPMLDAVADNVDFVDVFCERGAFTEEQSRRVLEAARAKGLATKVHGN FT QLGPGPGVQLAVEFGSHSVDHVNYLEEEDIQALAGSWAGWDSATRTGTPGTVATCLPAC FT DLSTRQPLAPGRELLDAGVRIALASNCNPGTSYTSNMNFCVATAVLQMNLSLAEAIEAA FT TYGGALALGVAGQTGSIEVGKRADLHVLDAPVAAHLAYRPGMNLTHSVYRAGKAI" FT CDS complement(1027582..1028208) FT /transl_table=11 FT /locus_tag="AARI_09100" FT /product="putative SAM-dependent methyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.1.1.-" FT /note="identified by match to protein domain PF08241" FT /db_xref="GOA:E1VU26" FT /db_xref="UniProtKB/TrEMBL:E1VU26" FT /protein_id="CBT75129.1" FT /translation="MGTNYDAYAAKMRALTLDGTDLEVVARFTDMLCHRESQVLDIGCG FT VGNTVNALRRMGHHAYGIDPTPQVLEVAAELFDGTWFRQLSANQLESASLRSHGLPEQY FT DAILLAGNVPAFIPREQLRGIFSLADQVLSSSGVLIIGTTSHTKGGSADQDELRQGTSL FT QLMQRFSDWHLSPYQSDSPWSVSVYAHIKQRSGFPIPDGIFVLPS" FT CDS 1028307..1028804 FT /transl_table=11 FT /gene="tpx" FT /locus_tag="AARI_09110" FT /product="putative thiol peroxidase" FT /function="4.2 Detoxification" FT /EC_number="1.11.1.-" FT /note="in Escherichia coli, Tpx is an antioxidant protein FT with a thiol peroxidase activity" FT /db_xref="GOA:E1VU27" 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:E1VU27" FT /protein_id="CBT75130.1" FT /translation="MANTAFKGTPVQTIGELPAVGSQAPAFTLTDTGLADVTSESLAGR FT RVVLNIFPSVDTGVCAASVRRFNELAAGLENTTVVCVSADLPFALGRFCGAEDIENVTA FT ASVFRSDFGSDYGVTQIDGPLAGLLARSVIVLDETGKVTYTQVVPEITTEPDYDATIAA FT LS" FT CDS complement(1028953..1029387) FT /transl_table=11 FT /locus_tag="AARI_09120" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.999) with cleavage site probability 0.515 FT between position 29 and 30. Match to PS00383 pattern FT (aldehyde dehydrogenases glutamic acid active site)" FT /db_xref="UniProtKB/TrEMBL:E1VU28" FT /protein_id="CBT75131.1" FT /translation="MTLKNAFALTIIVGTSMAFTGCSASDSSSPATPATESMMPLQGHE FT LAALTTVVDQKDQNISLAIPLRGGDYAVALECSGKDTLSTIAWQSDDKKENGEISVPCT FT FEGVNVREQISLNGYSSSLTFVTSELQGYELTVSIASTAN" FT CDS complement(1029609..1030502) FT /transl_table=11 FT /locus_tag="AARI_09130" FT /product="aminoglycoside phosphotransferase-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF01636. This family consists FT of bacterial antibiotic resistance proteins, which confer FT resistance to various aminoglycosides. It also includes FT homoserine kinase" FT /db_xref="GOA:E1VU29" FT /db_xref="InterPro:IPR002575" FT /db_xref="InterPro:IPR011009" FT /db_xref="UniProtKB/TrEMBL:E1VU29" FT /protein_id="CBT75132.1" FT /translation="MTFNSQITSPQQAAEELALNRGAHELRLLGAGVEFLFFSTRAGTR FT REGYRVPRARVFDTVNNPGIQALELQRKELRLSAWALGHGVPSANPTELVDQGGYSVLV FT TEVIDDDQTPVNQQALGAVLAKMHQVEPLASEVARCPDIYDYLAQRIGDRHSRISTDHQ FT LPALPKPTHLAKVLQRSLHRVSQLHLDIRRQNIRVAAGEPRALFDWSNALTAAPELEMA FT RIREYAQIPENALDYMDILAGYRAYGGTIDESTTAWAVLRLDAALMLAGVFTSVSPNEE FT LASVFLNRVRILLQAL" FT CDS complement(1030499..1031344) FT /transl_table=11 FT /locus_tag="AARI_09140" FT /product="aminoglycoside phosphotransferase-like protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="identified by match to PF01636. This family consists FT of bacterial antibiotic resistance proteins, which confer FT resistance to various aminoglycosides. It also includes FT homoserine kinase" FT /db_xref="GOA:E1VU30" FT /db_xref="InterPro:IPR002575" FT /db_xref="InterPro:IPR011009" FT /db_xref="UniProtKB/TrEMBL:E1VU30" FT /protein_id="CBT75133.1" FT /translation="MSRPATKEELQIARQLCPDLSWDDAAVNEGGQFHKVIIANPQAAI FT RMARTPQATEQMPRTLDLLDRLESQLDYQIPVATSQILSVDGLSTVAMSFIPGSAHEPH FT YGDPQVLGKVVKDLAEIPLEPISDHLATPFAFRGPWTEERQQQCYDALPDELRPAARSL FT WAQLDELAQVPAALVHGDLAGHNMHWVGEELIGILDWDLAAAWDPALNTAYLSLWHGLE FT MVDLIAPSPDEACRAKIWLGLMSLERLSDTLSRTDNPKMGKLMRKIGPRILNAAEAVLV FT " FT CDS 1031441..1032223 FT /transl_table=11 FT /locus_tag="AARI_09150" FT /product="putative CAAX amino terminal protease family FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF02517: CAAX FT amino terminal protease family. Members of this family are FT probably proteases (after a prenyl group is attached to the FT Cys residue in the C-terminal CAAX motif of a protein, the FT AAX tripeptide is removed by one of the CAAX prenyl FT proteases). The family contains the Q03530 CAAX prenyl FT protease. 6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VU31" FT /db_xref="InterPro:IPR003675" FT /db_xref="UniProtKB/TrEMBL:E1VU31" FT /protein_id="CBT75134.1" FT /translation="MIENVNAEQIEQKATRKTFGFEIVLVLALSLGQSAVYSLLSFADK FT VTRAPLREQTTSLNNQLSTREFFDFSYQLLDIIFALVPVVLALYLMKRTTGRTIRDIGF FT DIRKPGKDALLGAGLFLAMGVGTLGVYAAGRALGITTALSAANLGDYWWSVPVLLLSAV FT RHAVLEEVLMLGFLFTYTRKLKMGPWSIIILSAVIRGSYHLYQGAGPMIGNMLMGVVFG FT WIYQKYGRVMPLVIAHFLLDAIGFVGYALIGPAIGIGQ" FT CDS 1032242..1032679 FT /transl_table=11 FT /locus_tag="AARI_09160" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VU32" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VU32" FT /protein_id="CBT75135.1" FT /translation="MQITELSEKYLHQAVDLWETTGLTRPWNDPLADARRALREPTSTV FT LAMIENDQVVGTAMTGHDGHRGWLYYVAVDPRRQGNGLGRSLVDAASRWLRERAVPKVQ FT LMVRSENASVIDFYEPLGFEDQQVVVLGRRLDQSEARAGKE" FT CDS complement(1032729..1033373) FT /transl_table=11 FT /locus_tag="AARI_09170" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VU33" FT /protein_id="CBT75136.1" FT /translation="MMRLDHVSYACGPDGLMPTAQRISESLGLEFVKGGVHPRFGTRNV FT IFPLKHGQYLEVVEVLNHPASDKAPFGQAVRARSELGGGWMGWCVSVEDLSSAEDRLGR FT KSVPGNRKFPDGRELTWQQIGIKGLIADPQCPYLISWDDGTEDLHPSKSLEPVGAISEI FT AIAGSRERVLDWLGQPQNVNLGAVTMQYEAPNGTPGIMSVTFETESGTVVL" FT CDS 1033757..1035100 FT /transl_table=11 FT /locus_tag="AARI_09180" FT /product="O-acetylhomoserine aminocarboxypropyltransferase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.5.1.49" FT /note="catalyses several reactions, including the formation FT of L-homocysteine from O-acetyl-L-homoserine and H2S, and FT the formation of L-methionine from O-acetyl-L- homoserine FT and methanethiol" FT /db_xref="GOA:E1VU34" 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:E1VU34" FT /protein_id="CBT75137.1" FT /translation="MSSNWSFETRQIHSGQTPDPTTGARALPIFQTTSFVFPSAKSAAA FT RFALQELEPIYTRIGNPTTDAVETRIADLEGGVGALLLSSGQAATTFAILNLAEAGDHL FT VASPSLYGGTQNLLKHTLKRLGIEVTFVSDPDNLDEWRAAVRPNTKAFFGESISNPRQD FT VLNIEDISAIAHEAGVPLLVDNTLATPYLIRPIEWGADIVIHSATKFLGGHGNAIAGVI FT VDSGKFDFGKDAERFPGFNTPDESYNGLVFARDLGVNGILGANLAYILKARVQLLRDLG FT ASVAPFNAFLIAQGLETLSLRIERHGQNAVEVANWLEARGEVRKVAYAGLKSSPWYERA FT QKYSDQGAGSVIAFELEGGSEAGQAFVDALVLHSNVANIGDVRSLVIHPASTTHAQLSE FT AEQVAAGVSPGLVRLSVGLENIKDILADLELGFAAVGALENKELQETL" FT CDS 1035103..1036248 FT /transl_table=11 FT /gene="metX" FT /locus_tag="AARI_09190" FT /product="homoserine O-acetyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.3.1.31" FT /note="first reaction in L-methionine biosynthesis" FT /db_xref="GOA:E1VU35" FT /db_xref="InterPro:IPR000073" FT /db_xref="InterPro:IPR008220" FT /db_xref="UniProtKB/TrEMBL:E1VU35" FT /protein_id="CBT75138.1" FT /translation="MASIVTTEDTLRAEELAGGQDGILRRSSVGEHRFEFGGYLPEVEL FT GFETWGTLAADGSNAVLVMHALTGDAHVAQGDSQSDGWWEGFVGPGATIDTNEYFVVSI FT NMVGGCNGSTGPASLDEQAVPYGSRFPFVTIKDSVRLEARLAKQLGIDSWHAVIGGSMG FT GARALEYAVQFPQQVKNLVVMASSAQATAEQIAFAQVQTQSIRLDPHFCNGDYYGNEAR FT PDAGLGLARRLAHITYRSEAELETRFSRNPQEGEKPTGQLDGARGRYQVESYLDHQASK FT LVNRFDANSYLVLTEALMSHDVARGHESLEAALARLAKVNVVVAAVTSDRLYFPVQSVK FT LASSLAKPKPVHYIDSPIGHDGFLTDAKQLDGVLRTLVFGD" FT CDS complement(1036332..1037189) FT /transl_table=11 FT /locus_tag="AARI_09200" FT /product="GDSL-like lipase/esterase" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.1.-" FT /note="identified by match to protein family PF00657" FT /db_xref="GOA:E1VU37" FT /db_xref="InterPro:IPR001087" FT /db_xref="InterPro:IPR013830" FT /db_xref="InterPro:IPR013831" FT /db_xref="UniProtKB/TrEMBL:E1VU37" FT /protein_id="CBT75139.1" FT /translation="MPNEFSPESTESLETPAHPWRRYVAIGDSFTEGIGDPDPANVGRH FT LGWADRLAHELSSTVPDFAYANLAIRGRLIGQIVSEQLDPCIELKPDLISLCAGGNDVL FT RPGGDPDKIADILDNAVAKLTSTGATLLLFTGPDIRDTPVLGSIRGKVAIYNENVRTVA FT ARHDAIVADMWALQELHQSQMWAPDRLHFSPIGHQRIAAMALDSLNVPHQLDTEIAPVV FT EQRSWREARKEDLQWAREHLAPWVLRRLRHQSSGDGITAKRPSAAPFANTMPNDSLGAG FT DSAN" FT CDS complement(1037258..1037674) FT /transl_table=11 FT /locus_tag="AARI_09210" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VU36" FT /protein_id="CBT75140.1" FT /translation="MGKIEYRIALPGLAPEDLEDFGYIEEFGYIESDLGNTSSPYESAD FT TVFSIGLPLFGILFVAVLGFIIFVSVRNYRKAKSAGFDPLTMETELMARAANSAMLAPK FT KSLEDKLSELESLHSRGVITRDEYLQARRDALSE" FT CDS 1037977..1039038 FT /transl_table=11 FT /locus_tag="AARI_09220" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="7 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VU38" FT /protein_id="CBT75141.1" FT /translation="MSNLLPIIVIVGIGIVLVALTRRGVLSQRRAHLTLQSREASGPDR FT ELVLRILRAIRTRNLTAVGAAVLGVVLAVVVHQGFTKAAGLPLVLAPGAAGVLSTLVFL FT WWPLPHEARSTSQLKHDQICADLTPRTKGMFGPGWGVALPSVLSAITVVGLLLGGIFSS FT PDERGLYRQLHYVTHSGASIDANSVVTENLVGYGSSGPFPGWYYGIPVGAVVVLGYMLT FT MWALNSNVRRPSLRSLELREFDKAVRTHNGYVLSTGFSALLCFQLVPLLAMAAISTYGA FT SYNAIYEVGQRFDAGADIFRDPWLATLGWTMGGLCMLLLIIGVLLLGHLVGWMAAAYGT FT EVQHQSKGREMPA" FT CDS 1039035..1039397 FT /transl_table=11 FT /locus_tag="AARI_09230" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="GOA:E1VU39" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VU39" FT /protein_id="CBT75142.1" FT /translation="MITLESAHPAGPSEQIRAQLAAMIRSGELAEDAKLPTVRQLAGDL FT RVAVGTVAKAYKELEAAGLVRTGRANGTRVNAGHMLAPRLLSDARVLASSAKESGMGLE FT ELQNLVEAAWKSAQAT" FT CDS 1039471..1040121 FT /transl_table=11 FT /locus_tag="AARI_09240" FT /product="phospholipase/carboxylesterase family protein" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.-.-" FT /note="identified by match to protein family PF02230. This FT family consists of both phospholipases and FT carboxylesterases with broad substrate specificity" FT /db_xref="GOA:E1VU40" FT /db_xref="InterPro:IPR003140" FT /db_xref="UniProtKB/TrEMBL:E1VU40" FT /protein_id="CBT75143.1" FT /translation="MTNQEHAPVAIISRNDETRLGTPLLVFLHGYGSNEQDLMGLSQHL FT PEEFTYLSVRAPLQAGPGYSWFPLTQEIDYSIDAVAHSVQALWVLLEPLAQQHSSVTLL FT GFSQGMAMATSLARYQRDSIDAVVGLSGFAVDPQPLEIFDDAKLEEYPLPMFWGRDLAD FT PVITQDKIEYTLAWVPKHTELTSETYPQIGHSVCMEELQDVAEFLNTVVLKKN" FT CDS complement(1040122..1040352) FT /transl_table=11 FT /locus_tag="AARI_09250" FT /product="S4 domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF01479. The S4 domain was FT detected in proteins such as the bacterial ribosomal FT protein S4, two families of pseudouridine synthases, a FT novel family of predicted RNA methylases, a bacterial FT tyrosyl-tRNA synthetases, and a number of uncharacterized, FT small proteins that may be involved in translation FT regulation. The S4 domain probably mediates binding to RNA" FT /db_xref="GOA:E1VU41" FT /db_xref="InterPro:IPR002942" FT /db_xref="UniProtKB/TrEMBL:E1VU41" FT /protein_id="CBT75144.1" FT /translation="MSANEAFDLEIRDESIRLGQLLKLASLAEDGIHAKEMISDGIVTV FT NGQVDTRRGAQIRPGDVVCVNGECVKVTAQQ" FT CDS 1040533..1041918 FT /transl_table=11 FT /gene="glyS" FT /locus_tag="AARI_09260" FT /product="glycine--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.14" FT /note="activates glycine and transfers it to tRNA(Gly) as FT the first step in protein biosynthesis" FT /db_xref="GOA:E1VU42" FT /db_xref="InterPro:IPR002314" FT /db_xref="InterPro:IPR002315" FT /db_xref="InterPro:IPR004154" FT /db_xref="InterPro:IPR006195" FT /db_xref="InterPro:IPR022961" FT /db_xref="UniProtKB/TrEMBL:E1VU42" FT /protein_id="CBT75145.1" FT /translation="MAPQSKLDQVISLAKRRGFVFQAGEIYGGSRSAWDYGPLGTELKE FT NIKREWWQSFVRGREDMVGLDSSIILPKAVWEASGHVATFTDPLVECIQCHKRHRQDHL FT IEAFEAKKGRAPKDGMSEIACPDCGTKGQFTEPQMFSGLMKTFLGPVDSEAGLAFMRPE FT TAQGIFVNFANVLTASRKKPPFGIGQIGKAFRNEITPGNFIFRTREFEQMEIEFFTAPE FT DAPAFFDQWVKDCWAWFLDLGIKEENLRQFDVPEDERAHYSAGTIDFEYRFGFQGSEWG FT ELMGVANRTDYDLSSHAKASGAELSYFNQATGERYTPYVIEPSFGLTRSMMAFLVDAYT FT EDEAPNTKGGVDKRTVLKMDPRLAPVKAAVLPLSRNENLSPKAKDLAAELRKRWNIDFD FT DAGAIGRRYRRQDEIGTPFCITVDFDTLDDQAVTIRERDTMAQERVSLDQVTAYLSERL FT NGA" FT CDS 1041925..1042854 FT /transl_table=11 FT /locus_tag="AARI_09270" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VU43" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VU43" FT /protein_id="CBT75146.1" FT /translation="MNELEFRPWRSGDDLQLLQIFGDPRSPQAHQDRTMLRENSDAPFS FT RTLVATIDEVAIGAGVVFASSLHPQRLWLYVEVAAEQRRTGVGTALVQQLRKQIPAGQA FT TELKARYTVTAGDPAAAAAGFCQSLGLGEIQVSRDVILEPGALAEPVFDTNDRVIEDLS FT TGSVELTKLVMDFYNAVHTDWDPAKMTVGSAQRMLLDEHTGAQGALVLRDKPKRDGGVP FT LAFAVSYVPARENAPTDVLVGHNPAFSDDEVAEAVRDMVAMLIHQYPVKLEVDSSMFVL FT SSLIDALAVVDQATVISTTHILASDAAK" FT CDS 1042935..1043936 FT /transl_table=11 FT /locus_tag="AARI_09280" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.937) with cleavage site probability 0.418 FT between position 40 and 41. 9 transmembrane helices FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="InterPro:IPR006750" FT /db_xref="UniProtKB/TrEMBL:E1VU44" FT /protein_id="CBT75147.1" FT /translation="MTTTTMTAQVRTGGKFLFTVLAIASGLLLCVQSRINGALGAKLGD FT PIAASTISFGVGLAALILLALLVPAVRSSVRQVPRALAQGRFPRWYLVAGAVGALIVFS FT QAAAVPLIGVALFTVCLVTGQAIGSMFMDRVGFGGATPRKINALRLLGVVLTILGVIWA FT VSPRGADAQLSTLLLPMALSMAVGMLMGFQGAANGVQAAAYGSATAATLVNFAVGFVVL FT VLVMIVRLPAGVELHPLPSTWWHYIGGLLGCLFVGITAMVVKRLGVLVTSLSAVGGQLV FT GSLLLDAFFPAPGSVITTATVMGTLLTLLAVGLASVSGARNAKKVHSQSSAA" FT CDS 1044003..1045208 FT /transl_table=11 FT /locus_tag="AARI_09290" FT /product="putative chromate transporter" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="Chromate Ion Transporter (CHR) family (TC 2.A.51.y. FT z). match to PF02417: this region is found in known and FT predicted chromate transporters, these proteins reduce FT chromate accumulation and are essential for chromate FT resistance" FT /db_xref="GOA:E1VU45" FT /db_xref="InterPro:IPR003370" FT /db_xref="InterPro:IPR014047" FT /db_xref="UniProtKB/TrEMBL:E1VU45" FT /protein_id="CBT75148.1" FT /translation="MNSQQLEKGSAGEVFKVFLKLGLTSFGGPIAHLGYFRTELVDRRR FT WLDDQQYGQLVALSQFLPGPASSQVGFGLGLHRAGMRGALAAFLAFTLPSAVVLAVFAF FT GASLFSGPVGTGLLSGLKIVAVAIIAQAVLGMAKNLTPDRTRAAIAVVAAGSALLVAGT FT FGQILAIVLGALAGYFWCRDLENTSATALHFPVSKAMGISCLLLFAVLLFGLPVLALAT FT GWDLVAFIDAFYRSGALVFGGGHVVLPLLQSAVVDPGLISSQEFLTGYGAAQAVPGPLF FT TFAAFLGVLVESGPGGALGALIALLAIFLPGFLLLLGVLPYWNRVSHWPAARAIMRGAN FT AAVVGVLAAALYNPVFTSAITSASAFVLALACFVLLTAWKMAPWIVVAIGALGGMLLGV FT VA" FT CDS complement(1045205..1046848) FT /transl_table=11 FT /locus_tag="AARI_09300" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="12 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VU46" FT /protein_id="CBT75149.1" FT /translation="MATNAPVLNAQSSSVLRPVILHSLLFVLLMVTATGLSALFTAVFH FT GFNAQQVSTDQLAMALTFTLVGIPLAWLLWRSVRKRLARPTAFDSAIWSLQASAVYLVT FT LAASSCALLGLLAGFVPSSNYAWQSTLAVALGWGAVCLWQHRQITSARTAPRQFAQLAA FT TVGNYFSLVLFALSLVATLKASLEILIRPEGTLAGPTGMPNLLAALIWLAGSLGLWVWH FT WKLRRVQQMADLLNNILLVVLGLAAPALAFLLMIAELFSWVWPQAWTAQERAGLFHEGG FT PNLLAILIASAVVWIYHQSQLHTGLHSRAVISAARLALSAVSLAVLATGLGMVVNALFA FT AIGSTVSVSYSADLLGHGLGLLGFGTAAWLWHFKPWKPSPAESRSAYLVLFFGASSLVA FT LISLLVFGYRIFEFYLEPESRLDSLLNTVRAPLGWLVATAAVASYHFALWRTDKDAKAG FT SSGKSTTTRDAVTRRAVVIVAPAASEPMAAQLKARPELSLIWIASAGSALDDRAEVSVL FT ARIDEYLACESGPVLAIANEDGTVQFTELA" FT CDS complement(1046848..1047312) FT /transl_table=11 FT /locus_tag="AARI_09310" FT /product="hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.867 FT between position 34 and 35" FT /db_xref="UniProtKB/TrEMBL:E1VU47" FT /protein_id="CBT75150.1" FT /translation="MTSKFSAARAVLLALAAAIVALVIAALLVVSLRSAPQPYEESTPE FT GVVQRYLIAFEAENMQTMQDYTIDGQSRSLCNPEPYNTQPLDVQLLRSSVGTNSATVHV FT RFDTRDSQFLPLPDLSAYDDVFELRKINGTWLIERMPWQVGLCTEKEMGY" FT CDS 1047416..1048600 FT /transl_table=11 FT /locus_tag="AARI_09320" FT /product="putative tRNA-dihydrouridine synthase" FT /function="3.6 RNA modification" FT /note="identified by match to protein family PF01207. FT Members of this family catalyse the reduction of the 5,6- FT double bond of a uridine residue on tRNA. The role of FT dihydrouridine in tRNA is currently unknown, but may FT increase conformational flexibility of the tRNA" FT /db_xref="GOA:E1VU48" FT /db_xref="InterPro:IPR001269" FT /db_xref="InterPro:IPR004652" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR018517" FT /db_xref="InterPro:IPR024036" FT /db_xref="UniProtKB/TrEMBL:E1VU48" FT /protein_id="CBT75151.1" FT /translation="MTTLTDAPTNTPTLKLPPLQLGKLTIDTPVVLAPMAGVTNRAFRR FT LCREYGGGLYVTEMVTARALVERNPESLRIISHDPDEEIRSIQIYGVDPGTVRAAVRMV FT VDENLADHVDLNFGCPVPKVTRKGGGSALPWKSDLYTSIIEAATSEAAKGDIPLTVKMR FT IGIDKDHLTYLESAKIARDHGAAAVTLHARTAGQYYAGHSDWDAITTLREAMDDMPVLG FT NGDIFSAEDAIEMVEQTGAAGVMVGRGCQGRPWIFGDLQAAFEGREDRFRPGVRKVADT FT VYRHGELLTEFFEDEGKGMRDIRKHIAWYFKGYPVGGEIRSQLAQVPSLAVLRELLDQL FT DLGLPYPGEAAEGTRGRAGHPKKTHVPDGWLDNRVMSDAHREMIKAAELDISGG" FT CDS 1048678..1049961 FT /transl_table=11 FT /gene="dgt" FT /locus_tag="AARI_09330" FT /product="putative dGTPase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.1.5.1" FT /note="dGTPase catalyses the formation of deoxyguanosine FT from dGTP. It is involved in purine metabolism" FT /db_xref="GOA:E1VU49" FT /db_xref="InterPro:IPR003607" FT /db_xref="InterPro:IPR006261" FT /db_xref="InterPro:IPR006674" FT /db_xref="InterPro:IPR023023" FT /db_xref="InterPro:IPR023279" FT /db_xref="InterPro:IPR023293" FT /db_xref="UniProtKB/TrEMBL:E1VU49" FT /protein_id="CBT75152.1" FT /translation="MTQIPGYTEADQQRWVPEPAKKSYRTAFERDRARVLHSSALRRLS FT AKTQVVAPNQNDFVRNRLTHSLEVAQVGRELGAALGCDPDVVDTACLAHDLGHPPFGHN FT GEKALDKAAKDIGGFEGNAQTLRLLTRLETKTFRHNGHSAGLNLSRASLDAACKYPWLK FT ADAPEVNGKKTKKFGVYEDDAIVFNWLRNVPEATAGTVCMEGQVMDLADDISYSVHDVE FT DAIVGGKLQLRWLNQQLQRERAVQVTQEWYLPGIDEADIDAALRRLEASEEWVAHYDGS FT RRSMAALKDMTSQFIGRFASAAMDATRARFGEGNLTRYNASLIVPEETEHEIAVMKGIA FT ASYVMTDEVRQPLYADQRTLLAELVELLFETGRDNLEPIFAADWDDAADEAAQLRVVID FT QVASLTDISATEWHSYLVKGEAPETKLF" FT CDS 1049971..1051854 FT /transl_table=11 FT /gene="dnaG" FT /locus_tag="AARI_09340" FT /product="DNA primase" FT /function="3.1 DNA replication" FT /EC_number="2.7.7.-" FT /note="a nucleotidyltransferase which synthesizes the FT oligoribonucleotide primers required for DNA replication on FT the lagging strand of the replication fork. It can also FT prime the leading strand and has been implicated in cell FT division" FT /db_xref="GOA:E1VU50" FT /db_xref="InterPro:IPR002694" FT /db_xref="InterPro:IPR006171" FT /db_xref="InterPro:IPR006295" FT /db_xref="InterPro:IPR013264" FT /db_xref="InterPro:IPR019475" FT /db_xref="UniProtKB/TrEMBL:E1VU50" FT /protein_id="CBT75153.1" FT /translation="MAGLIKREDIDEVRNRVDLREVVESYVTLKSAGIGSYKGLCPFHD FT ERSPSFHIRPQLGTFHCFGCGESGDVIAFIQKMDHSSFTETVELLAARINYELHYEDGG FT PGPRREDYGKRQRLVDAHKVAEEFFRAQLATEEGSAGREFLAGRGFDPEVTAQFSVGYA FT PKGWDALLKHLRSKGFADDELKLTGMFSEGNRGIYDRFRGRVMWPIRDLSGATIGFGAR FT KLYEDDQGPKYLNTPETSLYKKSQVLYGLDLAKKQISKSRQIVVVEGYTDVMACHLAGI FT TTAVATCGTAFGTDHIKIARRLLQDDGTGGEVIFTFDGDAAGQKAALRAFEEDQRFIAQ FT TYVCVEPSGADPCDLRLHRGDEAVRELIELKRPLFEFAIRAELKKFNLNTVEGRVQALR FT QTAPIVAQIKDSAIRPAYARELAGWLGMNNEDVNRSVGASIKRARLPKNAEAQAPRPQP FT GEAEQALPAAPAFERPDHRDPVMRLERQALEVVIQQPQRLKDEQWQAFYEARFLAPAHS FT AVHDGIVAASSAGASATSWVEVIRDEVPEQLRSFVSELAVTSIPASDEHSLNRYCADII FT NGLIELQITHRKAELIGRLQRAEMMPEGEEYAQINRELMELEMRRRILRGT" FT tRNA 1051908..1051980 FT /locus_tag="AARI_36660" FT /product="transfer RNA-Asn" FT /anticodon=(pos:1051941..1051943,aa:Asn) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(1052110..1052937) FT /transl_table=11 FT /locus_tag="AARI_09350" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="8 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VU51" FT /protein_id="CBT75154.1" FT /translation="MATSIERSPGRSTLRYVRLMLLVVPLLLVVAIVIYGIANQRIEDS FT LSSYYLGPARDLFVAMLVTTGVLLVVYTGEEMEDLALNLAGFYAMFVAVVPTRLGETLA FT DLPIGEQRRLIFSVQVSVIAVLVVSVVFVWLGIRTSNAPHRALFQSNLTKILGLLSTML FT LIAFVLLLLWRTIEGEQFAGVHASAAFLLIFSMGIAIASHLDHRPLCSMDTSGGKKTHY FT AIVLVLMLLGLIGWPILLALGIEEALFIVEWFEIGLFSYFWYLESRRLWNPAN" FT CDS 1053167..1053976 FT /transl_table=11 FT /locus_tag="AARI_09360" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VU52" FT /db_xref="InterPro:IPR015250" FT /db_xref="InterPro:IPR021652" FT /db_xref="UniProtKB/TrEMBL:E1VU52" FT /protein_id="CBT75155.1" FT /translation="MSVQNPLDPNVVPPAPQTKTTAGKGLGIAALVVGIVALALCWVPI FT VNNIAAVLGFIALVLGVISLIVASKRRGSKGLGIASSIISIVAIILVFATQAAYVKAID FT EVANDIADASDGEVAAPVEVIEQAKDESQVLALGEAATVGEYSVNVSAVDLDAGAEIAK FT ANEFNEKAEGQYVLVDLSVVYNGDEEGDAWLDLNPELVGSDASIYSTGSATVIPAKPGM FT DLPTLANGGKGSYQVVFDVPAEAVEDAKIRVSETISFSDESVLWATK" FT CDS complement(1054193..1054351) FT /transl_table=11 FT /locus_tag="AARI_09370" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VU53" FT /protein_id="CBT75156.1" FT /translation="MMRDGRIGLVGKSLAGTCQSRWHGQHDEDEKYATNHVLNIKKPRD FT LALSPGL" FT CDS 1054428..1055948 FT /transl_table=11 FT /locus_tag="AARI_09380" FT /product="putative signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VU54" 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="UniProtKB/TrEMBL:E1VU54" FT /protein_id="CBT75157.1" FT /translation="MTDLQENQGSTVSARLRIVGWIVLTTALALLAVTASMRSIMSGQV FT AESANVGIAQEIEEFRTFAAEGLDPKTARPFSSMDELMERYLARQQPMAGEAIIGQANG FT RVLAAGTAANQAGSWLAEDPVLLGRILDDAKPSGILESNHGTVRWAKAEAKDASGANGA FT GHQAHLVVAHFIGGAQEEADRQATMLFGVAAGGLALTAGIAWLAAGQIMRPIRTMSETA FT ASITANDLSARVPVEGRDDLAQLASTLNAMLDRVEASHLAQRHFISEAREHLGSPQRKL FT AAALQKLNEEEVPRKQRGRIISTAQAHISLMGQTLADLELLAQSSDPDFIQRRMVPVGE FT VTADVAAAAARPGAYPDRQFRIAESAKAQAWLDPLRVAQAMHQLIQNAVAHTEDGESIR FT IGSAAAKGMASFWVANDGPALDPDQARALLENYRSAPEAGQQGSGMGLGLAVVKAVAQA FT HGGTAWVESGNGHGTSFGFSLPQADAGQGIRCEEEFAQSMASSLGGES" FT CDS 1055945..1057504 FT /transl_table=11 FT /locus_tag="AARI_09390" FT /product="conserved membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="11 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VU55" FT /db_xref="InterPro:IPR001898" FT /db_xref="UniProtKB/TrEMBL:E1VU55" FT /protein_id="CBT75158.1" FT /translation="MSIKPTAPRSGFRYTAQRSMDQAAEQGNAGAARSRWSKQNAARII FT AALVLLGFLGWCAYGAFGPDAGTVQALPAQGALTLAVFALAIWLWVFSPVGDTFIALGA FT AVVLVLMGVLPEADLFSSLGEDTIWLLLAAFVIAAGITATGLATRAAAWIAAGANTPRQ FT LIHLTTGVLVATAFAVPSTSGRAALAIPVFIALAKALADRRRIVLALSLVFPSVILLSA FT VASYLGAGAHLITSQILATAGHEGFSFAGWLVYGLPLAFVSSHLCAELVLWMFTRKEDR FT AEPLAVGIERLQQYSPVPLSGPLTVGQSRAALLVSAVVVLWCTEPLHQLHPAIVALLGS FT LLVASPGYGSVGLAKALKAVPWSMLIFMAATLTLGTALAGSGAAEWLARKVLGPVEQLG FT AAAPWVFTVLVVVVSATAHLVIQSRSARSAVLIPLVVSLAPGVGVNAVAIALASTAAAG FT FCHTLTSSSKPVNLFSEIEGIETYKPADLLRLSAVLGPLMVLLVLVFAFWIWPAMGLPL FT FL" FT gene 1057563..1058540 FT /pseudo FT /locus_tag="AARI_09400" FT /product="truncated glycerate kinase" FT /note="N-terminal section of a glycerate kinase (EC 2.7.1. FT 31). Presence of one or more frame-shift mutations which FT are not the result of sequencing errors" FT gene 1058255..1058788 FT /pseudo FT /locus_tag="AARI_09410" FT /product="truncated glycerate kinase" FT /note="C-terminal section of a glycerate kinase (EC 2.7.1. FT 31). Presence of one or more frame-shift mutations which FT are not the result of sequencing errors" FT CDS complement(1058833..1059207) FT /transl_table=11 FT /locus_tag="AARI_09420" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR012544" FT /db_xref="InterPro:IPR023363" FT /db_xref="UniProtKB/TrEMBL:E1VU56" FT /protein_id="CBT75159.1" FT /translation="MIDFNNSSVFKLGPWDLSQVAPEIVPMMVTGEELLSAFKGARDYV FT VFSNKRLIAVNVQGMTGKKRDYTSLPYSKVQSFSVETAGTFDLDAELDLWFSGLGKVRL FT EFKGKVDVRALSQLIASYVL" FT CDS 1059344..1060000 FT /transl_table=11 FT /locus_tag="AARI_09430" FT /product="conserved hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VU57" FT /protein_id="CBT75160.1" FT /translation="MQLRSKVDFSTAVEDVRDYFGTMGNGRPKYSGSRFETLGEGVDTD FT PHRITATDLVAVSMLSVDVPAQASLGILETLAEQISELLSQIPQDLKFENLTPELFEKY FT LDEGSPADKLWSLLRQHEDPWKVGQTTASKIMARKRPDLIPVYDSVVKAVAGIEGSGEQ FT WIVWYSAFHDGSSEAAEFVGKLRAIRAEAGQPHLSLLRILDIALWKQGKREIRHL" FT CDS complement(1060096..1060533) FT /transl_table=11 FT /gene="ribH" FT /locus_tag="AARI_09440" FT /product="riboflavin synthase subunit beta" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.5.1.9" FT /note="catalyzes the condensation of 5-amino-6-(1-D)- FT ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4- FT dihydrohy-2-butanone-4-phosphate yielding 6,7-dimethyl-8- FT lumazine" FT /db_xref="GOA:E1VU58" FT /db_xref="InterPro:IPR002180" FT /db_xref="UniProtKB/TrEMBL:E1VU58" FT /protein_id="CBT75161.1" FT /translation="MSKPLNVAFIKASWHADIVDQSLAGFKAEMEASGQEYSINVVSVP FT GAYEMPLQAQRLAKTGKYDAVVAAALVVDGGIYRHDFVAQAVVGGLMRVQLDTDVPTFS FT VSLTPHHFHSNDEHQTFYFEHFLKKGAEAARAVRAVAAIEL" FT CDS complement(1060644..1061648) FT /transl_table=11 FT /locus_tag="AARI_09450" FT /product="putative luciferase-like monooxygenase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00296. Bacterial luciferase FT is a flavin monooxygenase that catalyses the oxidation of FT long-chain aldehydes and releases energy in the form of FT visible light, and which uses flavin as a substrate rather FT than a cofactor. There are structural similarities between FT bacterial luciferase and nonfluorescent flavoproteins FT (LuxF, FP390), alkanesulfonate monooxygenase (SsuD), and FT coenzyme F420- dependent terahydromethanopterin reductase, FT which make up clearly related families with somewhat FT different folds" FT /db_xref="GOA:E1VU59" FT /db_xref="InterPro:IPR011251" FT /db_xref="UniProtKB/TrEMBL:E1VU59" FT /protein_id="CBT75162.1" FT /translation="MSFGHWTDHPQSGTRSASDALLQAIDLAVAAEELGADGAYFRVHH FT FAQQYASPFPLLAAIGARTSRIEIGTGVIDMRYENPLYMAEDAGSADLISNRRLQLGIS FT RGSPEQVIDGWRHFGFEPREGESDADMGRRHTERLLEVLSGEGFAEPSPKPMFPNPPGL FT LRIEPHSDTLRERIWWGSGSNATAVWAAKLGMNLQSSTLKDDESGKPSHVQQAEQIQLY FT RDAWKEAGHAREPRVSVSRSIFALTDERDWQYFGRDRYSSDQVGNIDAKTRAVFGKSYA FT GEPDELAKKLAEDEAIAAADTLLLTVPNQLGVDYNAHVIESVLKHVAPLMGWR" FT CDS complement(1061723..1062007) FT /transl_table=11 FT /locus_tag="AARI_09460" FT /product="helix-turn-helix domain-containing protein" FT /function="3.5.2 Transcription regulation" FT /note="match to PF01381: helix-turn-helix. This is large FT family of DNA binding helix-turn helix proteins that FT include a bacterial plasmid copy control protein, bacterial FT methylases, various bacteriophage transcription control FT proteins and a vegetative specific protein from FT Dictyostelium discoideum (Slime mould)" FT /db_xref="GOA:E1VU60" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VU60" FT /protein_id="CBT75163.1" FT /translation="MVRLPLTAREIEQGKNLGALLREARGERTILDVALQAGLSPETLR FT KIETGRVATPAFSTIAAVASVLDLSLDAIWSALEEANGWHRPESPILAH" FT CDS 1062054..1062836 FT /transl_table=11 FT /gene="map" FT /locus_tag="AARI_09470" FT /product="methionyl aminopeptidase" FT /function="3.8 Protein modification" FT /EC_number="3.4.11.18" FT /note="responsible for the removal of the amino-terminal FT (initiator) methionine from nascent eukaryotic cytosolic FT and cytoplasmic prokaryotic proteins if the penultimate FT amino acid is small and uncharged" FT /db_xref="GOA:E1VU61" FT /db_xref="InterPro:IPR000994" FT /db_xref="InterPro:IPR001714" FT /db_xref="InterPro:IPR002467" FT /db_xref="UniProtKB/TrEMBL:E1VU61" FT /protein_id="CBT75164.1" FT /translation="MIEILTASEVERARETGRLVGNILNTLKHRVQVGTNLLEIDAWTK FT EMIEEAGAESCYVDYAPSFGSGPFGHYICTGVNDAVLHGLPRDYQLADGDLLTLDLAVT FT LKGIASDAAISFIVGTAARAEDLKMIETTQRALDAAIAQARPGAKVGDLSFAIGSVLTA FT EGYKVNMEFGGHGIGSTMHQDPHVSNDGRQGRGYTLRPGLLLAIEPWVMADTNKLVTDG FT DGWTLRSATGCRTAHTEHTIAITETGAEILTLPSGPLA" FT CDS complement(1062833..1063561) FT /transl_table=11 FT /gene="bioD" FT /locus_tag="AARI_09480" FT /product="dethiobiotin synthase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="6.3.3.3" FT /note="catalyses the following reaction: ATP + 7,8- FT diaminononanoate + CO(2) <=> ADP + phosphate + FT dethiobiotin" FT /db_xref="GOA:E1VU62" FT /db_xref="InterPro:IPR002586" FT /db_xref="InterPro:IPR004472" FT /db_xref="UniProtKB/TrEMBL:E1VU62" FT /protein_id="CBT75165.1" FT /translation="MIHVITGTDTEVGKTVSTAVLAARALQLGQSVAIYKPAQTGVQGQ FT EPGDAQDAARWLGHPERLTASEGVRLAEPMAPADAALCAGLDPVLALPSLDNHVQRIRE FT LAARHDAVLVEGAGGLLVELTAQGQNIADLAATLSAELVVVARPDLGTLNHSALTLEAC FT LARGFDRGTLLLGSYPAQPSVLHARNLDNLRQLAAGRGWHFAGALPANLVADPAGSRGA FT LHRAAGSLEWRQAAAPVTAT" FT CDS complement(1063558..1064736) FT /transl_table=11 FT /locus_tag="AARI_09490" FT /product="putative cytochrome P450" FT /function="4.6 Miscellaneous" FT /EC_number="1.14.-.-" FT /db_xref="GOA:E1VU63" FT /db_xref="InterPro:IPR001128" FT /db_xref="InterPro:IPR002397" FT /db_xref="InterPro:IPR017972" FT /db_xref="UniProtKB/TrEMBL:E1VU63" FT /protein_id="CBT75166.1" FT /translation="MNCPYAATASALDQAPLAGDLPAAYPAAINRRYRSIEDPATVRAI FT LARPEHFSPANALATAVPLAPAALRILSRVKFALPEVLASASGPEHLAVRRITAGFFSP FT AKVRAQREQVRARVREICAGLDTRLRRGEVLDLGTELAAVVPVEIMARMTGFPVPPRSS FT LKAWSQDSLELFWGWPDEPRQLELARSAAQYYAWLDGAVHEAVQRDDENLFAQLRRTGI FT GERQLRSLAYFLGIAGQETTSMLISTALHAGLRDHRWSALAHRDTGMAAARQLVGEVLS FT RASSVPTWRRIATSSIRLGDQEFQAGDELVLRLSGGELGTAADASLAFGHGIHRCLGAG FT LARMEAELVLAETARLLPTLVADPKAVRFGYSLSFQAPDAVFCRYPNESRHP" FT CDS complement(1064736..1065908) FT /transl_table=11 FT /gene="bioF" FT /locus_tag="AARI_09500" FT /product="8-amino-7-oxononanoate synthase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.3.1.47" FT /note="catalyzes an intermediate step in the biosynthesis FT of biotin, the addition of 6-carboxy-hexanoyl-CoA FT (pimeloyl-coA) to alanine to form 8-amino-7-oxononanoate: FT 6-carboxyhexanoyl-CoA + L-alanine <=> 8-amino-7- FT oxononanoate + CoA + CO(2)" FT /db_xref="GOA:E1VU64" 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:E1VU64" FT /protein_id="CBT75167.1" FT /translation="MAEPAPRWETWLGTRARVRELRGLQRNDAPRGRVFDLASNDYLGL FT AGHRQVRRAAADAALEHGAGAGASRVAGGTFAVHRELEAGLCSYAHRQSALVFSSGYTA FT NLGVLGALGGPGSLFIIDAHAHASLIDGAKLSASAVATAAHNDLEDVARLLHANREDPQ FT GKPRVLVVVESIYSVFGDAAALPKLAALCAQYGALLLVDEAHSLGAVPRGSAVHAAGLA FT GASHVLSTATLSKALGSQGGAVLLGGSGAQALREQLVNASRTFIFDTGLSPVAAAAALA FT ALRLATPERLAALQSNARLVFEQLRSYSHLADRVDAGAGAVHSVRMSSSAAAFRATAKL FT AAAGIAVACFRPPSVPDSISRLRLTAHAQHQGPELEIAIRTVARTIAEED" FT CDS complement(1065901..1067265) FT /transl_table=11 FT /gene="bioA" FT /locus_tag="AARI_09510" FT /product="adenosylmethionine--8-amino-7-oxononanoate FT transaminase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.6.1.62" FT /note="catalyzes an intermediate step in the biosynthesis FT of biotin, the transamination of 7-keto-8-aminopelargonic FT acid (7-KAP) to form 7,8- diaminopelargonic acid (DAPA): S- FT adenosyl-L-methionine + 8-amino-7-oxononanoate <=> S- FT adenosyl-4-methylthio-2-oxobutanoate + 7,8- FT diaminononanoate" FT /db_xref="GOA:E1VU65" FT /db_xref="InterPro:IPR005814" FT /db_xref="InterPro:IPR005815" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:E1VU65" FT /protein_id="CBT75168.1" FT /translation="MIATGSKLLARDAGLLWHPYAPLDDGARYAVTAARGTRLSLEDAR FT GERHEVFDGMSSWWSAVHGYRHPALDAAARGQLERFSHVMFGGLTHRPAIELAERLVTL FT APEGLSHVFLADSGSISVEVALKLALQYQDAKGRSGRSRFAALRGGYHGDTFATMGICD FT PVDGMHSAFAPLSAAQVFLPKPPAARRTEQGSWEHSESGMQQWEQATRRLLAAHAPELA FT GIVCEPVLQGAGGMHVYPPEVLRILRELADDYDLVLIADEIATGFGRTGELFAVQHAGI FT VPDIMCVGKALTGGYLTLAAMLCTTRIASALASGRGGTGSALLHGPTFMGNPLACAVAC FT ASLDLLTGAPGTGSPAQGPWRAQVSALEAGLRAALAPAAQLGHVIDVRVLGGVGAIELD FT GPVDVTALTRAAVDRGLWVRPFRNLAYVMPPYTSTPSDIAALGQSLVGALEQVHG" FT CDS complement(1067262..1068494) FT /transl_table=11 FT /gene="bioB" FT /locus_tag="AARI_09520" FT /product="biotin synthase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.8.1.6" FT /note="catalyses the following reaction: dethiobiotin + FT sulfur + 2 S-adenosyl-L-methionine <=> biotin + 2 L- FT methionine + 2 5-deoxyadenosine" FT /db_xref="GOA:E1VU66" FT /db_xref="InterPro:IPR002684" FT /db_xref="InterPro:IPR006638" FT /db_xref="InterPro:IPR007197" FT /db_xref="InterPro:IPR010722" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR024177" FT /db_xref="UniProtKB/TrEMBL:E1VU66" FT /protein_id="CBT75169.1" FT /translation="MSISPQRSTTIDCTELATRIEQGHELNAEEALELLSVDDAEVFRL FT VAAAGILRRKHFGNTVKVNYLVNLKSGLCPEDCTYCSQRLGSKAEILKYTWLKPEEAVH FT QAGLGIAGGASRVCMVASGKGPTDRDIDRVAAMIGSLKEEHPQVEVCACIGILKEGQAQ FT RLKAAGADAYNHNLNTAESLYPDICSTHSYAERVSTVEQSKSAGLSPCSGLIVGLGETA FT EQLVEAIFALRALDADSIPVNFLMPFDGTPLQGTWNLTPLACLRILAVVRMACPDKEIR FT MAGGREMHLRSLQANALEVANSLFLGDYLTSEGQDAKTDLAMIADAGFVVLGQEDQDPA FT SIARALGEAAAHAARQPEDAGNAGANGCSGSCCSSDASPACGSGSSGCGPAASQPLLRR FT RGAGTRETPNA" FT CDS complement(1068645..1069217) FT /transl_table=11 FT /locus_tag="AARI_09530" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF03807: NADP oxidoreductase coenzyme F420- FT dependent" FT /db_xref="GOA:E1VU67" FT /db_xref="InterPro:IPR004455" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VU67" FT /protein_id="CBT75170.1" FT /translation="MVNVSIIGTGNMGQAISSVLNKGGATIQMLGSGDSATAAYGDIIV FT LAVPYPAIESIIAERGEQFAGKVVVDITNPLNFETFDSLTVPADSSATAEIAKALPEAT FT VIKAFNTNFAATIAEGQVGGTQTAVLIAGDDETAKGELSALVTAGGLRAIDAGATKRAR FT ELEGIGFMQISLAAGEKIEWTGGFGIN" FT CDS 1069468..1070097 FT /transl_table=11 FT /locus_tag="AARI_09540" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VU68" FT /db_xref="InterPro:IPR017517" FT /db_xref="InterPro:IPR024344" FT /db_xref="UniProtKB/TrEMBL:E1VU68" FT /protein_id="CBT75171.1" FT /translation="MDTTQLWSLVRAERETLCEFLGNLNQSHWQQESLCPPWTVRHIVA FT HIAAAGSTATGAWLANMLRSGFNTDRHNARLLEKFLGDSPDQTFDNFQNSCGNSIAALN FT SVPALLGEVVVHSQDIAVPLGITLQPGAESIREVAEFFVSDNFAVNSKTLAKGLKIVAV FT DQEFAVGTGPEVRGKLLDIVMVLAGRRHGLPQLEGDGVQELQRRLG" FT CDS complement(1070165..1072513) FT /transl_table=11 FT /locus_tag="AARI_09550" FT /product="putative siderophore biosynthesis protein" FT /function="4.6 Miscellaneous" FT /note="may be involved in aerobactin-like siderophore FT biosynthesis" FT /db_xref="GOA:E1VU69" FT /db_xref="InterPro:IPR007310" FT /db_xref="InterPro:IPR016181" FT /db_xref="InterPro:IPR019432" FT /db_xref="InterPro:IPR022770" FT /db_xref="UniProtKB/TrEMBL:E1VU69" FT /protein_id="CBT75172.1" FT /translation="MTNYTFRTISLPEDTALLHSWIATEHAAFWGMPTASETEIAAEYR FT SLLETDDYEVLLGLDGAGSARFLVELYNPATSALAEAYNYVRGDRGLHFLAPAASTPQP FT GFTLDALSAAVQQAFSRPGTERIIVEPDQRNKAIHALNARVGFRPVRPVQLAEPDGSTK FT QALLSICTRNDFETATGRSLDSSFLSPERWERANRHVLAKALGEFSHERLLEPADHGEN FT RYSVQKDGHRYSFTARRYQLNHWLVDPHSLEHQQFADGIWHQAEVDAIDFITLFYRELT FT LSEAQLPTYLEELSSTLSSHCYKQVHATHDAAQLAQFPGDAAQSFQLIESSMTEGHPCF FT VANNGRMGVGRSDYLRYAPETGAALRLGWAAAHKSRAQFDAIDTLDYESLLSGELHPAE FT RQRLDDALEAALFGTGLSAEDYIFMPVHPWQWENRLSITFANDIARKQLIWLGTSEDEY FT QAQQSIRTFFNLSNPTRNYVKTAMSILNMGFMRGLSAEYMKVTPAINQWLGELFENDPV FT LSSQPVALLREIAAVGYRNPQFEAATDKSAPQRKMFAALWRESPISTLGNNEKLATMAS FT LLHVDVHGKSFAGALIRRSGLDPQTWLNQYLDAYLIPLVHCLAAYDLVFMPHGENVIMV FT LENGAVKKVLLKDLGEEIAVLSDRVELPEEIRRVRTGGDPVLSVFTDVFDSFFRFLAPL FT LDAEGLISEEEFWKSVVGRLLDYRDRHPEFTERFDELGLFAQSFPLSCLNRLQLRNNQQ FT MLDLTDQSGGLLYAGDLENPLASALAPLG" FT CDS complement(1072527..1073873) FT /transl_table=11 FT /locus_tag="AARI_09560" FT /product="putative L-lysine 6-monooxygenase (NADPH)" FT /function="4.6 Miscellaneous" FT /EC_number="1.14.13.59" FT /note="L-lysine 6-monooxygenase (NADPH) catalyzes the FT conversion of lysine to its N6-hydroxy derivative, the FT initial event in the biosynthesis of aerobactin, a FT siderophore which functions as a virulence determinant in FT many septicemic organisms" FT /db_xref="GOA:E1VU70" FT /db_xref="UniProtKB/TrEMBL:E1VU70" FT /protein_id="CBT75173.1" FT /translation="MNQPAEHFDAIAIGAGPFNLGFAALTDGLDDLKVAVLDASEKFVW FT HPGMMLPGTHLQVPFMADLVTMADPTSKHSFLNYLKEQGRIYPFYIRENFYALREEYSN FT YLAWAATNIDSVRFGHRVLEVEYRGGRYHLSVLTASGLSSFTANKLVLGTGTQPYLPPV FT VSDAARGTGKVVHSSDYMFHREQLLAPRAAESRPQVTCVLGSGQSAAEIFLDLLRCLPE FT DGHLIWATRSERYFPLEYTKLTLEMTSPEYIDHFHGLSMEQRDVLSAEQKGLYKGINAD FT LINEIHEELYQRSVNGAANVHLRTGCTATSIEAAAEQLAVTLRHERTAQDLEFVTDNLV FT MATGYRAGTPDFLDGITERINYLDDGRLNVDREYSIGLDEDIFVQNAELHTHGFTAPDL FT GMGAYRNSVIINRVAGRTVYPVEAQIAFQRFGAAELAGLPTADTANSRA" FT CDS complement(1073870..1075390) FT /transl_table=11 FT /locus_tag="AARI_09570" FT /product="putative pyridoxal-dependent amino acid FT decarboxylase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.1.1.-" FT /note="identified by match to protein family PF00282" FT /db_xref="GOA:E1VU71" FT /db_xref="InterPro:IPR002129" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="UniProtKB/TrEMBL:E1VU71" FT /protein_id="CBT75174.1" FT /translation="MGTSLPTLQIPDLPLPLYDDALLCADTARSYETASHLAASLVAQQ FT FAAVTSPTTGPTPQQLAAKIDRVDLHQPLGSSEASFSELHELYFKDAVYFHDPKYAAHL FT NCPVAIPAVVAENFVTSINTSMDTFDQSAGATLIERKLIAFTAGLIGFDAEQADGVFTS FT GGTQSNLQAMLIARNTATAKLQGSLPERLANLRIYCSQDAHFSIRNAAMLLGLGYDAAV FT AIPTDAQHRMDAQALRDRLAKDLAAGLVPMAISATSGNTDFGAIDPLPELRAIATEAGA FT WFHVDAAYGCGLLISNKHRHRLDGIEQADSVTVDYHKSFFQPIGSSSLVVRNAPTLESI FT AHYAEYLNPRAEAEAVPNQVAKSLQTTRRFDALKLWVTLRSLGATRLGDMFDKVIALAE FT DAQQEVAMRTQLHMAADVQLSTLVFSFEDPQHPLELAEHNALANQIRHRLYASGEAMIA FT ATTVAGKRMLKLTLLNPNTTLADISQILDAICRIGTSILAERTLGEKK" FT CDS 1075719..1076972 FT /transl_table=11 FT /locus_tag="AARI_09580" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VU72" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VU72" FT /protein_id="CBT75175.1" FT /translation="MTTESQGKIQGAQRLLLGSNATDAAGRSLVDITIDLVFVGTLGAT FT AMHMGLLNMLSSLAFVIASLPAGHLVDKYSALRVLRIGLGTKFALLICLALLAFTGTLS FT IPLGMLLCTLLGICNVFSETSQTTAVPQLIEEDPAHRTSSISKLIARLSAADQTMTVVI FT PAVAGTGFTLLGAPAMLGLATGLALLGLLLALRVRSYRQQLGAGPSDAAPKQKAKVLSG FT LQYLAKHRTLMAITLAVALANLGLAIGSAVEAIFIIKDLGFGELGYGLLASVGGAGGLV FT GAALAGRISGAYSPAKLLVFTGSAQALLAGCVLLAAFTTEAISLILLIVQALGWGVAAL FT MFNIASSSWVVDIVPEELLGRVLSARRLFTFGAVPLGGLLGGWLGSSFGTTAGLIGWVC FT ATSLAVLCFLLMRSSATR" FT CDS 1077015..1078088 FT /transl_table=11 FT /locus_tag="AARI_09590" FT /product="putative group 1 glycosyl transferase" FT /function="1.1 Cell wall" FT /EC_number="2.4.-.-" FT /note="match to PF00534: Glycosyl transferases group 1. FT Proteins containing this domain transfer UDP, ADP, GDP or FT CMP linked sugars to a variety of substrates, including FT glycogen, fructose-6-phosphate and lipopolysaccharides. The FT bacterial enzymes are involved in various biosynthetic FT processes that include exopolysaccharide biosynthesis, FT lipopolysaccharide core biosynthesis and the biosynthesis FT of the slime polysaccaride colanic acid" FT /db_xref="GOA:E1VU73" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VU73" FT /protein_id="CBT75176.1" FT /translation="MKLVIDARYTRITHHDGISRYTAGLIEATSKLADVTMLINDTRQL FT AMLPEVPYLKISGPTSVLEPLVALQINKLNPDVVFSPMQTIGTLGRKYPVILTLHDLIY FT YSHPHAPKFLPAPIRAGWFLFHQVYWPQRLLLNRADAVATVSNTTADLMRKHRLTKKHI FT GLVSNAPTGHFARRDVAKKPKKTLLYMGSFMEYKNVETLIRAMEYLPDYELHLLSGINE FT QRYAELAALVPAPGRVHFHNGVSDAEYERLLSECTALVTLSREEGYGLPLVEAMSMGTP FT VVVTDMPIFKEVAQDAALYASADDAKGFADQVRILDEQATWQEYSQRAVERAGSYSWQR FT SAQQLLDLAGYAADHKK" FT tRNA 1078227..1078302 FT /locus_tag="AARI_36670" FT /product="transfer RNA-Asn" FT /anticodon=(pos:1078260..1078262,aa:Asn) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 1078575..1079420 FT /transl_table=11 FT /locus_tag="AARI_09600" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR009937" FT /db_xref="UniProtKB/TrEMBL:E1VU74" FT /protein_id="CBT75177.1" FT /translation="MSEAESTQADESLKSSVKSAKAQVDGLKELVPQQLSDEIKLATTV FT LKGKGISIGMAAALAGAALLVVLLFVIAVVVTLVNVLALWLPGWAAALIVAGFFLLIAV FT ILGLGGYAKVKKALPLKPEAAIRGLRHDLGVLKDGSAFDVSTLDEPLKKKPAEDEDEAD FT KKKEPKPPAPSADELLLRTKRRRRQIQALRDNLGESVQAPLAKIDKVRSFTQSAGEKFS FT GAAAKAKGFVRPSSSSSSEDQSEADRAGSNRLEQVRPYIVMAGSGVALAAVLRALFKRS FT " FT CDS 1079507..1080418 FT /transl_table=11 FT /locus_tag="AARI_09610" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.990) with cleavage site probability 0.909 FT between position 29 and 30. 7 transmembrane helices FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="InterPro:IPR008521" FT /db_xref="UniProtKB/TrEMBL:E1VU75" FT /protein_id="CBT75178.1" FT /translation="MVWIAIAAALCSAFCLAFGAHFQSQAVRSAVGGLDLTIKNVGKLA FT SNKRWTSGLGLMGLGMALNVFALASAPLTVVQPIGAIALVITAMVNAKETDLTMNRPTV FT VAIISCMIGSVGFVLLAVTVTNGNQSVSEAEAHLIEMILAVVVGIVGLATIFFHKKLGA FT FFYILSAGVLFGFVAVLVRTIAIAVLGLGDSSFMQLPWLAGLAVVVAGLLGSYFVQKAY FT SKGPPDLVIAGLTVIDPIVGIAIGIGILGELRPDVPMVVTVLMLVAAILAIVGVTALSR FT HHPDVIERRNQTEAGKIMPESK" FT CDS 1080477..1081658 FT /transl_table=11 FT /locus_tag="AARI_09620" FT /product="putative group 1 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00534: Glycosyl transferases group 1. FT Proteins containing this domain transfer UDP, ADP, GDP or FT CMP linked sugars to a variety of substrates, including FT glycogen, fructose-6-phosphate and lipopolysaccharides. The FT bacterial enzymes are involved in various biosynthetic FT processes that include exopolysaccharide biosynthesis, FT lipopolysaccharide core biosynthesis and the biosynthesis FT of the slime polysaccaride colanic acid" FT /db_xref="GOA:E1VU76" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VU76" FT /protein_id="CBT75179.1" FT /translation="MAKEKPLTIVIAADTYPPDVNGAAMFCYRLATEMHARGHRMHVLA FT VRGDKGKTYTEVRDEAIVHRLESHSVPTHEYFRIVFPWEVNQQIDKLLADINPDVVHAQ FT SHYMIGQRTLGWARKNKVRSVATNHFMPENLDPFLPFPRWFKRIVAHNSWKDMGKIFGR FT ADFVTTPTPLAAKAMRERAKLSKVLPLSNGIEVGNYELAAGEVITKNEFPTILFAGRLA FT VEKNINELIEALPLMSKVPNAIIEIVGGGEQRTHLEKTADDLQLRDRVRFLGHVSDEQL FT RQAYLRCDVFCQPGTAELQSLVTLEALSASKPVVLANAMALPHLVDEGVNGYMFTPGDR FT QDLADKLDRILSMEEQERAKMGEAGHNKVKNHAQEKTMNSFEALYRGQEVSTQ" FT tRNA 1081759..1081835 FT /locus_tag="AARI_36680" FT /product="transfer RNA-Met" FT /anticodon=(pos:1081793..1081795,aa:Met) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(1082277..1082774) FT /transl_table=11 FT /locus_tag="AARI_09630" FT /product="putative secreted M23 family peptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.24.-" FT /note="identified by match to protein family PF01551. FT Members of this family are zinc metallopeptidases with a FT range of specificities. Peptidase family M23 are also FT endopeptidases. Signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.993) with cleavage site probability 0. 690 FT between position 27 and 28" FT /db_xref="GOA:E1VU77" FT /db_xref="InterPro:IPR011055" FT /db_xref="InterPro:IPR016047" FT /db_xref="UniProtKB/TrEMBL:E1VU77" FT /protein_id="CBT75180.1" FT /translation="MTVSVALTTVSTVPPSQPQPPAPAALSASNGWRWPLAGEPKIVGP FT FDKPAENWLPGHRGVDLGASEGDKVFAPQRGKVTFASRVVDRPVLVIDHGNGFKTSIEP FT VIAEAKVGDWVQAGAHVGNVGTGAHCSARCIHWGVRLNGEYIDPVLLIRDLRPSILLPL FT NQ" FT CDS 1083214..1084038 FT /transl_table=11 FT /gene="rpsB" FT /locus_tag="AARI_09640" FT /product="30S ribosomal protein S2" FT /function="3.7.1 Ribosomal proteins" FT /db_xref="GOA:E1VU78" FT /db_xref="InterPro:IPR001865" FT /db_xref="InterPro:IPR005706" FT /db_xref="InterPro:IPR018130" FT /db_xref="InterPro:IPR023591" FT /db_xref="UniProtKB/TrEMBL:E1VU78" FT /protein_id="CBT75181.1" FT /translation="MPVVTMRELLDSGVHFGHQTRRWNPKMKRFIFTERNGIYIIDLQQ FT SLSFIDRAYEFVKQTVAHGGTVLFVGTKKQAQEAIAEQANRVGQPYVNQRWLGGMLTNF FT QTVSKRVQRMKELEEINFEDVAGSGHTKKELLLLKRELTKLQNNLGGIRNLTRTPSAIW FT IVDTKKEHLAIDEAQKLGIPVVAILDTNCDPDEVTYPIPGNDDAIRSVNLLTRVVADAV FT AEGLIAKNNKAAGKSEGAAEPMAEWERELLEGEKAKAEAPAEEAATKADEAK" FT CDS 1084184..1085020 FT /transl_table=11 FT /gene="tsf" FT /locus_tag="AARI_09650" FT /product="elongation factor Ts" FT /function="3.7.4 Translation elongation" FT /note="associates with the elongation factor-Tu.GDP complex FT and induces the exchange of GDP to GTP. It remains bound to FT the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP FT hydrolysis stage on the ribosome" FT /db_xref="GOA:E1VU79" FT /db_xref="InterPro:IPR000449" FT /db_xref="InterPro:IPR001816" FT /db_xref="InterPro:IPR009060" FT /db_xref="InterPro:IPR014039" FT /db_xref="InterPro:IPR018101" FT /db_xref="UniProtKB/TrEMBL:E1VU79" FT /protein_id="CBT75182.1" FT /translation="MANYTAADIKALRERTGAGMMDVKKALDEANGDAEKAIEIIRVKG FT LKGATKREGRSTAEGLVAAKVDGNVGVMVEINCETDFVAKNDKFIALADKVLNAAVASG FT AADAEALLAFELEGKTIGDTVIEEGAILGEKIVVRRVARIEGAKVASYLHKTSKDLPAQ FT VGVLMAVDADSEAAATVAHDVAVHTAAMAPTYLSREEVPEDKVADERRIADETARAEGK FT PEAALTKIVEGRLTGFFKEIVLVDQAFAKDAKKTVGKVFEEAGTKPVAFARFRVGA" FT CDS 1085224..1085946 FT /transl_table=11 FT /gene="pyrH" FT /locus_tag="AARI_09660" FT /product="uridylate kinase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.7.4.22" FT /note="catalyses the reversible transfer of the gamma- FT phosphoryl group from an ATP donor to UMP, yielding UDP, FT which is the starting point for the synthesis of all other FT pyrimidine nucleotides" FT /db_xref="GOA:E1VU80" FT /db_xref="InterPro:IPR001048" FT /db_xref="InterPro:IPR011817" FT /db_xref="InterPro:IPR015963" FT /db_xref="UniProtKB/TrEMBL:E1VU80" FT /protein_id="CBT75183.1" FT /translation="MPTTPATKRRRVLLKLSGEVFGGGKVGVDPDTVRGVARQIAETVG FT EVEVAIVVGGGNFFRGAELSAAGMDRSRADYMGMLGTVMNCLALQDFLEQCGVETRVQS FT AIAMAQVAENYIPRRAIRHMEKDRVVIFGAGAGLPYFSTDTVAAQRALEVDADEVLMAK FT SGVDGVYTADPKKDPTAQKLDTLTYSEALLKNIRVMDQTAMTMCQDNKLDMLVFGMEGE FT GNVAAAIRGERIGTTVTV" FT CDS 1086024..1086581 FT /transl_table=11 FT /gene="frr" FT /locus_tag="AARI_09670" FT /product="ribosome-recycling factor" FT /function="3.7.5 Translation termination" FT /note="responsible for the release of ribosomes from FT messenger RNA at the termination of protein biosynthesis. FT May increase the efficiency of translation by recycling FT ribosomes from one round of translation to another" FT /db_xref="GOA:E1VU81" FT /db_xref="InterPro:IPR002661" FT /db_xref="InterPro:IPR023584" FT /db_xref="UniProtKB/TrEMBL:E1VU81" FT /protein_id="CBT75184.1" FT /translation="MIEETLAETAEKMERTIDAAKEDFATIRTGRAHPGMYSKVMVDYY FT GSPTPLQQLASFAVPEARTITITPFDVTALREIEKALGDPEVGANPSSDGKMIRVVLPV FT LTEERRKEYVKLAKAKGEDARVALRNHRRKAKDTIDKLVKDGEIGEDEGTRAEKDLDAL FT TKKHVDSVDEILKNKEAELLEV" FT CDS 1086581..1087846 FT /transl_table=11 FT /gene="cdsA" FT /locus_tag="AARI_09680" FT /product="putative phosphatidate cytidylyltransferase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.7.7.41" FT /note="phosphatidate cytidylyltransferase catalyzes the FT synthesis of CDP-diacylglycerol from CTP and phosphatidate. FT It produces key intermediates in phospholipid biosynthesis" FT /db_xref="GOA:E1VU82" FT /db_xref="InterPro:IPR000374" FT /db_xref="UniProtKB/TrEMBL:E1VU82" FT /protein_id="CBT75185.1" FT /translation="MPGSTENTGGNASAVPSVASGNAQPMTRREARALREAQEKAEKRG FT GKKRSEPAQAPAPQASQEQPAVDLAPSAEDKAKTAHAKQRTKIVFGADKEQPKKVAQPA FT SGQPVSVQPEPPQSDSEDLAETGEPDAQEAAIPPELLIGNPEPKKSRAGRNLPAAIGVG FT VVLLGIVLAGLFLYEPLLVFAVTVLSGIGCWEVARATTHAKTAVPQLPLYLASVLLPAS FT AVLGGVEALGFSFVACILIALLFRVMEGLKGAVASVMSSVFIITWVPLLLSFALLMLEG FT DNGQWLIATILLLAVANDTFGYIVGVLIGKHPMAPKISPKKSWEGFSGSMIGSMAIGAC FT AMYFWLDMPWWTGVILAFFTTIAATTGDFAESMVKRELGIKDMSNLLPGHGGIMDRLDS FT VLFVIPLGYLISHLLAWSVAVF" FT CDS 1087970..1088542 FT /transl_table=11 FT /locus_tag="AARI_09690" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR019932" FT /db_xref="InterPro:IPR019933" FT /db_xref="UniProtKB/TrEMBL:E1VU83" FT /protein_id="CBT75186.1" FT /translation="MSQQQDAPFSHVPDSEFGYNAKQVDAFLSRARATFNGGGNDDSVV FT TSHLIRRTTFAPQKGGYQAREVDGALDRLEDVFAKRERDDLIAHQGEEVWLQQVGRLAA FT ILRGRLHRSKGERFRRPSRSNASSYNVEDVDRLCDQLIDYFENDVPMAVDAVRRVEFRS FT AQGTDGYEESQVDAFLDRVVELMASID" FT CDS complement(1088613..1089821) FT /transl_table=11 FT /locus_tag="AARI_09700" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VU85" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VU85" FT /protein_id="CBT75187.1" FT /translation="MFTSTRGKTGYLYVACAVFMIAWGGNHFTPLLHLYEVLEGFHPWQ FT ANLLLGTYVGGLIPGLLLLGPLSDQHGRKPVLIAGTVISIFASLLLALDSHSLLLLCLG FT RLMSGVGVGAAMSVGSSWIKELSSHPFDTHAGPTAGAKRSSLTLTLGFGLGAAVSGAMA FT QWAPMPEQAPYFIHLVLSLVALAFLLRAQESLAPAQRTEGAWYKDLRIPSASHHRFRKV FT IIPTAPWIFAAAGVAYAIIPAAVQDRLGTWSTLYATVLTVLTLGTGALSQNLVPWIAKI FT TGGRALPVGMTLMTIGMLLSVLVAWVDTPVLALCAAVLLGAAYGICTVAGLIQVQTIAT FT AQDLAGLSGLYYSLAYSGFLLPTLLATLLPLMSYAVSLALVAAVCGICAIYCARSLRIP FT NAT" FT CDS complement(1089822..1090493) FT /transl_table=11 FT /locus_tag="AARI_09710" FT /product="GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF00392. This FT family of regulatory proteins consists of the N-terminal FT HTH region of GntR-like bacterial transcription factors. At FT the C-terminus there is usually an effector- FT binding/oligomerisation domain. The GntR-like proteins can FT be divided into six sub-families: MocR, YtrR, FadR, AraR, FT HutC and PlmA. Many of these proteins have been shown FT experimentally to be autoregulatory, enabling the FT prediction of operator sites and the discovery of cis/trans FT relationships" FT /db_xref="GOA:E1VU84" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VU84" FT /protein_id="CBT75188.1" FT /translation="MSYLLPWEPDQADGSLARRVAAHAAQRIVERSIPAGHLLTEAELS FT IEMGVSRTPSREAMLQLARWGLVRLMPKKGAVVTAITFEERRDLLATRGLFERGALEAL FT TSTPGRLAELSNSLNEPLQAQRAALASGDLLGFASADFAFHAALVQAGGNYVITDLLTE FT LAPRLARLTFEAALEHPEQLATYLQEHERLADLASQANATEFAQCLNAHLTKAHFPKKA FT N" FT CDS complement(1090603..1092078) FT /transl_table=11 FT /locus_tag="AARI_09720" FT /product="Na+/solute symporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="Solute:Sodium Symporter (SSS) family (2.A.21.y.z). FT Members of the SSS family catalyze solute:Na+ symport. The FT solutes transported may be sugars, amino acids, organo FT cations such as choline, nucleosides, inositols, vitamins, FT urea or anions, depending on the system" FT /db_xref="GOA:E1VU86" FT /db_xref="InterPro:IPR001734" FT /db_xref="UniProtKB/TrEMBL:E1VU86" FT /protein_id="CBT75189.1" FT /translation="MASALSISALVVVCLTTMLIAFYGLRISRTTSDFYVASRTVRPWW FT NASAIGDEYLSAASFLGVAGLIVLSGQSGLWFPIGYTAGYLMLLLFVAAPLRRSRAYTI FT PDFAQIRFENSPMLRKLTTYLVVVICWLYIVPQMHGAALTLSIATGLPGWVGPVVVATV FT VCVTVLSGGMRSVTFVQAFQYWFKLAALVIPTIFLLVRAIPQQSAGERAHSLYAQLESV FT NTMNLYETVSIILALLFGTLGLPHVLVRFYTNPTGQTARTTTVIVLCLLSAFYLLPTTL FT GVLGILYTPELGANNETDATILLLPGRLLDGVVADALTAIVVGGAFAAFLSTTSGLVVS FT LAGAISQEFFNGTVRGFRISTILATALPVLIAVLTSSLALAGAIGNVFAFTASTICPLL FT LLGIWWRSLTAKGAIAGLLTGAITCGLSLSIGIFLPTIDLWWVHLLRQPAAWSVPLAFV FT VMIVVSRRTRRAVPQNTDRVMALLHVPDPSRNS" FT CDS complement(1092071..1092478) FT /transl_table=11 FT /locus_tag="AARI_09730" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VU87" FT /protein_id="CBT75190.1" FT /translation="MHRSDAGPQPQPHEPPGRFAQQRPQRVRVQAPQDASLLPPNQSPE FT HTAEEFYVRQLIRSQLRLACAVAAGLLALLVGICSLLVFWPVVSIIQLFSIPLSWWVLG FT VGMYPLIIVAGLLYNRAAARNEQRYRSISRG" FT CDS complement(1092494..1093210) FT /transl_table=11 FT /locus_tag="AARI_09740" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VU88" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR007492" FT /db_xref="InterPro:IPR011006" FT /db_xref="UniProtKB/TrEMBL:E1VU88" FT /protein_id="CBT75191.1" FT /translation="MINVVVADDELPAVEEISFLLSQDSRIGKIHRATSGAAALKALEE FT NDVDALFLDIHMPALSGLDIARVISRFTHPPLIVFVTADEDQALQAFELAAIDYVLKPI FT RPQRLAESVRRICELVEETPAKPEMITVDQGGITKLIPRSDIAYVQAQGDYARLHTKDS FT SYLIRVPLNDLEQQWGESGFVRIHRSYLVCMDKIETVRLQTGKAAVIVHGAELPISRRA FT LPYLRERLAANRVRPL" FT CDS complement(1093240..1094421) FT /transl_table=11 FT /locus_tag="AARI_09750" FT /product="putative signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions. 1 FT transmembrane helice predicted by TMHMM2.0" FT /db_xref="GOA:E1VU89" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR010559" FT /db_xref="UniProtKB/TrEMBL:E1VU89" FT /protein_id="CBT75192.1" FT /translation="MSPALQVTLIAVTVVLGITIVGYFGFKISRSTREMGTDAEEATYK FT TLHHMSVAVPHLERGLTEEGAAKSAKALRRLLNCQVLLISDTSRILATDAGIDFTAQLE FT EDASKASASTLATGKTQVKHSAGMDIVAAPITVGDQGVGTVVALSVRAGASFVRAVSEV FT AVFVSAQVSTAQLDESRAMLLEAQMRALRAQISPHFIYNSLNAIASFINTDPARARELV FT IEFADFTRYSFRRRGEFTTLAEELEAIDRYLLLEKARFGERIKVSLQIAPEVLPTQIPF FT LALQPLVENAVRHGLEARPDGGVISITATEDGLHAVISVEDDGMGMDPEQLASVLAGTT FT TTMHVGLRNVDLRLRQLYGNSNGLVIETAPGAGTLITLRVPKFRAPDTSGQDV" FT CDS 1094617..1094961 FT /transl_table=11 FT /locus_tag="AARI_09760" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR007436" FT /db_xref="UniProtKB/TrEMBL:E1VU90" FT /protein_id="CBT75193.1" FT /translation="MSANPEHDVTGDVDFVTESQSEEFQELRKTHRSFVFPMAIFFLVW FT YFAYVLLADYFHDFMSIKVLGNINMGIVLGLLQFVSTFAITAAYVSFSNKKLDPKATKI FT RERLEREGVN" FT CDS 1094962..1096587 FT /transl_table=11 FT /locus_tag="AARI_09770" FT /product="Na+/solute symporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="Solute:Sodium Symporter (SSS) family (2.A.21.y.z). FT Members of the SSS family catalyze solute:Na+ symport. The FT solutes transported may be sugars, amino acids, organo FT cations such as choline, nucleosides, inositols, vitamins, FT urea or anions, depending on the system" FT /db_xref="GOA:E1VU91" FT /db_xref="InterPro:IPR001734" FT /db_xref="InterPro:IPR019900" FT /db_xref="UniProtKB/TrEMBL:E1VU91" FT /protein_id="CBT75194.1" FT /translation="MNQLSILAQAAGESTQVGNPLVNIAIFLAFVGVTLVIVLRASKNN FT KTAADYYAGGRSFTGTQNGTAIAGDYLSAASFLGIVGAIAINGYDGFLYSIGFLVAWLV FT ALLLVAELLRNTGKFTMADVLSFRLKQRPVRIAAAISTLAVCVFYLLAQMAGAGALVSL FT LLGIDEKLGQSLVIVIVGALMILYVLVGGMKGTTWVQIIKACLLIAGALIMTVWTLALF FT GFNFSELLGKAAEVAGNPEILNPGMKYGASDTSKLDFISLALALVLGTAGLPHVLMRFY FT TVPTAKEARKSVVWAIWLIGAFYLFTLVLGFGAGALIGPDRIAAAPGGVNSAAPLLAYE FT LGGTVLLGLISAVAFATILAVVAGLTITAAASFAHDVYASVIAKDKSTPEKEMKVARRT FT VLVIGVFAIAGGIGAQGQNVAFLVALAFAVAASANLPTILYSLFWKGFKTRGAVWSMYG FT GLGSALLLIIFSPVFSGSETAMIPSVDMVIFPLANPGIVSIPLAFFLGWLGSVTDKGIE FT DVTKQAEMEVRSLTGVGAEKAVDH" FT CDS complement(1096672..1097145) FT /transl_table=11 FT /locus_tag="AARI_09780" FT /product="AsnC/Lrp-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01037" FT /db_xref="GOA:E1VU92" FT /db_xref="InterPro:IPR011008" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR019887" FT /db_xref="InterPro:IPR019888" FT /db_xref="UniProtKB/TrEMBL:E1VU92" FT /protein_id="CBT75195.1" FT /translation="MQLLDSTDRRILLTLSTTAKRTGSAIATALNLGRNTVQTRMTRLE FT NEVLDSVDRRIPPEALGYGLLSFVELHVEQRCLEEIAAKLETIPEVLEAHGLTGSADIL FT VRVAAKDAEELFRVHGQLLHIEGVNRADSALSMAELVPYRTTALIKHSLSTDA" FT CDS 1097296..1098411 FT /transl_table=11 FT /locus_tag="AARI_09790" FT /product="pyruvate dehydrogenase E1 component subunit FT alpha" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.2.4.1" FT /note="the pyruvate dehydrogenase complex catalyzes the FT overall conversion of pyruvate to acetyl-CoA and CO2. It FT contains multiple copies of three enzymatic components: FT pyruvate dehydrogenase (E1), dihydrolipoamide FT acetyltransferase (E2) and lipoamide dehydrogenase (E3)" FT /db_xref="GOA:E1VU93" FT /db_xref="InterPro:IPR001017" FT /db_xref="InterPro:IPR017596" FT /db_xref="UniProtKB/TrEMBL:E1VU93" FT /protein_id="CBT75196.1" FT /translation="MPIVSTQHIDVAAGCLPTHQLLNVDGKRIPDEELDHYLKDLKEAD FT LADFLRDMVVLRRMDNEATALQRQGQLGLWAPLLGQEAAQIGSVRATEDDDFIFPSYRE FT HGVAWARGVKAEDLLSVWRGAQASGWDPNEVNIACQQIVIGSQALHAAGYGMGIKFDGG FT KQVSVAYFGDGATSQGDVNEAMVFAASYQAPVLFFCQNNQWAISEPVHLQSRTQIADRA FT HGFGLKTWRVDGNDILAVYAATKAALNHARNGLGPTFIEAVTYRMGSHTTADDPTRYRK FT NEQLEEWKAKDPIDRLVKYLHEMGADVQSYEQRAQNAADELAAKLRAAITTMEDPKVEE FT LFTNVYSEKHEPTERAARDYLGYLAEFEGGE" FT CDS 1098414..1099415 FT /transl_table=11 FT /locus_tag="AARI_09800" FT /product="pyruvate dehydrogenase E1 component subunit beta" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.2.4.1" FT /note="the pyruvate dehydrogenase complex catalyzes the FT overall conversion of pyruvate to acetyl-CoA and CO2. It FT contains multiple copies of three enzymatic components: FT pyruvate dehydrogenase (E1), dihydrolipoamide FT acetyltransferase (E2) and lipoamide dehydrogenase (E3)" FT /db_xref="GOA:E1VU95" FT /db_xref="InterPro:IPR005475" FT /db_xref="InterPro:IPR005476" FT /db_xref="InterPro:IPR009014" FT /db_xref="InterPro:IPR015941" FT /db_xref="UniProtKB/TrEMBL:E1VU95" FT /protein_id="CBT75197.1" FT /translation="MATTMLKALNKSLHDALAEDEKVILLGEDIGTLGGVFRVTDGLKN FT KFGEHRVVDTPLAESGIVGSAIGLAYRGYRPVVEIQFDGFTYPAFDQLVSQLAKMHYRS FT KGRVKMPVTVRIPYGGGIGSPEHHSESPEAYFAHTAGLRVFAPSSVEDAYTMLRQAIDC FT DDPVIFFEPKRRYHEKTDAELAAPAPDGSPKAKVIRSGEDVTVVGYGPTTYTLIDAAMA FT AEDEGISMEVIDLRTLDPLDIDTVAASVQRTGKLVVVHEASRTSGIGAEICAEITERCF FT DYLEHAPLRVTGFDIPYPPSRLESHHLPDLDRVMHAVDTVMRHHEATEGAAK" FT CDS 1099415..1100764 FT /transl_table=11 FT /locus_tag="AARI_09810" FT /product="dihydrolipoamide acetyltransferase component of FT pyruvate dehydrogenase complex" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="2.3.1.12" FT /note="the pyruvate dehydrogenase complex catalyzes the FT overall conversion of pyruvate to acetyl-CoA and CO2. It FT contains multiple copies of three enzymatic components: FT pyruvate dehydrogenase (E1), dihydrolipoamide FT acetyltransferase (E2) and lipoamide dehydrogenase (E3)" FT /db_xref="GOA:E1VU94" FT /db_xref="InterPro:IPR000089" FT /db_xref="InterPro:IPR001078" FT /db_xref="InterPro:IPR003016" FT /db_xref="InterPro:IPR004167" FT /db_xref="InterPro:IPR011053" FT /db_xref="InterPro:IPR023213" FT /db_xref="UniProtKB/TrEMBL:E1VU94" FT /protein_id="CBT75198.1" FT /translation="MTAQTFKLPDLGEGLTESEVLNWKIKVGEHVALNQIIAEVETAKA FT VVELPSPFAGFVQVLHATEGETVQVGGALVTFDDAPGGAESQSPGEGQKIAERTPTLVG FT YGAPAATGSRPTRKSRTAPAARPAPASTPVPAASPAPATKMPAAHKAAGSAVARCTPPV FT RKLARDHGIDISSLSGSGEDGLVLRRDVEQAIESGGAAAPASSASTASALAAQEGDRHV FT KITAVRRATAKAMVQSAFTAPHATEFLTVDVTDSMDLVERMRAHRLLKDVKLNITTLAA FT LVVTRLLKTYPALNSTWDEKADEIIEFGSVNLGMAVASDRGLLVPVLKNAQAKTLPVLA FT AELSEIILQGREGTLSPAQLTGGTFSITNVGVFGVDAGTPILPPGQSGILALGQVKRRP FT WEYQDQVALRHTMTLALSFDHRVVDGKEASEFLAGVGSVLEDPRMTNIFI" FT CDS 1100961..1102592 FT /transl_table=11 FT /locus_tag="AARI_09820" FT /product="dipeptide/oligopeptide ABC transporter, FT substrate-binding protein" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, binding protein (BP), FT OPN-family (oligopeptides and nickel), oligopeptides FT import" FT /db_xref="GOA:E1VU96" FT /db_xref="InterPro:IPR000914" FT /db_xref="UniProtKB/TrEMBL:E1VU96" FT /protein_id="CBT75199.1" FT /translation="MRYSHASKAVVLSAALALTLSACGGGSNETAGGEGDGSYVVTANT FT TEPQNGLLPANTNEVGGGRVMDLIFTGLVSYDANGAPVNELAESIETEDSQNYTIKLKA FT DQTFSDGSPVTAASFVDAWNFGAAAKNAQLNSYFFESIKGFDEVNKEGSKKEEMEGLKV FT VDDTTFTVELSQPESDFPLHLGYTAFMPLPEAAFEDPKAFGEKPVGNGPYKLTEWNHDV FT NLKLDVNESYDGPRKAANGGIDFKVYQSTDSAYNDLLSNNLDVLDQIPPSSLASYATDL FT GDRSVNSPYAGNATITIPGYLDHFKQGEEGNLRRAAISRAIDRQLIIDKVYSGGKVKAD FT DFTAPVLEGYKADIPGKEVTDFDADAAKKLWDEADAISEWKSGDEFSIGYNVDGAGNKE FT YVEAVVNQLKSNLGINAVAKPFSSFKELREKVTSHKMTGAFRTGWQADYPSLYNFLGPL FT FGTGAGSNDGQYSSEEFDNKLSEGLAATDPAEGAKIFNEAQEILFKDLPAIPLWYLAVQ FT GGWSENVDNVEFGWNGVPLYNEITGK" FT CDS 1102785..1103711 FT /transl_table=11 FT /locus_tag="AARI_09830" FT /product="dipeptide/oligopeptide ABC transporter, inner FT membrane subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, permease (IM), OPN- FT family (oligopeptides and nickel), oligopeptides import" FT /db_xref="GOA:E1VU97" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VU97" FT /protein_id="CBT75200.1" FT /translation="MLSFTLKRIVQLFPVFLGATLLVYFLVFATPGNPIAALSGGKPMS FT PATEAALTAQYNLDKPFWVQYGLYLKNLVTLDLGTSFSGQEVRDLLARAFPVTARLAIL FT ALLIESVFGILFGVIAGMRKGKLFDSTVLVASLLVIAVPTFVLGFLLQFVVGVKLEWAK FT PTVSGAATWGELFLPALVLGLVSLAYVLRLTRTSVIENKTADYVRTATAKGLSRNRVVT FT VHILRNSLIPVVTYLGADLGALMGGAIVTEGIFNVPGVGHLLYQAIQKGETPTVVAVVG FT VLVIVFVLANLIVDMLYALLDPRIRYA" FT CDS 1103704..1104726 FT /transl_table=11 FT /locus_tag="AARI_09840" FT /product="dipeptide/oligopeptide ABC transporter, inner FT membrane subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, permease (IM), OPN- FT family (oligopeptides and nickel), oligopeptides import" FT /db_xref="GOA:E1VU98" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VU98" FT /protein_id="CBT75201.1" FT /translation="MPENQNFNPEDGLPIRSNRAGKVSKYKIEHYVAPLDEAPLQAVDS FT VKETGKPLSMWAEAWRSLRKQPLFIISTVMILAVVIVAAFPQLFTSIDPNGNQACLLEN FT SNEPGRAGHFMGFNLQGCDIYARTIYGTRASLLVGLFTTIIVVLLGGAIGALAGYYGGW FT IDIILARLGDIFFALPLILGAIIVMQLPAFRENRSVWTVIVTLSIFGWPQLARITRGAV FT IEARNADFVKASRALGLSKFSALVKHVIPNSLAPIIVVATVNLGVYIVAEATLSFLGVG FT LPPDVMSWGNDISSAQTQLRNNPTMLMWPALFLSITVLSFIMLGDAVRDALDPKARKGA FT " FT CDS 1104730..1106373 FT /transl_table=11 FT /locus_tag="AARI_09850" FT /product="dipeptide/oligopeptide ABC transporter, FT ATP-binding subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, fused ATP-binding FT protein (ABC2), OPN-family (oligopeptides and nickel), FT oligopeptides import" FT /db_xref="GOA:E1VU99" 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:E1VU99" FT /protein_id="CBT75202.1" FT /translation="MTETATPKPLLEVKDLAITFSTPDGPVHAVRDANFTVMPGETVAI FT VGESGSGKSTSALAAIGLLAGNGRVSSGQILFDGEDISKASEKRFVELRGNHIGMVPQD FT PMSNLNPVWKIGFQVKETLKANGLAGDNPNKRVAQVLADAGLPDPETRARQYPHEFSGG FT MRQRALIAIGLACRPRLLIADEPTSALDVTVQQQILDHLDTMTSELGTAVLLITHDLGL FT AAERAEKVVVMYKGRVVEYGPALEILRNPQHPYTKRLINSAPSLSAQRGDKHEAIVDEV FT VPGKAEPLLKISNLTKVFDIRKGFGKKEKFTAVDNVSFEIPKGTTTAVVGESGSGKSTI FT AQMVLNLLDKTAGEIIFDGEQIGNLNEKHLFKYRRRVQPIFQDPYGSLDPMYSIFRTIE FT EPLRIHGIGNAASREKKVKELLEQVSMPASTMHRFPNELSGGQRQRIAIARALALQPEM FT IVCDEAVSALDVLVQAQVLELLDELQREMGLTYLFITHDLAVVRQIADNVCVMERGKIV FT EQGTADEIFASPKSAYTRNLLAAIPGASLI" FT CDS 1106978..1108315 FT /transl_table=11 FT /gene="trt" FT /locus_tag="AARI_09860" FT /product="reverse transcriptase/maturase" FT /function="3.6 RNA modification" FT /note="identified by similarity to protein SP:Q6DKY2 FT (Bacillus stearothermophilus). Heat-stable reverse FT transcriptase. Possible group II intron associated protein" FT /db_xref="GOA:E1VUA0" FT /db_xref="InterPro:IPR000123" FT /db_xref="InterPro:IPR000477" FT /db_xref="InterPro:IPR013597" FT /db_xref="UniProtKB/TrEMBL:E1VUA0" FT /protein_id="CBT75203.1" FT /translation="MNPGEYFLACSVEPAADGKDIRDQQVDLWEQVFSRGNLLIALKRV FT ERNKGSAGVDGLEAHELRDWCREHWIETRKSLDAGTYAPLPVRQVMIPKPDGGERMLGV FT PSVLDRLIQQALAQVLSPIFDEGFAPMSYGFRPGKSAHDAASMARKVIEQGYRWVVEVD FT LDAFFDRVNHDVLMSRIARKVKDKRVLKLVRKYLTAGIMAQGVRRETAEGTPQGSPLSP FT LLSNIMLDDFDQEFWSRDHRFVRYADDIRIFVKSKRAAERVLDQATKVLEQRLKLKVNR FT QKSVINPASVATLLGFGFYFVKGSKVRIRVAPKAWIRMKERIRRLTSRRWSVSMEYRIE FT QLNRFVRGWMGYFRLSMTADKFATLDQWFRRRLRQIRWVEWKRPRTRVANLRRLGIVKD FT KAYQWGNSSRAYWRVAKSPILHRALPTSYWEELGVLFFRRAWDRFQ" FT CDS 1108770..1110572 FT /transl_table=11 FT /locus_tag="AARI_09870" FT /product="dipeptide/oligopeptide ABC transporter, FT substrate-binding protein" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, binding protein (BP), FT OPN-family (oligopeptides and nickel), oligopeptides FT import" FT /db_xref="GOA:E1VUA1" FT /db_xref="InterPro:IPR000914" FT /db_xref="UniProtKB/TrEMBL:E1VUA1" FT /protein_id="CBT75204.1" FT /translation="MRFQRVSKAVAVGAALALALSACAPGGGDTGADASKDAGAGNGSA FT EAANSGKADLGDIKTAEDNINVTVGAVEFISYNGFTPNTYSTYNSAIVDRMFSGFAYTG FT TDGKLYPNEDMGSYEKISDDPLTIKYTINEEAKWSDGTPITVADSVLAWAVQNLNLNEG FT SKDKPLFNSVSVDLGDTVPEGPQGDWDGKEFTVEFTDPDPDWALQSWMLHPAHVVAEEG FT GLSTEELVTAIREGDSKKLEKAAKFWNEGWMTDPGTLTDEKIAPVSGPYKLGSWKAGES FT VTLVANENYYGTPPATKELTFRFIEDASMVQALQNKDVDVINPQPTVDTLAQLENLGDA FT VAIQKGDTLTWEHLDFNFAEGNAMTNLELRKAFAMCVPRQQIVDNLVKPLNPDAVVMNA FT REVFPFQENYQEVVDAAYDGRYDEVDIEGAKKILEEQDAVGTEVRIGYSAPNERRANQV FT STIKSSCDEAGFKISDEGSADFFSPNGAQDRGDYEVALFAWAGSGQITSGQNIYATGKP FT QNFGKYSNEEVDAAWNTLATSLDPAVHAEQTKKIEKLLWDDLFGIPVFAHPGLSASGSD FT IQNVRHTAAQDQIVWNAEQWVRAE" FT CDS 1110715..1112232 FT /transl_table=11 FT /locus_tag="AARI_09880" FT /product="dipeptide/oligopeptide ABC transporter, inner FT membrane subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, permease (IM), OPN- FT family (oligopeptides and nickel), oligopeptides import" FT /db_xref="GOA:E1VUA2" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VUA2" FT /protein_id="CBT75205.1" FT /translation="MWKFIAKRLGSAIAVLFAASLLLYVLVINSGDPLKDLRESNADNR FT EYLMAQRMEYMNLDEPWYGRYWDWLTGASKCLIGQCDLGRNINGVEVSGLLANAASSTL FT RLVVLATVIAAVLGIAIGVLTAIRQYSGLDYIVTFMTFLFFSLPVFWAAVLLKEYLAIS FT YNDWLADPQISVGTSIAIGIVVGLTLQMFLGGSLKRRGITFIAAAVFVPLVLQYSLWLN FT FYRYPQMGPAIIVVLTALVALSATTMSVGLKEKRVLYPALITVVLVLAMYYATFYMLLE FT PNSWILLFGLILAVLIPAAIGRFMGGRLRKAAMSVSIATGVVGAGLTIIDHMFRAWPGF FT LDVKGRPIATIGSSTANLEGGFWDHFLDNGTQLLMPTILLAVISLASYSRYTRSSMLEV FT QRQDYIRTARSKGLSERTVIFRHAFRNAMIPIATIAAFDFAGLIGGAVITERVFGWKGM FT GEMFATGLDHVDPAPVMAFFLVTGTAAILFNLLADIVYALLDPRIRV" FT CDS 1112284..1113354 FT /transl_table=11 FT /locus_tag="AARI_09890" FT /product="dipeptide/oligopeptide ABC transporter, inner FT membrane subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, permease (IM), OPN- FT family (oligopeptides and nickel), oligopeptides import" FT /db_xref="GOA:E1VUA3" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VUA3" FT /protein_id="CBT75206.1" FT /translation="MSTTNKNLNEREPQNLTSVAEVEDAKLARIHEKPKSQGRIVLERF FT VSHKPAMVSSVILIFITVFAFSSIGWGPLPGWWGQNFYQAGAVIDGGKPTLSLVPTWLG FT GEGIRIGEHPFGQDSVGKDYFALVMNGTQKSIIIGVVVGLVATFLGTVIGAVSGYFRGW FT VDEILMRITDLFIVIPLLVLAAVLGKMAGASTGSIIILALVLGLVTWTGLARLVRGEIL FT SLREREYVAAAQAMGSKTSRVIFKHLIPNTMGVIIVNATFAIAGAILLESSLSYLGFGV FT KSPESSLGLLISQYQNAFTTRPYLFWWPGMIIVTIALSVNFLGDGLRDAFDPRQVGKKR FT RRRAGMFALPTRKEKP" FT CDS 1113351..1115048 FT /transl_table=11 FT /locus_tag="AARI_09900" FT /product="dipeptide/oligopeptide ABC transporter, FT ATP-binding subunit" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, fused ATP-binding FT protein (ABC2), OPN-family (oligopeptides and nickel), FT oligopeptides import" FT /db_xref="GOA:E1VUA4" 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:E1VUA4" FT /protein_id="CBT75207.1" FT /translation="MSHAAPMNEQGSEDFALSFDDLNVVFETSGPEVHAVKGLSLAVRP FT GQVVALVGESGSGKSVTSTAAMGLLPGNANVTGVAKVGNVNVVGLDEGKLRKMRATDIA FT MVFQEPMTALNPVLTIERQLTEALELHDIAYGKEATDRAVQLLEMVGIPDPAKRIKQYP FT HQFSGGQRQRIVIAMAISCDPKVIIADEPTTALDVTVQAEILDLLRELKDRLNTGILLI FT THNMGVVADMADEVAVMFQGNLVETGTVEQVLLHPEHPYTQRLLSSVPRLSAPAVTSVQ FT GTHSSETAPAGRELVLEAKDLVLEYDMRGKIFRAVENVSFDVAKGEVLGIVGESGSGKS FT TIVKAVLGLLPVASGTLSVKGHDLPKLSPKEARKVRKQIGVIFQDPAASLNPRFPIGDC FT ITEPMVVHKVGTKAERIKRAEELLDAVKLPRNVINRYPHELSGGQRQRVCIARALTLNP FT ELLIADEPTSALDVSVQAVVLEMLQDLQRDFNFACLFVSHDLAVVDMLADAVVVMRSGK FT AVEQGMVESVLHAPTHDYTRRLLAAAPVPDPHEQALRREAWRVLNSTK" FT CDS 1115181..1115672 FT /transl_table=11 FT /locus_tag="AARI_09910" FT /product="cation binding domain-containing protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="match to protein domain PF01814: Hemerythrin HHE FT cation binding domain. Members of this family occur all FT across nature and are involved in a variety of processes. FT For instance, in Nereis diversicolor, protein P80255 binds FT cadmium so as to protect the organism from toxicity" FT /db_xref="InterPro:IPR012312" FT /db_xref="UniProtKB/TrEMBL:E1VUA5" FT /protein_id="CBT75208.1" FT /translation="MSAPNSGTAAGRLAQAFTREHHQIDEGIENYIANAGADPHARAQS FT LLSGIDALRRHIYLEEAIVFPHLPQDTLMMPLMVMHREHGELWRRMNALEASLRATTAP FT EQLETSCQELLSVLEQHNSKEEPIIYPYMDTALSPEEQSHLESLLDGGGLPEGWVCKAA FT " FT CDS 1115703..1115897 FT /transl_table=11 FT /locus_tag="AARI_09920" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUA6" FT /protein_id="CBT75209.1" FT /translation="MDLASILIVLAIIVLCALPFIFGSFRGLDRTADDLEGRDPQTARA FT LRKARKDIDHGKGYYGPRQ" FT CDS complement(1115967..1116428) FT /transl_table=11 FT /locus_tag="AARI_09930" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VUA7" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VUA7" FT /protein_id="CBT75210.1" FT /translation="MQLREVHPSDLDAFFAHQQEPEANLMAAYQARNPADRAVFDHHWN FT SILNDPNILVRTIEHEGDVVGSILVFDGDMPEINFWTSTKYWGKGLTTSAVDAFLAEYT FT KRPLTAHVVQDNLGSIKVLERRGFKTVGTEQIFSNARAEVVTENIMQLD" FT CDS complement(1116498..1117118) FT /transl_table=11 FT /locus_tag="AARI_09940" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00440: bacterial regulatory proteins, FT tetR family" FT /db_xref="GOA:E1VUA8" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023772" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:E1VUA8" FT /protein_id="CBT75211.1" FT /translation="MLASKYQSLNEPTDRERAKAERREALLREATRLFALNGYAGVSLE FT DLGAACGISGPAVYRHFAGKQAVLIALLVDMSKDIYAGGCAATEAGGTPLEILSRLVDF FT HTDFSLSRPDILQVQDRDLKSLPKAELALVRKLQNSYIGLWTTELAKLHPSGSKQSHRF FT RAHAVFGLLNSTAHSAHSPRTKKSGLKPLLSNMALAALTSPVV" FT CDS 1117358..1118512 FT /transl_table=11 FT /locus_tag="AARI_09950" FT /product="putative acyl-CoA dehydrogenase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.3.99.-" FT /note="possibly involved in the metabolism of lipids. Match FT to protein domains PF08028, PF02771 and PF02770. Acyl-CoA FT dehydrogenases catalyze the alpha,beta- dehydrogenation of FT acyl-CoA thioesters to the corresponding trans 2,3-enoyl FT CoA-products with concommitant reduction of enzyme-bound FT FAD" FT /db_xref="GOA:E1VUA9" 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:E1VUA9" FT /protein_id="CBT75212.1" FT /translation="MIDLELDDQHQDLVDMVREFAQEVVAPQSAQHDADHTFPYDIVKQ FT MGQMGLFGLPISEEHGGSGGDYFHLALALEELGKVDQSVAITLEAGVSLGAMPIYRFGN FT EAQKQKWLPALATGERLAGFGLTEPGAGSDASAALTKAKLEDGHWVIDGAKEFITNSGT FT DITSHVTATAVTGVDEATGKKEISAIIVPTGTEGFTAEKAYNKVGWHASDTHPLSFNGA FT RVPEENLLGERGRGYAYFLEILDEGRIAIAALATGAAQGCVDESVKYAKTRTSFGKTIG FT QYQSISFMIARMQSRAHAARLAYYAAAAKMLAGKDFKIEAAHAKLIASEAAMDNAREAT FT QIFGGYGFMNETLVARHYRDSKILEIGEGTTQVQQMLIARGLGL" FT CDS 1118594..1119817 FT /transl_table=11 FT /gene="dxr" FT /locus_tag="AARI_09960" FT /product="1-deoxy-D-xylulose-5-phosphate reductoisomerase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.1.1.267" FT /note="catalyses the formation of 2-C-methyl-D-erythritol FT 4-phosphate from 1-deoxy-D-xylulose-5-phosphate in the FT presence of NADPH. Forms part of a non-mevalonate pathway FT for terpenoid biosynthesis" FT /db_xref="GOA:E1VUB1" FT /db_xref="InterPro:IPR003821" FT /db_xref="InterPro:IPR013512" FT /db_xref="InterPro:IPR013644" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VUB1" FT /protein_id="CBT75213.1" FT /translation="MDWVSSQKTFIPAGHPRRVSLIGSTGSIGTQGLDVIDGAPELFTV FT AAISGGYNLERLAQQAVKHRPALVGSAVESKEELARAIQQAAEQASVSGYAPELAVGEL FT AATEVAAYTEADVVLNGITGAIGLAPTIAALEAGHLLALANKESLIIGGQVVKQIAAPG FT QISPVDSEHSALAQALRSGAPEEVAKLLVTASGGPFFGYSYEQLRNVTPAQALAHPTWD FT MGRMVTTNSATMVNKALEVIEAHLLFDVPLEKIEPVVHRQSIIHSMVEFIDGSVIAQAS FT PPDMRLPIALGINWPHRVPGAAKACDFSTAASWTFEPLDEEVFTAVKLAKQAASASGTH FT MALYNAANEVAVDAFHDGKIGFTDIVETIERVLNEYTPASDELSVATVMDTDRWARAHA FT AKIVEAKA" FT CDS 1119814..1121163 FT /transl_table=11 FT /locus_tag="AARI_09970" FT /product="zinc metallopeptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.24.-" FT /note="match to protein family PF02163: Peptidase family FT M50. Match to PS00142 pattern: neutral zinc FT metallopeptidases, zinc-binding region signature. 4 FT transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VUB0" FT /db_xref="InterPro:IPR001478" FT /db_xref="InterPro:IPR008915" FT /db_xref="UniProtKB/TrEMBL:E1VUB0" FT /protein_id="CBT75214.1" FT /translation="MSALLFIGGVLFMVVAVGLSIALHEIGHLVPAKLFKLRVPQYMIG FT FGKTLVSFKRGETQYGIKALPLGGYISMVGMYPPREQVASEKPGKKPNLFQKVFGQMVD FT DARSQANENVLPSDEGRLFYQLPIYKRIIIMLGGPIMNLIIGFVVITIVLTSFGQATPT FT TTVAEVYQCIASAQNANQTECTDEDVTAPAYEAGLLPGDTITAVNGAAVAQAEWNKLTD FT VIRDHPGEPITLDYVRDGQSHSTELTPYLTERPATDENGYVLLDEQGEYIMTKVGFVGM FT GSLQQDLTQPLSAVPGVIGDQLLKIGDVILHLPQRMVDVAQAAFGSEERDPNGPVSIVG FT VGRIAGEISAEGSISVADKFATLLSLVGGLNLALFAFNLIPLLPLDGGHVVGALYEGLK FT RMVARIFKIKKIKPVDTVKLLPLTYVVVVAMLVMGGLLIYADIFKPIQLF" FT CDS 1121187..1121486 FT /transl_table=11 FT /locus_tag="AARI_09980" FT /product="YCII-related domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein domain PF03795" FT /db_xref="InterPro:IPR005545" FT /db_xref="InterPro:IPR011008" FT /db_xref="UniProtKB/TrEMBL:E1VUB2" FT /protein_id="CBT75215.1" FT /translation="MTVFAVEYAYAENSTELRNEHRPAHREYLGGFLGEGAVRLLASGP FT TPVNDGALLIFAAESPEALNEVLLNDPFKKVGGVGKATVTEWNPVMGLLNEFAS" FT CDS 1121601..1122023 FT /transl_table=11 FT /locus_tag="AARI_09990" FT /product="peptidyl-tRNA hydrolase domain-containing FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF00472. This domain is FT found in peptide chain release factors, and a number of FT smaller proteins of unknown function" FT /db_xref="GOA:E1VUB3" FT /db_xref="InterPro:IPR000352" FT /db_xref="UniProtKB/TrEMBL:E1VUB3" FT /protein_id="CBT75216.1" FT /translation="MDVQITATLAIPAAELNWQFSRSSGPGGQHLNTTDSRVELSWVIG FT ASRVLSDWQRQRLLSKLGSKLVAGALVVTAAEERSQWRNRQIAQEKLAHLIQRALAPDA FT PVRKATKPTRGSQRRRLSSKANRSATKALRRKPGME" FT CDS 1122145..1122699 FT /transl_table=11 FT /locus_tag="AARI_10000" FT /product="putative FMN reductase" FT /function="2 Intermediary metabolism" FT /EC_number="1.5.1.29" FT /note="identified by match to PF03358. FMN reductase FT reductase catalyses the following reaction: NAD(P)H + FMN = FT NAD(P)(+) + FMNH(2)" FT /db_xref="GOA:E1VUB4" FT /db_xref="InterPro:IPR005025" FT /db_xref="UniProtKB/TrEMBL:E1VUB4" FT /protein_id="CBT75217.1" FT /translation="MATKVLTLVGSLREGSTNQQLAEAGSRNAPEGVEVAVFSGLENIP FT FYNEDHDIEGGVPAAAQALRDAAGDADALMLVTPEYNGTMPAVLKNAIDWLSRPFGAGA FT LKDMPTVVVGTAFGQYGGVWAQDEARKALNIAGANVLENVKLAIPNSVVRFAELHPKDD FT VEVVEQVSGVLKSIQEIAEAN" FT CDS 1122840..1124006 FT /transl_table=11 FT /gene="ispG" FT /locus_tag="AARI_10010" FT /product="4-hydroxy-3-methylbut-2-en-1-yl diphosphate FT synthase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.17.7.1" FT /note="part of the non-mevalonate pathway for terpenoid FT biosynthesis" FT /db_xref="GOA:E1VUB5" FT /db_xref="InterPro:IPR004588" FT /db_xref="InterPro:IPR011005" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR016425" FT /db_xref="UniProtKB/TrEMBL:E1VUB5" FT /protein_id="CBT75218.1" FT /translation="MTSVSLGMPAGPPPVLAPRRKTRQFQVGSVGVGSDSPISVQSMTT FT TKTYDINATLQQIAELTAAGCDIVRVACPTDKDAEALKIIAMKSQIPVIADIHFQPKYV FT YAAIEAGCGAVRVNPGNIRQFDDQVKEIAQAAKDHGTSIRIGVNAGSLDRRLLAKYGKA FT TPEALVESAVWEASLFEEHGFHDFKISVKHNDPVIMVRAYEMLAERGDWPLHLGVTEAG FT PAFQGTIKSATAFGALLSKGIGDTIRVSLSAPPVEEVKVGNQILESLNLRPRKLDIVSC FT PSCGRAQVDVYTLAEQVTAGLEGMKAPLRVAVMGCVVNGPGEARDADLGVASGNGKGQI FT FVKGEVIKTVPEDQIVETLIEEANRLAAEMGLDNDENPSSGSPVVSVS" FT CDS 1124044..1124856 FT /transl_table=11 FT /locus_tag="AARI_10020" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VUB6" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VUB6" FT /protein_id="CBT75219.1" FT /translation="MGRHDTTALIELLDRDPVANIFTRSQMSLHRSAVPDGFSHIIGLD FT GDDGLESACWVGANLAPTAMPAEDAKRYAAHALESRQRFASVFGPAETVLAMHDVLQGG FT QLEIFDVRDNQPLMAITECPASIRRNQLRPAQVQEFDLVLPASAAMFEEELGYSPLENG FT GSFYRNRVRQLIRDGHTLIDCDQRGNIIFKADLGTVTDKAVQIQGVWVNPKYRGQGLAA FT GYMAATVDYAKQFAPIVSLYVNDYNTAAIKTYQRIGFEQVGTFATILF" FT CDS 1124959..1125651 FT /transl_table=11 FT /locus_tag="AARI_10030" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUB7" FT /protein_id="CBT75220.1" FT /translation="MPAVFTGKKIMAVSCVFSVLLLASCSEDGPIEGNNSNSTAVVLDA FT KQLETELQEFAESMPEAKVFGDKALRSSIPAAQDWMENIEVNPSKCGVTFAAPIAEQLE FT NATMGAIEYPGGYLTVALFKDEEVLKEQWQAKSEESSGCSRYTVKSGDESRAYHLAKQP FT VDTQAALNESYVVTSSDGSTTEQQLIVRSANSNVLIGLQEKRKSGTAAEQVSSATVAVQ FT TLLGQLNQ" FT CDS 1125704..1126453 FT /transl_table=11 FT /locus_tag="AARI_10040" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUB8" FT /protein_id="CBT75221.1" FT /translation="MTKRLTLWTLPIAFMLAVTGCSAEQSSESTDSASGQAQSQKASPP FT AGEGKAGKLSGEQIEAIAKNLLDGDQAVQVIGNAQMQQQLKIAKEADLPSGIKPEKCAE FT LNAKYTVTDLTASVSATATSSSQAVGKVVQIFALTDDATRHNISKALKLDDLEGCEKVK FT LQLGGEQIEAERQILPLDVKADQSLTMSTSMDAGGGQTLTSVAVQALKGDKFVLVTLQT FT GTQQAAELSAQAVQLTDQAFAGLEAAQ" FT CDS 1126789..1126905 FT /transl_table=11 FT /locus_tag="AARI_10050" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUB9" FT /protein_id="CBT75222.1" FT /translation="MKKRSLWVLPVAAAFVLAGCGSNAGTEAETGSSEAPQQ" FT CDS 1126927..1127478 FT /transl_table=11 FT /locus_tag="AARI_10060" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUC0" FT /protein_id="CBT75223.1" FT /translation="MSAEQAAAVAKTLGGEGENVQVLDSEALSGSLESAKGLIDQMEIK FT PEKCAEYVSQQGTQDLEGINMAVAIEVNATGESNSYSVAGYEDASKLDTVKKMIDAKDL FT QGCDEFAMSVAGQEVSASAQILEADSDADSTIATHTAVVMNGTEVPGGSYQIQGVVGEN FT VVSVSQTITAEQSGSSQMRV" FT gene complement(1127461..1128078) FT /pseudo FT /locus_tag="AARI_34760" FT /product="partial transposase of ISL3 family" FT /function="4.5 Transposon and IS" FT gene complement(1128098..1128667) FT /pseudo FT /locus_tag="AARI_34770" FT /product="partial transposase of ISL3 family" FT /function="4.5 Transposon and IS" FT CDS 1128780..1128872 FT /transl_table=11 FT /locus_tag="AARI_10070" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUC1" FT /protein_id="CBT75224.1" FT /translation="MKSQQSDDEAVKALVEELNKAVEEVKAAAK" FT CDS 1128984..1130150 FT /transl_table=11 FT /locus_tag="AARI_10080" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domains PF01590 and PF00486" FT /db_xref="UniProtKB/TrEMBL:E1VUC2" FT /protein_id="CBT75225.1" FT /translation="MTLEHGITREPIQAALTAGEDPASKVRSLKNLYQHWAQGASIPEL FT VRPVVARSWSRAGSLGKGIVPLDSAAIGERRESNQELNGLVGLFRDRLLSMATQAGNQL FT VISDQQGYVLWVHGPSTVRRRSDGIGFIPGARWREADVGTNGIGAAMAERAPVQIFGPE FT HAREEQHSWVCTSAPVINPCTTGLVGTITLAGSFRTAHPHSLALATSVAREAESMLRAA FT HALKMQHLALSAAVPKGEYLLVDAQGSVAAAHGYSVGSRVSLPRSMSEGQNWIAGVGLV FT DARSTAGGWVLLRTQEDASLELIAGTNPQAVVHSPSGATRIPLSAKHWQILALLASCPS FT GVALQELQQLWPAGTPNVTIRAEISRLRSKLHGLIVSRPYRLVVPVLP" FT CDS 1130270..1132060 FT /transl_table=11 FT /locus_tag="AARI_10090" FT /product="putative FAD-dependent pyridine FT nucleotide-disulphide oxidoreductase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VUC3" FT /db_xref="InterPro:IPR000103" FT /db_xref="InterPro:IPR020946" FT /db_xref="UniProtKB/TrEMBL:E1VUC3" FT /protein_id="CBT75226.1" FT /translation="MSSNELQAQAQAWATQLQQALEVGDVQSATELFGDECYWRDLTAL FT TWNLHTSEGKEDIAKMLLGIERGAWPRNIQVTSAADADGVIEAWFSFENDRMEGLGLFR FT LRDNKCWTLLSTAQGLREFPEPAGLRRELGAEHGSSMSKENWLDRRIAQQQSLGITEQP FT YTLIIGGGQGGIGLAARLKRMGVPALVIDKHPRPGDQWRSRYHSLALHDPVWYDHMPYI FT EFPDHWPVFTPKDKMGDWLESYTKLMELDYWPLTEATSARQDPESDGWIVEVQRDGVPL FT TLRPTQLVLATGMSGIPNIPQYPGAEQFTGEQNHSSTHPGGERYAGKNVVVIGANNSAH FT DICADLVQNGAHPTMVQRSSTHIVRSESLMKHVLGGLYSEEALASGIDHNKADLIFASI FT PYKVLPEFHKPAFAQIREQDAGFYQSLENAGFDLDFGDDDSGLFLKYLRRGSGYYINIG FT ASELVADGSIALAKGEVSHLTESSVVLANGTQLPADAVVYATGYGSMNGWAAKLISQEV FT ADEVGKCWGLGSDTAKDPGPWQGELRNMWKPTKVKNLWFHGGNLHQSRHYSKYLGLQLK FT ARFEGIPTPVYALAETHHRA" FT CDS complement(1132354..1132470) FT /transl_table=11 FT /locus_tag="AARI_10100" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUC4" FT /protein_id="CBT75227.1" FT /translation="MVWNFPAHLAETRFLAPHATGARALSARDRAAHGVISQ" FT CDS 1132879..1134666 FT /transl_table=11 FT /gene="proS" FT /locus_tag="AARI_10110" FT /product="proline--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.15" FT /note="activates proline and transfers it to tRNA(Pro) as FT the first step in protein biosynthesis" FT /db_xref="GOA:E1VUC5" FT /db_xref="InterPro:IPR002314" FT /db_xref="InterPro:IPR002316" FT /db_xref="InterPro:IPR004154" FT /db_xref="InterPro:IPR004500" FT /db_xref="InterPro:IPR006195" FT /db_xref="InterPro:IPR007214" FT /db_xref="InterPro:IPR023717" FT /db_xref="UniProtKB/TrEMBL:E1VUC5" FT /protein_id="CBT75228.1" FT /translation="MVLKLSTTFLRTLREDPVDAEVASHKLLVRAGYIRRAAPGIYTWL FT PLGLKVLARVEAIVREEMNAIGAQEVHFPALLPREPYEQTGRWAEYGDGLFRLKDRKDA FT DYLLAPTHEEMFTLLVKDLYNSYKDLPVYLYQIQNKYRDEARPRAGLLRGREFIMKDSY FT SFNIDDEGLDEAYMAHRGAYLKIFERLGLEVVPVFAQAGAMGGSKSEEFLHPTAIGEDT FT FVRSPGGYAANVEAVTTVVPEAIEYTNAPAFEVLDTPDTPTIETLVAAANSLRPRESGA FT WEAKDTLKNVVLAVIDPEGNRQLVVIGVPGDRQVDLKRVEATVGIALDITGEVIVEAAN FT AADLAKHPELVAGYIGPGNGLDNAVLGTEGTSGITYLVDPRVVSGSSWITGANEKGKHV FT FGLVAERDFSFDGTIESVNVVAGDPAPDGSGPLRTERGIEMGHIFQLGRKYAEALNLKV FT LDQNGKQTVVTMGSYGIGVTRAVAALAEAYHDENGLAWPKQVAPADIHIVVTGKGPELL FT EAAEKLAGQFEAAGKEVILDDRPKVSAGVKFSDAELIGIPTIVVVGRGLADGVVEVKDR FT ATGERRDVNVENVVAELTA" FT CDS 1134703..1135518 FT /transl_table=11 FT /locus_tag="AARI_10120" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="6 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VUC6" FT /db_xref="InterPro:IPR002781" FT /db_xref="UniProtKB/TrEMBL:E1VUC6" FT /protein_id="CBT75229.1" FT /translation="MQEILEFLSVNGEPVSIWPLVLLLLAALGAGWIDAVVGGGGLIQL FT PALLLFPGVTPVQALATNKLGSIFGTTTSAVTYYRRTSPDLKTAIPMAITAMAGAFGGA FT ALATILPAEAIQPIIIAALIAVLLFTILKPKAGELSRLRYTGRAHYLRAIMIGLVIGGY FT DGMIGPGTGSFLIIAMVTVLGYNFLQSSAKAKIVNLCTNMGALLLFVPTGHVLVGLGLA FT MGVMNMLGGYLGARMAISKGSAFIRIVFVIVVSGLILKLGSDLILAGRA" FT CDS complement(1135519..1135950) FT /transl_table=11 FT /locus_tag="AARI_10130" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VUC7" FT /protein_id="CBT75230.1" FT /translation="MRSKIAELVSEAIGSRQGREQLSAHGWVQGMPIVIAQPEEIVKDV FT MSLVAAHQPPVLVATFNPEDNELWFLYVAIGCTALKVEDPLEEHTSIGELYKMAVGSSF FT LTFRIAQMPTSSVVHAMEPQRVRNHAGYRPVNISAVNGR" FT repeat_region 1136003..1136004 FT /rpt_type=DIRECT FT repeat_region 1136005..1136027 FT /rpt_type=INVERTED FT mobile_element 1136005..1137159 FT /mobile_element_type="insertion sequence:ISAar31" FT /rpt_family="IS630" FT CDS 1136091..1137125 FT /transl_table=11 FT /locus_tag="AARI_34780" FT /product="transposase of ISAar31, IS630 family" FT /function="4.5 Transposon and IS" FT /db_xref="UniProtKB/TrEMBL:E1VUC8" FT /protein_id="CBT75231.1" FT /translation="MGMRNPEVTDKERQQLKDYKNTAPHKLVVKKAEALLLLSAGVDPV FT IVADFVDREPSTLEDWVRDWCTQRMASLFTGHAGNLNRSFLTAEQKEAVEQVLSQPPGD FT EYLPAQFWDVPKLDRWLSTTFNVEYASPTSYQFLLRMAGLSFHKPEKFDRRRADDKLID FT QRIKEIREELAVPLADEDTLVSAADEVRIDQEAVVRRAWYEKNTKTVLQVDRQKASQSF FT IGFLDQNTGQCLTLRLDWQNSATILEAVQTLVGLYPGKKIVIVWDNATWHKNQLLRAEL FT GLGQSLRDVHLINFPPYAPDHNPIEHVWNDAKNAISNVQRDDFESTVTAFEAHTRSRSF FT DYKI" FT repeat_region 1137137..1137159 FT /rpt_type=INVERTED FT repeat_region 1137160..1137161 FT /rpt_type=DIRECT FT CDS complement(1137567..1138640) FT /transl_table=11 FT /locus_tag="AARI_10140" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUC9" FT /protein_id="CBT75232.1" FT /translation="MTEKSPHSPSRTTTSVRRAPGWIAPVLSGVLVAAVTWGIGSTVFR FT SALVERGLPETVNEASDDERTMWELGTQLEDLASQARKLAELAPGESASSVAALASSLS FT QGSALLGQLRFDDQQPVALAQSYSPEAVVELASKVSAVSASMPDFSQAELGRDSMLAQI FT AFQINLDARGTVAALGEEQDLGLALPLSEVSGEADQNDQPVACLPDAALLDPAKKITEA FT QNIEPTAVARALDRGYALDFLLQLKAARGADAAKDAIEARRSELGRQLHALRSIVDGQC FT ADLREPAYALPEDGLANLAALAQGAEQDFADALVIAAGNTDGEAGTQISATAFSVVQAL FT HSSDPANRILKNAAAGE" FT CDS 1138816..1139382 FT /transl_table=11 FT /locus_tag="AARI_10150" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VUD0" FT /db_xref="InterPro:IPR003728" FT /db_xref="UniProtKB/TrEMBL:E1VUD0" FT /protein_id="CBT75233.1" FT /translation="MTGMPADTEQEAQRLTALLSKEVESHGLLLEEVSLRPSGKQMIVQ FT IIVDKADGHESLNLDELGEVTTTISNALDKDAVYASAAPYELEVSSPGLSRPLTAQRHW FT IRAINRMVKISLADGTKLRGRLLEVNDSDVLVAEHREPAKKGMKVKVLDPATHAFENIR FT KAVVDPELNFDDALLDTIDTEDLEG" FT CDS 1139385..1140368 FT /transl_table=11 FT /gene="nusA" FT /locus_tag="AARI_10160" FT /product="transcription elongation protein NusA" FT /function="3.5.3 Transcription elongation" FT /note="participates in both the termination and FT antitermination of transcription. Interacts with RNA FT polymerase and binds RNA" FT /db_xref="GOA:E1VUD1" FT /db_xref="InterPro:IPR003029" FT /db_xref="InterPro:IPR004087" FT /db_xref="InterPro:IPR004088" FT /db_xref="InterPro:IPR009019" FT /db_xref="InterPro:IPR010213" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR013735" FT /db_xref="InterPro:IPR015946" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR022967" FT /db_xref="UniProtKB/TrEMBL:E1VUD1" FT /protein_id="CBT75234.1" FT /translation="MDIDLNALRILEKDRDIPMDVLIPTIESALLLAYNKTEGAMPGAR FT AHIERSNGHVAILVEDRDNAGVLLGEFDDTPHGFGRIAASTARQVIMQRLREAEDAQVV FT GEYAARVGTLISGVIQQGYSSHMVQVKIGDLEALLPPVEQSPGEKYQHGNRLRAYVVSA FT ERGNKGPAVTLSRSHPNLVRLLFEMEVPEIADGTVAVEALAREAGHRTKIAVHATKAGV FT NAKGACIGEMGTRVRAVMNELNDEKIDIVDYNEDPAKFIAAALSPSKVISVEILDAEER FT RARVVVPDSQLSLAIGKEGQNARLAAKLTGWRIDILAASGGKEPQL" FT CDS 1140509..1140829 FT /transl_table=11 FT /locus_tag="AARI_10170" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007393" FT /db_xref="UniProtKB/TrEMBL:E1VUD2" FT /protein_id="CBT75235.1" FT /translation="MKLHQQRTCIGCRTVTSKNELIRWVLKEGAPLRAVSLDQQGSASG FT RGTWTHGTQKCVQQAVQRRAFARAFRSAVDDSQVLQEFTAYEDQLAGNQLSGKHDESGS FT EI" FT CDS 1141006..1143948 FT /transl_table=11 FT /gene="infB" FT /locus_tag="AARI_10180" FT /product="translation initiation factor IF-2" FT /function="3.7.3 Translation initiation" FT /note="one of the essential components for the initiation FT of protein synthesis. Protects formylmethionyl-tRNA from FT spontaneous hydrolysis and promotes its binding to the 30S FT ribosomal subunits. Also involved in the hydrolysis of GTP FT during the formation of the 70S ribosomal complex" FT /db_xref="GOA:E1VUD3" FT /db_xref="InterPro:IPR000178" FT /db_xref="InterPro:IPR000795" FT /db_xref="InterPro:IPR004161" FT /db_xref="InterPro:IPR005225" FT /db_xref="InterPro:IPR006847" FT /db_xref="InterPro:IPR009000" FT /db_xref="InterPro:IPR015760" FT /db_xref="InterPro:IPR023115" FT /db_xref="UniProtKB/TrEMBL:E1VUD3" FT /protein_id="CBT75236.1" FT /translation="MAKPRVHELAKELGITSKEALTKLQDMGEFVRSASSTVEPPVARK FT LRDAFPGSNGAAKPAAAKPAAAKPATPGAPKPASKPAASAPKPGSKPAPAAPAAPAAPA FT PAAPAAPAAPAAPAAPAAPAAPTAKATPGAPLPGAAPAPKPGAKPAPKPGAPRPGNSPF FT SSQQGMRGAESGERRGGGNREGGRAPRPGAPRPGGPRPGNNPFSSQQGMRGEGGQGGPR FT PPRDGQRSPRPARDGQGGPRPPRDGQRGPRPAGAGGPRPAGQGAPRPAGAGGPRPGAGA FT GTTATPRMMPNRTDRPAPAGGGRPGAGAGGRGRPGGGNGGGTGGGFRPGAPRGRGGVGG FT AFGKGGAGRGKQRKSKRAKRQELEQMSAPSLGGVNVPRGTGDTEIRLRRGASITDFADK FT IGANPAALVTVLFHLGEMATATQSLDEATFEVLGEELGYKVLVVSPEDEDKELLEGFGL FT DLEAELEAEGEDVLEERAPVITIMGHVDHGKTRLLDAIRKSNVIEGEHGGITQHIGAYQ FT ITHEHEGRERAMTFIDTPGHEAFTAMRARGAEVTDVAVLVVAADDGVMPQTVEALNHAQ FT AAGVPIIVAVNKVDKEGANPDKVMGQLTEYGLVPEEYGGDTMFVKVSALQKLGIDELLD FT AVLLTSDVLELKANPDKSARGVAIEANLDKGRGSVVTVLVQSGTLCVGDTMVVGTAHGR FT VRAMFNENGENLDVALPSRPVQVLGMSSVPRAGDGFLITEDERTARQIADKRETAERNA FT MLAKRRKRITLEDFDKAVADGKIDTLNLILKGDASGAVEALEDSLMKIEVGDDVQLRVI FT HRGVGAITQNDVNLATVDNAIIIGFNVRPAERVAELADKEGVDMRFYSVIYSAIDDIEN FT ALRGMLKPEYEEVALGTAEIRMVFRSSKFGNIAGSIIRSGTIKRNTKARLVRDGNVVGD FT NLAIDSLRREKDDVTEVREGFECGIGLGSFNDIKEGDIIETFEMREKPRD" FT CDS 1144050..1144484 FT /transl_table=11 FT /gene="rbfA" FT /locus_tag="AARI_10190" FT /product="ribosome-binding factor A" FT /function="3.7.1 Ribosomal proteins" FT /note="associates with free 30S ribosomal subunits. FT Essential for efficient processing of 16S rRNA" FT /db_xref="GOA:E1VUD4" FT /db_xref="InterPro:IPR000238" FT /db_xref="InterPro:IPR015946" FT /db_xref="InterPro:IPR020053" FT /db_xref="InterPro:IPR023799" FT /db_xref="UniProtKB/TrEMBL:E1VUD4" FT /protein_id="CBT75237.1" FT /translation="MADSARAARLAKRVQVLMAQSLRTVIKDERIDNVTVTDARVTNDL FT QHATVYYTVFGDDEMKKDIATMLEKRGGALRKELGRNLTIRLTPTLAFVADEIPEGASH FT LEELLAKAREKDAEVAALREGKDFAGDQDPYKKDEDAEEA" FT CDS 1144674..1145141 FT /transl_table=11 FT /locus_tag="AARI_10200" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR015018" FT /db_xref="UniProtKB/TrEMBL:E1VUD5" FT /protein_id="CBT75238.1" FT /translation="MPEFTTTLSAVVGNNVGIIVPDDIVFGFGRGKRVPVTVCIDGDYT FT YRNTISSMHGQFLISFNAETRTATGKGAGDEISVKLELDEEPRTVEVPEPLAVLLAAEP FT ELLDAWNQLSYSKQRGHVDPIISARGEDTRTRRVEKVIKTLRTNIGEDTRD" FT CDS complement(1145665..1146120) FT /transl_table=11 FT /locus_tag="AARI_10210" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VUD6" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VUD6" FT /protein_id="CBT75239.1" FT /translation="MSMDPPQQLSVGTLLFIAQRAFEEEIATALHEQGFQFTLAQGRLA FT ARIAQQGSRLTELADAAGITKQSAAYLLKELERSGLVLRQPDPSDARAQRVLLTTRGLA FT AQQAARGIEQGIERRWAQLIGAANFARLKSALEDLRPHLDRHQGDSD" FT gene 1146373..1146663 FT /pseudo FT /locus_tag="AARI_10220" FT /product="truncated protein" FT /note="C-terminal section of a conserved protein" FT CDS complement(1146696..1148180) FT /transl_table=11 FT /locus_tag="AARI_10230" FT /product="putative molybdopterin oxidoreductase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF00174, which corresponds FT to the molybdopterin binding domain of oxidoreductases that FT require a molybdopterin cofactor" FT /db_xref="GOA:E1VUD7" FT /db_xref="InterPro:IPR000572" FT /db_xref="InterPro:IPR005066" FT /db_xref="InterPro:IPR014756" FT /db_xref="UniProtKB/TrEMBL:E1VUD7" FT /protein_id="CBT75240.1" FT /translation="MFAVAQFASAFFNSASSPFFALGSAIIDLTPPWLKDFAIATFGTN FT DKLALFISIGVVATALSVLVGLLAKRSFALACAAIIGLAVVMASAVVTRASTSLIDVLP FT TVLGAVAGMGVLQWLNRLASATAARPGEDAGSHGPSRRTFLLSSALSLAAAAIATGVST FT SLSASRNMADAARKALRLPAARTKAKALPAGVQVAEANMPRFVTPNQNFYRIDTALSVP FT QIDPAQWSLRIHGMVENEFTMSFDELLNQELVETYLTLTCVSNPVGGDLVGNAKWLGYP FT LRKLLERAVPQDGADMVLSASHDGFSASTPIQALTDDRMALLAIGMNGEPLPFEHGFPV FT RMVVPGLYGYVSATKWVVDLEVTRFQDKAAYWTTRGWSERGPIKMSSRIDTPRPFAKVP FT AGEVVLGGTAWAQTRGISRVQVQIDDSPWEDAELAAEASVDTWRQWRFAWKDAAPGMHS FT ATVRAYDAQGQLQTSEKANPVPNGASGWQRLQFTVQ" FT CDS complement(1148379..1149200) FT /transl_table=11 FT /locus_tag="AARI_10240" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="GOA:E1VUD8" FT /db_xref="InterPro:IPR018764" FT /db_xref="UniProtKB/TrEMBL:E1VUD8" FT /protein_id="CBT75241.1" FT /translation="MDKHENERTDTFALDALGEHEREELNQYPDSAPARHELDALQETA FT GLLGLDAQPIAPPARLKSSVMAAIRTTEQLPPAEDQEPAMDSAPVSAPTSDAKIESGSP FT VQPPAPQAGSGRGTQRFFALAAGVLLLAAVALGGLAINQTSQQRELENKLAAMASHQEE FT LTKILSAPDAKSKTQTLDDGARITLSYSAAEGLMAVSTSGMPELSSDKGYELWLISSDG FT AIPAGMLAGGDADGMIMLSDPMQGVTHFGITVEPATGSPAPTTDPIMVQSL" FT CDS complement(1149200..1149757) FT /transl_table=11 FT /locus_tag="AARI_10250" FT /product="RNA polymerase sigma factor" FT /function="3.5.1 Transcription initiation" FT /note="match to protein family TIGR02937. Sigma-70 family" FT /db_xref="GOA:E1VUD9" FT /db_xref="InterPro:IPR000838" 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:E1VUD9" FT /protein_id="CBT75242.1" FT /translation="MEDDSVRTPDALMQQVALGEESAFELLYDAMASRVFGLVLRVLRD FT RAQSEEVTQEAFVEAWQQARRFDPARGTAASWLLTIAHRRAVDRVRSSQASQARDLRIG FT IKDFEDSYDDVEENAILQDEAQRVSQALQRLTVPQREAIHLAYFGGYTHLEVAEMLKIP FT VGTAKTRIRDGMSKLRDLMGVA" FT CDS complement(1149951..1150613) FT /transl_table=11 FT /locus_tag="AARI_10260" FT /product="putative lipoprotein precursor" FT /function="1.1 Cell wall" FT /note="match to protein domain PF02469: Fasciclin domain. FT This extracellular domain is found repeated four times in FT grasshopper fasciclin I as well as in proteins from FT mammals, sea urchins, plants, yeast and bacteria (for FT example in the bacterial immunogenic protein MPT70)" FT /db_xref="InterPro:IPR000782" FT /db_xref="UniProtKB/TrEMBL:E1VUE0" FT /protein_id="CBT75243.1" FT /translation="MKRTYSKVAGAFGLIAVAAMGLSACSTGSETMESPTASASESSSP FT MASESAMDPASNLVGSGCAAYAEAVPTGDGSVAGMAKDPVAVAASNNPLLTTLTSAVSG FT KLNPDVDLVDTLNGDEFTVFAPVDDAFAAIPKDDLAAVAKDADTLSSILTYHVIPGQIA FT PDDLPGTHATVQGEDVEVTGSGDDLEVNGASVICGGVQTANATVYLVDTVLMPPAKK" FT CDS 1150927..1151850 FT /transl_table=11 FT /gene="truB" FT /locus_tag="AARI_10270" FT /product="tRNA pseudouridylate synthase B" FT /function="3.6 RNA modification" FT /EC_number="4.2.1.70" FT /note="responsible for synthesis of pseudouridine from FT uracil-55 in the psi GC loop of transfer RNAs" FT /db_xref="GOA:E1VUE1" FT /db_xref="InterPro:IPR002501" FT /db_xref="InterPro:IPR014780" FT /db_xref="InterPro:IPR015225" FT /db_xref="InterPro:IPR015947" FT /db_xref="InterPro:IPR020103" FT /db_xref="UniProtKB/TrEMBL:E1VUE1" FT /protein_id="CBT75244.1" FT /translation="MSKAGQNTEEQASGLVLVDKDQGMTSHDVVGRIRRLAGTRKVGHA FT GTLDPMATGVLVIGVNKATRLLTYIVGHDKTYTATIRLGQNTVTDDAEGEIISERIAAA FT VSDEDIEREVAKLRGDIEQIPSSVSAIKVDGKRSYARVRAGEQVELKARPVTISRFEIH FT EVRRENGGKILDVDVTVSCTSGTYIRALARDLGEALNVGGHLTALRRTEVGPYKIELTR FT TLEQLAQEFEILPIEKAAAALFPNRTVSVDEAVELSFGRTIPASHLSMDVAEGQTVAAF FT APNGVLVALLEDKGEKARTALVFTAK" FT CDS 1151868..1152230 FT /transl_table=11 FT /locus_tag="AARI_10280" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUE2" FT /protein_id="CBT75245.1" FT /translation="MISLNGFFIAGAVICALALVVAVIATAIRKHPDDWALIGAAATEL FT FLVVYGISAAIRQIGGNQVQGDPVEFWGYLITALVMPPVAFFWAISEKSRWSNSVLAAS FT AAVTFVMLFRMEQIWQ" FT CDS 1152241..1152708 FT /transl_table=11 FT /locus_tag="AARI_10290" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUE3" FT /protein_id="CBT75246.1" FT /translation="MGEKPRNSRIMQAAQNRNADKAPKPSRTTGLGRVIIAVYGILALA FT ATVRAVYQIMSKFDEAQVAYSLSLISGLIYIVATFSLSSAKRGAWLVSLYAVGIELVGV FT IVVGILSLTHPEVFAHPSVWSGFGEGYGYIPLVLPIVGLWWLYRNRSERHA" FT CDS 1152772..1153725 FT /transl_table=11 FT /gene="ribF" FT /locus_tag="AARI_10300" FT /product="bifunctionnal riboflavin kinase/FAD synthetase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.1.26" FT /EC_number="2.7.7.2" FT /note="EC 2.7.1.26 catalyses the following reaction : ATP + FT riboflavin = ADP + FMN. EC 2.7.7.2 catalyses the following FT reaction : ATP + FMN = diphosphate + FAD" FT /db_xref="GOA:E1VUE4" 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:E1VUE4" FT /protein_id="CBT75247.1" FT /translation="MHYWKGLDAVPADMAPTVVTIGNFDGVHLGHCEVLDAAVTQAKAR FT SAQSVAITFDPHPALVHRPDDAPELIMGIADRVDTLASVGLDATLMIHYTLEFADQSAE FT DFVRSIIVEKLNAVAVVVGHDVRFGHGNSGDFSYMQELGTKYGFDVIGVEDVGDKRRLS FT STWVREELAAGNVEAAAAILGRPHRMRGEVVHGHARGRELGFPTANLDPEATGIIPADG FT VYAGWVIDEAEVRWPAAISVGSNPTFEGVKRVVEAHVIDRPEEGVEDFDLYGQQIVVEF FT ISHLRPMVAYRGIEALIEQMTEDVDQARAVLATERH" FT CDS 1153730..1154515 FT /transl_table=11 FT /locus_tag="AARI_10310" FT /product="putative SAM-dependent methyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.1.1.-" FT /note="identified by match to protein domain PF08241" FT /db_xref="GOA:E1VUE5" FT /db_xref="InterPro:IPR013216" FT /db_xref="UniProtKB/TrEMBL:E1VUE5" FT /protein_id="CBT75248.1" FT /translation="MAEIPSLPQRAFVVGAQRRTELASAFQTDAESYDKIRPSYPQESL FT DFTLQHQPSTAIDIGCGSGIFTEQLVSEGLEVRAVDPSAEMLSVLSQRLPQIQITCAPG FT EDTGLASDSADLVTYAQAWHWVDHPKASAEAARLLHDGGWLTLLWNQLDVSIPWVHRLA FT RIMHAGDVHRPELEPPLGAQFQKPEHGIWHWSMPLEFQEIIELTKSRSYYRRSSEATRA FT KVEANLDWYWHEHLGHEQGEKVQVPYLTHAWRSRRRTRR" FT CDS 1154623..1154892 FT /transl_table=11 FT /gene="rpsO" FT /locus_tag="AARI_10320" FT /product="30S ribosomal protein S15" FT /function="3.7.1 Ribosomal proteins" FT /note="one of the primary rRNA binding proteins, it binds FT directly to 16S rRNA where it helps nucleate assembly of FT the platform of the 30S subunit by binding and bridging FT several RNA helices of the 16S rRNA" FT /db_xref="GOA:E1VUE6" FT /db_xref="InterPro:IPR000589" FT /db_xref="InterPro:IPR005290" FT /db_xref="InterPro:IPR009068" FT /db_xref="UniProtKB/TrEMBL:E1VUE6" FT /protein_id="CBT75249.1" FT /translation="MALDATIKNEIIKAYATHEGDTGSPEVQIAVMSRRISDLTEHLKM FT HKHDHHTRRGLMALVGRRRRMLGYLKNTDIERYRSLIERLGLRK" FT CDS 1155283..1155414 FT /transl_table=11 FT /locus_tag="AARI_10330" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUE7" FT /protein_id="CBT75250.1" FT /translation="MIFISAKCLTKIKNVTRGKKGCRWRYHPNKRNTSVHLFYGIST" FT CDS 1155488..1156045 FT /transl_table=11 FT /locus_tag="AARI_10340" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUE8" FT /protein_id="CBT75251.1" FT /translation="MTDYQELLQATRAHYGVCAAPRVSEAAALLTSLGGKTFDYSRFAG FT NLIDEYVDSARVVAAYDISDPELLASRSLPVEREMMEWPPEEDEDIYDVVFTKDEELWN FT VIQDELGGMRRAIVLLEHAEGDAGAVGNFRVAGFAQWLRETLWAATGVVPRDPGWPDES FT ATLYEKAFAMHGRPGCEPDPID" FT CDS 1156042..1156650 FT /transl_table=11 FT /locus_tag="AARI_10350" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUE9" FT /protein_id="CBT75252.1" FT /translation="MTSIIGLIRDTCQAARITSLAFGKGTASAAFIFLAQLLSLVSAGS FT RHIHLTSNRLGVFVLLRNRPVPALLRLCLFLVALCVPALLALAVRFLQVGSAWVQIAGF FT GISALLMIWLAAGMATMARQGEVALGIRGLPVGELYILSSLAQIPGSTSGVLADLRSAI FT SVLPSKSVVAAIAADETMAMRYEKLGFTRGSGLQVFVQR" FT CDS complement(1156849..1157595) FT /transl_table=11 FT /locus_tag="AARI_10360" FT /product="DJ-1/PfpI family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF01965: DJ-1/PfpI family. The family FT includes the protease PfpI Q51732. This domain is also FT found in transcriptional regulators such as Q9RJG8" FT /db_xref="InterPro:IPR002818" FT /db_xref="UniProtKB/TrEMBL:E1VUF0" FT /protein_id="CBT75253.1" FT /translation="MRKEHALKKILMVLTSVSEIGEDKEPTGYNVAEAAHPWKVFRDSG FT HFVDFASIKGGQPPRDTVDQDDPIQVQFTQDETTRAGLYNTARVGVVDPEQYDAVYLVG FT GHGTMWDFPDNEGLQKLVGAIYNKGGVVGAVCHGPAGLLDVELHHGLKLLSGKTVAAFT FT NDEEVAVGKDKIIPFFLADKLTEQGATHIAADNFEENVQVSERLVTGQNPASAAGVAKE FT MEKLLAEVIHQEKAAEAEAAAQDGAE" FT gene complement(1157683..1158159) FT /pseudo FT /locus_tag="AARI_10370" FT /product="truncated MFS superfamily transporter" FT /note="C-terminal section of a MFS superfamily transporter" FT gene complement(1158181..1158303) FT /pseudo FT /locus_tag="AARI_10380" FT /product="truncated MFS superfamily transporter" FT /note="section of a MFS superfamily transporter" FT gene complement(1158466..1158849) FT /pseudo FT /locus_tag="AARI_10390" FT /product="truncated MFS superfamily transporter" FT /note="N-terminal section of a MFS superfamily transporter" FT CDS 1159258..1160355 FT /transl_table=11 FT /locus_tag="AARI_10400" FT /product="putative aminotransferase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF00266: aminotransferase FT class-V. This domain is found in aminotransferases, and FT other enzymes, including cysteine desulphurase" FT /db_xref="GOA:E1VUF1" FT /db_xref="InterPro:IPR000192" FT /db_xref="InterPro:IPR015421" FT /db_xref="InterPro:IPR015422" FT /db_xref="InterPro:IPR015424" FT /db_xref="InterPro:IPR024169" FT /db_xref="UniProtKB/TrEMBL:E1VUF1" FT /protein_id="CBT75254.1" FT /translation="MSKTVLQRHLFGPGPCNPYPEATAALGLPLLGHLDPEFIARMDRV FT ANGLRTLWGTENSRTLPLSATGSAGMEAAFVSTINPGDVAVIAINGLFGERMCEVASRV FT GAEVVRVDHEYGTPINAQRVAQAHPNPAVIAGVHAETSTGVVSDIAALGAIKGDALLIT FT DAVTSIGGMPVLADEWGIDVGYAGTQKCIGVAPGLAPFTISDRAFERRVEKPQSWYLDL FT GLLGGYATGATGGQRTYHHTAPVSMVASLEAGIDRILAEGLDAVTARHQEAGTLLQEGL FT QEVGLELFAQEGFRLPQLTTVNVPEGVDSAKVRGYLLDRFNIEIGGGVGKYASTVWRIG FT MMGPNANPGSVALLLTALKEAIDKA" FT CDS complement(1160448..1161464) FT /transl_table=11 FT /locus_tag="AARI_10410" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF02016. This signature is FT found in the Escherichia coli microcin C7 self-immunity FT protein mccF and in muramoyltetrapeptide carboxypeptidase FT (EC 3.4.17.13). EC 3.4.17.13 belongs to MEROPS peptidase FT family S66 (clan SS). The entry also contains FT uncharacterised proteins including hypothetical proteins FT from various bacteria" FT /db_xref="InterPro:IPR003507" FT /db_xref="UniProtKB/TrEMBL:E1VUF2" FT /protein_id="CBT75255.1" FT /translation="MQTQVSPSIVPARLRTGDTLRAIAPSCSRTFVLEFDNRKWINERF FT AAMGLKQEFGKHVDENDSFDSSPISSRIADMHAAFADPSVAGIISVIGGFNSNELLPHL FT DWELIAANPKVFCGYSDFTALANAVHAKTGLVTYVGAHWSSFGMRDHFEPTGQWFQTAT FT HEHSWSIEHTSEFTDDLWFMDQDHRTVHTTEGPWVLTPGTATGKVIGGNLGTLHLLQGT FT EFMPSLDGTILFIEEDSSEDIHEVARKLASILQSPAGALITGLAIGRFQLESGITRSLL FT EQVIAKHPILQRIPVVANLDFGHTSPMFTLPIGGYAALSSNNGSVQLRFAHEQEQLG" FT CDS 1161645..1162043 FT /transl_table=11 FT /locus_tag="AARI_10420" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUF3" FT /protein_id="CBT75256.1" FT /translation="MKSLFDLEFKRFITPSIIKIVYILVMILLAIGYIGLVVTSFQADA FT LLGFLMFLIVGPLFVLIYLVMVRAGLESLIAQIRTAENTAELVRLAGGTPPADGGPRPF FT PGNPPAPQQPQDPTANGGHTPPANPYQK" FT CDS complement(1162113..1162514) FT /transl_table=11 FT /locus_tag="AARI_10430" FT /product="universal stress family domain-containing FT protein" FT /function="4.1 Adaptation to atypical conditions" FT /note="identified by match to PF00582: universal stress FT protein family. The universal stress protein UspA is a FT small cytoplasmic bacterial protein whose expression is FT enhanced when the cell is exposed to stress agents. UspA FT enhances the rate of cell survival during prolonged FT exposure to such conditions, and may provide a general FT stress endurance activity" FT /db_xref="GOA:E1VUF4" FT /db_xref="InterPro:IPR006015" FT /db_xref="InterPro:IPR006016" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VUF4" FT /protein_id="CBT75257.1" FT /translation="MTIVVGYIPSPEGESALARAILEAKCRESRLIVVNTSKGDQLIDD FT KLIDAKQFHDLEARLSEAGIDFWIERHPQGADAADQILDIARAQRAELIVIGMRKRTPM FT GKFLMGSNAQRILLQASCPVLSLKASSNW" FT CDS complement(1162511..1164124) FT /transl_table=11 FT /gene="tctA" FT /locus_tag="AARI_10440" FT /product="citrate transport protein TctA" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="Tripartite Tricarboxylate Transporter (TTT) Family, FT tricarboxylate transporter (TC 2.A.80.1.1). Identified by FT similarity to protein SP:Q6M234 (Corynebacterium FT glutamicum). Component of the TctCBA citrate uptake system" FT /db_xref="InterPro:IPR002823" FT /db_xref="UniProtKB/TrEMBL:E1VUF5" FT /protein_id="CBT75258.1" FT /translation="MGGFASALTPVNLLFAFAGVILGTAVGVLPGIGPAMAVALLLPLT FT FGMETSSALIMFAGIYYGGMYGGSTTSILLNTPGESATVITAIEGHKMAKAGRAAQALA FT TAAIGSFVAGTIGTALLVTVAPIVVKFAVSLGAPSYFAIMVLALVTVTAVLGSSKIRGF FT AALGLGLALGLVGMDPVSGQQRLTFGFAPLVDGLDIVVVAVAIFAIGEALWIAAHLRTS FT PARTIPVGAPWMGKEDWKRSWKPWLRGTAFGFPFGALPAGGAEVPTFLSYVTEKKLSKH FT PEEFGHGAIEGVAGPEAANNASAAGTLTPMLALGLPTNATAAVMLAFLTMKGIQPGPLL FT FENEPDLVWALIASLFIGNTLLLLINLPLAPLWAKLLKIPRPYLYAGILFFATLGAFSV FT NMQVADLWLLLLIGLLGFALRRFGLPVLPLILGVIIGPMAEEQLRKSFQLSAGEVSGLW FT SEPLAVGIYVLIAILLLLPVVISSIRRKRGTGTAASDALLAGTAAETAKPVLHGTGSAS FT EQEPSAKRTEHANAAESDES" FT CDS complement(1164146..1164649) FT /transl_table=11 FT /gene="tctB" FT /locus_tag="AARI_10450" FT /product="putative citrate transport protein TctB" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="possible TctB component of the TctCBA citrate uptake FT system (TC 2.A.1.1)" FT /db_xref="InterPro:IPR009936" FT /db_xref="UniProtKB/TrEMBL:E1VUF6" FT /protein_id="CBT75259.1" FT /translation="MSEVSTAKMKRVELLFAAFLLIVGIIVFVDASQLHVTYSQADVVG FT PKALPYVVSGILVLSAIALAITVLRGNLATGEEGEDVDLRQPSDWKVLIPLIGIFMLNL FT LIVNWVGWVISGTIMFFGTATCLGARRWVLTLVISLALAFGSFYGFYLGLGIKLPAGIL FT SGVL" FT CDS complement(1164646..1165659) FT /transl_table=11 FT /gene="tctC" FT /locus_tag="AARI_10460" FT /product="citrate transport protein TctC" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="Tripartite Tricarboxylate Transporter (TTT) Family, FT tricarboxylate transporter (TC 2.A.80.1.1). Identified by FT similarity to protein SP:Q8NLW1 (Corynebacterium FT glutamicum). Component of the TctCBA citrate uptake system" FT /db_xref="GOA:E1VUF7" FT /db_xref="InterPro:IPR005064" FT /db_xref="UniProtKB/TrEMBL:E1VUF7" FT /protein_id="CBT75260.1" FT /translation="MKPFKPFRALSALAAAAALALTATGCGVTSESSSTDAAESKGPIA FT NLRIMVPNTPGGGYDTTARVAAKVMDDASLASNPEVFNLAGAGGTVGLARMINEKGNGD FT LAMLMGLGVVGASYTNETEAKLTETTPIAKLIEEPGAIMVSKDSPYKTIDDLVKAWKED FT PSKLSVGGGSSPGGPDHLLPMQLAEAVGVDPKDVNFVSYDGGGDLLPAILGNKLAFAAS FT GAGEYMQQIEEGSVRVLATSGEERLEGVDAPTLTESDIDLVFSNWRGLVAPPEISEEDK FT AKWVQLITEMHDSAEWKEALATNGWSDAFMTGEEFSTFLAEQDERVASVLKTLGLA" FT CDS 1165889..1167499 FT /transl_table=11 FT /locus_tag="AARI_10470" FT /product="signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VUF8" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR016120" FT /db_xref="InterPro:IPR016121" FT /db_xref="UniProtKB/TrEMBL:E1VUF8" FT /protein_id="CBT75261.1" FT /translation="MGAVRFWLANLYTRRKLTLAGQYLILQLLIIAVVLAGVITVSLTQ FT ATNNFEKIEGRRSLSAAESLAANPLLRVLLPEAEPEMGSALPAMGESVRSTSGLQFVTI FT ADPRGTVVTSSYPDEVGTSILHPESAVTEGRGWTGEIWRNGNHVLIAQVPVLDDEGKMV FT GIVSAGQSYPSTGEMIQEIAPNALFTLVISLLLGTSGSVLLARWVKHQTRGLEPREIAE FT LFEHREALLHGVKEGIISVSPDSRVMLANDVAIELLQLPSHCVGKTLDELDVVPQVRHA FT LTTSQELPDRQFLVGERVLVFNRMPVKTARRDLGSVTTFRDKTELTLLEQELGDSKATA FT DMLRAQTHEFANQLHAISGLIQLGEYDEVVGFIDGVSFSRSKIFEDVSACIAEPTIAAL FT LIAKSSVAAERGVHLKMAPSSTLGRCEDQLARDLTTVIGNLVDNAMDAAAAAANPEIQV FT RIEETSELVRITVRDNGEGIAEDAMDEIFTQGFSTKDSAVSGGRGFGLAISRLVCRRRG FT GELAAANVQGARFTATLRK" FT CDS 1167510..1168184 FT /transl_table=11 FT /locus_tag="AARI_10480" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VUF9" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR024187" FT /db_xref="UniProtKB/TrEMBL:E1VUF9" FT /protein_id="CBT75262.1" FT /translation="MIKVLVIDDDFMVAKVHSGFVNSEPGFTVVGVAHSAGDAIKAAGA FT LSPDLILLDIHLPDMNGLDLLQRLREVQPELDVLVISAAREMDTVRRALRGGIVHYLMK FT PFSRDDLRERLEHYAKAYQPLGEAADQELQQADVNMLFGLGGQKRRPLPKGCSAETMEL FT VESIVKEAAEPISATETAQKLGTSRVSARRYLEYLAEENLAQVNLRYGGVGRPERRYSW FT RG" FT CDS complement(1168269..1169663) FT /transl_table=11 FT /locus_tag="AARI_10490" FT /product="putative flavin-containing monooxygenase" FT /function="4.2 Detoxification" FT /EC_number="1.14.13.8" FT /note="identified by match to protein family PF00743. FT Flavin-containing monooxygenase is a broad spectrum FT monooxygenase that accepts substrates as diverse as FT hydrazines, phosphines, boron-containing compounds, FT sulfides, selenides, iodide, as well as primary, secondary FT and tertiary amines. Generally converts nucleophilic FT heteroatom-containing chemicals and drugs into harmless, FT readily excreted metabolites" FT /db_xref="GOA:E1VUG0" FT /db_xref="InterPro:IPR020946" FT /db_xref="UniProtKB/TrEMBL:E1VUG0" FT /protein_id="CBT75263.1" FT /translation="MTQRVAIIGAGPSGIAQLRAFDSAKKTGQDIPEIVCFEKQDDWGG FT QWNYNWRSGIDKYGEPVHSSMYRNLWSNGPKEALEFAEYTFDEHFGRPISSYPPRAVLW FT DYINGRAEKSDIKKYVRFATVVRWVDYNESTELFTVTTEDLKTGKTASSDFTHVVVGTG FT HFSFPNVPEFAGIGTFPGELMHAHDFRGAERFAGKDILLIGASYSAEDIGVQSFKMGAR FT SVTYSYRTAPMGFDWPQGIEELPLIDRFEGSTAHFSNGVSRKFDAVILCTGYLHHYPFL FT PSGLALDSPNNVYPDTLYRGVASENNNKLYYLGAQDQWFTFNMFDAQAWYVRDLITGKA FT SIPAAGDQRISIDAWLKRFNAIETAEDEVKFQADYIRDLIEQTDYPMFDLDEVTRTFMA FT WKNDKKKNIMTYRDKVYPSVMTGTMAATHHTPWLSELDDSLERYMAPVPSESVEDLAAT FT EKAKSK" FT CDS complement(1170180..1171040) FT /transl_table=11 FT /locus_tag="AARI_10500" FT /product="prephenate dehydratase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.1.51" FT /note="catalyzes the decarboxylation of prephenate into FT phenylpyruvate. Involved in phenylalanine biosynthesis" FT /db_xref="GOA:E1VUG1" FT /db_xref="InterPro:IPR001086" FT /db_xref="InterPro:IPR018528" FT /db_xref="UniProtKB/TrEMBL:E1VUG1" FT /protein_id="CBT75264.1" FT /translation="MSNKISYQGEAGSNSNMACTELFPDKEAVPCASFEDAFSMVENGE FT ADLAMIPIENSLAGRVADIHVLLPESQLQIVAEHYLRIRFDLLGLPGSTIAGATEVHSH FT IHALGQCRKIIREHQLTPVIAGDTAGSAREVRDWNDPTKLSLAPPLAAELYGLEALATG FT VEDDQTNTTRFVVLARRQDLPNRSTMPESVITTLVFQARNVPSALYKALGGFATNGVNL FT TRLESYMVGSGFVATTFMVDIEGHPDDLPVRRALEELDFFTWEIKILGSYPASEHRQNT FT VASFV" FT CDS 1171231..1171974 FT /transl_table=11 FT /locus_tag="AARI_10510" FT /product="IclR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF09339: IclR helix-turn- FT helix domain and PF01614. This family of bacterial FT transcriptional regulators groups several proteins, FT including gylR, a possible activator protein for the gylABX FT glycerol operon in Streptomyces, and iclR, the repressor of FT the acetate operon (also known as glyoxylate bypass operon) FT in Escherichia coli and Salmonella typhimurium" FT /db_xref="GOA:E1VUG2" FT /db_xref="InterPro:IPR005471" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014757" FT /db_xref="UniProtKB/TrEMBL:E1VUG2" FT /protein_id="CBT75265.1" FT /translation="MAEPTLIGSVQKALRLLEAVASSAMPLPAKKLARMTELPLPTTYH FT LLRTLEFEGYLSKVDGGYAIGASALTVQNETVQEFLPRIRPVLRSLSAELGAATYLTTY FT QEGEIHLLAMVEGPEGRSVDLWVGIHESGHATAFGKAILANVSEELRDAYINSHDLHDL FT TPHTITSKGNLERSLAENVPIWSDKEEYLLGISCHAAPIRSNGLVGAVAVSLPSQRTLA FT AEETVSLKRAARRLGLAMGTPLITI" FT CDS 1172041..1173015 FT /transl_table=11 FT /locus_tag="AARI_10520" FT /product="2-oxoisovalerate dehydrogenase subunit alpha" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.2.4.4" FT /note="also named branched-chain alpha-keto acid FT dehydrogenase E1 component alpha chain. The branched-chain FT alpha-keto dehydrogenase complex catalyzes the oxidative FT decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2- FT oxopentanoate and 3-methyl-2-oxobutanoate (branched chain FT 2-oxo acids derived from the transamination of leucine, FT valine and isoleucine). It contains multiple copies of FT three enzymatic components: branched-chain alpha-keto acid FT decarboxylase (E1), lipoamide acyltransferase (E2; EC 2.3. FT 1.168) and lipoamide dehydrogenase (E3; EC1.8.1.4). The E1 FT component is composed of alpha and beta chains" FT /db_xref="GOA:E1VUG3" FT /db_xref="InterPro:IPR001017" FT /db_xref="UniProtKB/TrEMBL:E1VUG3" FT /protein_id="CBT75266.1" FT /translation="MDSNTQRELYQQMVMIRTYEETILREYHADKKPVFDIGAGLIPGE FT MHLAAGQEPVAAGVCAHATEGDSVTATHRPHHFALAHGVEINAMTAEIFGRVDGLGRGR FT GGHMHLFDPKAKFSCSGIIGEGLPVAVGQALAMKRRGTNNVAIAVAGEGAANQGAFHES FT LNLAALWKLPVIFVVEDNDWGISVPRSQSTSVPSNAVRAAAYGIPGVRVEDNAVESVYE FT EAGKAFERARNGGGPSLLEVSTLRLWGHFEGDAQGYRSDLEGVPGRDPIPTYEQTLRDA FT RVIDDSFVEQTRSEAVKRVEAAVEFAKSSPEPDPSTAGDYVFA" FT CDS 1173033..1174058 FT /transl_table=11 FT /locus_tag="AARI_10530" FT /product="2-oxoisovalerate dehydrogenase subunit beta" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.2.4.4" FT /note="also named branched-chain alpha-keto acid FT dehydrogenase E1 component beta chain. The branched-chain FT alpha-keto dehydrogenase complex catalyzes the oxidative FT decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2- FT oxopentanoate and 3-methyl-2-oxobutanoate (branched chain FT 2-oxo acids derived from the transamination of leucine, FT valine and isoleucine). It contains multiple copies of FT three enzymatic components: branched-chain alpha-keto acid FT decarboxylase (E1), lipoamide acyltransferase (E2; EC 2.3. FT 1.168) and lipoamide dehydrogenase (E3; EC1.8.1.4). The E1 FT component is composed of alpha and beta chains" FT /db_xref="GOA:E1VUG4" FT /db_xref="InterPro:IPR005475" FT /db_xref="InterPro:IPR005476" FT /db_xref="InterPro:IPR009014" FT /db_xref="InterPro:IPR015941" FT /db_xref="UniProtKB/TrEMBL:E1VUG4" FT /protein_id="CBT75267.1" FT /translation="MATDATGTRRLNTAKATVEAIAREMERDENVFVMGEDVGPYGGIF FT SSTTGLLERFGPERIIDTPISETGFIGAAIGAATEGMRPIVELMFVDFFGVCMDQIYNH FT MAKIHYESGGNVKVPLVLTTAVGGGYSDGAQHSQCLWGTFAHLPGMKVVVPSNPADAAG FT LMTAAIRDDNPVVFMYHKGIQGLAWMKKNRRSIGPVPGGDHVVEIGKAAVPRSGKDVTI FT VTLSLSVHHALDVAEELAGEGVDVEVIDLRSIVPMDTQAIIDSVTKTGHLVIVDEDYQS FT FGLSGEIAARIAEHDPTILKAPIGRVANPDLPIPYARTLEYTVLPTPARIKEAVLKQVG FT R" FT CDS 1174055..1174288 FT /transl_table=11 FT /locus_tag="AARI_10540" FT /product="possible lipoamide acyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.3.1.168" FT /note="possible lipoamide acyltransferase or N-terminal FT section of lipoamide acyltransferase (lipoyl-binding site). FT The branched-chain alpha-keto dehydrogenase complex FT catalyzes the oxidative decarboxylation of 4-methyl-2- FT oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2- FT oxobutanoate (branched chain 2-oxo acids derived from the FT transamination of leucine, valine and isoleucine). It FT contains multiple copies of three enzymatic components: FT branched-chain alpha-keto acid decarboxylase (E1), FT lipoamide acyltransferase (E2; EC 2.3.1.168) and lipoamide FT dehydrogenase (E3; EC1.8.1.4). The E1 component is composed FT of alpha and beta chains" FT /db_xref="GOA:E1VUG5" FT /db_xref="InterPro:IPR000089" FT /db_xref="InterPro:IPR003016" FT /db_xref="InterPro:IPR011053" FT /db_xref="UniProtKB/TrEMBL:E1VUG5" FT /protein_id="CBT75268.1" FT /translation="MSQVLFPVLSEKDPDAEGTVATWFVDSGATVAEGELIAEVAVDKI FT DMEINAPAAGVLTHLVEEGAVVIQNSAIASIA" FT CDS complement(1174413..1175423) FT /transl_table=11 FT /locus_tag="AARI_10550" FT /product="NAD dependent epimerase/dehydratase family FT protein" FT /function="2.4 Metabolism of lipids" FT /note="possibly involved in the metabolism of lipids. Match FT to protein family PF01370: NAD dependent FT epimerase/dehydratase family. This family of proteins FT utilise NAD as a cofactor. The proteins in this family use FT nucleotide-sugar substrates for a variety of chemical FT reactions" FT /db_xref="GOA:E1VUG6" FT /db_xref="InterPro:IPR001509" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VUG6" FT /protein_id="CBT75269.1" FT /translation="MNSSENTGTARRVLVTGASGMLGGAVAQLLRDKGHHVRTFQRGAS FT ASATDEVRGSLADQQAVAAAVESMDAVIHLAAKVSFTGAWEDFVATNITGTSNLLEASK FT DAGVKDFVFVSSPSVAHFGDSLAGAGAGQADPDKAHGSYARSKAAAELQALGADSPAFR FT VTAIRPHVVWGPGDTQLVERVIQRAKAGRLPLLDQGAALIDTTYIDNAAAAIVRGLERM FT DHAHGRALVVTNGEPRPVGELIAGICQAGGAPAPKLNVPGWLARGAGSVIEKLWLAAGS FT RNLVHDEPPMTRFLAEQLSTAHWFDQRETHEVLDWKPEVGIDEGLQKLAEHYRAS" FT CDS complement(1175420..1178008) FT /transl_table=11 FT /locus_tag="AARI_10560" FT /product="putative fatty acid Co-A ligase" FT /function="2.4 Metabolism of lipids" FT /EC_number="6.2.1.-" FT /note="match to protein family PF00501. This family of FT enzymes includes luciferase, long chain fatty acid Co-A FT ligase, acetyl-CoA synthetase and various other closely- FT related synthetases" FT /db_xref="GOA:E1VUG7" FT /db_xref="InterPro:IPR000073" FT /db_xref="InterPro:IPR000639" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR020845" FT /db_xref="UniProtKB/TrEMBL:E1VUG7" FT /protein_id="CBT75270.1" FT /translation="MTELFPGVNAIYSKYLDVPSTSQVDSPGTEHRWHFLDNNEELEQR FT GIKPVGTLVCVHGNPTWSYIWRSLLNHVSEHQLPWRVVAVDQLDMGFSERTGKFRRLAD FT RVNDLNDLTQALDLTGKITTVGHDWGGIISLGWAVAHPDQLENVVLTNTAIHPAGFELP FT SALKLASHPAVHGWGTKTSPAFLQVTHALAQPALAPAVRKAFMAPYTSADKREGVANFV FT ADIPFSQEHPSRPALDEISEAVRSLKVPALMLWGPKDPVFSDRYLRDLMSRLPHAQVHR FT FEGSSHLVGEDNDIATPIFQWLAGEQNSKNISRAEALGEYRPMLAELDSRTEDQTTAVV FT DINPARSLSWAELGERVNALAAGLQQIGVKAGDRVNLLVPPGIELTTLIYACLRLGAVI FT VVADAGLGTKGMGRAIKGAGPSYLVGIDRALTGARLFGWPGIKIAAEDLPTAKRKLLGV FT AHTLPELYAAGGKASAQELAFEPATPDADAAVLFTSGSTGPAKGVVYTHRELAAMRDTL FT RETYNLKAGSALVAGFAPFALLGPALGATSVTPDMDVTAPRTLTAAALADAALAVDATT FT VFASPAALANVLETQDALNPAQRETLEGVSLMLSAGAPIPEHLLAKVQDLVPNARVHTP FT YGMTEALPVTDIDLPGIRAAGAGNGVCVGTAVAGATVAIAPIDALGVAGDQPEYTPNAT FT GEILVRAPHVKDRYDRLWITEQLSTSIPGWHRTGDVGHLDEAGRLWVEGRLGHVLRTSK FT GAITPVAAEHAVESVAGAGRAALVGVGPAGTQAAVVVMETVPPARKPGPAANDLARQVR FT TAVGATGTEVAAVLVVPNLPTDIRHNSKIDRAALADWATATLAGGRIRKP" FT CDS complement(1178005..1179030) FT /transl_table=11 FT /gene="fabH" FT /locus_tag="AARI_10570" FT /product="beta-ketoacyl-acyl-carrier-protein synthase III" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.3.1.180" FT /note="catalyzes the condensation reaction of fatty acid FT synthesis by the addition to an acyl acceptor of two FT carbons from malonyl-ACP. Catalyzes the first condensation FT reaction which initiates fatty acid synthesis and may FT therefore play a role in governing the total rate of fatty FT acid production. Possesses both acetoacetyl-ACP synthase FT and acetyl transacylase activities. Its substrate FT specificity determines the biosynthesis of branched-chain FT and/or straight-chain of fatty acids" FT /db_xref="GOA:E1VUG8" FT /db_xref="InterPro:IPR013747" FT /db_xref="InterPro:IPR013751" FT /db_xref="InterPro:IPR016038" FT /db_xref="InterPro:IPR016039" FT /db_xref="UniProtKB/TrEMBL:E1VUG8" FT /protein_id="CBT75271.1" FT /translation="MNGNATFKHHNVALLSVNSVLAPEVVSSAEFDERLAPSLKRLRLS FT KKLLERVSGVKERRWWSDGVEFDDAAILAGKKALAQAGVDASEIGLLINTSVTRRNLEP FT SVASKVHNGLGLPSSAMNFDVANACLGFVNGMSLAANMIDSGQIKYALIVAGEDAKPTQ FT ETTFQRLNAETSTRDDYMREFATLTLGSGAAAAVIGPADAHPEAHRIVGGVSRAGTEHH FT ELCVGGPSGMYTDTKGLLDNGLELVVDAWDEAHQSGWNWKSMDRYVTHQVSKSYTNAII FT KAVGLVKDRVPITFSKWGNVGPASLPMTLSQEADSLKKGDRVLCMGVGSGLNTAMMEIA FT W" FT gene 1179548..1180771 FT /pseudo FT /locus_tag="AARI_10580" FT /product="truncated protein" FT /note="C-terminal section of a conserved protein" FT CDS complement(1181069..1181197) FT /transl_table=11 FT /locus_tag="AARI_10590" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUG9" FT /protein_id="CBT75272.1" FT /translation="MPVELSDQPDAPVLVQKDPTAQEAQSDHLAATGWAVHQVAMG" FT CDS 1181595..1182569 FT /transl_table=11 FT /locus_tag="AARI_10600" FT /product="putative ADP-ribosylglycohydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF03747. This FT family includes enzymes that perform ADP-ribosylations, FT such as ADP-ribosylarginine hydrolase (EC 3.2.2.19), which FT removes ADP-ribose from arginine residues in ADP- FT ribosylated proteins. The family also includes FT dinitrogenase reductase activating glycohydrolase" FT /db_xref="GOA:E1VUH0" FT /db_xref="InterPro:IPR005502" FT /db_xref="UniProtKB/TrEMBL:E1VUH0" FT /protein_id="CBT75273.1" FT /translation="MAYPLQAQDRIRGVLTGMASGDALGAGYEFNAPMPESAEISMIGG FT GLGNFAPGEWTDDTSMAIVIARGLLGSGGRFDAAASDYMIREWAKWAVQAPDVGNQTRA FT VLSHAQRVASEGGRTEPNTADALSGSEELHRRTGRSGGNGSLMRTAPVALAYLSEPPAA FT AFHAAVEISKLTHFDDEAAEACGLWTVAIQHAILTGELEIRAGLPLLNPERAMTWEQRI FT EQAENRQPREFSRNGWVVEAFQGAWSAITNAKETSKEHHLVSALEAAVRGGVDTDTVAA FT IAGSLLGAARGYSSIPLPWMEIVHGWPSLRIQHLLDISTELAG" FT CDS complement(1182592..1182903) FT /transl_table=11 FT /locus_tag="AARI_10610" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR015073" FT /db_xref="UniProtKB/TrEMBL:E1VUH1" FT /protein_id="CBT75274.1" FT /translation="MTEPEFAEYSWDFLERGSILVVILSGPAHLRLMDPENFAAFQDGE FT EFDAFGGLARRAPYRIKVPHSGPWFLAIDVAGLNVRGVRHEVSVVPPQKLEQRRSGKD" FT CDS 1183248..1183841 FT /transl_table=11 FT /locus_tag="AARI_10620" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUH3" FT /protein_id="CBT75275.1" FT /translation="MDILSGIDLEQLRMWIWILAIGFAVGMGLWRRHQLALVGFASTLL FT FATLNAGAGIYVLKRLGDSRWTVGDPPMSAPELSNVPFAGQYLEPLESSLESITGRVNS FT FWEFSQALPVALDFFTRSGWALVVAIPLIVIVLVRSYRTASRRRKDLQNLNGTVAQLQS FT ELAAIKLALPAESYLALPPENEEQPRQQRTRRKQ" FT CDS complement(1183933..1184976) FT /transl_table=11 FT /locus_tag="AARI_10630" FT /product="Zn-dependent alcohol dehydrogenase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.1.1.2" FT /note="catalyses the following reaction: an alcohol + FT NAD(+) <=> an aldehyde or ketone + NADH" FT /db_xref="GOA:E1VUH2" FT /db_xref="InterPro:IPR002085" FT /db_xref="InterPro:IPR002328" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR013149" FT /db_xref="InterPro:IPR013154" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VUH2" FT /protein_id="CBT75276.1" FT /translation="MTTMVNAYAAPSATEGLVPTQIERRELGPHDILIDIKFSGICHSD FT IHTVRGEWGPPTFPLVPGHEIAGIVAEIGSAVSKHKIGDRVGVGCLVNSCMECENCLAG FT DQQFCEQSVGTYGSTDRDGTMTQGGYATHVVVTENFALKIPEGINLDVAAPLLCAGITT FT FSPLKHWGAGPGKKVAVVGLGGLGHMAVKIASAMGAEVTVLSQSLKKKDDGLKLGASDY FT RATSDESTFKDLHKHYDLIINTVSASINISDYLGLLRVNGTMVNVGAPAEPLPVNAFAL FT IGGRRSFAGSQIGGIEETQEMLDFCAEHGLGAEIEVISADQINDAYERVLKSDVRYRFV FT IDTATLA" FT CDS complement(1185279..1186529) FT /transl_table=11 FT /locus_tag="AARI_10640" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="InterPro:IPR006970" FT /db_xref="UniProtKB/TrEMBL:E1VUH4" FT /protein_id="CBT75277.1" FT /translation="MGLYGETPEPTEEPTAEPTAEPTEEPTAEPTAEPTEEPTEEPTAE FT PTAEPTEEPTAEPTAEPTAEPTAEPTEEPTAEPTTEPTEVPEAVAPESGDQVAPGEEEL FT AYDSDPSNPAEGIYAFNVDADVEEGETVVTYRTSPSSEPQTIEGTVKDGQLVIKDGDSF FT GNNVKDFNQILVTVEDPKGNAISALLSGENVLKLQSEIIDDRLGVLLSEAGSDALRFDI FT PAGFPTVASDNFSFDLEYVAADGTPAVLSDADYVVDGETLVINDSRVSSLTAGTYYLSG FT KQQEETSDTAAAAAAFVNPAAEETGLTVSTWVGLYAPSDESSPNEEKTEEPTESSSAEP FT TAEPSASPSVEPTQENTPTASATQEAPDEDDNQKKQRDELADTGVNSALLIAGGLALGL FT IIVGGIAMAIRRRSRHS" FT CDS complement(1186629..1187342) FT /transl_table=11 FT /locus_tag="AARI_10650" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.351 FT between position 44 and 45" FT /db_xref="UniProtKB/TrEMBL:E1VUH5" FT /protein_id="CBT75278.1" FT /translation="MRKARLPLAVVAAGSLALGGVVGGTTMFTPAVAAPQTTSSQVAAE FT QAAYPIYNDEEFTLVDKGQEFWTFNYDESDPANGVVVLTDNTGLVSSGDKVWLSSSSVP FT NTGSTQEAKHENGQVVLNGPLDSPDGYSTWPDQLRQVSFSVSTGPEVGPDMVQHGGVPY FT VPEQGISLVTNEVGQKYAVPFLPVGTEVWSFDIPSGLSWLSQATVSINYYSDAADAPNG FT GFIDVELTDVDISDG" FT CDS 1188017..1190254 FT /transl_table=11 FT /gene="pnp" FT /locus_tag="AARI_10660" FT /product="polyribonucleotide nucleotidyltransferase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.7.7.8" FT /note="bifunctional enzyme, with a phosphorolytic 3 to 5 FT exoribonuclease activity and a 3 -terminal oligonucleotide FT polymerase activity. It is involved in mRNA processing and FT degradation" FT /db_xref="GOA:E1VUH6" FT /db_xref="InterPro:IPR001247" FT /db_xref="InterPro:IPR003029" FT /db_xref="InterPro:IPR004087" FT /db_xref="InterPro:IPR004088" FT /db_xref="InterPro:IPR012162" FT /db_xref="InterPro:IPR012340" FT /db_xref="InterPro:IPR014069" FT /db_xref="InterPro:IPR015847" FT /db_xref="InterPro:IPR015848" FT /db_xref="InterPro:IPR016027" FT /db_xref="InterPro:IPR018111" FT /db_xref="InterPro:IPR020568" FT /db_xref="InterPro:IPR022967" FT /db_xref="UniProtKB/TrEMBL:E1VUH6" FT /protein_id="CBT75279.1" FT /translation="MEGPEIQFAEAQIDNGRYGTRTIRFETGRIAKQAAGSAMVYIDDE FT TALLSATTAGKHPREGFDFFPLTVDVEERMYAAGRIPGSFFRREGRPSTEAILACRLMD FT RPLRPAFVKGLRNEVQVVVTVLSIEPDELYDVVAINASSMSTQLSGLPFSGPIGGVRVA FT LVDDGNGAQWVAFPKHSELKNAVFNMVVAGRIAGDDVAIMMVEAEATDNAWELIKERGA FT QAPTEEVVAEGLEAAKPFIKVLCEAQADLAARAAKETVEFPVFRDYEEDAYTAVEAAAS FT TRLAEIYTIADKQERDNAAGEFKDEIVAQLTAEGSAFAERAGEISKAFGAVTKHIVRQR FT ILTEQVRIDGRGLADIRQLSAEVEVLPRVHGSAIFERGETQIMGVTTLNMLKMEQQIDS FT LSPVKSKRYMHNYNFPPYSTGETGRVGSPKRREIGHGALAERALVPVLPSREEFPYAIR FT QVSEALGSNGSTSMGSVCASTLSLLNAGVPLKAAVAGIAMGLVSDTVDGETRYAALTDI FT LGAEDAMGDMDFKVAGTSEFVTAIQLDTKLDGIPASVLAAALTQAREARLHILNVLNQA FT IDAPDELNVNAPRIISVKIPVDKIGEVIGPKGKMINQIQEDTGADISIEDDGTVLIGAT FT NGESAEAARSAINAIANPQVPEVGERYLGTVVKLTTFGAFVSLTPGKDGLLHISELRKI FT NGGKRVEDVEDVVGVGQKLQVEITKIDDRGKLSLAPVVEDEEEAEEAVAAE" FT CDS complement(1190327..1191598) FT /transl_table=11 FT /locus_tag="AARI_10670" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR018723" FT /db_xref="UniProtKB/TrEMBL:E1VUH7" FT /protein_id="CBT75280.1" FT /translation="MVHLMTYVRESLRGIWFRATVFTIAGIVLAMSAPLLSGLIPEGLS FT NAFGNDAAGTLLQILASSMLAVTTFSLTTMVSAYSTATQIGTPRSIQLLIADRTSQNAL FT STYVGAFAFSIVGIIALSIGVYSDSERAFLLLGTILVIAMVLVTLLRWISFLTIFGRMS FT DIIDRVGKASSKAMQEYASQPLLGGQHWVQPPASAIPVEGTGSGFIVKVHVAELQRIAE FT SEGCQIWVERRTGSRIFAQHPVAYLSKPVSQESHQAVQRAFTIAAHRTFEQDPRLGLTS FT LSEISSKALSPGINDPGTVIEVLAATHKVLDIALTAKATETPSAPLVHVRQLDPRDLLE FT DAFRATSRDGAANVEVMMRIQKELGALIAIADSSWDEALKALAVDSLRRAELCLELEED FT LREVRLMHRQALSSNGISKDAGQG" FT gene complement(1191839..1192708) FT /pseudo FT /locus_tag="AARI_10680" FT /product="truncated short chain fatty acid transporter" FT /note="C-terminal section of a short chain fatty acid FT transporter (TC 2.A.73.y.z)" FT gene complement(1192712..1192891) FT /pseudo FT /locus_tag="AARI_10690" FT /product="truncated short chain fatty acid transporter" FT /note="section of a short chain fatty acid transporter (TC FT 2.A.73.y.z)" FT gene complement(1192898..1193206) FT /pseudo FT /locus_tag="AARI_10700" FT /product="truncated short chain fatty acid transporter" FT /note="N-terminal section of a short chain fatty acid FT transporter (TC 2.A.73.y.z)" FT CDS complement(1193448..1194008) FT /transl_table=11 FT /locus_tag="AARI_10710" FT /product="putative purine nucleoside phosphorylase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /note="identified by match to protein family PTHR21234. FT This family includes purine nucleoside phosphorylase (EC:2. FT 4.2.1) from most bacteria, which catalyzes the cleavage of FT guanosine or inosine to respective bases and FT sugar-1-phosphate molecules; uridine phosphorylase (EC:2.4. FT 2.3) from bacteria and mammals, which catalyzes the FT cleavage of uridine into uracil and ribose-1- phosphate, FT the products of the reaction are used either as carbon and FT energy sources or in the rescue of pyrimidine bases for FT nucleotide synthesis; and 5 -methylthioadenosine FT phosphorylase (EC:2.4.2.28) from Sulfolobus solfataricus" FT /db_xref="GOA:E1VUH8" FT /db_xref="InterPro:IPR000845" FT /db_xref="UniProtKB/TrEMBL:E1VUH8" FT /protein_id="CBT75281.1" FT /translation="MSDQKSLLVFAHADEAVAFADVEHLISGVGKVNASVALAGALASG FT DIKNVVVLGTAGVVGHAGEDRPSLDTIYQITKLIQHDFPLPSADVDPTGEVLLPDNKVT FT MATGDVFVSDGEQRIHIKSLGASLVDMEGYAYASICQRFNVPLQIFKIPSDYADDSASI FT DEWDEIAKQKSVQLREFYDKHLS" FT CDS 1194129..1194620 FT /transl_table=11 FT /gene="luxS" FT /locus_tag="AARI_10720" FT /product="S-ribosylhomocysteine lyase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.4.1.21" FT /note="takes part in the activated methyl cycle, by FT salvaging the homocysteine moiety from the cycle FT intermediate S-D-ribosyl-L-homocysteine. As a by-product of FT this reaction, 4,5-dihydroxy-2,3-pentanedione is formed, FT which is the precursor of the autoinducer AI-2, a signal FT molecule, which may be used by a variety of bacteria for FT communication among and between species" FT /db_xref="GOA:E1VUH9" FT /db_xref="InterPro:IPR003815" FT /db_xref="InterPro:IPR011249" FT /db_xref="UniProtKB/TrEMBL:E1VUH9" FT /protein_id="CBT75282.1" FT /translation="MSDIELAEVESFALDHTKVKAPYVRKIAVEHGPKGDAITNYDIRF FT VQPNHGEIPTAGLHTIEHTMAGLLRTRMEGLIDFSPFGCRTGFHMILWGEPTPEVVAAA FT IKSSLEDIAEKVTWEDVPGTEAVSCGNYRDHSLHSAREWAKVILEQGISLDAFDRSKLA FT " FT CDS 1194759..1195142 FT /transl_table=11 FT /locus_tag="AARI_10730" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.977) with cleavage site probability 0.233 FT between position 29 and 30" FT /db_xref="UniProtKB/TrEMBL:E1VUI0" FT /protein_id="CBT75283.1" FT /translation="MRKVHSLAAVLAAIAISISGCANFDAVRTSTISEECQSAIQKQNE FT AWSDPETPEKQIKEAEQASLGACKNLDEWSSAVSSNPGSMGYQELDTEAAANTVYLSCA FT SNDPERQTPVCADAAQRGYLDAS" FT CDS 1195318..1196688 FT /transl_table=11 FT /locus_tag="AARI_10740" FT /product="putative M16 family peptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.24.-" FT /note="identified by match to PF05193 and PF00675. These FT metallopeptidases belong to MEROPS peptidase family M16 FT (clan ME). They also include proteins, which are classified FT as non-peptidase homologues either have been found FT experimentally to be without peptidase activity, or lack FT amino acid residues that are believed to be essential for FT the catalytic activity" FT /db_xref="GOA:E1VUI1" 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:E1VUI1" FT /protein_id="CBT75284.1" FT /translation="MAMIPLPLHSVETTQFSPIDPADPTLVHRGEGGSEVRRSILPGGV FT RVLTEAMPGQRSTTVGFWVPVGSRDEEAGHYGSTHFLEHLLFKGTAKRTALEIAQSFDA FT VGGESNAATAKESTCYYARVLDTDLPMALDVIADMVTSAVIDPQELEQERGVIIEELAM FT DADDAMDVAHERFVANVLGDHPLGRPIGGTPEEIMEISREAVMEHYRAHYRPGELIITA FT AGSLEHDKLCELVLKALTEAGWELDPMAVPEPRRMGEPAKINSKAGLEVINRPGEQANI FT IIGCAGITGHDDRRQVLAVLNAVLGGGMSSRLFQEIREKRGLVYSTYSFSAAYTDAGYF FT GMYAGCAPAKAAQVIGLLGAELDRLAKDGITESELAQAKGQLSGGTVLALEDPGSRMSR FT LGRAEMITGEFQDIDEALARVNAVSAQDVQDLARELAAKDRVITVVGPFENEAALGL" FT CDS complement(1196759..1197493) FT /transl_table=11 FT /locus_tag="AARI_10750" FT /product="putative hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00561: alpha/beta hydrolase fold. This FT catalytic domain is found in a very wide range of enzymes" FT /db_xref="GOA:E1VUI2" FT /db_xref="InterPro:IPR000073" FT /db_xref="UniProtKB/TrEMBL:E1VUI2" FT /protein_id="CBT75285.1" FT /translation="MRHKYFGKLPETLKTRLSVRIAGRGPDVVLIHGLGASSRYFTPLA FT NIVAKKYRVIVPELPGHGKNLDGGRPVTVVRFAHEVALAMRELEVENAIVLGHSMGAQL FT AIELARAWPDLVKHLIIAAPAVNDREATLVRQARRIIEDFQHELNSVKAILLVDYLRCG FT IPWWAKSCAQMLEYSTIEMLRTVRCSIDVVCGTRDPLSPPEFGLRLVAKAPQANLTVMR FT QGAHGFNFSHAPELADLIDAVP" FT CDS complement(1197583..1197993) FT /transl_table=11 FT /locus_tag="AARI_10760" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.769 FT between position 35 and 36" FT /db_xref="UniProtKB/TrEMBL:E1VUI3" FT /protein_id="CBT75286.1" FT /translation="MGQKIKRFGFGVGTALTVAFAITSCGLASEPTALSDEDQASIVEL FT VQEQGTVIEAPTCSVEVFRIEDSTTYGWASCAPSSNESADAMAQVDAFPFRIDGQDLRR FT PDDGSKFDEDVKELFPEDLRSAINQHATGAGS" FT CDS 1198189..1198947 FT /transl_table=11 FT /gene="dapB" FT /locus_tag="AARI_10770" FT /product="dihydrodipicolinate reductase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.3.1.26" FT /note="catalyzes the second step in the biosynthesis of FT diaminopimelic acid and lysine, the NAD or NADP-dependent FT reduction of 2,3-dihydrodipicolinate into 2,3,4,5- FT tetrahydrodipicolinate" FT /db_xref="GOA:E1VUI4" FT /db_xref="InterPro:IPR000846" FT /db_xref="InterPro:IPR011770" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR022663" FT /db_xref="InterPro:IPR022664" FT /db_xref="InterPro:IPR023940" FT /db_xref="UniProtKB/TrEMBL:E1VUI4" FT /protein_id="CBT75287.1" FT /translation="MSAQIKVAVLGAAGRMGSEAVKAVTEAADMELVAELGRGDDLSQI FT LESGATHIVDLSVPASTVSNVRFAVENGLHAVVGTTGWDDERRANLEALLAEHPEAGVL FT IAPNFALGSVLASAFAATAAKYFESVEIIELHHPNKVDAPSGTAVRTAELIAKSREAAG FT VPASPDATETQIDGARGAVVDGINVHSVRLRGLVAHQEVLFGGPGEQLTLRHDSYDRAS FT FMPGVFLGLRTVASRPGLTYGLDGYLELGK" FT CDS 1198944..1199399 FT /transl_table=11 FT /locus_tag="AARI_10780" FT /product="tetratrico peptide repeat-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF07719. The tetratrico FT peptide repeat (TPR) is a structural motif present in a FT wide range of proteins. It mediates protein-protein FT interactions and the assembly of multiprotein complexes. FT TPR motifs have been identified in various different FT organisms, ranging from bacteria to humans. Proteins FT containing TPRs are involved in a variety of biological FT processes, such as cell cycle regulation, transcriptional FT control, mitochondrial and peroxisomal protein transport, FT neurogenesis and protein folding" FT /db_xref="GOA:E1VUI5" FT /db_xref="InterPro:IPR011990" FT /db_xref="UniProtKB/TrEMBL:E1VUI5" FT /protein_id="CBT75288.1" FT /translation="MKTKLWVGGILLLFTLYIGMTFTQAIRLLKTGELVAQIMGIAILV FT IPALCVWILIREVLFGLRTEKMGKSLAASGELPEDLPRMPSGRFIRSAADADFPRHQQD FT VEENPESWKSWYRLALAYEACGDKPRARKSLRTAIGFWRTDQNVNQR" FT CDS complement(1199454..1200695) FT /transl_table=11 FT /locus_tag="AARI_10790" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="10 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR012429" FT /db_xref="UniProtKB/TrEMBL:E1VUI6" FT /protein_id="CBT75289.1" FT /translation="MGLNLHSRMLQWHPWCNSWCDVFMNETRSSRRLLGVDAARLVAIL FT GMFAAHIFPLYETSGIPAYSPTFTGTFASGRASVLFMVLAGLSLTLLSTSLTRKRFSHP FT KVYSVLVLRALIIAVLGMAIGSINEGIAIILVHYGLLFLLLPLVLKLPRITIWVVSALW FT LVLMPILWRPLAAAALGQSLGHNPSFGDLLNPQLLFKDLTVTGYYPLLVWLGFGLLGVA FT LGSCNLRSKKTAGLLALVGSLIAILTYIGSRLISLQNAELIARELNLKASLVPTMITTG FT RLPGMNLEPLLDHSAYLWLPTGHSNSLLSTLHNAACAVAIIGLLLLIIGYLGPLGRIVA FT GAGRAPLTLYVGHLILLPAMQDYLEPSTIWWILVAATAIFGIWLGFSKASGPLEYGVRV FT LSGADVDAAAKDKL" FT CDS 1200694..1201605 FT /transl_table=11 FT /gene="dapA" FT /locus_tag="AARI_10800" FT /product="dihydrodipicolinate synthase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.1.52" FT /note="catalyses the condensation of aspartate semialdehyde FT and pyruvate, the first reaction specific to the FT biosynthesis of lysine and of diaminopimelate" FT /db_xref="GOA:E1VUI7" FT /db_xref="InterPro:IPR002220" FT /db_xref="InterPro:IPR005263" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR020625" FT /db_xref="UniProtKB/TrEMBL:E1VUI7" FT /protein_id="CBT75290.1" FT /translation="MATSAIDNQAYPFGTVLTAMVTPFDEAGEVDYALAAKLATKLVDD FT GCDGLVVTGTTGETSTLTDEENIEMFRTVVNAVGDRAAVLAGSTTNDTRHSIKLSLAAK FT EAGVDGVLLTTPYYNKPSQAGVIAHVRAIAEAVELPIMLYDIPGRAGISLAPETIIELS FT KIPQVIALKDAKADYQSTTTVLANTDLHVYSGDDGLTLPLMAAGAVGVVSVTAHVAAAK FT YRTLVNAMHAGDLATARTTHFELDAIQRGIMGHIQGAVAAKYGLHWQGVLPNTVVRLPL FT LAPSDAELDAIRADLREGGWDL" FT CDS 1201625..1203331 FT /transl_table=11 FT /locus_tag="AARI_10810" FT /product="putative RNA-metabolising metallo-beta-lactamase" FT /function="3.6 RNA modification" FT /note="identified by match to PF00753 (metallo-beta- FT lactamase superfamily) and PF07521 (RNA-metabolising FT metallo-beta-lactamase motif)" FT /db_xref="GOA:E1VUI8" FT /db_xref="InterPro:IPR001279" FT /db_xref="InterPro:IPR011108" FT /db_xref="UniProtKB/TrEMBL:E1VUI8" FT /protein_id="CBT75291.1" FT /translation="MTESSVGKADAARMQTPAKLKKGTMRIVPLGGLGEVGRNMTVFEL FT NGKLLIIDCGVLFPEEHQPGVDLILPDFSYIKDRLDDVVGVVLTHGHEDHIGAVPYLLR FT LREDIPLYGSKLTLAFVEAKLAEHRIKANSNIVVEGEVAQIGNFECEFVAVNHSIPDAL FT AVFLRTEAGTVLHTGDFKMDQLPLDGRITDLRHFARLGEEGVDLFLPDSTNAEVPGFTV FT AEREIGPVLEAKFSRARRRIIVASFSSHVHRVQQVLDAAAVHGRKVAFIGRSMVRNMGI FT AERLGYLEVPQGVLVDLKQIDSLPDHKVVLMSTGSQGEPMAALSRMANGEHKVQINPGD FT TVILASSLIPGNENSVFRVINGLMRLGAEVIHKGMAKVHVSGHASAGELLYCYNILRPK FT NVLPVHGETRHLIANGRLAAQSGVPEENVLLAEDGSVIDLKDGVAKLVGQVECGYVYVD FT GSKVGTITDDDLKDRVTLGEEGFISVITVINRQNGTIISGPDIHARGVAEEDSVFNEIK FT PKIAAAIVEAVSNNPNHSTHQLQQITRRVIGSWVSRKLRRRPMIVPVVLEA" FT CDS complement(1203412..1203642) FT /transl_table=11 FT /locus_tag="AARI_10820" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUI9" FT /protein_id="CBT75292.1" FT /translation="MRKRMLGLAAAPVILGCLALSTPATAGQHAPAQTGEWNSVILMDA FT ETGEVLNYENSPAVEDSTTAAHPYLQFVGWH" FT CDS 1203863..1204690 FT /transl_table=11 FT /locus_tag="AARI_10830" FT /product="osmoprotectant (glycine FT betaine/carnitine/choline/L-proline) ABC transporter, FT ATP-binding subunit" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT quaternary amine uptake transporter (QAT) family (TC 3.A.1. FT 12.z). ABCISSE: ABC transporter, ATP-binding protein (ABC), FT OTCN-family (osmoprotectants, taurine, cyanate and FT nitrate). Part of an uptake system of osmoprotrectants such FT as glycine betaine, carnitine, choline, proline betaine and FT L-proline" FT /db_xref="GOA:E1VUJ0" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VUJ0" FT /protein_id="CBT75293.1" FT /translation="MIEFENISKRYPDGTVAVDDFSLQIPAHQTTVFVGSSGCGKTTLL FT RMINRMVEPSQGTVRIDGEDIESKPAVQLRRSIGYVMQNSGLLPHFTVAENIATVPRLM FT GSTRQDSHKRALELMETVGLPASMAQRYPHQLSGGQQQRVGVARGLAADPNILLMDEPF FT GAVDPIVRAELQEELIRLQKELGKTIVFVTHDIDEAFLLGDQVVILAAGAQKLQVGSPS FT EIIEHPADDFVASFIGAQRGARALRVKHTEHGAVLVDGQGRTQGRLVDGRDSQ" FT CDS 1204699..1205373 FT /transl_table=11 FT /locus_tag="AARI_10840" FT /product="osmoprotectant (glycine FT betaine/carnitine/choline/L-proline) ABC transporter, inner FT membrane subunit" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT quaternary amine uptake transporter (QAT) family (TC 3.A.1. FT 12.z). ABCISSE: ABC transporter, permease (IM), OTCN- FT family (osmoprotectants, taurine, cyanate and nitrate). FT Part of an uptake system of osmoprotrectants such as FT glycine betaine, carnitine, choline, proline betaine and L- FT proline" FT /db_xref="GOA:E1VUJ1" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VUJ1" FT /protein_id="CBT75294.1" FT /translation="MENLGLIGSLSVEHLRQSAMAILIGFALSIPLGWVAWRYKLVRGP FT LVTLTGLLYTIPSLALLMILPVITGMSAISEANLVVALSIYAVAIMVRGVVDGLNSVDP FT ATRSAATAMGYGPARRFFAVDLPLAGPVILAGLRVTAVSTISLATVGILVGVTNLGYLF FT TNGLQRRIIAEVFAGILAVALIALVIDLLLLLAGRWLMPWNSSGSKTKRSVQQASGEQV FT DA" FT CDS 1205370..1206101 FT /transl_table=11 FT /locus_tag="AARI_10850" FT /product="osmoprotectant (glycine FT betaine/carnitine/choline/L-proline) ABC transporter, inner FT membrane subunit" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT quaternary amine uptake transporter (QAT) family (TC 3.A.1. FT 12.z). ABCISSE: ABC transporter, permease (IM), OTCN- FT family (osmoprotectants, taurine, cyanate and nitrate). FT Part of an uptake system of osmoprotrectants such as FT glycine betaine, carnitine, choline, proline betaine and L- FT proline" FT /db_xref="GOA:E1VUJ2" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VUJ2" FT /protein_id="CBT75295.1" FT /translation="MNLIAKALEWIFDAEQWNGDSGLQVLLGQHLLYTALAVLLASLVA FT IPAGWAIGHTGKGREIAVAAAGIARAVPSFGLLILLVLLFGVLHKPEAALVTFVVLAIP FT SLLAGAYTGFEAIDRKTIDAARAMGMTEWQILFKVEIPLGLGLLVGGIRSAVLQVVATV FT TIAAYVNLGGLGLPIISGLNLRRFDMVLGGALLVAALALLLDLVLALAQKAAEPRGLHS FT SKTKPQPEDSAYRKTLEREPS" FT CDS 1206098..1207000 FT /transl_table=11 FT /locus_tag="AARI_10860" FT /product="osmoprotectant (glycine FT betaine/carnitine/choline/L-proline) ABC transporter, FT substrate-binding protein" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT quaternary amine uptake transporter (QAT) family (TC 3.A.1. FT 12.z). ABCISSE: ABC transporter, binding protein (BP), FT OTCN-family (osmoprotectants, taurine, cyanate and FT nitrate). Part of an uptake system of osmoprotrectants such FT as glycine betaine, carnitine, choline, proline betaine and FT L-proline" FT /db_xref="GOA:E1VUJ3" FT /db_xref="InterPro:IPR007210" FT /db_xref="UniProtKB/TrEMBL:E1VUJ3" FT /protein_id="CBT75296.1" FT /translation="MILKKILPATALVLASGLVLAGCSSSDPLAGGSSSGDSGNETIVV FT GSQAYYSNEIVAEIYAQALEDAGMEVERKFNIGQRDAYMPQLEDGSIDVSPEYTGNLLQ FT FYKKDTEARSGDEVYSELEKALPDSLAVLEAAQASDQDSYTVTKKFAEENKVTSIEDLA FT DVGKKLTVGGPPELEQRPYGPKGLESTYGVKAGFSATGDTTVEDLVAGTVNVANVFTAD FT PRIKTEQLVVLEDPKSLFLASNVVPLVSAEQSEKLAAVLDPVSQKLSAQTLVELNVQST FT VGQQSAADIASAWLEAQDL" FT CDS 1207239..1208258 FT /transl_table=11 FT /locus_tag="AARI_10870" FT /product="iron-siderophore ABC transporter, FT substrate-binding protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, binding protein (BP), ISVH- FT family (iron siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VUJ4" FT /db_xref="InterPro:IPR002491" FT /db_xref="UniProtKB/TrEMBL:E1VUJ4" FT /protein_id="CBT75297.1" FT /translation="MKRINPWMLAVPAIILATATGCSTPAGTANENVPGSEAEKTVLDS FT CGREVVFDQEPQSVLAIGSEAPALLTAAGAGEKITHYAGRYQVPFDEETEKAVRNAQRV FT IEDSHDVSYEMILDSGVDVVIGTDIAAGIDLNALAQRLERAGVKMLTVSGYCAGFEDRS FT TSGVSGFDQIYKDVESYGELFGTEDHAAQSVKDMRARVDAAAKRVAQQEEQRGLPLYVP FT TAGTLGSYGHESLVAEQMEVLGMENVFNNVPKRYFEPSNEELVDSAADKVFAMYLPTGS FT SNLETDQQVIDELRQRTELKGLPAIEDEDGIVPLNYYYSSPGPLAVDGVELIADRLTR" FT CDS 1208366..1209163 FT /transl_table=11 FT /locus_tag="AARI_10880" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VUJ5" FT /protein_id="CBT75298.1" FT /translation="MKLSPASNTTVLVTSRHPETQYLAIADRLLRAEHVHAEQVGFILP FT PRKPQAHTRLHMAGDEFCANATLSLAAWHAATRPGPDRAELLIETSGARQSLHCRVEPS FT EAGYRCELSIPWPQSIEPYKVPGIERAGLVRYPGAVHLVAEGDGSDPLLRERAQQLAVE FT LGAREAVCVVGIMLYDRHRQELAPLVSVPALGSMIWEGSCGSGTAAVGAYLAAVTGTPI FT NASVKQPGGTTQAFADSSRAEATALRICTEVNIVAEGTAYIHV" FT CDS 1209156..1209992 FT /transl_table=11 FT /locus_tag="AARI_10890" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VUJ6" FT /protein_id="CBT75299.1" FT /translation="MSETPLITLNGSTWELAGALRGYLECFTAAVASYDGSTRHAAELE FT ELLASYSQLVTDPANEADYEQLAATGTGTELIAQLRSESARCVASIEKYRALRLLEGGG FT GAEGYFANIESCIAEEFGAVAPDASSMVLLVGSGSFPMTLLNLAARTGASARGIDIDPE FT ALELGRKVVAQLGESLDIELLGERIEQLDFLAEITHIVFSSTVSVKYELLHQLHALTRD FT DVVVAMRFGDGLKSLFNYPLQPVDPDLWHCSAVIRQPEQVFDIALYTKTRTRMESN" FT CDS 1209996..1211291 FT /transl_table=11 FT /locus_tag="AARI_10900" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR016935" FT /db_xref="UniProtKB/TrEMBL:E1VUJ7" FT /protein_id="CBT75300.1" FT /translation="MDELGNILIAGTGPVAVQSAVLLGTLPGELGIAGRGSQRANAFFD FT ALDATAGTAQSTVQNPAHGALAGTVRFAHRYRGYQQVAGRWDTLVLAVTADAYLAVLRE FT LAPEVLVSLRRVVLLSPTLGSAALVREFAGGQAADLEIISFSSYLGDTRPLEGTGGALV FT LSAGVKARIYAGSTHGHTPALQALCAIHAEAGTQVQLMDQPLEAEARNMSLYVHPALFF FT NEVALRAVFAPAPPIQYVYKLYPEGPVTPALIHALAQTWRELTAITTALGGKGVNLLAF FT MLQDGYPLHPQSISPAQAASFEQLPPIEQEYLLYVRYASLLIDPFSQPDDQGRYFDFSA FT IAFRPVFINELGQWDVPRMPKEDYYRTKIIAGLARKLAVPCPMIDSLLAAYETALEQAA FT HELAGQRRAPAFAVQDFAADLDMISAGIGSAV" FT CDS 1211288..1212550 FT /transl_table=11 FT /locus_tag="AARI_10910" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VUJ8" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VUJ8" FT /protein_id="CBT75301.1" FT /translation="MSQPEAETIQALPSERRIIVEIWPALLASALGLLPFTVLSTFLVP FT IADWAGAGYAETGTLRGLAGVGAVLAGIGLAPLIGRIAPGTVAAAALGLMGAAAIVGTF FT SGLAALAIFCLATGVSNALLYPALSTAAADRFGSTPAAGRAATLVMTAQTLASTLGAPL FT LILPAMFWGWQGNLIAIGIISIALIPAVLRYGRRGAVQADPAQIAPAKPPARVGYLAAF FT KLLSQVPGARALLLVSFGRAGAFMGHLAFLAPLYAHKFALDASWFAWVWSVSGGAFFLG FT HLLAGRMLNAEDSQRRTRTVMIICLATGLVALFGVYLAPVLPLAVASTAMLSASHAVVS FT AAVTSLLVARCTQVRGTALSLNAAGMSLGLFLGTAASGAAMAAAGYLAAAAVLGVLTGI FT ALLAALSLRAATTDEILEGQS" FT CDS 1212547..1213653 FT /transl_table=11 FT /locus_tag="AARI_10920" FT /product="iron-siderophore ABC transporter, inner membrane FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, permease (IM), ISVH-family (iron FT siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VUJ9" FT /db_xref="InterPro:IPR000522" FT /db_xref="UniProtKB/TrEMBL:E1VUJ9" FT /protein_id="CBT75302.1" FT /translation="MRQPGPVLEAAPAALVFSADDLEHRQRSRQTWWWIAGLLAAVLVS FT LPMAIGLGPVSIEPGAVVGILKSQWWDDPALASWSASDESIVLLLRVPRVLLGAAVGAG FT LALAGVALQALTRNILAEPYLLGVTSGASTLSAASILFGATAGIGSASLATSAFAGALI FT AGIGVYLLARVGNEMTSTRLVLAGVSVGYVLHALTSLLIFASDDPNAGRSVLFWTLGSL FT AQATGQSVLITWVVVLGTLALLVYWSRPLDALAIGDGTAQTLGISPAKLRAAVMIVTAL FT CVGALVASSGGIGFVGLVIPHVARLCVGSTHRKLLPVAALLGALFLVWADVLARTALAP FT QELPLGIVTALLGAPLLFVLVRRLNSAQ" FT CDS 1213684..1214469 FT /transl_table=11 FT /locus_tag="AARI_10930" FT /product="iron-siderophore ABC transporter, ATP-binding FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, ATP-binding protein (ABC), ISVH- FT family (iron siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VUK0" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VUK0" FT /protein_id="CBT75303.1" FT /translation="MITATDISVGYGGKLVIESVGLSAGPGEVVGLIGPNGSGKSSFLR FT TLYSALRPQTGQVSLDGQPVSALRGNELARRIAVVAQETPTDLPVSVAEMVLLGRTPHR FT TALASFTREDHQAVAAALSRVGARSLADRRYSTLSGGEKQRVLVARSLAQQADHLLLDE FT PTNHLDIRYQHELLRMLRSLGTTTVIVLHDLNLAARYCTKLVMLDGGGVVAAGSAEQVL FT DPDLLLQVYGIHAEAVQVNGTLQLVFSMVDEPLAQHTAG" FT CDS 1214557..1215960 FT /transl_table=11 FT /gene="lpdA" FT /locus_tag="AARI_10940" FT /product="dihydrolipoyl dehydrogenase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.8.1.7" FT /note="E3 component of pyruvate dehydrogenase and 2- FT oxoglutarate dehydrogenase complexes" FT /db_xref="GOA:E1VUK1" FT /db_xref="InterPro:IPR001327" FT /db_xref="InterPro:IPR004099" FT /db_xref="InterPro:IPR012999" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR016156" FT /db_xref="InterPro:IPR017817" FT /db_xref="InterPro:IPR023753" FT /db_xref="UniProtKB/TrEMBL:E1VUK1" FT /protein_id="CBT75304.1" FT /translation="MTSPAAFQVDKHYDLIILGTGSGNSIPGPEFDGKSIAIIEKGAFG FT GTCLNVGCIPTKMYVYAADVALETKESARLGLDAQVNSVHWQDIVRRVFEKRIDPIAQG FT GEEYRRGEQTPNIDVYDQHARFVAERTLRTGQGEQAATISADQIVIAAGSRPFIPQDII FT DSKVTFHTNEDIMRLERQPESMVIVGGGYIAMEFAHVFDALGTKVTILSRSELLRHLDA FT DLREPFNELAAARFDVRAGRTMASATEDEQGITLTLDDGSTVNAEVLLVATGRIPNGDQ FT LDLDKAGIEAENGSISVDEFGRSTSAQGIWALGDISSPYMLKHVANAEMRAVRHNLLHP FT EDLKQMPHEHVPAAVFTHPQIANVGLTEGEAREAGHDITVKVQKYGDVAYGWAMEDSTG FT IAKLIADRQSGKLLGAHYMGPQASTLIQQMITVMAFGLDVREVATNQYWIHPALPEVTE FT NALLGLDFS" FT CDS 1216015..1216500 FT /transl_table=11 FT /locus_tag="AARI_10950" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUK2" FT /protein_id="CBT75305.1" FT /translation="MNAKTAAPVSSIALRIFLIAGAAGALFGVLALLALFWEVVASGFA FT GGFQPGTVAAALQFIAIACGIGLAVGLLCASGMYVALEIRAVRNEGDSPARQAACAALG FT AGIGGLLPASILMLIGGSEGQWGLLSLIAVGFLAVCSAAGYLITAGLNCQHQRSMGF" FT CDS 1216860..1219841 FT /transl_table=11 FT /gene="ftsK" FT /locus_tag="AARI_10960" FT /product="DNA translocase FtsK" FT /function="1.7 Cell division" FT /note="DNA motor protein, which is both required to move FT DNA out of the region of the septum during cell division FT and for the septum formation. Tracks DNA in an ATP- FT dependent manner by generating positive supercoils in front FT of it and negative supercoils behind it" FT /db_xref="GOA:E1VUK3" FT /db_xref="InterPro:IPR002543" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR018541" FT /db_xref="UniProtKB/TrEMBL:E1VUK3" FT /protein_id="CBT75306.1" FT /translation="MAPRTQSQGAKKPTTRKPKASSSSSSKKTPENPEAELALPLRAIR FT SVWMGVARIFGGAFRRIGGTVKPDFEVRRDGTGLFLALISITVAIIEWWGLREAGWFGV FT GVHAVAGGTLGFMAVLLPIILFIGAFRLFRYPEEVTSNNRIGIGLLIMTLSGSSIASLA FT NGSPAVSDEFETLWNAGGMAGSILGTPLGLLISVPGAMAVFIFLVFMSILIVTATPFTQ FT IPSRLRAGYNRLLGQDPDAPRASSARSTMELDPTREDHDQSYLYPEEDAPAPAPKKKKP FT GFFERRAAAARQVTEVYDVDGTETSERPGDVAYDTAVIDPNEPSTDALPAINRNSGKIF FT DADEAATQAIARPDFTEESSSSQDDSATVAIPKPSGPPPGVKRPTKAETEMAEIMANIG FT LQSEPEATTSAMDQVSSRAAGLSASPQAPIPARSEQLQLSGDVTYTLPEEHFLPAGPPA FT KEASEANQVVVDALTNTLQQFKVDAQVTGFSRGPTVTRYEIELSPGTKVEKVTALSKNI FT SYAVASSDVRILSPIPGKSAIGIEIPNTDKEVVALGDVLRSSNARKSEHPMVMGVGKDV FT EGGFVVANLAKMPHLLVAGATGAGKSSFVNSMITSILMRSTPDEVRMVMVDPKRVELTA FT YEGVPHLITPIITNPKKAAEALGWVVREMDTRYDDLANFGFKHIDDFNKAVKAGKVHPP FT EGSKRVLKPYPYLLVIVDELADLMMVAPRDVEESIVRITQLARAAGIHLVLATQRPSVD FT VVTGLIKANVPSRMAFATSSVTDSRVVLDQPGAEKLLGQGDALFLPMGTSKPMRVQGAW FT VTESEIHRVVEHVKSQLAPEYRDDVIPAAEKKKQIDEDIGDDLDLLLQATELVVTSQFG FT STSMLQRKLRVGFAKAGRLMDLMESRGVVGPSEGSKARDVLIQPDELPMVLAAMRGDDP FT STTAPSATEAALVQEANVNHAEPVAEYAEDLVAKDLDDRPQAVDYFDGSDEPGEDAWDL FT TGRN" FT CDS 1219847..1220449 FT /transl_table=11 FT /gene="pgsA" FT /locus_tag="AARI_10970" FT /product="putative CDP-diacylglycerol--glycerol-3-phosphate FT 3-phosphatidyltransferase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.7.8.5" FT /note="involved in phospholipid biosynthesis" FT /db_xref="GOA:E1VUK4" FT /db_xref="InterPro:IPR000462" FT /db_xref="InterPro:IPR004570" FT /db_xref="UniProtKB/TrEMBL:E1VUK4" FT /protein_id="CBT75307.1" FT /translation="MSEQAGSSAQQPVPTLNIANVLTTIRIIMVPFFVWALLFDDHEQR FT LWRWVALGLFVVAMYTDKLDGDLARSRGLVTNFGKIADPIADKLLTGSALVCFSILDEL FT HWWVTIVILVREWGITLLRVVVIRYGVIAANMGGKIKTVLQAIVIGLYLLPYTYDIDWL FT GTVAWYLMLLTLAVTVVTGLEYLVKAGQLVATAKKQK" FT CDS 1220460..1220942 FT /transl_table=11 FT /locus_tag="AARI_10980" FT /product="CinA-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF02464: competence-damaged FT protein. CinA is the first gene in the competence- FT inducible (cin) operon, and is thought to be specifically FT required at some stage in the process of transformation" FT /db_xref="InterPro:IPR008136" FT /db_xref="UniProtKB/TrEMBL:E1VUK5" FT /protein_id="CBT75308.1" FT /translation="MKPKAPEVIAKAIDSAVQLATAESLTAGMIAARLAEVPGASAVLR FT GGVVSYSSEVKASLLGVDAQLLEAHGSVDPEVARQMAVGAQRACGAEAAVSATGVAGPE FT PHDGKAVGTVYIGWAMGTESGSEVHHFVGDRAQIREQSTQAALHQFIAILDKASSQ" FT CDS 1221232..1221552 FT /transl_table=11 FT /locus_tag="AARI_10990" FT /product="helix-turn-helix domain-containing protein" FT /function="3.5.2 Transcription regulation" FT /note="match to PF01381: helix-turn-helix. This is large FT family of DNA binding helix-turn helix proteins that FT include a bacterial plasmid copy control protein, bacterial FT methylases, various bacteriophage transcription control FT proteins and a vegetative specific protein from FT Dictyostelium discoideum (Slime mould)" FT /db_xref="GOA:E1VUK6" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VUK6" FT /protein_id="CBT75309.1" FT /translation="MVVLRHEIGDVLRDVRQRQGRTLREVSHSARVSLGYLSEVERGQK FT EASSELLSSICVALEIPLSVMLREVSERVALAEGIAIPDTVPTDMANEFAAKGSNKPLA FT SV" FT CDS 1221663..1221887 FT /transl_table=11 FT /locus_tag="AARI_11000" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021408" FT /db_xref="UniProtKB/TrEMBL:E1VUK7" FT /protein_id="CBT75310.1" FT /translation="MKNSDFWRNMENEFGSRYSHVLADSMSLTELDSLTAAEALNKGVK FT PKMIWEAICRAQDVPAERWLGVDIEPKDS" FT CDS 1222129..1223181 FT /transl_table=11 FT /gene="recA" FT /locus_tag="AARI_11010" FT /product="RecA bacterial DNA recombination protein" FT /function="3.3 DNA recombination, and repair" FT /note="RecA is a DNA-dependent ATPase and functions in DNA FT repair systems. RecA protein catalyses an ATP-dependent DNA FT strand-exchange reaction that is the central step in the FT repair of dsDNA breaks by homologous recombination" FT /db_xref="GOA:E1VUK8" 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/TrEMBL:E1VUK8" FT /protein_id="CBT75311.1" FT /translation="MAAKNDREKALEAVLGQIDKAYGKGSVMRLGDETRAPIEVIPTGS FT VALDVALGIGGLPRGRVVEIYGPESSGKTTVALHAVASAQKAGGVAAFIDAEHALDPEY FT AKKLGVDTDALLVSQPDTGEQALEIMDMLVGSGALDIIVIDSVAALVPRAEIEGEMGDS FT HVGLQARLMSQALRKITGRLSASKTTAIFINQLREKIGVFFGSPETTTGGKALKFYASV FT RIDIRRIETLKEGTNAVGNRTRCKIVKNKMAPPFKQAEFDILYGHGISREGSLIDMGVE FT HNLVKKSGAWFTYDGDQLGQGKENARRFLRDNPDLANELERQILQKLGVTPMEEVEEDE FT TELRVVEGDK" FT CDS 1223181..1224068 FT /transl_table=11 FT /gene="recX" FT /locus_tag="AARI_11020" FT /product="putative regulatory protein RecX" FT /function="3.3 DNA recombination, and repair" FT /note="RecX is a putative bacterial regulatory protein. The FT gene encoding RecX is found downstream of recA, and is FT thought to interact with the RecA protein" FT /db_xref="GOA:E1VUK9" FT /db_xref="InterPro:IPR003783" FT /db_xref="UniProtKB/TrEMBL:E1VUK9" FT /protein_id="CBT75312.1" FT /translation="MASGFQRRSVRPGKKSGADATSVSKEFQGDLDDMPDWAKPSPEEL FT EKQAAEEAARQERAAARAAAPSMPAGSTSRTIASLANESKAPGSIEELRAAMEQIVAAP FT AVAQPSKKERREARQARQVAREAGEPEQLSDDQWREKARSILLRQLTASDKTAKQLKDK FT LLEKECPEDIADEVIDRYVEINLVDDQRFAKSWVVARARSRGLARGAIKHELRSKGIDD FT ESAAEALEQIDDESEEQRARELVRAKLRPESMGADRDRALRRLVGMLGRKGYHGGMAFK FT VAREEWEERFGNRY" FT CDS 1224546..1226075 FT /transl_table=11 FT /gene="miaB" FT /locus_tag="AARI_11030" FT /product="tRNA-i(6)A37 thiotransferase enzyme MiaB" FT /function="3.6 RNA modification" FT /note="the MiaB enzyme is responsible for the modification FT of the isopentenylated adenine-37 base of most bacterial FT and eukaryotic tRNAs that read codons beginning with FT uracil. Adenine-37 is next to the anticodon on the 3 side FT in these tRNAs, and lack of modification at this site leads FT to an increased spontaneous mutation frequency" FT /db_xref="GOA:E1VUL0" 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/TrEMBL:E1VUL0" FT /protein_id="CBT75313.1" FT /translation="MTELEPLSRIGSEDHPRTYEVRTFGCQMNVHDSERLSGLLENAGL FT SRKPEEQAEEVADVVVFNTCAVRENADNKLYGHLGLLKNLKAERPGMQIAVGGCLAQKD FT RDTIVKKAPWVDVVFGTHNIGSLPALLDRATHNKKAQLEILESLDVFPSTLPTRRESVY FT AGWVSISVGCNNTCTFCIVPSLRGKERDRRPGEILAEIQALVDDGAIEVTLLGQNVNSY FT GVEFGDRLAFGKLLRACGEIEGLERVRFTSPHPAAFTDDVIEAMAETPNVMPQLHMPLQ FT SGSDKVLKDMRRSYRSKKFLGILDKVRERIPHAAITTDIIVGFPGETEEDFQATLDVVQ FT ASRFSSAFTFQYSKRPGTPAAELEEQLPKAVVQERYERLTQLQDRIAKEENAKQLGRTV FT EVMVTEQSGRKSAETHRLTGRAQDQRLVHFSVPDGAETPRPGDLATLPITEVAAFHLIS FT DPSASQYSLRRSRAGDAWDRAQAESCGVPSPGAASSTGATNLGMPTLKVRS" FT CDS 1226080..1226982 FT /transl_table=11 FT /gene="miaA" FT /locus_tag="AARI_11040" FT /product="tRNA isopentenyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.5.1.75" FT /note="catalyzes the first step in the biosynthesis of 2- FT methylthio-N6-(delta(2)-isopentenyl)-adenosine (MS[2]I[6]A) FT adjacent to the anticodon of several tRNA species" FT /db_xref="GOA:E1VUL1" FT /db_xref="InterPro:IPR002627" FT /db_xref="InterPro:IPR018022" FT /db_xref="UniProtKB/TrEMBL:E1VUL1" FT /protein_id="CBT75314.1" FT /translation="MTNSNLPVIAVVGPTGTGKSDLAISLAQELGGEIVNSDALQFYRG FT MDIGTAKLPINERGGIAHHLLDTMSIREEASVAAFQAQAREQFAQIRARGKVPVMVGGS FT GLYVRAALDVIDFPPTDPDARRRLEAEVEAEGDGSLRRRLAEVDPVSAGRNLDLRRAIR FT ALEVYEISGRAFSSFMPQREYFAPAIQIGLNYERQALHAALENRVHKMDSMGLAEEVAG FT LLEQGLREGKTASRAIGYQQYIDYLDSQITRAEAIEQTVIATRKFARRQITWFNADARV FT SWLDPTEPDLLEKALKIIG" FT CDS 1227015..1227950 FT /transl_table=11 FT /gene="dapF" FT /locus_tag="AARI_11050" FT /product="diaminopimelate epimerase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="5.1.1.7" FT /note="catalyzes the isomerization of L,L- to D,L-meso- FT diaminopimelate in the biosynthetic pathway leading from FT aspartate to lysine" FT /db_xref="GOA:E1VUL2" FT /db_xref="InterPro:IPR001653" FT /db_xref="InterPro:IPR018510" FT /db_xref="UniProtKB/TrEMBL:E1VUL2" FT /protein_id="CBT75315.1" FT /translation="MYRTELGQLAGQRFAKGHATGNDFVLVADPEAKLELSPEQVAAVC FT HRRFGIGADGLIRAVPTSLVPGYEEQFLDNPKAYWFMDYRNNDGSIAEMCGNGVRAFAH FT YLIAEGLISLQVGQSFQIGSRAGVKEITRLADGYAVNLGPWGLIFEQEATERSIDSMVK FT PRGWEQALPALSITMGNPHTVVALPDAQMLEELDLFQAPEVSPVPVNGTNVEFVVPSEP FT LIEEDGVAQVQMRVYERGVGETLSCGTGACAAAAAVRYWARSTALINQWAVTVPGGVVG FT VEFRSNEAGGEDTILSGPADLVARGVIGTE" FT CDS 1228107..1228406 FT /transl_table=11 FT /locus_tag="AARI_11060" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUL3" FT /protein_id="CBT75316.1" FT /translation="MNPTGKFVPVGESSTDVRSRISLGKAGVRRDDRYAIAVNEEGEIL FT LTPLVSIPKRELLVWENSVIRDSLGRALQDSATGRVKRRGSFSKFAEESSDDIS" FT CDS 1228417..1228716 FT /transl_table=11 FT /locus_tag="AARI_11070" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VUL4" FT /protein_id="CBT75317.1" FT /translation="MPSFELLFTEEASSQLDELESRADMAVKLKKVYKALGFLENDPKY FT PGLNSHKYSSLSGISGEDVWDSYVENRTPAAWRIFWHYGPKSGEITVLMITPHP" FT repeat_region complement(1229163..1229177) FT /rpt_type=DIRECT FT mobile_element complement(1229178..1230770) FT /mobile_element_type="insertion sequence:ISAar28" FT /rpt_family="IS481" FT repeat_region complement(1229178..1229227) FT /rpt_type=INVERTED FT CDS complement(1229257..1230612) FT /transl_table=11 FT /locus_tag="AARI_34790" FT /product="transposase of ISAar28, IS481 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VUL5" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VUL5" FT /protein_id="CBT75318.1" FT /translation="MKNDPVNSTIRLAIARWPQDAPRGAVTAFCTEHEISRKTFYQIRK FT RAQTEGQAAALEPRSRRPKKAPTATNDAVKDQAVAMRKALQASGWDHGPISVHDHMKKL FT GMPTVSISALARIFSERGLVTPAPQKRPRSSYRSFRYPMPNSCWQLDATEYVLEGGRKC FT VIFQLIDDHSRLAVASLAAKTENGQDAVKVFRKGIESCGVPQRLLTDNGDALNPIRRGV FT LSELVAYANGLGIATITGKPHKPTTQGKNERLHSTLFKWLKKQPFATDLAQLQAQLDVF FT DHAYNTQRGHQSLEDRMTPQEAWDATPAAEPLELGQWKELSTKPGPSQAQVALGVQAGS FT ERVARQLAAARTPPEPAKLSATLRSELMGESGSHVLRANKNRCLRVAGVEIYLGKLLRS FT TVVNVVWDPTDLMVLSMEGELVAKFDYPFPQGVKYLSLKHATEKFQNMPDPV" FT repeat_region complement(1230721..1230770) FT /rpt_type=INVERTED FT repeat_region complement(1230771..1230785) FT /rpt_type=DIRECT FT CDS 1230848..1231909 FT /transl_table=11 FT /locus_tag="AARI_11080" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="GOA:E1VUL6" FT /db_xref="InterPro:IPR011990" FT /db_xref="UniProtKB/TrEMBL:E1VUL6" FT /protein_id="CBT75319.1" FT /translation="MSATLADTILALISLPTLRKHGYLVPAIETVESEIENCWIDLATT FT SFNKFRENDVPEADVRPQKVLIIPKALRPKELQSDEIVRIARNDEFLSYIFHPDFFVRV FT HQWFSKILLEGPEAALARIVPNASLFSSLEKKSQQDEYGRWLWDRLTVTQLDQWALTSL FT THEWNWIKNADDHGIDRRFLRARETELERVTDTYFEKLLSVKTVQRSSNFSTASFTHAA FT VEKLRAGNPNEAAEIFAGLTEILPSSGEAWNNLGFCRMAFDLDSALKAFARSAQFSRSF FT APIWIANHILALHLGGRTEEALLLSKLPVPPEHVDAVWAWEITSLPHRPTLIQMDNSNE FT YLEQVIAFVSRSS" FT CDS complement(1231963..1232568) FT /transl_table=11 FT /locus_tag="AARI_11090" FT /product="putative methyltransferase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF05175. This domain is FT found in ribosomal RNA small subunit methyltransferase C as FT well as other methyltransferases" FT /db_xref="GOA:E1VUL7" FT /db_xref="InterPro:IPR007848" FT /db_xref="UniProtKB/TrEMBL:E1VUL7" FT /protein_id="CBT75320.1" FT /translation="MTSDHYFTASPASADERRTIEVELNGSLRKVQTASGIFSPAGLDK FT GTAVLLQYVPTPRGRILDIGCGWGPITLTAAEQSPDSEVYGVDVNERSIDLARLNATAF FT GLSNVVVGSPDSIDPSLQFDTIWSNPPIRIGKDALHELLMLWLPRLAPGGEAWMVVQKN FT LGSDSLQKWLVAQLPSAWKVTREATSKAFRVLKVSRPA" FT CDS 1232894..1234555 FT /transl_table=11 FT /locus_tag="AARI_11100" FT /product="putative GTPase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF01926" FT /db_xref="GOA:E1VUL8" FT /db_xref="InterPro:IPR006073" FT /db_xref="InterPro:IPR016496" FT /db_xref="UniProtKB/TrEMBL:E1VUL8" FT /protein_id="CBT75321.1" FT /translation="MFDEPSETERATSQSGAHRHYSGKRSTSKETMTNSESHEHDSASM FT DDAQIQAAIDRILEADDAQSPQIQHFGEEESSIFTGQATALNRFSSGLSHFDGDQEDLD FT DRRALRRVAGLSTELEDVTEVEYRQLRLERVVLAGIWSEGTVTDAENSLRELAALAETA FT GSEVLDGLVQRRSKPDPSTFLGSGKAEELRAIVASSGADTVVVDAELAPSQRRALEDIV FT KVKVIDRTSLILDIFAQHAQSREGKAQVELAQLEYLLPRLRGWGESMSRQAGGRVGAAG FT GGIGSRGPGETKIEMDRRRIRDRMAKLRREIKAMKPAREAKRANRKRNAVPAVAIAGYT FT NAGKSSLLNRLTNAGVLVENALFATLDPTVRQSATEDGLTYTLADTVGFVSNLPTQLVE FT AFRSTLEEIADSDLILHVVDGSHPDPEGQIQAVRTVLGEVDALNIPEIIVVNKADVADP FT FVIERIRNRESNTAVVSAHTGEGIEELLEKISSSIPRPGIQLEVLIPYNRGDLIAKLHQ FT SESEILESEHLENGTRLIVKVRDSFAAELETFNLHG" FT CDS 1234548..1236542 FT /transl_table=11 FT /locus_tag="AARI_11110" FT /product="putative ATP-dependent helicase" FT /function="3 Information pathways" FT /EC_number="3.6.1.-" FT /note="possible DNA or RNA helicase" FT /db_xref="GOA:E1VUL9" FT /db_xref="InterPro:IPR006555" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR014001" FT /db_xref="InterPro:IPR014013" FT /db_xref="UniProtKB/TrEMBL:E1VUL9" FT /protein_id="CBT75322.1" FT /translation="MDKQEQALGLLEAAVTSMGGAMRTGQQEMVKHVVSALEDEKHLLV FT QAGTGTGKSMGYLIPALAHAQTSAKPVIVSTATLALQSQIVGRDVPRLLESLKGKLSRP FT MDVALLKGRSNYLCQYKLGGGYPDDEGTLFSMDEPAVPAGTTYSPLASEVMKLREWAEE FT TETGDRDELVPGVSDKAWKQVSVSAMECLGSQKCPMADECFSEMARARAAESDVVITNH FT ALLAVSAFEGLSVLPDFEVAIIDEAHELQDRVTSSVSGALSSRMVLTAAGGAKRHCGVN FT VDEMVKAANRLEKALTGVPTGLLEQGLREDMGIALNDIVEQARLALALSKPEANAPADG FT GRQTARSQLQAVMDDAIRMLECEERREVLYTTRPREFVEGRGYVEADETQPATLNVAPL FT SVAGKLREGLFDGRTVILTSATLAIGSQFDSVAGSLGLMGAGAPSWTGVDVGSPFDYPK FT QGILYVAKHLPKPGRQLAAETLDEIEDLIKSSGGGALALFTSKRSAEEAASILRERLDV FT EILCQGEASMKSLVEQFSSERDTCLFGTMTLWQGVDVPGDSCRLVIIDKIPFPRPDDPI FT SKARSEDVAKHGGNGFMQVAATHAAIRLAQGAGRLIRSVGDKGVVAILDSRMATARYGS FT FLKATLPPMWPTVDKKVISGVLKRLNPGE" FT CDS 1236681..1237736 FT /transl_table=11 FT /locus_tag="AARI_11120" FT /product="putative glycosyl hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VUM0" FT /db_xref="InterPro:IPR005198" FT /db_xref="InterPro:IPR008928" FT /db_xref="InterPro:IPR012341" FT /db_xref="UniProtKB/TrEMBL:E1VUM0" FT /protein_id="CBT75323.1" FT /translation="MDSMQVLAHQTAIDTHARFGHRLMGLPGTWIGRSYSTAQRLLDGS FT MLSDLNGLSHPFSEWNYWWQAHYLDAIIDDGYAYLNEGNDKLAGEALALANALLRGIHL FT RNFGVLPNYFFHDMAWLALASERLVRFTHEASGKKNKHAQLAVRVLGKQLHQGKDDVLD FT GGLYWSRKRDFKNTPANAPAALFFARTGQKDISRELLQWLEAKLFSSEHGLYLDGLRIN FT ERGHRLEPAVYSYNQGTVLGALLELGEPADLAHAQVLIKATAQSLASESGVLAFNHGGD FT GNLFAGILCRYLALAATDERLEASSRDTAKTLVMATSHHLKDQEPRRLSAAVQRWMIFC FT AAAGLESSTGR" FT CDS complement(1237793..1238512) FT /transl_table=11 FT /gene="lexA" FT /locus_tag="AARI_11130" FT /product="LexA repressor" FT /function="3.5.2 Transcription regulation" FT /EC_number="3.4.21.88" FT /note="LexA represses around 20 genes of the cellular SOS FT response to DNA damage in Escherichia coli. In the presence FT of single-stranded DNA, the recA protein interacts with FT lexA causing an autocatalytic cleavage which disrupts the FT DNA- binding part of lexA, leading to derepression of the FT SOS regulon and eventually DNA repair" FT /db_xref="GOA:E1VUM1" FT /db_xref="InterPro:IPR006197" FT /db_xref="InterPro:IPR006199" FT /db_xref="InterPro:IPR006200" FT /db_xref="InterPro:IPR011056" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR015927" FT /db_xref="InterPro:IPR019759" FT /db_xref="UniProtKB/TrEMBL:E1VUM1" FT /protein_id="CBT75324.1" FT /translation="MSASQRTPRSNARSLTIRQKKILETIQRSIGKNGYPPSMREIGDA FT VGLKSLSSVTHQLSQLEKLGYIRRDPRRPRAMEILLPLQLAEDSEAAEASKPAEPVINE FT DAKIIELSTSADTTMVPLVGRIAAGGPILAEQSVEDVFSLPRQLVGHGELFMLKVSGDS FT MVDAAICDGDWVVVRRQQTADNGDIVAALLDEEATVKTFRQRDGHTWLLPQNSRYEPIL FT GDAATIMGRVVSVMRSL" FT CDS 1238771..1239124 FT /transl_table=11 FT /locus_tag="AARI_11140" FT /product="LysM domain-containing protein" FT /function="1.1 Cell wall" FT /note="match to protein domain PF01476. This domain is FT about 40 residues long and is found in a variety of enzymes FT involved in bacterial cell wall degradation. It may have a FT general peptidoglycan binding function" FT /db_xref="GOA:E1VUM2" FT /db_xref="InterPro:IPR002482" FT /db_xref="InterPro:IPR018392" FT /db_xref="UniProtKB/TrEMBL:E1VUM2" FT /protein_id="CBT75325.1" FT /translation="MATVALDSNQTQTPLKIRINRRGWAVLVGLPIFALTVAAAFFIAM FT FSSDAHAAANTPAGIETVDVTVIPGDTLWSLAREYATGYDVTSAVDHIAELNALNSSEI FT QIGETLSIPVLAG" FT CDS 1239206..1240312 FT /transl_table=11 FT /gene="hisC" FT /locus_tag="AARI_11150" FT /product="histidinol-phosphate transaminase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.6.1.9" FT /note="catalyzes the the transfer of an amino group from 3- FT (imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to FT form histidinol phosphate and 2-oxoglutarate. Involved in FT histidine biosynthesis" FT /db_xref="GOA:E1VUM3" FT /db_xref="InterPro:IPR001917" 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:E1VUM3" FT /protein_id="CBT75326.1" FT /translation="MNDRSELLSQLPLRENLRGLSPYGAPQIDVPIQLNVNENTHPLPP FT TVVDAISQEVAKAAATLNRYPDREFTELRELLADYLGHSLTKENIWAANGSNEILQQIL FT QAFGGPGRSLMSFAPTYSMYPLLASGTDTSYIAGTRAADFTLSAESAAAQVREHKPNIV FT FLCSPNNPTGTALGLDVITEVYEALSEHDGVLIVDEAYAEFSLASTKSALTLLDGRQRL FT IVSRTMSKAFGLAGARVGYLAAAPEVTDAIRLVRLPYHLSAVTQATAIAALKNIELLLA FT QVEDIKSQRDRIVTRLKELGLKPSVSDSNFVFFGGVEDPHAIWEGLLEAGIIIRDNGIP FT GTLRVTAGTESETTAFLERLAELLGSQK" FT CDS 1240335..1240955 FT /transl_table=11 FT /gene="hisB" FT /locus_tag="AARI_11160" FT /product="imidazoleglycerol-phosphate dehydratase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.1.19" FT /note="catalyzes the following reaction: D-erythro-1- FT (imidazol-4-yl)glycerol 3-phosphate <=> 3-(imidazol-4-yl)- FT 2-oxopropyl phosphate + H(2)O. Involved in histidine FT biosynthesis" FT /db_xref="GOA:E1VUM4" FT /db_xref="InterPro:IPR000807" FT /db_xref="InterPro:IPR020565" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/TrEMBL:E1VUM4" FT /protein_id="CBT75327.1" FT /translation="MSAELIGARRARMERVTSESSVFVELDLDGTGVSEISTSVPFYDH FT MLTALSKHSLIDLTVRATGDTHIDVHHTVEDTAITIGEVLRVALGNKAGIRRFGTSYAP FT LDEALSRSVVDVSGRPYLVHSGEPAGQEYHLIGGHFTGSMTRHVFEAITFHAQICAHIE FT VLSGRDPHHIVEAQFKSFARALREAVERDERMGDKIPSTKGAL" FT CDS 1240956..1241591 FT /transl_table=11 FT /gene="hisH" FT /locus_tag="AARI_11170" FT /product="imidazole glycerol phosphate synthase, glutamine FT amidotransferase subunit" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.4.2.-" FT /note="imidazole glycerol phosphate synthase converts N1- FT (5-phosphoribulosyl)-formimino-5-aminoimidazole-4- FT carboxamide ribonucleotide (PRFAR) to imidazole glycerol FT phosphate (ImGP) and 5-(5-aminoimidazole-4-carboxamide) FT ribonucleotide (AICAR). Involved in histidine biosynthesis" FT /db_xref="GOA:E1VUM5" FT /db_xref="InterPro:IPR010139" FT /db_xref="InterPro:IPR017926" FT /db_xref="UniProtKB/TrEMBL:E1VUM5" FT /protein_id="CBT75328.1" FT /translation="MEKKTVVVLDYGSGNVRSAVRALEAAGAEVELTADPKKIVAADGL FT VVPGVGAYASVMEQLTETGALRWIGRRIAGGLPVLGICVGHQVFFEEGVEHGAKTEGIG FT EWPGKVERLQSEVIPHMGWNTVRPPEGSKLFAGIEDERFYFVHSYAVLHWAFDVTQPAM FT TPPQVTWSTHGTPFVAAVENGPLSAVQFHPEKSGDAGAQLLRNWLGTL" FT CDS 1241594..1241743 FT /transl_table=11 FT /locus_tag="AARI_11180" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUM6" FT /protein_id="CBT75329.1" FT /translation="MWTLILGVVGAFLAGGAISLKSQKAHISWIIALWVLAGLSLIAAW FT TLTY" FT CDS 1241771..1242508 FT /transl_table=11 FT /gene="hisA" FT /locus_tag="AARI_11190" FT /product="1-(5-phosphoribosyl)-5-((5-phosphoribosylamino) FT methylideneamino)imidazole-4-carboxamide isomerase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="5.3.1.16" FT /note="catalyses the following reaction: 1-(5- FT phosphoribosyl)-5-((5- FT phosphoribosylamino)methylideneamino)imidazole-4- FT carboxamide <=> 5-((5-phospho-1-deoxyribulos-1- FT ylamino)methylideneamino)- 1-(5-phosphoribosyl)imidazole-4- FT carboxamide. Involved in histidine biosynthesis" FT /db_xref="GOA:E1VUM7" FT /db_xref="InterPro:IPR006062" FT /db_xref="InterPro:IPR010188" FT /db_xref="InterPro:IPR011060" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR023016" FT /db_xref="UniProtKB/TrEMBL:E1VUM7" FT /protein_id="CBT75330.1" FT /translation="MSEQPILELLPAVDIAGGQAVRLVQGEAGSETGYGDPLEAALSWQ FT NAGAEWLHLVDLDAAFDRGSNVDIVQRIAKELNIKVELSGGIRDDASLDRALEFGATRV FT NLGTAALENPEWTKQAIARHGDKIAVGMDVRGTTLSGHGWTKDGGDLWDVLARLEDAGC FT ARYVVTDVTKDGTLRGPNVELLREIATKTSKPIVASGGISSLEDLRVLRELVPEGIEGA FT IMGKALYSGQFTLQEALDVAGRR" FT CDS 1242732..1243613 FT /transl_table=11 FT /locus_tag="AARI_11200" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VUM8" FT /protein_id="CBT75331.1" FT /translation="MSTEQPPSAPKRHLPGHIVAALAQAGSQTDSAGQDWEGRDLSGEG FT NPLHNFDKDDGKADANVLAALTALREGSAGESEVHKSLANARVFVAVVAQLGEEAMTEH FT GFASDKEADMALVKIKAPDGRMALPIFTTVERLQAWHKEARPVAVYAPRAALSAVSEEC FT QLLVLDPGSDFTFVLRRPGLWTLAKQVDWIPSYQSQQVASLVQNAIEDFNQLRTVKVAP FT GKGVGSRSKDGQVVLGGGPGPELNLQLIFAPGTSQDDARETTRALHGRLSQNTEFAEAV FT DSLELSLHSAPN" FT CDS 1243655..1244992 FT /transl_table=11 FT /locus_tag="AARI_11210" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VUM9" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="UniProtKB/TrEMBL:E1VUM9" FT /protein_id="CBT75332.1" FT /translation="MKSYWQILRQPQISLLLLIGMIARLPHSALSMLLLLHLVNNLDQS FT WVSAGLVTAVMTLGIAIGAPWRGARVDIWGLRRAMIPSVIVETLVWCTVPHVPLVWVYP FT LAFIGGLFALPVFSVVRTALGIMTTGEQRRTAFALDATATELVFIVGPASAGIVATQIS FT SVIGLSVIGVTSTVAGLALMILNPPTRSDDPKALATRANVHEERLGAEASFIAAAPMGV FT HEVEGELIAAGMKSARARIKQRGRAFKNRFNWVSASVLAVFIASAGAGMLLTGTEVAIV FT AELDASQESHQLGLVFLFWCGASLIGGLIYGSMKRVISPLVLLLSMAILTIPMYFAWDT FT WSLALFSALPGFLCAPTLSAASEWLTDLVAEKRRGEAMGWYGSAMTAGTALGSPITGIF FT VDTFGAAPAFIGIGAMASFVVVVALIAQQIRRRVRRARRQRLEPIA" FT CDS complement(1244989..1245540) FT /transl_table=11 FT /locus_tag="AARI_11220" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VUN0" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VUN0" FT /protein_id="CBT75333.1" FT /translation="MQLLEQPVIDAGAYRLRPFQHSDIPTVRQASADSYITQITTVPVQ FT GTEAEYADFIERQHRRVAEGSGYSFAIAEATTDRAVGQIGFWLRNANHGRASIGYWTAP FT EYRRRSVAKHTLEALARWGLEHPGIERVELYVEPWNEGSWRTAEACGFQCEGLMRSWEQ FT VGATRRDMYMYSRLKDTASA" FT CDS complement(1245638..1246003) FT /transl_table=11 FT /locus_tag="AARI_11230" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VUN1" FT /protein_id="CBT75334.1" FT /translation="MTNEDTNSHQHAVDQQVRDIAEVAAVEIITTAAVHLMSAAAVKCG FT LAEGEDANELKDLDEARKLITALAGLVTAGAPEIGSQHAAPLRDGLRSLQLAFREASII FT PDAPGKGPGEKFTGPVN" FT CDS 1246334..1246984 FT /transl_table=11 FT /gene="infC" FT /locus_tag="AARI_11240" FT /product="translation initiation factor IF-3" FT /function="3.7.3 Translation initiation" FT /note="IF-3 binds to the 30S ribosomal subunit and shifts FT the equilibrum between 70S ribosomes and their 50S and 30S FT subunits in favor of the free subunits, thus enhancing the FT availability of 30S subunits on which protein synthesis FT initiation begins" FT /db_xref="GOA:E1VUN2" FT /db_xref="InterPro:IPR001288" FT /db_xref="InterPro:IPR019814" FT /db_xref="InterPro:IPR019815" FT /db_xref="UniProtKB/TrEMBL:E1VUN2" FT /protein_id="CBT75335.1" FT /translation="MPEVRLVGPNGEQVGIVRIEDALRLALESDLDLVEVAPSAKPPVC FT KLMDFGKYKYEAAVKAREARKNQTNTVLKEVRFRLKIDTHDYETKVGHALRFLGAGDKV FT KAMIQFRGREQQRPEMGIRLLEKFAADVAEVGIIESSPRIDGRNMVMVVGPLKNKAEAR FT REQQQKSGGRNSAKRKIRTDAPAETEGQNVAASMDDEARAKLEQARQAAEGDA" FT CDS 1247151..1247345 FT /transl_table=11 FT /gene="rpmI" FT /locus_tag="AARI_11250" FT /product="50S ribosomal protein L35" FT /function="3.7.1 Ribosomal proteins" FT /note="L35 is a basic protein of 60 to 70 amino-acid FT residues from the large (50S) subunit" FT /db_xref="GOA:E1VUN3" FT /db_xref="InterPro:IPR001706" FT /db_xref="InterPro:IPR018265" FT /db_xref="InterPro:IPR021137" FT /db_xref="UniProtKB/TrEMBL:E1VUN3" FT /protein_id="CBT75336.1" FT /translation="MPKFKTHSGAKKRFKLTGSGKLARQQANRRHYLEHKSSRVTRRLA FT SDQIVAKADVKTIKRMLGL" FT CDS 1247450..1248097 FT /transl_table=11 FT /gene="rplT" FT /locus_tag="AARI_11260" FT /product="50S ribosomal protein L20" FT /function="3.7.1 Ribosomal proteins" FT /note="binds directly to 23S ribosomal RNA and is necessary FT for the in vitro assembly process of the 50S ribosomal FT subunit. It is not involved in the protein synthesizing FT functions of that subunit" FT /db_xref="GOA:E1VUN4" FT /db_xref="InterPro:IPR005813" FT /db_xref="UniProtKB/TrEMBL:E1VUN4" FT /protein_id="CBT75337.1" FT /translation="MARVKRAVNAHKKRRVVLERAKGYRGQRSRLYRKAKEQLLHSFVY FT SFNDRRKRKGDFRRLWIQRINAASRANGMTYNRLIQGLKAAQIEVDRRMLAELAVSDSN FT AFATLVKVAKDALPADVNAPKAAAEVAAPKAAKAPKAAAKSVEGEGVVKAVEGEAAPEG FT FVIKGNAGSNKYHVPGSTWYDQTEAEFWFNSIDAAKAAGFEPAGGESRQQMK" FT CDS 1248209..1249087 FT /transl_table=11 FT /locus_tag="AARI_11270" FT /product="putative RNA methyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.-" FT /note="identified by match to protein family PF00588: SpoU FT rRNA Methylase family. Possible role in rRNA modification" FT /db_xref="GOA:E1VUN5" FT /db_xref="InterPro:IPR001537" FT /db_xref="InterPro:IPR013123" FT /db_xref="UniProtKB/TrEMBL:E1VUN5" FT /protein_id="CBT75338.1" FT /translation="MSSFPPEVMSNPRAERVKAIARLAKSKGREATGEYLVEGPQAVRE FT ALKAHLEDDNLVQNVYVVGGFLESHEEFETLLEDAKIQPRIVTGEVLHAMADTQTPQGI FT LAVVAMSQPQLSEVLDTKPKLIAVLCRIQDPGNAGTILRAADAAGADAVILTKGSVDIY FT NPKAVRSTVGSLFHLPVLNNVEFDHLIAAAKTTGSQVLAADGYAAHNLDTLQDAAVLRA FT NQPGTEAPEGQPVLEAPTLWLFGNEGQGLDEHEKQAADYRVAVPLYGVAESLNVGTAST FT VCLYASARAQR" FT CDS 1249113..1249553 FT /transl_table=11 FT /locus_tag="AARI_11280" FT /product="NUDIX domain-containing protein" FT /function="4.6 Miscellaneous" FT /note="identified by match to PF00293. Members of the Nudix FT hydrolase superfamily catalyze the hydrolysis of nucleoside FT diphosphates linked to other moieties. Substrates of nudix FT hydrolases include intact and oxidatively damaged FT nucleoside triphosphates, dinucleoside polyphosphates, FT nucleotide-sugars and dinucleotide enzymes. These FT substrates are metabolites or cell signaling molecules that FT require regulation during different stages of the cell FT cycle or during periods of stress. In general, the role of FT the nudix hydrolase is to sanitize the nucleotide pools and FT to maintain cell viability, thereby serving as surveillance FT and house- cleaning enzymes" FT /db_xref="GOA:E1VUN6" 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:E1VUN6" FT /protein_id="CBT75339.1" FT /translation="MPAELKQIVAVAIVDDLAQPTKLLAARRNRPEALAGLWEFPGGKV FT EPGESEVEAVRRELREELGVQLRLGAPIPGPHPQGWQLNEKAAMRMWFAQITDGEPATL FT DGHDQLSWLELDDQVGEVVDWIPADAPIVAACLAQARSGSQQ" FT CDS 1249640..1250269 FT /transl_table=11 FT /locus_tag="AARI_11290" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.878) with cleavage site probability 0.809 FT between position 28 and 29. 1 transmembrane helice FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="UniProtKB/TrEMBL:E1VUN7" FT /protein_id="CBT75340.1" FT /translation="MSVIALAFAAVLALSGCVNMNAEVNVLGKDKVAGAMQLTLHKSTL FT NGVTFEEVLNSQIDVAAMEEQLGDQWSYSKVDDGENVGLRFETTSPMTYVQLADAFSLF FT GFEINLSDDGKEYTFSMPGDKAAVDSSFTEANLHVTFPGAVTSHSPGTAQHHTVTFDMI FT QGAASYQATGKVDHTMFYAAVFGGALLVLTFVFVGAFAPKASKEAH" FT CDS 1250412..1251491 FT /transl_table=11 FT /gene="pheS" FT /locus_tag="AARI_11300" FT /product="phenylalanine--tRNA ligase subunit alpha" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.20" FT /note="activates phenylalanine and transfers it to FT tRNA(Phe) as the first step in protein biosynthesis" FT /db_xref="GOA:E1VUN8" 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/TrEMBL:E1VUN8" FT /protein_id="CBT75341.1" FT /translation="MSDQTTGQAPDGESNVPHPTDEAGIANAVDAALAAIEAAGDLNEL FT KEARLSHTGEKSALSLANRQIGKLDKSEKAVAGKLVGSARGRVNKALAARTVVLEEAEA FT ARILIEETVDVTAAARRRSVGARHPLSVLQDRVADIFVGMGWEIAEGPEVESEWFNFDA FT LNFKPDHPAREMQDTFFVEPADAHLVLRTHTSPVQVRSMLEREVPVYVLCPGRTFRTDE FT LDATHTPVFHQFEGLAVDKGLTMADLRGTLEHFARQMFGAEAQIRLRPAYFPFTEPSAE FT LDIWHPGAKGGPRWIEWGGCGMINPNVLRAAGIDPEEYSGFAFGMGIERTLMFRNDVPD FT MHDMIEGDIRFSQHFGMEI" FT CDS 1251495..1254038 FT /transl_table=11 FT /gene="pheT" FT /locus_tag="AARI_11310" FT /product="phenylalanine--tRNA ligase subunit beta" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.20" FT /note="activates phenylalanine and transfers it to FT tRNA(Phe) as the first step in protein biosynthesis" FT /db_xref="GOA:E1VUN9" 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:E1VUN9" FT /protein_id="CBT75342.1" FT /translation="MRIPLSWLREYAQVPADASAEDVMADLVKVGLEEEDVHRPSDELS FT GPIVVGQVLSLEKEVASNGKTINWCQVRVVPEGTEQTLTGKGIDPTGVQGIVCGAHNFV FT EGDKVVVTLPGAVLPGDFKISPRKTYGHTSAGMIASSRELGIGEDHDGIMVLSNYGLDP FT EVGTDVLALFGLDDQAAEINVTPDRGYCFSIRGVAREYALATGTSFTDPASIVTVSDAS FT EAGHEVVLADAAPIYGVPGCTRFVTREVTGIDPTRPTPRWMASRLQLAGMRSISLVVDI FT SNYVMLELGAPLHFYDADKLTSAITVRRANSGEKLTTLDDKERELSVEDLLITDESGAI FT GIAGVMGGAATEVSDSTSRVLIEAAHFDTVSIGRSRRRHKLPSEASKRFERGVDPRIMQ FT IAAQRAVNLLVELAGGTETAKATDAGAVPADTQIQLPAGFAGALIGVDYTDEQTISALE FT GIGAAVQQNAEGFLVTAPSWRPDLDIKEDLVEEVARVIGYDKIPATLPVAPPGRGLTRT FT QSQRRRLLQGLADAGLTEVLNYPFVSQAQNATFGAAQAGTEVKAVSLANPISKEFRFLR FT TSLLPGLLETARRNIGRGFRDLALYEGGLVFLPGQQLGSSVLPPLGAKPSDEVLAELFN FT GVPNQPWHLAAVFTGHEASAAAGFAPRAWDWADALDAAHNVADILGVELEVAQGSHQAF FT HPGRVAALKLAGEVVGYAGELHPQLLKDQDLPARTVAMELDAAALMSAAPAVVVAQQHL FT SSQPLATQDVALVVDQDVVAGDVLATLREGAGELLEDIALFDVYQGQGIEEGKKSLAFG FT LRFRAADRTLTADEASEVRAAAVDAAAKKFGATQR" FT CDS 1254173..1254400 FT /transl_table=11 FT /locus_tag="AARI_11320" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUP0" FT /protein_id="CBT75343.1" FT /translation="MPDGVAVKGLRSCGAVLLVFLLGIAAVAVLIAAGWAAVIFIQRGA FT GTHLEEPSTPSATLEQQAPNSLRPSETFAP" FT CDS complement(1254397..1254882) FT /transl_table=11 FT /locus_tag="AARI_11330" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VUP1" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VUP1" FT /protein_id="CBT75344.1" FT /translation="MGPSLVLTAMTKADAEFVARLAADERVTAYIGDGHTWSHEYTAQR FT VDHALLNAGICWYIARRQNSPVGLFTATERPAATEIGYWIDPEFWGQGLAKSLVGEGLA FT TLQAEGRSALIARVDSANIASLKVLKRHGFIAQAKEGPGLITLTRAMPAEPIPASGG" FT CDS complement(1254964..1255245) FT /transl_table=11 FT /locus_tag="AARI_11340" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUP2" FT /protein_id="CBT75345.1" FT /translation="MRIDSLDVFDDALLRAACQLEAAANAKASPGWQRHRNRTSNLQLH FT GEPYFDQSLFGQALDCFRRSLSIRQSLNLPEDQITSSRLAVAAAESRL" FT CDS 1255361..1255834 FT /transl_table=11 FT /locus_tag="AARI_11350" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VUP3" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VUP3" FT /protein_id="CBT75346.1" FT /translation="MSSVSENTRQARAGDSAEVYRLARMFTPELGLGAEDFEENFQMLV FT NDSNWFICVAESGRGLSGYAAAQDYGPGLRTPFTVGRLHDLFVEPGTRRTGLGNKMVEE FT VFRWARQSSMPMMLDWQATEESISFYASFGLEADFVGDFPQCPGFTLDLRPKT" FT CDS complement(1255895..1256416) FT /transl_table=11 FT /locus_tag="AARI_11360" FT /product="phosphoribosyl transferase domain-containing FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF00156. This family FT includes a range of diverse phosphoribosyl transferase FT enzymes" FT /db_xref="GOA:E1VUP4" FT /db_xref="InterPro:IPR000836" FT /db_xref="UniProtKB/TrEMBL:E1VUP4" FT /protein_id="CBT75347.1" FT /translation="MTSIDDSGVSVLSEPEREILTWDTFGEASRELAQTIVDDGFEPDI FT VLAVARGGLLLAGSISYALGVKACGALNVEFYTGIGTVLPEPVVLPPMLDDGHLRDKKI FT LIVDDVSDSGRTLEKVVDLVSAWGAEVKTVCLYTKPRTIMVPDYEWRRTDKWITFPWSD FT LPPVTASAAK" FT CDS 1256711..1258225 FT /transl_table=11 FT /locus_tag="AARI_11370" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.971 FT between position 30 and 31. 1 transmembrane helice FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="UniProtKB/TrEMBL:E1VUP5" FT /protein_id="CBT75348.1" FT /translation="MSLRTWSIRIASTATVLAIGVASAIPAAQAGNSIQLAAGQNLESV FT TIEDSTGMLNEQRLREALEELDFNEPTDVAVYARNGEYSDDINTKTLEFAKSSHPEWIS FT AKPEDYGDYWADGLFIITLSIEGRGDGQIGTYFGEDRKVSESAMESIHEAGYDDFNLSR FT WTDGVIAVADQAAVIMNRPWYEHPALWIAGGSAGVVGAIVGGAVMHTRSKRRETFAEEL FT RQGGLHLTNVTMDLDETELAARTLPATSQHAIELEQRFAKFMTKYRACFEAQQALESSG FT KKERSGYEGVRFAKEFKESAQSLDLTDDAIIAASALYTRSASWKDAWHAQTKPLEDDLA FT EIRELLQDVEPELMGSAAALASYREVATEQLRELSVQLEEESITVDQALDSLSALRAEL FT TEKLDIFAQAQIEVYAESAEEKADMQSELKKSRYESRANQNSVGTILDVLNPSSMYWRV FT GSYHHGYTAGVSAVTASREAASSSGGISSGYSGGGSFSGAGGSSRF" FT CDS 1258267..1258905 FT /transl_table=11 FT /locus_tag="AARI_11380" FT /product="putative holo-[acyl-carrier-protein] synthase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.8.7" FT /note="identified by match to PF01648: 4- FT phosphopantetheinyl transferase superfamily. Holo-[acyl- FT carrier-protein] synthase catalyses the following reaction: FT CoA-(4-phosphopantetheine) + apo-[acyl-carrier- protein] => FT adenosine 3,5-bisphosphate + holo-[acyl- carrier-protein]. FT All polyketide synthases, fatty-acid synthases and FT non-ribosomal peptide synthases require post- translational FT modification of their constituent acyl- carrier-protein FT (ACP) domains to become catalytically active. The inactive FT apo-proteins are converted into their active holo-forms by FT transfer of the 4-phosphopantetheinyl moiety of CoA to the FT sidechain hydroxy group of a conserved serine residue in FT each ACP domain" FT /db_xref="GOA:E1VUP6" FT /db_xref="InterPro:IPR003542" FT /db_xref="InterPro:IPR008278" FT /db_xref="UniProtKB/TrEMBL:E1VUP6" FT /protein_id="CBT75349.1" FT /translation="MHVVQTRTELDGGPRYWQEERYILGAAPQRQQEFRTVRVCARRAL FT ASLGFADFALVPDGKRAPIWPEGVLGSMTHCAGFRAAAVASSADLRSIGIDAELHMPLP FT EEIHGIVLLPEEQQLVQDLAASHPGIAWDRLIFSAKESVFKAWFPLTRQWLDFLECRIS FT IDIPTQRFQASIRDEHALAAKRGLSVMDGGWKAEGPSGQGLLGTCITVP" FT CDS complement(1258929..1259825) FT /transl_table=11 FT /locus_tag="AARI_11390" FT /product="polyphosphate kinase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein domain PF03976. This FT domain is about 230 amino acids in length and has FT polyphosphate kinase activity" FT /db_xref="GOA:E1VUP7" FT /db_xref="InterPro:IPR016898" FT /db_xref="InterPro:IPR022486" FT /db_xref="InterPro:IPR022488" FT /db_xref="UniProtKB/TrEMBL:E1VUP7" FT /protein_id="CBT75350.1" FT /translation="MTVETPLLDESFLGYSVLDNDDDDPVLVRADGSIVDTWRENYPYA FT EKLDRATYELQKRALQIELLKLQKWAKANGRRIMIVFEGRDAAGKGGTIKRFTEHLNPR FT GARVVALEKPSERESTQWYYQRYVQHFPSAGEIVLFDRSWYNRAGVERAMGFCTQEQVA FT HFLDQTPAFEKMVVDEGIDLIKFWFSVSASEQLTRFTIRRIDPVRQWKLSPMDLESLDK FT WDKYTEAKKEMFLKTDTEHAPWTVVKSNDKKRARLQAMRHVLNLFDYKGKDHELVGSPD FT PRIVGRAANVITHGEEF" FT CDS complement(1259958..1261259) FT /transl_table=11 FT /locus_tag="AARI_11400" FT /product="M1 family aminopeptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.11.-" FT /note="identified by match to protein family PF01433. This FT group of metallopeptidases belong to the MEROPS peptidase FT family M1 (clan MA(E)). Members of this family are FT aminopeptidases. The members differ widely in specificity, FT hydrolysing acidic, basic or neutral N-terminal residues. FT Match to PS00142 pattern: neutral zinc metallopeptidases, FT zinc-binding region signature" FT /db_xref="GOA:E1VUP8" FT /db_xref="InterPro:IPR001930" FT /db_xref="InterPro:IPR014782" FT /db_xref="UniProtKB/TrEMBL:E1VUP8" FT /protein_id="CBT75351.1" FT /translation="MPHTILDEYTKHHGSPKYTVEHYDLALVIKLASNLLDGRATLRIR FT ALEDLHEVALNLSGLKIIKATCQGRKVQVSKKHHRMVVSLPTPVPAGERVELNLRYAGS FT PQAEDGLWGELGWEELTDGILVSGQPVGASTWYPCNDHPSHKSTYRFEISTDAGYRVVA FT NGQLVDHRRSASRETWVYEQREPMASYLATLQIGRYQEIPFDQGGHLLAYAVPGSDLPV FT RGAFAKQAAMAQLFERKFGPYPFESYKIVVVDDELEIPLEAQGLSIFGKNHLSLQWEAQ FT RLIAHELAHQWFGNSLTPGRWKDIWLNEGFACFSEWVYSQEAGVMPLAERARTAWQMLK FT DLPQDIVVGDPGPADMFDDRVYKRGALALYALMVQLGEAQFYVMLREWTATHKHSTVST FT PMFAELLCRYAPESRVQPILDAWLFSEDLPPFPG" FT CDS complement(1261273..1265208) FT /transl_table=11 FT /locus_tag="AARI_11410" FT /product="putative non-ribosomal peptide synthetase FT component" FT /function="3.7.6 Nonribosomal protein synthesis" FT /note="match to protein domains TIGR02353 and TIGR01733. FT May be involved in enterobactin-like siderophore FT biosynthesis" FT /db_xref="GOA:E1VUP9" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR001451" FT /db_xref="InterPro:IPR006163" FT /db_xref="InterPro:IPR009081" FT /db_xref="InterPro:IPR011004" FT /db_xref="InterPro:IPR012728" FT /db_xref="InterPro:IPR020845" FT /db_xref="UniProtKB/TrEMBL:E1VUP9" FT /protein_id="CBT75352.1" FT /translation="MDTEQTPTPDAPIHQPQFPAGDRAPNARTLMDIVQATALAHPDAP FT AIDDGERIESYAELIEEVKAKALRLHEQGLGAGDRIGLRVESGTRHLYEWILAIMWVGA FT AYVPVDADDPDERAKTVFTEAQVAGIIKGRDTIVADAQRPKPFANPRMPSLQDDAWIIF FT TSGSTGKPKGVAVTHRSAAAFVDAEAKMFLPGNPLNTSDRVLAGLSVAFDASCEEMWIA FT WRNGSCLVPAPRALVRSGMDLGPWLISRSITAVSTVPTLAALWPAQALDSVRLLIFGGE FT ACPPELARRLATEGREVWNTYGPTEATVVACGATMDGSVPVRIGLPLDGWDLAVVDPDG FT IPVAEGESGELIIGGVGLARYLDPEKDAEKYAPMPTLGWERAYRSGDMVINDHLGLIFV FT GRVDDQVKIGGRRIELGEIDAALNSLPEVSAAAVAVRETATGNKILVGYLQADPGYDLA FT AARTALLADLPAPMVPILAVMDRLPMKTSGKVDRNALPWPLPGAAQDADASDLPQLDGT FT GQFIADCWKGALGATAAGWDADFFASGGGSLAAAQLVSALRARYPDLTVAELYDYPRFG FT ALVEYLGGQQQSAAPAQPRTVVRTQRGTQWVQSLLAVPLFVLSGLRWFTYLMFGHLFMV FT ALGVFDAPLPAPWYVLGGLWLLFVTPLGRMSLSIAANKLLLRGLQPGTYPRSGSLHLRL FT WLAQHIADVVDPISLASAPLLPWYARMLGARIDATATLHTLPPVTGLLTVGPGATIEPE FT VDISGYWIDGDKLHVGAIEVGAHASVGARSTLAPGAVIGERTIVEAGSALYGQARSHSR FT YAGSPAQREGRAKPKWPEHEPEHKLLPRFLGAVGSIALNLAQWIPVIAALLAIAPVLGT FT AQSLTGIGWRFIPAVLLGATVWFLSTMVLTIAVVRLLSIGLVEGWHPVTSRVGWQAWAT FT ERVLDTARDLLFPLYASLFTPIWLRLLGAKVGRDVEISTVLLIPKMTTISSGAFLADDT FT MVASYELGGGWMHIAPVRVGKKAFLGNSGILHAGRRVPKRSLIAVLSATPKKMKAGTSW FT IGSPPHMLRRTTVEGESDLTYRPTLKLKMLRAGWELTRALAVFTTVGIAGGVLWTLSAL FT TTYFSPLAAILLSGAVLVAAGAIAALVAVAAKWLVIGVIRPGEHALWSSFIWRTEMVDS FT FTELVCAQWFARLASGTPALVWFLRAQGARIGHGVWCESYWFPEADLVTLEDHATVNRG FT CVLQTHLFHDRIMSIDAVTLGAGATLGPHSVILPAARISEGTTTGPASLVLRGEVLPAN FT TYWRGNPAVRWNIEEEPESELPVDQQA" FT CDS complement(1265373..1266293) FT /transl_table=11 FT /locus_tag="AARI_11420" FT /product="putative amidohydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF04909" FT /db_xref="GOA:E1VUQ0" FT /db_xref="InterPro:IPR006992" FT /db_xref="UniProtKB/TrEMBL:E1VUQ0" FT /protein_id="CBT75353.1" FT /translation="MADLLSGHAGTGPSDDAALPAYLQALGIPGLIDLHVHFMPQNVLD FT KVWAFFDSAGERSGTPWPINYRLGEAQRVATLRELGVIAYGTLNYAHRPSMAAWLNAYS FT RDFAAGHPEAIRSGTFYPEPGVTQLVREAIADGVEIFKVHVQVGGFTPLDPQLDQAWEL FT LAEARTPVVIHCGNGPHRGEFTGIEPIRELIARHPSLVLVIAHAGLPDYLDFAQLAAEH FT PNVYLDTTMVGTGFMNRIAPLPADYPQVVAGLGHKIVLGSDFPNIPYSYSHQIQALAAW FT GLGGQWMREVLHDTPLKLLQAVRNR" FT CDS complement(1266296..1267264) FT /transl_table=11 FT /gene="qor" FT /locus_tag="AARI_11430" FT /product="putative NADPH:quinone reductase" FT /function="4.6 Miscellaneous" FT /EC_number="1.6.5.5" FT /note="NADPH:quinone reductase catalyzes the following FT reaction: NADPH + quinone <=> NADP(+) + semiquinone. FT Quinone or similar compounds may act as acceptor" FT /db_xref="GOA:E1VUQ1" FT /db_xref="InterPro:IPR002085" FT /db_xref="InterPro:IPR002364" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR013149" FT /db_xref="InterPro:IPR013154" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VUQ1" FT /protein_id="CBT75354.1" FT /translation="MQQQAIVVNEPADANGLELGQVPVPAPGPGQLLVKVAATGVNFIE FT TYQRSGVYKVDYPFTPGSEFSGVVEQIGDGVQNYKIGDRVATASGTAGYAQYALVEAKR FT AGKVPNAVDLRIAAALPLQGMTAHYLVHSSYMVHSGDVVLTYAGAGGVGLILTQLLKLK FT GATVITTASTQQKKDLAKAAGADYVVDYDQVAATVEQVTGGAGVHAVYDGIGKDTFETS FT LAALRRRGTLVLFGGASGQVPDFNLQRLNAGGSLSVTRPKLDDFLATEEEMHWRFGDIF FT GWVAAGDIDVRIGAQFELAEAAKAHAALESRATTGKVILVP" FT CDS 1267448..1268479 FT /transl_table=11 FT /gene="argC" FT /locus_tag="AARI_11440" FT /product="N-acetyl-gamma-glutamyl-phosphate reductase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.2.1.38" FT /note="catalyzes the third step in the biosynthesis of FT arginine from glutamate, the NADP-dependent reduction of N- FT acetyl-5-glutamyl phosphate into N-acetylglutamate 5- FT semialdehyde" FT /db_xref="GOA:E1VUQ2" FT /db_xref="InterPro:IPR000534" FT /db_xref="InterPro:IPR000706" FT /db_xref="InterPro:IPR012280" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR023013" FT /db_xref="UniProtKB/TrEMBL:E1VUQ2" FT /protein_id="CBT75355.1" FT /translation="MTISVAVSGASGYAGGEVLRILAAHPEVEIGAITAHSQAGQRLGS FT IAPHLHALADRVLVDTTVENLAGHDVVFLALPHGASAAVAAALPESTLVIDAGADHRLE FT SAVAWKKFYGSEHAGFWPYGLPELPGQREKLVGTKRVAVPGCYPTGAQLALAPGFGAGL FT LESDDVVIVSASGTSGAGKSLKPNLLGSEVMGSMSTYGVGGSHRHIPEMEQGFSKLAGE FT PVTVSFTPTLAPMPRGILTTATAKVKAGVTEAMLREAWTEAYAGELFVHLLPEGQWPTT FT GAVQASNHVQLQLAFDTHANRVIVTAALDNLTKGTAGAAVQSMNIALGLEENTGLLMQG FT VAP" FT CDS 1268476..1269690 FT /transl_table=11 FT /gene="argJ" FT /locus_tag="AARI_11450" FT /product="bifunctional glutamate FT N-acetyltransferase/amino-acid N-acetyltransferase protein" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.3.1.35" FT /EC_number="2.3.1.1" FT /note="glutamate N-acetyltransferase (EC 2.3.1.35) FT catalyses the production of L-ornithine and N-acetyl-L- FT glutamate from N(2)-acetyl-L-ornithine and L-glutamate. FT Amino-acid N-acetyltransferase (EC 2.3.1.1) catalyses the FT formation of N-acetyl-L-glutamate from acetyl-CoA and L- FT glutamate. Involved in arginine biosynthesis" FT /db_xref="GOA:E1VUQ3" FT /db_xref="InterPro:IPR002813" FT /db_xref="InterPro:IPR016117" FT /db_xref="UniProtKB/TrEMBL:E1VUQ3" FT /protein_id="CBT75356.1" FT /translation="MSLAHTNTHPSAAATGVTAPAGFSAAGVPAGLKSTGKNDVVVVKN FT HGPEFTAAGVFTSNRVAAAPVHWSKQVLADGRIDAVVLNSGGANACTGAEGFANTHKTA FT EYVAQLLEVSAGDVAVASTGLIGEQLPMDKLLPGVKAAADTLADDQNASDQAAAGIMTT FT DTVPKLVSRIVGESGSGQVIIGGMAKGAGMLAPALATMLVVLTTDAVLTSQQADDALRA FT ATAMSFDRADSDGCMSTNDTVLLLASGASGAAPVMEEFTAALTDACCELAAKLIEDAEG FT ADHTIAIRTYNAATEADALEVSKAVSRSNLVKTAVFGKDPNWGRVLSEVGTTKAAFEPD FT ELNVSINGVMVCKNGGVGEDRNLVNLDERNVSIEIDLNAGTEQATVLTNDLTHDYVHEN FT SAYSS" FT CDS 1269712..1270665 FT /transl_table=11 FT /gene="argB" FT /locus_tag="AARI_11460" FT /product="acetylglutamate kinase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.7.2.8" FT /note="catalyses the formation of N-acetyl-L-glutamate 5- FT phosphate from N-acetyl-L-glutamate. Involved in arginine FT biosynthesis" FT /db_xref="GOA:E1VUQ4" FT /db_xref="InterPro:IPR001048" FT /db_xref="InterPro:IPR001057" FT /db_xref="InterPro:IPR004662" FT /db_xref="UniProtKB/TrEMBL:E1VUQ4" FT /protein_id="CBT75357.1" FT /translation="MAQTIRTNLDIAQSKAEALIEALPWIQRFAGTTMVIKYGGNAMVN FT DQLRRAFAEDIVFLRHAGVNPVVVHGGGPQINKMLDTLGIESEFRGGLRVTTPEAMDVV FT RMVLTGQVQRDLVGLINSHGPYSVGMSGEDGATLQAVRTGTIVDGLPVDLGLVGEVTTV FT RTDQVDSLVDAGMIPVISTVAPEFDEHGEPTGAVLNVNADTAAAALASALGATKLVILT FT DVEGLYAAWPDKSSLISSITNDELRQMLPSLESGMIPKMGACLKAVDEGVGQAHIVDGR FT APHSMLLEIFTTAGVGTQVLPAGKPNCAANTAKKDA" FT CDS 1270665..1271930 FT /transl_table=11 FT /gene="argD" FT /locus_tag="AARI_11470" FT /product="acetylornithine transaminase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.6.1.11" FT /note="catalyses the following reaction: N(2)-acetyl-L- FT ornithine + 2-oxoglutarate <=> N-acetyl-L-glutamate 5- FT semialdehyde + L-glutamate. Involved in arginine FT biosynthesis" FT /db_xref="GOA:E1VUQ5" 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:E1VUQ5" FT /protein_id="CBT75358.1" FT /translation="MSQNAAETTAAQLAANPAPEVTELTGLSSKALSERYSKSLLGVFG FT TPQRVLVRGAGCHVWDADGNQYLDLLGGIAVNTLGHGHPLLTSVITSQLATLGHVSNFF FT TSPSQIALAEKLLEISAAPAGSKVFFANSGTEANEAALKLTRRNAGTEAAPRTKVIALE FT HSFHGRTLGALSLTYKEKYRAPFAPLPENVSWIPAGDIEALRAAVDETVSAVFIEPIQG FT EAGVLELSTEYLQAAREITRDSGALLVFDEVQTGMGRTGQFFASAPVIPDVMTLAKGLG FT GGFPIGAMIVFGQENTAWLTPGEHGTTFGGNPVACAAGLAVIHTIEKENLLAHVRATGD FT WLREQLAGIQGIGAVRGAGLLTAFELKSANAPKLVTAALDAGFIVNATDEKTIRLAPPL FT VITTEQLATLVTALPQLISAAS" FT CDS 1271981..1272940 FT /transl_table=11 FT /gene="argF" FT /locus_tag="AARI_11480" FT /product="ornithine carbamoyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.1.3.3" FT /note="catalyzes the conversion of ornithine and carbamoyl FT phosphate to citrulline. It is involved in the biosynthesis FT of arginine and, in some bacteria, it is also involved in FT the degradation of arginine (the arginine deaminase FT pathway)" FT /db_xref="GOA:E1VUQ6" FT /db_xref="InterPro:IPR002292" FT /db_xref="InterPro:IPR006130" FT /db_xref="InterPro:IPR006131" FT /db_xref="InterPro:IPR006132" FT /db_xref="InterPro:IPR024904" FT /db_xref="UniProtKB/TrEMBL:E1VUQ6" FT /protein_id="CBT75359.1" FT /translation="MSATRHFLTDLEFTPDEQSKVLDLAAKMKADKYGFKPYAGPQSVA FT VFFDKTSTRTRVSFHAGISELGGSPLIINSLDSQLGHKESISDSAKVLARMVSTIVWRT FT FAQSGLEEMAANSAVPVINALSDDYHPCQLIADLLTVREHKGKTQGLTMAYLGDAANNM FT ANSYLLAGVTAGMHVRIAGPEGYLPDAAIIAAAEIRAETTGASIMITTDAAAALADADV FT VVTDTWVSMGQEDEKEARLKLFTDYSVTAEAMKLAKDDAIVLHCLPAYRGYEIDAEVID FT GPQSVVFDEAENRVHAQKAVMTWLMVASGLAEDPRVEL" FT CDS 1272942..1273445 FT /transl_table=11 FT /gene="argR" FT /locus_tag="AARI_11490" FT /product="arginine repressor" FT /function="3.5.2 Transcription regulation" FT /note="regulates arginine biosynthesis when complexed with FT arginine by binding at site that overlap the promotors of FT the arginine biosynthesis genes" FT /db_xref="GOA:E1VUQ7" FT /db_xref="InterPro:IPR001669" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR020899" FT /db_xref="InterPro:IPR020900" FT /db_xref="UniProtKB/TrEMBL:E1VUQ7" FT /protein_id="CBT75360.1" FT /translation="MSSQPSTKTARQARIRAFLGNNSVKSQAELLGLLKDDGLEVTQAT FT LSRDLVEIGAVRIRDNSGQLIYAVRQEGGDRSPKTAITQEVLDARLAKICAEQLVTAEA FT SGNIVVLRTPPGAANLLALAIDHSQMPSILGCIAGDDTIMVTTRAVDGGADVAARFLQL FT AEPR" FT CDS 1273542..1275440 FT /transl_table=11 FT /locus_tag="AARI_11500" FT /product="HNH endonuclease domain-containing protein" FT /function="3 Information pathways" FT /note="identified by match to PF01844" FT /db_xref="GOA:E1VUQ8" FT /db_xref="InterPro:IPR003615" FT /db_xref="UniProtKB/TrEMBL:E1VUQ8" FT /protein_id="CBT75361.1" FT /translation="MEQAHSARIQPASLVDLGTALATVAQQLCSGTALSAQQLLRAERT FT CLDLFATLGAQAAQSTDPRLALAHAIFAQAFSQRATAANIAAASLVETTAAHALDLQEF FT ENLHAGTTDFSAPPCFAPGRTVYRDAPTVLAALLDLNYFEADRRIKDAHLLYARKDISG FT AACAPRFTKLAQCFAGSPLQSPHDAPATAAASTAPGGWALPDLHQLPDPREVLKTARAL FT DKFEPEDATFDGLPSYATAKAADGSLLEDQAAAHLRDEKISIRQKRINGLIKDYKDAHQ FT QTKTPKLGLFRGKVVNGVHEYIIRVRELDAELWESLIAQADNKRTQAGAAARKAAGLDT FT GTGTGSQEQESAEDQPHPENFDGDDNCAGDEAASNHASEEDSSHEESPDEEQPGEQAEG FT EQQMLTDELWSSGQPPPPWAGAQSQDSQNADPPDLKLLAPPVLGTPDTCTVPERRLNAL FT NAILRNIGPGSSSKRITPEIVVHARYEDLQDLGSLTGITAHGIKLSAPQLRTMLCEAKV FT LSPIYNADGVIMDIGRDSRLFPRWMKLAARDRDGGCLVPGCTMDPALVEFHHFEPWAKG FT GRTRLQDCCPLCSLHHTMVHAGYLKLVKIKGLPYVILPKHLDPQQLPRRNTYFARA" FT CDS complement(1275565..1276131) FT /transl_table=11 FT /locus_tag="AARI_11510" FT /product="macro domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF01661. This domain is an FT ADP-ribose binding module. It is found in a number of FT otherwise unrelated proteins" FT /db_xref="InterPro:IPR002589" FT /db_xref="UniProtKB/TrEMBL:E1VUQ9" FT /protein_id="CBT75362.1" FT /translation="MEIQLYRGDITTLHVDAIVNAANPSLLGGGGVDGAIHTAAGPSLL FT AACREIRANRYPDGIPSGIAVATKAGNLHAKWVVHTAAPNLALATANPVKPNPKILDDC FT FVNSLYVAARHEAHSVAFPAIGAGAFGWDPEQVADIAHVAISRWVETNKHISPIHKIIL FT VAHTDEVQAAFERAFSLDAVEDIAA" FT CDS 1276386..1277801 FT /transl_table=11 FT /gene="argH" FT /locus_tag="AARI_11520" FT /product="argininosuccinate lyase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.3.2.1" FT /note="catalyzes the formation of arginine and fumarate FT from argininosuccinate, the last step in the biosynthesis FT of arginine" FT /db_xref="GOA:E1VUR0" 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/TrEMBL:E1VUR0" FT /protein_id="CBT75363.1" FT /translation="MASSTNEGSLWGGRFSGGPADAMAALSKSTHFDWRLASYDIAGSR FT AHAKVLNRAGLLTDAELADMITALDQLEADVISEAYVAAETDEDVHGSLERGLLERAGI FT ALGGKLRAGRSRNDQIATLGRMFLRDHARIIARGIIDTLDAMVEQVKAHPYAPMPGRTH FT LQHAQPILLSHLLLAYSWPLLRDVQRLVDWDKRAAVSPYGSGALAGQTLGLDPNFVAAE FT LGFDSAVHNSIDGTAARDVFAEFSWIAAMIGVDLSRVSEEVILWATKEFSFVKLHDSFS FT TGSSIMPQKKNPDIAELARGKAGRLIGDLTGLLATLKALPLAYNRDLQEDKEPVFDAAD FT TLEMLLPAMAGMMGTLTFNTERMAELAPQGFALATDIAEWLVRQGVPFRDAHELSGAAV FT QLAESRGVELWDLTDEEYAGISEHLTPQVREVLSTEGSLNARNGQGGTAPSAVAAQLVE FT FERQLAQIKDWAK" FT CDS 1277918..1278658 FT /transl_table=11 FT /locus_tag="AARI_11530" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VUR2" FT /db_xref="InterPro:IPR017517" FT /db_xref="InterPro:IPR024344" FT /db_xref="UniProtKB/TrEMBL:E1VUR2" FT /protein_id="CBT75364.1" FT /translation="MTQLLAPGELIAQVTTALDELSVQLRDVPDTQYPKPSSLPGWSTA FT QLIAHLASFAKAAVRQFENAGTEQPPAMYDGGAEGRIEAINMTALMRPESLRALASDAL FT AQLRAALPGVEAKWEAPVGYRPTATAADMMYATWREMLIHATDLDEFVRPAASWPPAFS FT EHLFRALSARVPQGTRLVLQPHGKTPIVLGEGAKSWVLSGTDFDLAAWMAGRPASGPVQ FT VTAAADGAADPKLLPWPSDRLMNR" FT CDS 1278755..1279303 FT /transl_table=11 FT /gene="apt" FT /locus_tag="AARI_11540" FT /product="adenine phosphoribosyltransferase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.4.2.7" FT /note="catalyses the formation of AMP and diphosphate from FT adenine and 5-phospho-alpha-D-ribose 1-diphosphate. FT Involved in purine salvage" FT /db_xref="GOA:E1VUR1" FT /db_xref="InterPro:IPR000836" FT /db_xref="InterPro:IPR005764" FT /db_xref="UniProtKB/TrEMBL:E1VUR1" FT /protein_id="CBT75365.1" FT /translation="MVAVTTSESISDLLDRLCEIVPDYPQPGISFKDLTPVFADASGLR FT RMVDALIAPFEGQFDIVAGLEARGFVLAAAAAYASGKGMLTIRKAGKLPREVYRDEYTL FT EYGTGCLEVHKDEIAPGTRVLILDDVLATGGTVSSSVRLLEQTGAKIAGVGVVLELDGL FT NGRDKLPGQNVVSLQVVHS" FT CDS 1279544..1281823 FT /transl_table=11 FT /locus_tag="AARI_11550" FT /product="putative ATP-dependent DNA helicase" FT /function="3 Information pathways" FT /EC_number="3.6.1.-" FT /note="match to protein family PS51198: UvrD-like DNA FT helicase ATP-binding domain profile. UvrD-like DNA FT helicases belong to superfamily 1 (SF1)" FT /db_xref="GOA:E1VUR3" FT /db_xref="InterPro:IPR000212" FT /db_xref="InterPro:IPR014016" FT /db_xref="UniProtKB/TrEMBL:E1VUR3" FT /protein_id="CBT75366.1" FT /translation="MTDTIQADLLAESDYVGRLYARLDELRAEKVRQLERTRAQGAIGT FT FQNMSERDSFATLYEDRIAQLDAVEDRLVFGRLDMAGNGQEQAEDPGTGSSPRYIGRIG FT LSDDELNRMMIDWRASEAAPFYQATALNPRGVRRRRHLMLSGRTVAGIEDDVLDETWLD FT EGHTHHGEGALMAALREKRTGRMGDIVGTIQAEQDAIIRAGLPGAVVVQGGPGTGKTAV FT ALHRAAFLLYEYRERLKNAGVLIVGPSNSFMRYIERVLPSLGETGVVMSSVGELYHGLH FT AVPETNRTVARLKGQLSMAKVIANAVRNRQRLIPETRTVVVEGTRLSLTPKMVKNARER FT ARHTHKPYNEARETFVKVLVGDLAEQLRRKLEESAGQSSTTDRSYLPQEVRESHDVRVA FT LNLCWMPMTPQQLVAELFATPHLLAAAAPHLKEKDRDALYRRANSPFTEADVPLLDEAA FT QLLGEFADPLAGAHTAQYEADVENAKAALLNMHTMLENAGIDGVVTAEQVAGVNQETAA FT RLTAAERAVSDRTWAYGHIVVDEAQELSPMQWRLLVRRCPMKSFTIVGDIAQTSAASGA FT SSWSQALEPFFGDRFELEELTVNYRTPAQIADAAVRVAQAAGLRITTPQAVREGDWPPV FT LTKTTEAQVEATLLDALAQELEYSAGGLQAVIVPQQDLHRVRAAVTAVHGDRVGTGSGG FT LSQDIVVITARESKGLEFDGVLILEPAELVDEVDGGVGDLYVAMTRTTQRLHVVHTRQL FT PEGLEQ" FT CDS 1282025..1283350 FT /transl_table=11 FT /gene="tyrS" FT /locus_tag="AARI_11560" FT /product="tyrosine--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.1" FT /note="activates tyrosine and transfers it to tRNA(Tyr) as FT the first step in protein biosynthesis" FT /db_xref="GOA:E1VUR4" FT /db_xref="InterPro:IPR001412" FT /db_xref="InterPro:IPR002305" FT /db_xref="InterPro:IPR002307" FT /db_xref="InterPro:IPR002942" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR024088" FT /db_xref="InterPro:IPR024107" FT /db_xref="UniProtKB/TrEMBL:E1VUR4" FT /protein_id="CBT75367.1" FT /translation="MSISDTKQNPVIAGQGNDASFENVWQELKWRGLVHVSTDEAELER FT ALSEETVTYYCGFDPTAPSLHLGNLVQLLNMRRLQLAGHKPLALVGGSTGLIGDPRQTA FT ERTLNTKETVTEWVSKLQAQVSRFLSNEGENAVQLVNNLDWTQQLSALDFLRDVGKYFR FT VGTMVKKEIVAARLNSDEGISYTEFSYQVLQGYDFLELNRQYGCTLQTGGSDQWGNLTS FT GTELIRKVQGNSVHAYGTPLITNSDGTKFGKSEGNAIWLDAEMCSPYTFYQFWLNASDA FT DVIDRLKVFTFLTRKQIAELETEVAERPFKRIAQRTLAWEVTSLVHGQQATEQVIAASA FT AVFGNGDLAAIDLPTLESVIAELPTAKVEADNLGILNVLVASGLSKSLSEARRTVNEGG FT AYVNNEKVAGIDTELAEADFLHGRYAILRRGKKNMAVVELAK" FT rRNA 1283878..1285396 FT /locus_tag="AARI_36690" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 1286031..1289153 FT /locus_tag="AARI_36700" FT /inference="ab initio prediction:rRNAScan:1.0" FT rRNA 1289310..1289425 FT /locus_tag="AARI_36710" FT /inference="ab initio prediction:rRNAScan:1.0" FT repeat_region 1289561..1289568 FT /rpt_type=DIRECT FT mobile_element 1289569..1290908 FT /mobile_element_type="insertion sequence:ISAAr5" FT /rpt_family="IS256" FT CDS 1289641..1290840 FT /transl_table=11 FT /locus_tag="AARI_34800" FT /product="transposase of ISAar5, IS256 family" FT /function="4.5 Transposon and IS" FT /db_xref="InterPro:IPR018289" FT /db_xref="UniProtKB/TrEMBL:E1VUR5" FT /protein_id="CBT75368.1" FT /translation="MGIESISVKLTGQSHTCIICHSRLKKNGTTSKGTQRWRCITCNAS FT TVFKREDTTARNQLTGFVTWLMSKHSQAEFGGGTGRTFRHQTAWCWNVHPYLHHTGEVF FT DEIQVDGIYLRQGWCLLIAIAHGRVIGWQWCDREKAEAWTVLLQHFPEPKVVVTDGGSG FT LMKALKEFWPNVKIQRCLVHIQRNVRTYLTLNPRLPAGKSLRRLSLKLTKIRTQEAAAE FT WIAAFAAWHAENHELINERTYAADWSGAWPRGLRRNRKWWYTHDRLRSAYESMNKALRR FT GHLFTYLDKDLNGLGINATTNMIEGAVNSGIRAMIFYHRGMPIEHRRRACEWFCWTHAD FT EGNRPALRTLLRPEHYTPETKKKAQHMVDEAPIGPELYGTGPSAEDGQFIRSGWMRNIY FT " FT repeat_region 1290909..1290916 FT /rpt_type=DIRECT FT CDS 1291158..1293482 FT /transl_table=11 FT /locus_tag="AARI_11570" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VUR6" FT /protein_id="CBT75369.1" FT /translation="MSNEFRRNSDNGRGDFRNSDSNRNNSRDGFKRREDRGDFKRDDNR FT GGGFKRDDNRGGGFKRDDNRGGGFKRDDNRGGGFRSDRNDDRGGFRGERRDDNRAGGFK FT RDDNRGGGFKRDDNRGGGFRSDRNDDRGGFKRDDNRGGGFRGDRNDDRGGFRGERRDDN FT RAGGFKRDDNRGGGFKRDDNRGGGFRSDRNDDRGGFKRDDNRGGGFRGDRNDDRGGFKR FT DDNRGGGFKRDDNRGGGFKRNDDRGGFRSDRNDDRGGFKRDDSRGGFRGERRDDNRGGG FT FKRNDDRGGFKRDDNRGGGFRSDRNDDRGGFKREDNRGGGFKRNDDRGGFKRDDNRGGG FT FRGDRNDDRGGFKRDDNRGGGFRGDRNDDRGGFKRDDNRGGGFRGDRNDDRGGFKRGDN FT RGGGFNRDDNRGGGFRGERRDDNRGGGFNRPDDRRSQGERPAREDRFADKRGDAPRAHN FT PGDLRISNRADREQSPDIDEDVTGKELDRVARAQLRYLEERSASWVAKHLVMAGRLLEE FT DPELAYEHTLAASRRGGRVAVVREAVGIAAYHAGKYADALRELRTHRRISGSDYNLPLI FT ADSLRGLGRPEKAIELAQSEECANLETAVKVEMQIVAAGSYGDLGKLDKALAELESLEQ FT LDFNRAFSFSPRLFTAYADLLSAAGRAEDAKRWNAQVEVAENALGIERETDSFIMDLAP FT EMDEEEETPRAKDLIDPAEAETEDAAQADSVEADAEADADADADDAEAEQTGIDEEDDL FT NEVVESDTDAIEADAEEDSSK" FT CDS 1293531..1294538 FT /transl_table=11 FT /locus_tag="AARI_11580" FT /product="haloacid dehalogenase-like family hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00702. This family includes FT L-2-haloacid dehalogenase, epoxide hydrolases and FT phosphatases" FT /db_xref="GOA:E1VUR7" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006357" FT /db_xref="InterPro:IPR023214" FT /db_xref="InterPro:IPR023215" FT /db_xref="UniProtKB/TrEMBL:E1VUR7" FT /protein_id="CBT75370.1" FT /translation="MLISGFDSVLSDLDGVVYAGPNAIDDAVESLNTLAEVNVTLAFIT FT NNAGRSPMSVAAHLRQLGVKTSAEQVFGSADAGAEMLARELNPGSKVLVVGSPYLRECI FT AVRGLEVVESHSEEPVAVIQGFDPDISWKNLAEASYAINNGAKWVATNTDFTIPRAEGL FT APGNGSLVNAVKLATDVEPRVAGKPESYLFARAADRLDSKRPLVIGDRLDTDILGGFRA FT GFSTALVLTGVDTPRTALGAPVEQRPNYLINSMADLYRPYPTIKVLGYGVQVGDAVAKV FT DKGAIEVSGSEQDLNAWRAACHAWWLAHPRQSGHEEPEIRFTERGLDTLRKIRG" FT CDS 1294541..1294714 FT /transl_table=11 FT /locus_tag="AARI_11590" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUR8" FT /protein_id="CBT75371.1" FT /translation="MERQNHVPAPGPRGLGDEAVEQALSSLADHDITEHAGIYEQLLSG FT LQQELNRTEHGA" FT CDS 1294711..1295499 FT /transl_table=11 FT /locus_tag="AARI_11600" FT /product="putative haemolysin" FT /function="4.6 Miscellaneous" FT /note="identified by similarity to protein SP:Q50760 FT (Mycobacterium tuberculosis)" FT /db_xref="GOA:E1VUR9" FT /db_xref="InterPro:IPR002877" FT /db_xref="InterPro:IPR002942" FT /db_xref="InterPro:IPR004538" FT /db_xref="UniProtKB/TrEMBL:E1VUR9" FT /protein_id="CBT75372.1" FT /translation="MNRLDQELVVRDLARSRTEAAKLVEAERVLLNGQVAAKASKKIAE FT GDDLALIPSEGEEYVSRAGHKLAGALDVFTTINPEGLRCLDAGASTGGFTDVLLRRGAK FT SVVAADVGHGQLVDVIRNDPRVQVHEGLNVRYLTPEDIGGVVDLVVADLSFISLRLVID FT ALAGAAKDSGSLVLMVKPQFEVGREHLNRTGVVTNPELRRSSVEAVIASANAAGLHLRG FT LARSPLPGQDGNAEFFLWLASGENPQSADVPLIEQNVDYS" FT CDS 1295518..1296600 FT /transl_table=11 FT /gene="ppnK" FT /locus_tag="AARI_11610" FT /product="NAD(+) kinase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.1.23" FT /note="catalyses the phosphorylation of NAD to NADP FT utilising ATP and other nucleoside triphosphates as well as FT inorganic polyphosphate as a source of phosphorus" FT /db_xref="GOA:E1VUS0" FT /db_xref="InterPro:IPR002504" FT /db_xref="InterPro:IPR016064" FT /db_xref="InterPro:IPR017437" FT /db_xref="InterPro:IPR017438" FT /db_xref="UniProtKB/TrEMBL:E1VUS0" FT /protein_id="CBT75373.1" FT /translation="MVDRHGHFALREAERGTTALRRILIFTHTGRQEAITAALETCALL FT NSAGAIPVMRRKDQAAMAEAIGAAVPSVQVLGEDCQIEDVDLGVVLGGDGSVLRAAELV FT RASPMPLVGVNLGHVGFLAEAERSELASTVQALVNETYTVEERMTIEVKVWLDNVCLAE FT TWALNEAAVEKANRERMVEVVIEVDGRPISTFGCDGVVMATPTGSTAYSFSAGGPVVWP FT DVAALIMVPISAHALFAKPLVISPDSIMAVEMLTRTDAGAVLWCDGRRTIELPPGARVE FT VTRSDRPVYMARLHTTPFSERLVNKFELPITGWRGPAKEESRRPATTALPVIGPGLQSV FT DPHYRDEPGLPMVGKPESQG" FT CDS 1296718..1298472 FT /transl_table=11 FT /gene="recN" FT /locus_tag="AARI_11620" FT /product="DNA repair protein RecN" FT /function="3.3 DNA recombination, and repair" FT /note="RecN is thought to be involved in recombinational FT repair of damaged DNA" FT /db_xref="GOA:E1VUS1" FT /db_xref="InterPro:IPR003395" FT /db_xref="InterPro:IPR004604" FT /db_xref="UniProtKB/TrEMBL:E1VUS1" FT /protein_id="CBT75374.1" FT /translation="MIQEIQISNLGVITEATLPLGPGLTVVTGETGAGKTMVITALSLL FT LGRRADAGAVRNGAKHALAEAVVHLPPDHHVLDAAGQAGAFIEPAGENSELLLSRSLSA FT QGRSRATIGGRSAPVGLLAELGHDLVAVHGQSDQIRLKEPVAQRDALDRFAGSSLSRTL FT SNYQRAYRQWRSAAKELASLKTESRNRVREAENLRLALDEIDSLDPQPGEDESLREQSM FT KLGNVESLRTASQQAQAVIDSEDFENPGVTTLVETARGVLAQASDDDAGLAAFAERAAE FT LGILASELSSDLAAYVADLDEEGPERLAQIEARRADLSKLMRKYAPSIDEVLAWASESR FT IRLEQLGGDDSRIEALEVEVVDLEHKVASLASDLSDARRKAAKKLSTQVSAELKALAMP FT DAKLVIEVNELDEPGAFGQDAISMLLAPHAGASPRPLGKGASGGELSRVMLAIEVVLAA FT VDPVPTFVFDEVDQGVGGKAAVAIGERLAMLAKHVQVIVVTHLPQVAAYADRHIRVIKN FT SDAKSKAGAGYTASDVISLDQEARVKELARMLAGQEESDTAQAHAEELLEEAQNLVSSL FT TSKKPVKA" FT CDS 1298580..1300259 FT /transl_table=11 FT /gene="pyrG" FT /locus_tag="AARI_11630" FT /product="CTP synthase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="6.3.4.2" FT /note="catalyzes the ATP-dependent formation of CTP from FT UTP and glutamine" FT /db_xref="GOA:E1VUS2" FT /db_xref="InterPro:IPR004468" FT /db_xref="InterPro:IPR017456" FT /db_xref="InterPro:IPR017926" FT /db_xref="UniProtKB/TrEMBL:E1VUS2" FT /protein_id="CBT75375.1" FT /translation="MVQRNSTRDSRSSETTKHIFVTGGVASSLGKGLTASSLGHLLRAR FT GLSVTMQKLDPYLNVDPGTMNPFQHGEVFVTDDGAETDLDIGHYERFLDENLPGTANVT FT TGQVYSTVLERERRGEYLGDTVQVIPHITDEIKRRMRLAAIEPGAGKSAPDVIITEIGG FT TVGDIESQPFLEAARQVRQDIGRKNAFFVHVSLVPFIGPSHELKTKPTQHSVAALRSIG FT IQPDSLVIRSDRPIPAEMRAKLGRTCDVDTEAVINCADAPSIYDIPKVIHSQGLDAYIV FT QTLEMKFRDVDWTSWDRLLDVVHNPATELTVALVGKYIDLPDAYLSVTEALRAGGFANN FT AKVNIRWVPADDCATEAGAAKALEGAEAICVPGGFGIRGLEGKLGALRFARENQLPTLG FT LCLGLQSMVIEYARNMAGLTDASSTEFDPETSTPVIATMEEQLAIVDGKGDLGGTMRLG FT LYDAKLLEGSVLAETYGKTDVAERHRHRYEVNNSYRAQLEEAGLVFSGTSPDGNLVEFV FT ELPKDVHPYYVSTQAHPELSSRPTRPHPLFAGLVEAALKLRK" FT CDS 1300374..1301018 FT /transl_table=11 FT /locus_tag="AARI_11640" FT /product="NUDIX domain-containing protein" FT /function="4.6 Miscellaneous" FT /note="identified by match to PF00293. Members of the Nudix FT hydrolase superfamily catalyze the hydrolysis of nucleoside FT diphosphates linked to other moieties. Substrates of nudix FT hydrolases include intact and oxidatively damaged FT nucleoside triphosphates, dinucleoside polyphosphates, FT nucleotide-sugars and dinucleotide enzymes. These FT substrates are metabolites or cell signaling molecules that FT require regulation during different stages of the cell FT cycle or during periods of stress. In general, the role of FT the nudix hydrolase is to sanitize the nucleotide pools and FT to maintain cell viability, thereby serving as surveillance FT and house- cleaning enzymes" FT /db_xref="GOA:E1VUS3" FT /db_xref="InterPro:IPR000086" FT /db_xref="InterPro:IPR015797" FT /db_xref="UniProtKB/TrEMBL:E1VUS3" FT /protein_id="CBT75376.1" FT /translation="MPLHPIADEFSPRELLNRETVYKGRIWDVLHDSVKLSDDGATIDR FT DYISHPGAVSVLVLDDQERVLMINQYRHPVGMRLWEIPAGLLDVAGEPPLEAAKRELWE FT EADRTADHWAILTDVFLSPGSSAEAVRVYLARDAKLVADDQRHERTDEEAEMISTWVPL FT EEAVAAVLAGKIHNPTAMIAILAAQAARANQHLGLRDANEPFDVHPYLREG" FT CDS 1301015..1301938 FT /transl_table=11 FT /gene="xerD" FT /locus_tag="AARI_11650" FT /product="tyrosine recombinase subunit XerD" FT /function="3.3 DNA recombination, and repair" FT /note="site-specific tyrosine recombinase, which acts by FT catalyzing the cutting and rejoining of the recombining DNA FT molecules. The XerC-XerD complex is essential to convert FT dimers of the bacterial chromosome into monomers to permit FT their segregation at cell division. It also contributes to FT the segregational stability of plasmids" FT /db_xref="GOA:E1VUS4" FT /db_xref="InterPro:IPR002104" FT /db_xref="InterPro:IPR004107" FT /db_xref="InterPro:IPR010998" FT /db_xref="InterPro:IPR011010" FT /db_xref="InterPro:IPR011932" FT /db_xref="InterPro:IPR013762" FT /db_xref="InterPro:IPR023009" FT /db_xref="InterPro:IPR023109" FT /db_xref="UniProtKB/TrEMBL:E1VUS4" FT /protein_id="CBT75377.1" FT /translation="MSDQFETPLKRYLQHLAIERGLAENTLASYRRDLLRYVDTMQAAG FT VEQPQKITELAISGYLQDLSRGNEKHKALSARSVARHSVAIRQLHKYWELEGICVPNPA FT REIQPPAIGQSLPKAISIDQVTSILESVSIETPAGLRDRAILEFLYSTGARISEVVDLD FT VDDLHFAQDAVVRLFGKGSKERVVPVGGYAQRAVSDYLVRARPSLAAKGKGTPALFLNQ FT RGGRLSRQSVWLLLSKAAERAGITTEVSPHTLRHSFATHLLEGGADVRVVQELLGHASV FT TTTQIYTKVTVDSLREAYQLAHPRVN" FT CDS 1301941..1302441 FT /transl_table=11 FT /locus_tag="AARI_11660" FT /product="NUDIX domain-containing protein" FT /function="4.6 Miscellaneous" FT /note="identified by match to PF00293. Members of the Nudix FT hydrolase superfamily catalyze the hydrolysis of nucleoside FT diphosphates linked to other moieties. Substrates of nudix FT hydrolases include intact and oxidatively damaged FT nucleoside triphosphates, dinucleoside polyphosphates, FT nucleotide-sugars and dinucleotide enzymes. These FT substrates are metabolites or cell signaling molecules that FT require regulation during different stages of the cell FT cycle or during periods of stress. In general, the role of FT the nudix hydrolase is to sanitize the nucleotide pools and FT to maintain cell viability, thereby serving as surveillance FT and house- cleaning enzymes" FT /db_xref="GOA:E1VUS5" 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:E1VUS5" FT /protein_id="CBT75378.1" FT /translation="MASNLHGAKQIALVALVQHREGDVQILLGRKRRGFGQGNIVLPGG FT KIEPGETAKQAAIREFAEETGLRVAAEDLELAAQINFRFPAQPAADMQCTAFIARKATG FT QLELTEELEPLWADPAALPVTQMWQDSPLWLPQLAAGENFTVEIVLADDNQSVQQISFE FT YWQ" FT CDS complement(1302456..1302668) FT /transl_table=11 FT /locus_tag="AARI_11670" FT /product="helix-turn-helix domain-containing protein" FT /function="3.5.2 Transcription regulation" FT /note="match to PF01381: helix-turn-helix. This is large FT family of DNA binding helix-turn helix proteins that FT include a bacterial plasmid copy control protein, bacterial FT methylases, various bacteriophage transcription control FT proteins and a vegetative specific protein from FT Dictyostelium discoideum (Slime mould)" FT /db_xref="GOA:E1VUS6" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VUS6" FT /protein_id="CBT75379.1" FT /translation="MGIRVDIDVMLARRKMAVGELAERIGITPANLAVLKNGRAKAVRF FT STLEALCRELDCQPGDLLIFEPDQD" FT CDS complement(1302668..1303171) FT /transl_table=11 FT /locus_tag="AARI_11680" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.981) with cleavage site probability 0.558 FT between position 27 and 28. 3 transmembrane helices FT predicted by TMHMM2.0 after the signal peptide" FT /db_xref="InterPro:IPR021396" FT /db_xref="UniProtKB/TrEMBL:E1VUS7" FT /protein_id="CBT75380.1" FT /translation="MVMGKSSTILLRVVLALVFIGALAIQGQAAWWLYLASSADTADVS FT YVHRSTVLYVVLALLVIQVCCICVWKLAARVQHGTVFSPASYKFVNIIIAAISFGSIMT FT FALGAIMAPGPEVAPGVVLLAGGLGVVLAGISLIVWVLRQLLAQASHTEAQAADLRTEL FT NGVI" FT CDS complement(1303300..1304439) FT /transl_table=11 FT /gene="prpC" FT /locus_tag="AARI_11690" FT /product="2-methylcitrate synthase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="2.3.3.5" FT /note="2-methylcitrate synthase catalyses the conversion of FT oxaloacetate and propanoyl-CoA into (2R,3S)-2- FT hydroxybutane-1,2,3-tricarboxylate and coenzyme A. The FT enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and FT pentanoyl-CoA. Involved in the metabolism of propionate" FT /db_xref="GOA:E1VUS8" FT /db_xref="InterPro:IPR002020" FT /db_xref="InterPro:IPR011278" FT /db_xref="InterPro:IPR016141" FT /db_xref="InterPro:IPR016142" FT /db_xref="InterPro:IPR019810" FT /db_xref="InterPro:IPR024176" FT /db_xref="UniProtKB/TrEMBL:E1VUS8" FT /protein_id="CBT75381.1" FT /translation="MTATEEIKKGLAGVVVDYTAVSKVNPETNSLLYRGYPVQDLAANK FT SFEEVALLLWNGELPTPSELTEFSAFERANRALDPRVKAAIDLLPTDCHPMDVGRTAVS FT VIGANHPQAENSSPEAELLKAKELFAAFPAVVAYDQRRRRGQEPVAPREDLDYSANFLW FT MTFGEEAAPEVVDAFRVSMVLYAEHSFNASTFTARVITSTLSDLHSAVTGAIGALKGPL FT HGGANEAVMHTFNEIGIDKEESREDAAKRAKSWMEDALAAKKKVMGFGHRVYKHGDSRV FT PTMKAALDRMIEHYGRHEMLGLYDGLEAAMDEAKAIKPNLDYPAGPTYHLMGFDTEMFT FT PIFIAARITGWTSHIFEQRAANALIRPLSAYNGVEQRSL" FT CDS complement(1304534..1305463) FT /transl_table=11 FT /gene="prpB" FT /locus_tag="AARI_11700" FT /product="methylisocitrate lyase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="4.1.3.30" FT /note="catalyses the formation of pyruvate and succinate FT from (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate. Involved FT in the metabolism of propionate" FT /db_xref="GOA:E1VUS9" FT /db_xref="InterPro:IPR000918" FT /db_xref="InterPro:IPR012695" FT /db_xref="InterPro:IPR015813" FT /db_xref="InterPro:IPR018523" FT /db_xref="UniProtKB/TrEMBL:E1VUS9" FT /protein_id="CBT75382.1" FT /translation="MLYSTKTPAAKRLALRKMLTPGAARQFPGAFNPLSAKLIGEKEFD FT GIYISGAVLANDLGLPDIGLTSLTEVATRAGQIARMSDLPAIVDADTGFGEPMNVARTI FT QELEYAGLAGCHIEDQFNPKRCGHLDGKNVVDTETMLKRIAAAADARIDENFLIMARTD FT IRAVEGLDAAIDRAKAMVDAGADAIFPEAMKNVAEFEAVCNAVDVPVLANMTEFGKSEL FT FNRQELADAGVALIIYPVTLLRSAMGAAERVLDAISEDGTQAREVDNMLTRSRLYELVD FT YEAYNRFDTGIFNFQVPTLDIDSNSANL" FT CDS complement(1305465..1306982) FT /transl_table=11 FT /gene="prpD" FT /locus_tag="AARI_11710" FT /product="2-methylcitrate dehydratase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="4.2.1.79" FT /note="involved in the metabolism of propionate" FT /db_xref="GOA:E1VUT0" FT /db_xref="InterPro:IPR005656" FT /db_xref="UniProtKB/TrEMBL:E1VUT0" FT /protein_id="CBT75383.1" FT /translation="MINHPVRVYRSEENLAREDQLAHKIATVAADPVEITAEVTDMIIN FT RIIDNASVAIASLNRGPIVAARAQALTHAPSTGGKGASVFGISEKVSPEWAAWANGVAV FT RELDYHDTFLAAEYSHPGDNIPPILAVAQHTGASGKDLIRGIATGYEIQVDLVKAICLH FT KHKIDHVAHLGPSAAAGIGTLLGLDVETIFQAVGQGLHTTTATRQSRKGEISTWKAHAP FT AFAGKMAVEAADRAMRGQTSPVPIYEGEDGVIAWMLDGKDAAYEVPLPEAGEAKRAILD FT TYTKEHSAEYQAQAWIDLARKLHGEHPEAADPKNVKSVLIKTSHHTHYVIGSGANDPQK FT YDPTASRETLDHSIPYIFTVALQDGAWHHVDSYAPERAGRADTVELWNKVTTEEDAQWT FT RRYHSLDIAEKAFGGSVQITLNDGTVITDEIAVADAHPLGARPFAREQYINKFRTLATG FT LVDDAEIDRFIAAAENLENLAAGELDQLNIQAAAGVIDAAAAPKGLF" FT CDS complement(1306979..1307632) FT /transl_table=11 FT /locus_tag="AARI_11720" FT /product="GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF00392. This FT family of regulatory proteins consists of the N-terminal FT HTH region of GntR-like bacterial transcription factors. At FT the C-terminus there is usually an effector- FT binding/oligomerisation domain. The GntR-like proteins can FT be divided into six sub-families: MocR, YtrR, FadR, AraR, FT HutC and PlmA. Many of these proteins have been shown FT experimentally to be autoregulatory, enabling the FT prediction of operator sites and the discovery of cis/trans FT relationships" FT /db_xref="GOA:E1VUT1" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VUT1" FT /protein_id="CBT75384.1" FT /translation="MKASDKVYESLRADIVEWRLAPGTVLAEVEQSERLGVSRTPVREA FT LGRLVADGLAVQQRGRGAIVSEVSEDHVEDLFVLRRALECASAREAAKSAQRSAFNQLA FT SRFEAAVAEVEIPGSQESYYQLVQLLDESIDKAADNKYLSNALRTLRVNLQRVRRMAKD FT NPERLKASASEHAAIARAIASGNPEVAAAATTVHLHQSFTHIMAHAAGSERQSP" FT CDS 1307820..1309736 FT /transl_table=11 FT /gene="prpE" FT /locus_tag="AARI_11730" FT /product="propionate--CoA ligase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="6.2.1.17" FT /note="catalyzes the synthesis of propionyl-CoA from FT propionate and CoA" FT /db_xref="GOA:E1VUT2" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR020845" FT /db_xref="InterPro:IPR024597" FT /db_xref="UniProtKB/TrEMBL:E1VUT2" FT /protein_id="CBT75385.1" FT /translation="MVQEYRQAFDQATNDPAAFWLQAARGISWDTEPQIALDDQRKPLY FT DWFPDGKLNLSVNALDRHVDAGRGGNTALIYDSAMLGTVTKYTYSELLREVEIFAGVLA FT GRGVKTGDRVLIYLPMIPQAAIAMLACARLGAIHSVVFGGFAPKELAARITDCAPVAIV FT TASGGIEPSRHIEYLPAVAEALSLAEPAVKDVIVAHRDGFAHSLQEYQDKEINGQQINW FT LDWEEQTKTATPTGPVPVDSTHPLYVLYTSGTTGSPKGVVRDTGGYATALQYSMNAVYD FT VHPGDTMFTASDVGWVVGHSYIVYAPLIAGATTVLYEGKPIGTPDAGVFGRIIADHKVT FT TMFTAPTALRAVRKADPEGALIASHDLSSLRALFVAGERLDPDTYHFASKLLGIPVVDN FT WWQTETGWPIASNPLGLEELPAKAGSPTTPVPGFDVQIRDALGEQLEANQEGNIVVKLP FT LPPGALTTLWGNDQRFIDTYLSQIEGCYLTGDSGFLDDDGYLFVMGRTDDVINVSGHRL FT STGAMEQVLASHPAVAECAVIGLADALKGQRASGYVVLKSGVETDEAELKKEIVALVRQ FT HIGAVADFREVTVVAALPKTRSGKILRKTMRQIADGKDYTVPSTIEDTAVLDELLPLLR FT PQA" FT CDS complement(1309762..1310511) FT /transl_table=11 FT /locus_tag="AARI_11740" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VUT3" FT /db_xref="InterPro:IPR001789" FT /db_xref="InterPro:IPR011006" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR013196" FT /db_xref="InterPro:IPR024187" FT /db_xref="UniProtKB/TrEMBL:E1VUT3" FT /protein_id="CBT75386.1" FT /translation="MRESHVSIPQPGSGSPVFKVLVVDDEPETAAAHAKYVNRVPGFST FT GAIAANGQQALGLLASAREAKQPFDLVLLDMTLPDLHGIDVAKRMRGRGLTTDIIAITA FT VRDLAVVRSAVATGITQYLIKPFAFAAFTEKLENHRRFISEISSTGPDTSQRALDNAFS FT ALRTTSASAPLPKGLIPETLAQITAHLRSKPDLCLSATELGEDLGISRVTARRYLEHLA FT DVKSVLKQPRHGTRGRPEYEYRAASYR" FT CDS complement(1310527..1312164) FT /transl_table=11 FT /locus_tag="AARI_11750" FT /product="signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VUT4" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR004358" FT /db_xref="InterPro:IPR005467" FT /db_xref="InterPro:IPR016121" FT /db_xref="UniProtKB/TrEMBL:E1VUT4" FT /protein_id="CBT75387.1" FT /translation="MTDHFTDQTRPPSARAAALAPLNSDGWSLAVATYKHQAQVILDDK FT QATVATISITLANGPFVSEALAGTQPTEELQPYTDKILDRGQGIDFITIMTPDERRVTH FT PNPQQLGKKYSGSTKQALAGQTYNEVALGTLGLSVRTIAPVFHEGTLVGMVATGITLES FT LESIYRSELPQILTVSALALLLAGFSSWSFSRYVNQATLGFGPHGLRRLYAFYFSALHS FT VREGLVLLDRQHHIVLYNQEAARLLGFPEQVPPNGLDLDQVQIPETLRTLMATGRSCKD FT EIHLGTHTVLSISQGPARLTNARLPRRGSLPIRWFRAQPLSGQVMTLRDLTEVQELTGE FT VQSLKTFSTALRAQTHEHANRLHTIATLIENGQSEKALAFAVDDRQHSQKLTDAIVHSI FT DDVYLSSLLVAKAAQAHERGIKLDINAQGIIPNNAYAATDIVTVVGNLLDNALDASVGT FT QEATVWVEVTAADDELIIAVADSGPGIEPEFFDQLMRFGVSTKDGSGHRGLGLALVQQA FT VLRLGGTMNVDNDAGAIFTVTLPLKNNN" FT CDS 1312340..1313638 FT /transl_table=11 FT /gene="dctA" FT /locus_tag="AARI_11760" FT /product="C4-dicarboxylate transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="identified by similarity to protein SP:Q8NMH8 FT (Corynebacterium glutamicum). Dicarboxylate/Amino FT Acid:Cation (Na+ or H+) symporter (DAACS) family, C4- FT dicarboxylate transporter (substrates: fumarate, D- and L- FT malate, succinate, succinamide, orotate, iticonate, FT mesaconate) (TC 2.A.23.1.3)" FT /db_xref="GOA:E1VUT5" FT /db_xref="InterPro:IPR001991" FT /db_xref="UniProtKB/TrEMBL:E1VUT5" FT /protein_id="CBT75388.1" FT /translation="MAVTEELTPSGNAPQGASKKKDKTHWLYIMVIVAVVLGAGIGLVA FT PEVGKSLKPLGAAFVALIKMIIAPVIFCTIVLGIGSIAKAATVGKVGGLAMLYFLVMST FT LALGIGLLVGNIIHPGEGLELKPYEAGGSGDSNATVDFLMSLIPGDIPVLPTLVLAMFV FT GFALQGMGKAGEPVLIGIQNIQKVVFRIMMMIMWAAPIGAFGAIAAVVGATGWAAIGSM FT AVLMGAFYLTCILFIVIILGSMLRVVTGLNIFALMKYLAREYLLIFSTSSSESALPRLI FT AKMEHAGVSKPVVGITVPTGYSFNLDGTAIYLTMSALFVSTAMGMPMNLGQQIGLLVFM FT IIASKGAAGVTGAGLATLAAGLQAHRPELLGGMGVIVGIDKFMSEARALTNFTGNAVAT FT LLIGKWTKEIDMDQAKAVLAGQIPFDENSVEGH" FT CDS 1313767..1314390 FT /transl_table=11 FT /locus_tag="AARI_11770" FT /product="GDSL-like lipase/esterase" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.1.-" FT /note="identified by match to protein family PF00657" FT /db_xref="GOA:E1VUT6" FT /db_xref="InterPro:IPR001087" FT /db_xref="InterPro:IPR013830" FT /db_xref="InterPro:IPR013831" FT /db_xref="UniProtKB/TrEMBL:E1VUT6" FT /protein_id="CBT75389.1" FT /translation="MGVAVRVCFVGDSFVAGVGDGSHRGWAGRLIARGIERGYELTGYN FT LGVRGDTSTMIRQRFEAECAARFPPGEHAVGIVFSFGVNDVIRWSSKPRVAVGERIANL FT SAILDQARVRRWPVLMIGPPPIADDALNEQLRELDAQMQDRCELADVPYLSVHEQLAGN FT EVWRSEVAADDGAHPRAAGYDVLAGLAEGAWDNWLRELAARLER" FT gene 1314387..1314764 FT /pseudo FT /locus_tag="AARI_11780" FT /product="truncated cytidine deaminase" FT /note="N-terminal section of a cytidine deaminase (EC 3.5. FT 4.5), which catalyzes the hydrolysis of cytidine into FT uridine and ammonia" FT CDS complement(1314847..1315197) FT /transl_table=11 FT /locus_tag="AARI_11790" FT /product="putative glyoxalase family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00903: glyoxalase/bleomycin FT resistance protein/dioxygenase superfamily" FT /db_xref="UniProtKB/TrEMBL:E1VUT7" FT /protein_id="CBT75390.1" FT /translation="MFTGMLGNATVSDLARAEHWYAQLIGRGPDRRPMPGLLEWQLGPG FT FGLQVYCEPERAGHSTVVLEVADLDAHAARLAEAGIEHPGIQPGGDGDILQLQDPDGNW FT IVLASAKAGPES" FT gene complement(1315296..1315736) FT /pseudo FT /locus_tag="AARI_11800" FT /product="truncated protein" FT /note="C-terminal section of a conserved protein" FT gene complement(1315733..1315888) FT /pseudo FT /locus_tag="AARI_11810" FT /product="truncated protein" FT /note="N-terminal section of a conserved protein" FT CDS complement(1315923..1316321) FT /transl_table=11 FT /locus_tag="AARI_11820" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUT8" FT /protein_id="CBT75391.1" FT /translation="MIREDPMRTLEKFLSLAEAEPNSEQVSVYVLLKAQLENGQCILVL FT DDRGWSTSENWSRAEPAAIRETTLTVVGPGEPAPGASRAQAFRDYWKCIRSLLAAQGIH FT LSIEKLMALEHEVRFGPRLQRLLTGPGH" FT CDS 1316490..1317386 FT /transl_table=11 FT /locus_tag="AARI_11830" FT /product="ParA-family protein" FT /function="3.1 DNA replication" FT /note="identified by match to protein family PF01656. FT Putative chromosome partitioning protein" FT /db_xref="InterPro:IPR002586" FT /db_xref="UniProtKB/TrEMBL:E1VUT9" FT /protein_id="CBT75392.1" FT /translation="MSEEQGNKHRGAGMLKEPRPVGPTGKPLTDFPVPAPLPSHGPARV FT IAMVNQKGGVGKTTSTINLAAALAEYGRKVLLVDFDPQGALSAGFGTNPHEMDITVYNV FT LMDRKVKITDAIVKTDVENIDLLPANIDLSAAEVQLVNEVAREQVLERALRNVIDDYDV FT VLIDCQPSLGLLTINALTAAHGVIIPLTAEFFALRAVALLMETIDKVKDRLNQVLELDG FT VVATMYDARTLHSREVITRLDEAFGDKLFETVIKRTIKFADANVAAEPITSYAANHPGA FT EAYRNLARELIWRGGAP" FT CDS 1317386..1318288 FT /transl_table=11 FT /gene="scpA" FT /locus_tag="AARI_11840" FT /product="putative chromosome segregation and condensation FT protein A" FT /function="3.1 DNA replication" FT /note="identified by match to protein family PF02616. ScpA FT participates in chromosomal partition during cell division. FT Component of a cohesin-like complex composed of scpA, scpB FT and smc" FT /db_xref="InterPro:IPR003768" FT /db_xref="UniProtKB/TrEMBL:E1VUU0" FT /protein_id="CBT75393.1" FT /translation="MSTTLSEETATDSTTPAEAEQESAGGFRLALQNFNGPFDVLLHLI FT TKRELDITDVALAEVTDEFIAYLRELQASSAADGSDGMKVLDETTEFLVVASTLLDLKA FT ARLLPRGEMADEEDFELLEARDLLFARLLQYKAFKQAAEFLGERYMSEGARHPREVSLE FT PQFAALLPELVFNIGPDALAAMAAKALAPKPEPATEVGIGHLHGANVTIAEEAETITAM FT LESRGTLAFTQLVADADGQLVVVVRFLALLEMFRQKAISFAQEDPLGPLLISLIQESSF FT DAQAVQDDYEGSSGEVNHE" FT CDS 1318281..1318871 FT /transl_table=11 FT /gene="scpB" FT /locus_tag="AARI_11850" FT /product="putative chromosome segregation and condensation FT protein B" FT /function="3.1 DNA replication" FT /note="identified by match to protein family PIRSF019345. FT ScpB participates in chromosomal partition during cell FT division. Component of a cohesin-like complex composed of FT scpA, scpB and smc" FT /db_xref="GOA:E1VUU1" FT /db_xref="InterPro:IPR005234" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VUU1" FT /protein_id="CBT75394.1" FT /translation="MSEFAPIDQLPGGLESGLEAVLMVADIPVSSARLAEIFEVPTARI FT ATALENLATEYDGKDRPRGFELRRVASGWRFYSRADYADFVSSYVLDGQTARLSQAALE FT TLAVIAYRQPVSRGRISAIRGVNVDSVVRTLLTRGLITEYPEVGDGGATLYQTTEYFLE FT RLGLGSLDELPALSPYLPGVADLESLDSATYDD" FT CDS 1318973..1320094 FT /transl_table=11 FT /locus_tag="AARI_11860" FT /product="pseudouridylate synthase" FT /function="3.6 RNA modification" FT /EC_number="4.2.1.70" FT /note="identified by match to protein family PF00849. FT Pseudouridylate synthases catalyze the isomerization of FT specific uridines in an RNA molecule to pseudouridines (5- FT ribosyluracil, psi)" FT /db_xref="GOA:E1VUU2" 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:E1VUU2" FT /protein_id="CBT75395.1" FT /translation="MSRGSSSGRNDRGNNSNFGGKPAGGRNNTGGKSGGKSYGKPGGAG FT RPGGKSYGEKSYGEKPYGKSASGKPGEKSNSAKRNTSAPRKNSERAFGKERFGNSVPTN FT YARPTQRARAQARAENQAHREQHGEQQDGIRLQKAMANAGVASRRVCEEMILEGRVEVN FT GNLVVELGSRVDPAKDRIHVDGMRIQMNQANRYFVFNKPKHVMCTMDDPEGRRTIADYF FT KNEHHSLRLFHVGRLDYKTEGVLILTNDGELANRLQHPKYEVPKTYLVQIPGPLPRAVS FT NQLREGVKLEDGWIKVDDLKIIATTPKHVMVEVTLHSGRNRIVRRMFDEVGHPVQRLVR FT VAVGPVQLGDQKQGTIRSLGNQEVGHLMAMVGM" FT CDS 1320098..1321198 FT /transl_table=11 FT /gene="tyrA" FT /locus_tag="AARI_11870" FT /product="prephenate dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.3.1.12" FT /note="catalyses the following reaction: prephenate + FT NAD(+) <=> 4-hydroxyphenylpyruvate + CO(2) + NADH. Involved FT in tyrosine biosynthesis" FT /db_xref="GOA:E1VUU3" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR003099" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VUU3" FT /protein_id="CBT75396.1" FT /translation="MLSSHLAGPVLVIGTGLLGTSVGLGLRAKGVHVYLSDISPTAAGV FT AQDIGAGTLLEHQQIAPELVVIGAPPDVTAALVGDALLAYPNATVVDIASVKGSILAGV FT LADERLGQSDTSRYVGTHPMAGREKSGPAAARGELFTSMPWVICAHEGAEASRVKAAES FT LAIDLGATMHRMSVTEHDESVALISHFPQAASSMIASRLLNAEGHQLALAGNGLRDTTR FT IAASDEKLWIQIFSHNAAALVPILTGMKDDLDRLINTLQNPQGPGALLDLSQLMTEGNA FT GKARIPGKHGAPPQAFALVTVLIDDRPGQIAQLLTEIGDAQINIEDLRMEHSAGHQVGM FT VDVSVVPGRRDELIDVLTKNGWKVAQ" FT CDS 1321195..1321875 FT /transl_table=11 FT /gene="cmk" FT /locus_tag="AARI_11880" FT /product="cytidylate kinase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="2.7.4.14" FT /note="catalyzes the transfer of a phosphate group from ATP FT to either CMP or UMP to form CDP or UDP and ADP" FT /db_xref="GOA:E1VUU4" FT /db_xref="InterPro:IPR003136" FT /db_xref="InterPro:IPR011994" FT /db_xref="UniProtKB/TrEMBL:E1VUU4" FT /protein_id="CBT75397.1" FT /translation="MSTLNNDKLVIAIDGPSGSGKSSVSKAVARKLGAAYLDTGAMYRA FT ITYSVLADGTDLSDANAIAQAVRDAKLSISLDPDAELVQIGGEDVTAAIREPRISEQVS FT TVATNLDARAELVRRQQQIIAENTRIVAEGRDITTVVAPDADARILLTASEEARLRRRG FT LQLGGTQNESQLATQVLARDAKDSTVVNFTQAADGVMTVDSSDLDFEQTIDAVLDAIST FT ATKN" FT CDS 1321941..1323473 FT /transl_table=11 FT /gene="engA" FT /locus_tag="AARI_11890" FT /product="GTP-binding protein EngA" FT /function="3.7 Protein synthesis" FT /note="possible role in ribosome assembly and stability" FT /db_xref="GOA:E1VUU5" FT /db_xref="InterPro:IPR005225" FT /db_xref="InterPro:IPR006073" FT /db_xref="InterPro:IPR015946" FT /db_xref="InterPro:IPR016484" FT /db_xref="UniProtKB/TrEMBL:E1VUU5" FT /protein_id="CBT75398.1" FT /translation="MSENNSTHDEEYIPVGDDDIAERLAELSEEEAAVRAQALLSGLED FT YELDEEDSALLAGLDSFDDDDEDVVIPPVLAVIGRPNVGKSTLVNRILGRREAVVEDTP FT GVTRDRVSYSAEWMGRPFTIVDTGGWEHDAKGIHASVADQAEIAADVADAILFVVDSHV FT GATATDEAVVKMLRKKGKPVFLVANKVDDFNQEAEAAVLWGLGFGQPWPVSALHGRGTA FT DLLDAVMEKLPAHSAFGGMIPSGGPRRVALIGRPNVGKSSLLNKVAGSERVVVDEYAGT FT TRDPVDELVELGGEIWRFVDTAGIRRRQHMAVGSDYYASLRTQTALEKAEVAVILLAAN FT EIISEQDVRIIQLAIEAGRAMVIVYNKWDEVDEDRRYYLDQEIERDLAHIEWAPRVNIS FT AKTGWHKDKLVPALNTALDSWDKRIPTGKLNAFLGELVAAHPHPVRGGKQPRILFGTQA FT SARPPRFVLFTTGFLDPGYRRFITRRLRETFGFDGSPIEVSMRIRERRGRNR" FT tRNA 1323575..1323651 FT /locus_tag="AARI_36720" FT /product="transfer RNA-Pro" FT /anticodon=(pos:1323609..1323611,aa:Pro) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 1323749..1324591 FT /transl_table=11 FT /locus_tag="AARI_11900" FT /product="PhzC/PhzF phenazine biosynthesis family protein" FT /function="4.6 Miscellaneous" FT /note="identified by match to protein family PF02567. FT PhzC/PhzF is involved in dimerisation of two 2, FT 3-dihydro-3- oxo-anthranilic acid molecules to create FT phenazine-1- carboxylic acid (PCA) by P. fluorescens. This FT family also contains a putative thymidilate synthase from FT Mycobacterium tuberculosis. Many phenazine compounds are FT found in nature and are produced by bacteria such as FT Pseudomonas spp., Streptomyces spp., and Pantoea FT agglomerans. These compounds have been implicated in the FT virulence and competitive fitness of producing organisms. FT For example, the phenazine pyocyanin produced by FT Pseudomonas aeruginosa contributes to its ability to FT colonise the lungs of cystic fibrosis patients. Similarly, FT phenazine-1-carboxylic acid, produced by a number of FT Pseudomonas, increases survival in soil environments and FT has been shown to be essential for the biological control FT activity of certain strains" FT /db_xref="GOA:E1VUU6" FT /db_xref="InterPro:IPR003719" FT /db_xref="UniProtKB/TrEMBL:E1VUU6" FT /protein_id="CBT75399.1" FT /translation="MQRRFQQVDVFSTTAYKGNPLGVVLDGQGLDTALMQDYSLWSNLS FT EVTYVLPANDARADYRFRIFAREREFPFAGHPALGTARAWLHAGGVPRDPKQLLAECEA FT GLVPIRIEGETLSFASPPAVRTGAIAPHELEEMIQILGIDPQQIVDSQWTDNGPGWAAV FT LLENSQQVLGIEPQIPNKPGRWKIGVFGALPQSSAPEKFEVRALAVENGALREDPVTGS FT LNGAAAQWLIDAGHATAPFANRQGVKVGRDGQVKLSVADGQLWVGGTASVLIEGSIEL" FT CDS 1324801..1326507 FT /transl_table=11 FT /locus_tag="AARI_11910" FT /product="putative drug resistance ATP-binding protein" FT /function="4.2 Detoxification" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT (putative) drug resistance ATPase-2 (Drug RA2) family (TC FT 3.A.1.121.z). ABCISSE: fused ATP-binding protein (ABC2), FT ART-family, ARE-subfamily (antibiotic resistance)" FT /db_xref="GOA:E1VUU7" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VUU7" FT /protein_id="CBT75400.1" FT /translation="MTQSQNIHQAAQHESEIEPDYVCSLQNIAVSFGERDVLAGIDLSI FT SGTDSIAVLGDNGSGKSTLMRVIAGNLVPDRGQRKMNAPGAVAYAAQNPSFAADMSVQQ FT VIDSYHRRFRELEGLIRVISAKLKDAPEPVAERLMKQLQQVTDLYEAADGYSLAPRLDS FT ALEQLGLGDLDRQRLVSQLSGGQRSRLSLACVLCSGAQLILLDEPTNDLDQSAMNWLER FT TVHKHRGALVLISHDRMFLKRFARTIVEVADGAITHYGNGYDGYLHAKEQERTAIRIAY FT ENWVQELERSQNLVDKYASRVSAIPRKQEKPGFGHGNFRARDSSHGSTSKIRQAKSRIE FT DLETHRAPEPAAQLSFRLPSSDENQRRGETLLRVRKAQRGAEPKLSTASFEIKLGERWL FT VTGPNGAGKTSLLKILAGELEITDGGIERTANLRHGWLRQEVSALPGQSLIEAFALATD FT QYVQDAAASLAPLGLFAPEDFRRHPMALSVGQRRRLELAIAVSTKAQLLFLDEPTNHLS FT PALVEQLEDALLNYAGTVVVVSHDRRWQQKMREHGQVHRLGVKHGVVEVIK" FT CDS 1326750..1328639 FT /transl_table=11 FT /locus_tag="AARI_11920" FT /product="putative phenol 2-monooxygenase" FT /function="4.2 Detoxification" FT /EC_number="1.14.13.7" FT /note="phenol 2-monooxygenase catalyzes the following FT reaction: Phenol + NADPH + O(2) => catechol + NADP(+) + FT H(2)O. Also active with resorcinol and o-cresol" FT /db_xref="GOA:E1VUU8" FT /db_xref="InterPro:IPR002938" FT /db_xref="InterPro:IPR003042" FT /db_xref="InterPro:IPR012336" FT /db_xref="InterPro:IPR012941" FT /db_xref="UniProtKB/TrEMBL:E1VUU8" FT /protein_id="CBT75401.1" FT /translation="MQFHHNGYVSADPRVEPAAGAGIDRPSQMPDVMDVLIVGAGPAGI FT ITAAQLSQFPDVHTRIIDRRPGRLEIGQADGIQSRTVETFQAFGFAEQITAEAYIIKET FT TFWNPDPQNPERIIRTDRTPDDPTGVSEFPHLVVNQARVIDYFAQFAANSPARTVPDYG FT WDFKELSVEEGQEYPVKVTLVGCGEDNEGLERVVRAKYVVGADGARSNVRRSIGAKLSG FT DKANHAWGVMDTLGLTNFPDVRTKCAIHSKAGSILLIPREGGQLFRLYVDLGEVPEGDN FT GKVRETPLEEIIERAKAILNPYSLEVKDVAWHSVYEVGHRLADRFDDVPVEEIGTREPR FT VFITGDACHTHSAKAGQGMNVSMQDGFNLAWKLGYVLSGQAPDSLLRTYSDERKVIAKD FT LIDFDKKWSSIMAATPEELVGQEGVAEFYVRTAEFPAGFMTEYAASELTAGKDHQELAA FT GFPMGKRFRSSQVMRVADVNPKHLGHHHRADGRYRIYVFADQQPVGQFEQLAELSRWLL FT EDEQSPVVRFTPKGADADALFDIKVIYQQDYTTMNVNDAPKVFRPNVGQFGLMDYEKVY FT TALEDSDIFDERQVSREGAIVIVRPDMYVANILPLSARDELASFFAPIMREQA" FT CDS complement(1328879..1329241) FT /transl_table=11 FT /locus_tag="AARI_11930" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR007438" FT /db_xref="UniProtKB/TrEMBL:E1VUV0" FT /protein_id="CBT75402.1" FT /translation="MTKILLKRAYAEPSAADGYRVLVDRLWPRGQSKIKLQLDQWAKSI FT APSTDLRKGWDHDEDRFEEFATYYRKELNQNPGVDEFLEVLDQHPVVTLVFGAKNEQIN FT HAVVLRDYLLEQLTGS" FT CDS 1329509..1329961 FT /transl_table=11 FT /locus_tag="AARI_11940" FT /product="FHA domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00498. The forkhead-associated (FHA) FT domain is a phosphopeptide recognition domain found in many FT regulatory proteins" FT /db_xref="InterPro:IPR000253" FT /db_xref="InterPro:IPR008984" FT /db_xref="UniProtKB/TrEMBL:E1VUU9" FT /protein_id="CBT75403.1" FT /translation="MSEHRPVDPNNESASETTNIALPAVHKGSEPSVIYTLSEDEKNAV FT QALPAGSALLIAHSGPNKGARFLLDTDQSIAGRHPNADIFLDDVTVSRRHAKFSREGER FT FTLSDIGSLNGTYINGDRIDEIPLSTGVQVQIGKFRLNFYQSVPNL" FT CDS 1330036..1330791 FT /transl_table=11 FT /locus_tag="AARI_11950" FT /product="putative MerR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00376. Members of the FT family include the mercuric resistance operon regulatory FT protein merR; Bacillus subtilis bltR and bmrR; Bacillus FT glnR; Streptomyces coelicolor hspR; Bradyrhizobium FT japonicum nolA; Escherichia coli superoxide response FT regulator soxR; and Streptomyces lividans transcriptional FT activator tipA" FT /db_xref="GOA:E1VUV1" FT /db_xref="InterPro:IPR000551" FT /db_xref="InterPro:IPR009061" FT /db_xref="UniProtKB/TrEMBL:E1VUV1" FT /protein_id="CBT75404.1" FT /translation="MPIFDAARSPRLEASRHETVRQAALNIGEVLAELKNEFPRVTASK FT IRFLEDKGLIIPQRTSAGYRKYSASDVSRLRFILSVQRDQYLPLKVIKDHLDAVDRGEA FT PAALPGGAPVAPQAVDNDMAEAVERKARSVSLAELQGLTGCSEELASELVKFGLIEPVA FT GLFDANSIEVTKSAVELASHGVEPRHLRQFRTAADREFSLIESIVGNELKKPEVSARAR FT AAEEAQEISRQCLKIHEALVQRAISQLDR" FT CDS 1330832..1331314 FT /transl_table=11 FT /locus_tag="AARI_11960" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR003729" FT /db_xref="UniProtKB/TrEMBL:E1VUV2" FT /protein_id="CBT75405.1" FT /translation="MLELEFAGIRIQLPANQPLLLLRYPEQNLYLPLWIGAPEASAIAM FT SEQGLTPPRPMTHDLLISVLETLGVELERIEIVSVHNAVFVAELVLSNGKRVDSRSSDA FT VALAVRAQCPIMCAEDVLQEAGVSIETETEGEEAPEEQLREFREFLDNIDPEDFSS" FT CDS 1331556..1332149 FT /transl_table=11 FT /locus_tag="AARI_11970" FT /product="putative MerR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="members of the MerR-family include the mercuric FT resistance operon regulatory protein merR; Bacillus FT subtilis bltR and bmrR; Bacillus glnR; Streptomyces FT coelicolor hspR; Bradyrhizobium japonicum nolA; Escherichia FT coli superoxide response regulator soxR; and Streptomyces FT lividans transcriptional activator tipA" FT /db_xref="GOA:E1VUV3" FT /db_xref="InterPro:IPR000551" FT /db_xref="InterPro:IPR009061" FT /db_xref="UniProtKB/TrEMBL:E1VUV3" FT /protein_id="CBT75406.1" FT /translation="MESRQTGPHYGVDGGNKQSSTQGLLFTDDLPELDEHAGYRGPIVC FT KAAGITYRQLDYWARTGLVEPAVRGAKGSGSHRLYSFRDILVLKVVKRLLDTGVSLQQI FT RSAVLHLRERGVEDLAQITLMSDGASVYECTSADEVIDLVQKGQGVFGIAVGRVWREVE FT GSLAQLPSESSVQQTLPEDELAARRAAKASRNVG" FT CDS complement(1332249..1333076) FT /transl_table=11 FT /locus_tag="AARI_11980" FT /product="ParA-family protein" FT /function="3.1 DNA replication" FT /note="identified by match to protein family PF01656. FT Putative chromosome partitioning protein" FT /db_xref="InterPro:IPR002586" FT /db_xref="UniProtKB/TrEMBL:E1VUV4" FT /protein_id="CBT75407.1" FT /translation="MVWSVHVVSISSLKGGVGKTSVTLGLASAALAAGIPTLVIDLDPH FT ADASTGLGVRANGKQPIGQMLKNARRARLQDQVVASAWQSKAAEKKSRTRIPVLDVAVG FT DAYTGIYDRPDLRTRDLRRLSQLLSRTSGYQLVLIDCPPSLNGLTRMAWSASDQLVLVA FT EPSLFSVAGTERTQRALELFRREFAPSLGPVRVVANRVRKDSAEHTFRLGEMRQMFGDS FT MVKPEIPEHPEWQQIQGAAYSVHQWPSKATAPMLAQFDALLKEVLSAAGPNNT" FT CDS 1333416..1336868 FT /transl_table=11 FT /gene="pyc" FT /locus_tag="AARI_11990" FT /product="pyruvate carboxylase" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="6.4.1.1" FT /note="biotin-containing enzyme that catalyzes a two step FT carboxylation of pyruvate to oxaloacetate" FT /db_xref="GOA:E1VUV6" FT /db_xref="InterPro:IPR000089" FT /db_xref="InterPro:IPR000891" FT /db_xref="InterPro:IPR001882" FT /db_xref="InterPro:IPR003379" FT /db_xref="InterPro:IPR005479" FT /db_xref="InterPro:IPR005481" FT /db_xref="InterPro:IPR005482" FT /db_xref="InterPro:IPR005930" FT /db_xref="InterPro:IPR011053" FT /db_xref="InterPro:IPR011054" FT /db_xref="InterPro:IPR011761" FT /db_xref="InterPro:IPR011764" FT /db_xref="InterPro:IPR013785" 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:E1VUV6" FT /protein_id="CBT75408.1" FT /translation="MFEKILVANRGEIAIRAFRAGYELGAKTVAVYPHEDRNSIHRQKA FT AEAYQIGEEGHPVRAYLDIDEIVRVAKEAGADAIYPGYGFLSENPDLARAAAAEGIKFI FT GPKADVLELAGNKVAALKAAREAGIPVLESSEPSDDVDFLIAEADRIGFPIFVKAVAGG FT GGRGMRRVDKREDLPELMGAAMREAGTAFGDPTVFLEQAVLRPRHIEVQILADEQGNIV FT HLHERDCSLQRRHQKVVEIAPAPNLDESIRQALFRDAVKFAQTLGYQNAGTVEFLVDTV FT GERAGQHVFIEMNPRIQVEHTVTEEVTDIDLVQAQMRIASGESLKDLGISQDTIQVRGW FT ALQSRITTEDPANGFRPDVGTITVYRSAGGSGVRLDGGTIYTGAEVSPHFDSMLVKLTC FT RGRDYATAVARARRALAEFRVRGVATNIPFIQNVLGDPQFLAGDVATDFIDSRPDLLTG FT NESQDRGTKALNFLAHVTVNQPNGERIEGIDPRKKLPTFPGDKSDEPERSPFDGPSKAA FT VPADGWRQKLLDLGPEGFAKALRESKAVGITDTTFRDAHQSLLATRVRTRDLLAAAPAY FT AHNVPQLFSMEVWGGATYDVSLRFLGEDPWKRLELLRAELPNIPLQMLLRGRNTVGYTP FT YPTEVTDAFVKEAAAAGIDIFRIFDALNDVSQMAPAIKAVRETGTAVAEVALCYTGNLL FT DANEKLYTLDYYLNLAQQIVDAGAHIIAIKDMAGLLRPAAAKKLVTALRERFDLPVHLH FT THDTSGGQLATLMAAIEAGVDAVDVASAAMAGTTSQPSASALVAALEFTERDPDLSLDA FT VAALEPYWEAVRAMYKPFESGLPAPTGRVYQHEIPGGQLSNLRQQAIALGLGERFEAIE FT SMYASVNDMLGNVVKVTPSSKVVGDLALQLVGSGVPAADFETNPQNYDIPDSVIQFLSG FT ELGNPPGGWPEPFRTKALQGRNVKNHIEDLSAEDLAALQADSDTIRGTLNRLLFAGPTR FT DFEKSVENYGDLSVLHTRDYLYGLVPGFEHVISLGTGVRLLVKLVSVSEADEKGLRTVV FT VNLNGQSRQVKVRDESVESTVKSAPKADPKNTGHVAAPFAGAVTVNVQVGDLVEAGQSV FT ATIEAMKMEAGITANAGGVVSQVTLDGTSQVQGGDLLLVIDPK" FT CDS 1336972..1337514 FT /transl_table=11 FT /locus_tag="AARI_12000" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VUV5" FT /protein_id="CBT75409.1" FT /translation="MRASKTNPAAVPAALKEQAAQLPSKAQSISVLVFTLDTHLPFCEI FT AEHLAEQFTELELTAQVGMAGPQRVKSVLEGKFTGVDVLVVVGDTSSESEDRLMELVEW FT LLANGRRDLAENLIYAVLGHEYQNHATSAFSRVVLPRSYYARTQQSGLKLPWAASARES FT WELANAVVDYAFGLGAE" FT CDS complement(1337487..1339298) FT /transl_table=11 FT /locus_tag="AARI_12010" FT /product="putative fatty-acid--CoA ligase" FT /function="2.4 Metabolism of lipids" FT /EC_number="6.2.1.-" FT /note="activates fatty acids by binding to coenzyme A. FT Possibly involved in the degradation of lipids via beta- FT oxidation" FT /db_xref="GOA:E1VUV7" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR020845" FT /db_xref="UniProtKB/TrEMBL:E1VUV7" FT /protein_id="CBT75410.1" FT /translation="MREYSSPIRIHSPQQSNITDLLLRHANSAANPALFSKPGSDGTWN FT DVTASQFAADARAIAKGFIANGIEPGDRIALMAKTRYEWSLVDFAIWFAGCVTVPIYET FT SSPSQVAWIVSDSGAKAVVVEAAAHEAVVRRAAHQEQLDGLDHVWQFEGGLEQLSEDGR FT NIEDQELETHRTSNSLDDVATIIYTSGTTGRPKGCELTHGNFVELAENAVATLPEAVYP FT GASTIMFLPLAHVFARFISVLNVAAGCRTGHTPDVKHLLDDLQSFKPNFILAVPRVFEK FT VYNSAMLKAEDGGKGKIFHAGVDVAVAYSRAQQEGKVPLVLSLKHMLFDALLYKKLRTA FT MGGNIRHAVSGGGPLGERLGHFFNGIGVTILEGYGLTETTAPISVNALDRIKIGTVGKP FT LPGNAVRIAEDGEILAKGVCVMRGYRNRPELQEETFTDGWFHTGDIGELDSDGFLKITG FT RKKEIIVTASGKNVVPALLEDQIRADALVSQCVVVGEGRPFISALVTLDPEALTGWLSR FT HQLDAKLSLEELSTHPKVLETVQAVIDKANTSVSKAEAIKSFRIVPADFTEETGHLTPS FT MKIKRAVVLKDFEAVIEEIYSAPKPKA" FT CDS complement(1339412..1339846) FT /transl_table=11 FT /locus_tag="AARI_12020" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUV8" FT /protein_id="CBT75411.1" FT /translation="MNPEDAQPSGRKDPQWDELVENFRQLDSNTPREPSAAERAAQLEK FT LFNTGPGAMRGPRDYVAEDTPEEFVPQEPAALGSGDPMLNLAWVVAAGGPLGLLLCVLF FT FRSAPGFIYFGLAIVALLGIAYLLKRLPTERDPGDDGAQV" FT CDS complement(1339843..1340616) FT /transl_table=11 FT /locus_tag="AARI_12030" FT /product="putative esterase/lipase" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.1.-" FT /note="match to protein family PIRSF017388" FT /db_xref="GOA:E1VUV9" FT /db_xref="InterPro:IPR012354" FT /db_xref="UniProtKB/TrEMBL:E1VUV9" FT /protein_id="CBT75412.1" FT /translation="MKLDTQDIAPEGRKRSDAVLLIHGFTGSPISMQPWASSLEQAGFD FT TAIPLLPGHGTQWKDMIGCDYGQWIHATEQAYDLLAQTHERVFAAGLSMGGALALHLAT FT RRNVAGVSLVNPGLVVDSPVAPYTPWLKHVVRSVAPISDDIAKRGVTEGAYPRTPVAAV FT AQLHSLFAQTRRRLALVDAPVQLFRSTVDNVVSERSVHELVEGLNSGTLAEHHMLLHSK FT HVATLDYDAEQIFHESARFFAQLAAAEHKPKQERP" FT CDS 1340750..1341421 FT /transl_table=11 FT /locus_tag="AARI_12040" FT /product="putative 1-acylglycerol-3-phosphate FT O-acyltransferase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.3.1.51" FT /note="1-acylglycerol-3-phosphate O-acyltransferase FT catalyzes the following reaction: Acyl-CoA + 1-acyl-sn- FT glycerol 3-phosphate <=> CoA + 1,2-diacyl-sn-glycerol 3- FT phosphate. It is involved in phospholipid biosynthesis" FT /db_xref="GOA:E1VUW0" FT /db_xref="InterPro:IPR002123" FT /db_xref="UniProtKB/TrEMBL:E1VUW0" FT /protein_id="CBT75413.1" FT /translation="MLYDFLKRFAVRPLIRIFFRVKIQGIDNVPESGAAILASNHLSVS FT DSVFLPAALDRPVIFLAKDEYFNGTGLKGRITAWFFRNINQLPMDRSGGKKSAASLASA FT KLALDEGKLLGIYPEGTRSPDGRLYRAKLGVAKLALESGAPVIPIAMINTDKVQPINQS FT IPRPGKIGIKIGKPLAFEHLAGKHDDPAAMRACADEIRKAINVLSGQSYVDIYAPRKPK FT K" FT CDS 1341503..1342897 FT /transl_table=11 FT /gene="aroG" FT /locus_tag="AARI_12050" FT /product="3-deoxy-7-phosphoheptulonate synthase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.5.1.54" FT /note="involved in phenylalanine, tyrosine and tryptophan FT biosynthesis" FT /db_xref="GOA:E1VUW1" FT /db_xref="InterPro:IPR002480" FT /db_xref="UniProtKB/TrEMBL:E1VUW1" FT /protein_id="CBT75414.1" FT /translation="MSEENRTPLPGSSVAGPATDPQLDLWRELPIAQQPTWREHKDYQS FT SINELGSRPPLVFAGEVDVLRERLAAAAQGKAFLLQGGDCAETFADATADKISSRVRTI FT LQMAVVLTYGASMPVIKMGRMAGQFAKPRSSNDETRDGVTLPAFRGDIVNGFDFTPESR FT AHDPKRMVQAYNTSSATLNLIRAFTQGGFADLRSVHSWNSGFMANPAHSAYEQLAGEID FT SAIRFMDACGADFEALKRTEFFASHEALLLDYERALTRTDSRTGLPYDTSGHFLWIGER FT TRQLDHAHVDFLSRVRNPIGVKLGPTSDPEDVLALIDKLDPNREPGRLTFITRMGAKNI FT REKLPNLVEKVTASGAQVLWVTDPMHGNTVTSQNGYKTRNFEDVMDEVRGFFEVHDALG FT TFPGGLHVEMTGDDVAECLGGADPIREEDFDSLYESLCDPRLNHRQSLEMAFLVSSALQ FT SRSRKR" FT CDS complement(1342969..1345185) FT /transl_table=11 FT /locus_tag="AARI_12060" FT /product="putative serine/threonine protein kinase" FT /function="4.6 Miscellaneous" FT /EC_number="2.7.11.1" FT /note="identified by match to protein domain PD000001. FT Match to PS00108 pattern. Protein kinases are a group of FT enzymes that possess a catalytic subunit which transfers FT the gamma phosphate from nucleotide triphosphates (often FT ATP) to one or more amino acid residues in a protein FT substrate side chain, resulting in a conformational change FT affecting protein function. They play a role in a FT mulititude of cellular processes, including division, FT proliferation, apoptosis, and differentiation" FT /db_xref="GOA:E1VUW2" FT /db_xref="InterPro:IPR000719" FT /db_xref="InterPro:IPR005543" FT /db_xref="InterPro:IPR008271" FT /db_xref="InterPro:IPR011009" FT /db_xref="InterPro:IPR017442" FT /db_xref="UniProtKB/TrEMBL:E1VUW2" FT /protein_id="CBT75415.1" FT /translation="MSTSLTDPTLGKTLDGRYRLDHLLALGGMSRIYRAMDKRLHRAVV FT VKVLNDNYASEHTVRERFESEAVIAANITHPNVVSIRDHNVSDNLVYLVMEYVRGRNLE FT QVIQERGRFTPRQALSVLEQICHGLSSAHSEGIIHRDMKPANVLLSDIGEVKVTDFGLA FT RAASAHTQSATLVATLSHVSPELVSGSPADSRSDIYALGITIYQMLTGQAPYTESNAAA FT LMKHHLDSPMPMPSDLVPGLAQDLDELVRWCTEKDPEKRPQDASLLLEEIIQIRSTLTD FT GQLDLGAEQLGGIEDLTPQTSTHMPTTLQQRLDAMQREREDERERLWLKRNSDQAETEY FT EVEDGELDPDQTTVIAAADATEVLDLRDAQATLAQPRATDVVSDSEINATTVYSRGSEL FT EKAEEAEADQSSELSVRGQKRAQKQAAKKWRKEAQVPTHRLSKPRTGSQKFVITLMWII FT IIALVTGAGWFFGRGPGTIIRIPSLSGMLQSQAVAQLDDQGIPVRIGTAYDDEIAIGRV FT VDSQPGIGENIMKFQGVDLIVSQGPELFEVPDLTGKSLEQATTVLNEIGFQDLKTDQAY FT SESSDKGEVISSSPAAGKELPRKNIITLTVSKGHAPVEVPSLTGLSKDAAQEKLESLGL FT KLNTADSIHSAVVEKGLIAAQDPATGTIEYGSTVSVNVSEGPEYVEIPSVIGQSVDEAT FT AILEAAGFTVKNHNVFGGFSQTVRMQSPLNQQAVRGSEISIYAF" FT CDS complement(1345388..1345636) FT /transl_table=11 FT /locus_tag="AARI_12070" FT /product="WhiB-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF02467. WhiB FT is a putative transcription factor in Actinobacteria, FT required for differentiation and sporulation" FT /db_xref="InterPro:IPR003482" FT /db_xref="UniProtKB/TrEMBL:E1VUW3" FT /protein_id="CBT75416.1" FT /translation="MDWRSRAACLEKDPELFFPVGNTGPALLQIEEAKSVCRRCEVTET FT CLQWAIESGQDAGVWGGMSEDERRALKRRAARARRAS" FT CDS 1345994..1346407 FT /transl_table=11 FT /locus_tag="AARI_12080" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUW4" FT /protein_id="CBT75417.1" FT /translation="MSNENTTSSRPTSVFVVAALVLIEALATLAYAISYMPNLDTNGTV FT NLGGQLFMLALCLLLAVWQGSVAINFFKGKAFTRAPIIVWQLFQLILSVSFLSSNIPMV FT TAVAVLAIVIAGTTVVMLFAPKTTAFLGDRPNR" FT CDS complement(1346270..1350085) FT /transl_table=11 FT /locus_tag="AARI_12090" FT /product="FtsK/SpoIIIE domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF01580. This domain is found extensively FT in a wide variety of proteins from prokaryotes and FT plasmids" FT /db_xref="GOA:E1VUW5" FT /db_xref="InterPro:IPR000253" FT /db_xref="InterPro:IPR002543" FT /db_xref="InterPro:IPR008984" FT /db_xref="UniProtKB/TrEMBL:E1VUW5" FT /protein_id="CBT75418.1" FT /translation="MVRYELLLISRKFQHPRQFELVMSGRVSGEQLAGLLEQQFPGQQW FT YSGTCRLEELELLPASERLLLSELPQPVRSAPTATSCLKLYIRRGPDAGAWIALSKGEH FT LIGRTAPLWLEDPLVSRVHAKLSVTTRGLHLSACANQQIAMPDGSRYESVDLEQGSRFI FT LGHTEFAIGDPLVEGSSISVSPDQLEIQAPPKPEMARLIALVLAAFVPILSGILLALVT FT GSMLFLILSGVSALMGVVPAGQLLIERRQWKREAKAQRAAAIAARKNYAPELGEYFVSE FT LDSASLGRPCAQVPPLVWGKGLWSPQDIAPSAPKGIRKVFRSLKKPKSDAPWYGPVFFP FT STTGIWQLKTTQGQYAGSILASVLARYLPAIHAGRIRLVIDPSIRCLPSSLLLMRHVSS FT AQLVAPEESRHFGNEDNALSTIYVTAQAPQPVPGALVLGIWPATAECAENWIAPHPVSA FT HLPDERLALQNLSPLSLARFDKMVHQLVALQKRSITSHLDSTQAPTLAVRAHLGMSDQG FT EEVFLDLHEDGPHVLICGTTGSGKSEALRRIISDFARNYSPAQLAFALIDFKGGAGLSV FT YESLPHVQLFASDLDGAAAERTLEQLEHEVRRREELLASHGCSDIAEYQALDESEYVLP FT RLLVVVDEFRVFIETLPQANLRIDRLAAVGRALGIHLILSTQRPAGALTGQTRANLNTT FT IALRVNDQSESVELVGSTAASKLIEPGQAIVKSATKPTRNMQCSLAIEPPLHGELFERN FT RHDLSLMSLCRFEKAFVPMASDPLRAHAAELASKWESTVRPVSGFAQPLPLPGESAQPP FT ETWEGIERGALYCGVVDNLHRARLEPLVIDRARSRSILICGLPEAGASELFASLANSPR FT KILCFGPAPIQGTTGNLRVVTGEDLYSFLDAVDFLESMPQDPSLIIIVHSLAQLQSNIH FT PQHFQRLDEALGSLLRFGGAGSPLVLCAVDRDQNTLKSTGLCTEQWFFPFNATESLRMI FT WPKIPTCSPLPGRGVRISSGHPPQVFQLTRVQAAEAASSTWLQLTPSDDATLGAGTEPQ FT NLLGYAPFDGAVVSRPMSQCVILLCPDVQQRLRISVALAQRWNGLQLSGLTDLENFVRT FT LREGPNSAREKLLCLFLEATNDSRLPSLLEVLRSAGLNVVLCVPPSSRLAFDLGMSSVG FT LDDRQVVVVEATHPQDLQPMNWPAIPQGSSAHSGDYWRAIISKHGKPRMIHIPHNLAQS FT PLAVRPVPEESCGLWREEHHYGGSGNHDGQYRHGRHHRDIRAEERD" FT CDS 1350334..1351557 FT /transl_table=11 FT /locus_tag="AARI_12100" FT /product="putative type II/IV secretion system protein E" FT /function="1.6 Protein secretion" FT /note="identified by match to protein domain PF00437" FT /db_xref="GOA:E1VUW6" FT /db_xref="InterPro:IPR001482" FT /db_xref="UniProtKB/TrEMBL:E1VUW6" FT /protein_id="CBT75419.1" FT /translation="MVDALSIVEDEVRELVRRRGLDPAKQPEKIRSLIGDVVRDYDERA FT LLGAVPSLGSLEAAQRSVFDNVAGFGALQPLLDDPSVEEIWINSPHQVFCARGGQSELT FT HIRMETAEIAALVERMLKSSGRRLDLSQPFVDCQLPDGSRLHVVIPDITHEHWAINIRK FT FIARAGKLDDLVDLGSLSEQAALFLSTAISAGLNVIVTGPTQAGKTTMLNCLASAIGPR FT ERIITIEEIFELNLSLRDVVAMQTRLANLEGTGEITMRRLVKEALRMRPERIIVGEVRE FT AESLDMLIALNSGIAGLCTLHANSARDAITKICTLPLLAGPNITSDFTVKTVAACIDLV FT VHCVRGPEGHRYVNEILSVRNRVEEGQIESSTLFERQTERLLPARGADWSHEKFDVAGI FT NIAELMAV" FT CDS 1351560..1352411 FT /transl_table=11 FT /locus_tag="AARI_12110" FT /product="putative type II secretion system protein F" FT /function="1.6 Protein secretion" FT /note="identified by match to protein domain PF00482" FT /db_xref="InterPro:IPR018076" FT /db_xref="UniProtKB/TrEMBL:E1VUW7" FT /protein_id="CBT75420.1" FT /translation="MVVFFALMGGLGIALMVDWLLFAPWAKSRNRSSAIKNALLHAGMG FT NLAPSKFIVICVVCGITFTLITLALTASWLFALVFCIFGSFAPWVYLRHQAAKRQAALQ FT EQWPEVVDHLRSAIRAGLSLPEALSQLAMVGPQILRPLFRDFALDYRATANFAVALDQL FT GERLADPVADKILTTLRITREVGGTDLGHTLTTLSAFLRDDVRTRGELAARQSWIVSAA FT RLAVAAPWILLLVLGTQEAAKDAYMTVGGVIVLSLGMLVSFICYRIMLRLGTLPVEERV FT LA" FT CDS 1352408..1353349 FT /transl_table=11 FT /locus_tag="AARI_12120" FT /product="putative type II secretion system protein F" FT /function="1.6 Protein secretion" FT /note="identified by match to protein domain PF00482" FT /db_xref="InterPro:IPR018076" FT /db_xref="UniProtKB/TrEMBL:E1VUW8" FT /protein_id="CBT75421.1" FT /translation="MSSYASWAALCGLGLGLGLWLIVVNLPGWRKMAFADRIAPHVRVG FT VRSSRMLEDSWHSESGYSALGQLAAPMLLQIKRLASLHSPSADTLRKRLDAAGLDMSVI FT DYRSQEIVYALTGLVAGSAFMAFAAIQYRVSLVLSVLVVVGFGIIGYAMRGWWLGEQIN FT RRARKILTQFPTVAEVLALTVGAGESTTGAIERISRICHGVIGDEFTKTLNDIHAGTPM FT VQAMQHMSDRMQVGAMTRFVDAIVVATERGTPLAQVLRDQAQDVRDASKRELMEVAGKR FT EISMLVPVVFGILPLTIVFAVFPGLALLEMSY" FT CDS 1353412..1353645 FT /transl_table=11 FT /locus_tag="AARI_12130" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUW9" FT /protein_id="CBT75422.1" FT /translation="MYRLQEVMLNLVLQIVATSEQVWGRFAPKLKDSRGDVPGWVMITL FT MSALLVAALLAIAGPRLQDLFNQAIDRVSGLG" FT CDS 1353691..1354071 FT /transl_table=11 FT /locus_tag="AARI_12140" FT /product="TadE-like family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF07811. The FT members of this family are similar to a region of the FT protein product of the bacterial tadE locus. In various FT bacterial species, the tad locus is closely linked to flp- FT like genes, which encode proteins required for the FT production of pili involved in adherence to surfaces. It is FT thought that the tad loci encode proteins that act to FT assemble or export an Flp pilus in various bacteria" FT /db_xref="InterPro:IPR012495" FT /db_xref="UniProtKB/TrEMBL:E1VUX0" FT /protein_id="CBT75423.1" FT /translation="MEPLGNERGSAVAEFVMITTLLVLIAMTLVQLALVLHVRNTLIDA FT ASNGAHYGALANRSAGDAEGRTRTLITESLHGGFASGIAVSTTNIGENQLVNVSVNTRV FT PLIGLLPNGWELHVEGEAVRYD" FT CDS 1354025..1354510 FT /transl_table=11 FT /locus_tag="AARI_12150" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VUX1" FT /protein_id="CBT75424.1" FT /translation="MDGSCTLREKRCVMTSVRHLAWKIRDRACADERGSAIVEFIFAST FT VLLIPMVYLILAAGQLQGGSYAVVGAADHAAKVFAVAQTPAQARSDAHAVVRRTMASFG FT YANARTSISCDKECLSPGSVVTIRVELDVPLPFVSDWVEASAFTVDSSASQRTDRFG" FT CDS 1354560..1354958 FT /transl_table=11 FT /locus_tag="AARI_12160" FT /product="conserved hypothetical secreted protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.997) with cleavage site probability 0.440 FT between position 27 and 28" FT /db_xref="UniProtKB/TrEMBL:E1VUX2" FT /protein_id="CBT75425.1" FT /translation="MLAIGLCAITLLTISVVLAASAVNLKARQLLSLADGAVVAAVDEF FT EFVADGGRPKIQLEQQRVHRAVQQYLSDVGAAGRVDNLRIARVQIMSDGQGARLKLSGS FT VQPPIVGWIIPSGVPITVESTARTVLSR" FT CDS 1355226..1356341 FT /transl_table=11 FT /gene="prfB" FT /locus_tag="AARI_12170" FT /product="peptide chain release factor 2" FT /function="3.7.5 Translation termination" FT /note="directs the termination of translation in response FT to the peptide chain termination codons UGA and UAA" FT /db_xref="GOA:E1VUX3" FT /db_xref="InterPro:IPR000352" FT /db_xref="InterPro:IPR004374" FT /db_xref="InterPro:IPR005139" FT /db_xref="InterPro:IPR020853" FT /db_xref="UniProtKB/TrEMBL:E1VUX3" FT /protein_id="CBT75426.1" FT /translation="MAKTDFSAEIRSLRSTFSAIEDVSDVDQIKADIAVLSEEAGVPNL FT WDDPAAAQIVTSKLSHRQSELERLTRLRTRIDDLEVLVELAELEDDADTLDEAEKELVS FT IQKSLADLEIVTLLSGEFDSRGAVVTIRSGAGGVDAADFAEMLLRMYLRWAERRGYKAT FT VMDTSYAEEAGLKSATFEIDAPYAFGTLSVEAGTHRLVRISPFDNQGRRQTSFAAVEVV FT PLIEQTDTIEIPESEIRVDVFRSSGPGGQSVNTTDSAVRMTHIPTGVVVSMQNEKSQIQ FT NRAAALRVLQSRLLLLKKEQEDAQKKEFAGDVKATWGDQMRSYVLNPYQMVKDLRTEHE FT VGNTQAVLDGEIDDFIDAGIRWRAGERRPSK" FT CDS 1356622..1357419 FT /transl_table=11 FT /gene="ftsE" FT /locus_tag="AARI_12180" FT /product="cell division ATP-binding protein FtsE" FT /function="1.7 Cell division" FT /note="TCDB: general secretory pathway (Sec) family, FT general secretory pathway (Sec-SRP) complex (TC 3.A.5.1.1). FT ABCISSE: ATP-binding protein (ABC), CDI- family. CDI family FT systems are found only in eubacteria and are comprised of FT two proteins: the FtsE ATP-binding protein and the FtsX FT permease. It is possible that CDI systems play a role in FT the proper membrane targeting or insertion of some proteins FT essential for septum formation" FT /db_xref="GOA:E1VUX4" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005286" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VUX4" FT /protein_id="CBT75427.1" FT /translation="MIKFENVSMVYEPKQQNAALEDVSIEIDRGEFAFLVGESGSGKST FT FLSLVLREKRSTGGSVYVAGQNLNRIPSRRVPKLRRDIGFVFQDFRLLRERTVFDNVAF FT AMEVIGASRAQIRERVPDALKMVGLEDKARRKPTELSGGEQQRVGIARAIVNRPSILLA FT DEPTGNLDRKNSIEVMNVLNRINQNGTTVLMATHAHELVSEYRHRVIELSRGQVIRDEI FT DGQYAPMTTVVNQDGSRELLVGDSAVEYDEESQVAEEKKDEDQ" FT CDS 1357416..1358330 FT /transl_table=11 FT /gene="ftsX" FT /locus_tag="AARI_12190" FT /product="cell division membrane protein FtsX" FT /function="1.7 Cell division" FT /note="ABCISSE: IM (permease), CDI-family. CDI family FT systems are found only in eubacteria and are comprised of FT two proteins: the FtsE ATP-binding protein and the FtsX FT permease. It is possible that CDI systems play a role in FT the proper membrane targeting or insertion of some proteins FT essential for septum formation" FT /db_xref="GOA:E1VUX5" FT /db_xref="InterPro:IPR003838" FT /db_xref="UniProtKB/TrEMBL:E1VUX5" FT /protein_id="CBT75428.1" FT /translation="MRLGFILREAAKGLRQNVVMVVSVVLVTFVSLTFVGASVLLQLQI FT NQMKGYWYDRMEVAVYLCDDTSTSPNCAGSAVSEEQRQNIEEMLKSEQLAPYIKEFAYE FT SKDQAYKNFLDQYENSALVDQVTAEQLPESFRVGLVDPEKYPVINEAFSTVEGVDSVID FT QRELLEKVFQLVRVASAAAAVVAIVMIVCAVLLTGTTIQLSAMHRRLETTIMRLVGASK FT ATIQLPFIIEGVIASLIGGLLASGTLWLLLRFLVEDKLANENVGVAFISTNEIWLVAPI FT LLIIGIVLATISSVVTLKRYLKV" FT CDS 1358383..1359846 FT /transl_table=11 FT /locus_tag="AARI_12200" FT /product="putative secreted M23 family peptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.24.-" FT /note="identified by match to protein family PF01551. FT Members of this family are zinc metallopeptidases with a FT range of specificities. Peptidase family M23 are also FT endopeptidases. Signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 1. 000 FT between position 32 and 33" FT /db_xref="GOA:E1VUX6" FT /db_xref="InterPro:IPR011055" FT /db_xref="InterPro:IPR016047" FT /db_xref="UniProtKB/TrEMBL:E1VUX6" FT /protein_id="CBT75429.1" FT /translation="MLSNAVRRKFLRASIGGAMALALTLPAGLVVADELDDKKAQVEKN FT IDNLENDMEFLDADIQETDQKLRNQQAQVPIAQQALADAQSRVANAQATVADLNNRLVS FT AQATRDEVAKQIEENAAKISEAEDAMAQIASEAYKRGGVSGGLDMILNMDSATKMADGL FT DMANRAMESQNAKYNDLAQEQASNESNKLRLVAVEKEISSLKAQAEEALEQEQAARDAA FT QSAKNELDALVASTEKLSAELESQKPRIQAKLDNQQKEYAAVNQQIKERQERLIREAAE FT RKRKAEEKARKEAEAERKRIAAEKAAYEAEQERKAAEAKAQKKTYKKKTYAAPKPEKKT FT SNYSEPSSWGLVKPTTSNRLTSTFGWRPTPAGTIDYGGRGGYVHAGIDWGFGGQCGSPI FT TAAAAGEVWMAGWGGSSGNKVTLSHGVIKGKALATNYHHMSRIAVSVGQHVKRGQVIGY FT VGTTGNSTGCHLHFETIINGSHVNPLGLL" FT CDS 1359901..1360380 FT /transl_table=11 FT /gene="smpB" FT /locus_tag="AARI_12210" FT /product="SsrA-binding protein" FT /function="3.7 Protein synthesis" FT /note="in bacteria, SsrA RNA recognizes ribosomes stalled FT on defective messages and acts as a tRNA and mRNA to FT mediate the addition of a short peptide tag to the C- FT terminus of the partially synthesized nascent polypeptide FT chain. The SsrA-tagged protein is then degraded by C- FT terminal-specific proteases. SmpB binds specifically to the FT ssrA RNA and is required for stable association of ssrA FT with ribosomes" FT /db_xref="GOA:E1VUX7" FT /db_xref="InterPro:IPR000037" FT /db_xref="InterPro:IPR020081" FT /db_xref="InterPro:IPR023620" FT /db_xref="UniProtKB/TrEMBL:E1VUX7" FT /protein_id="CBT75430.1" FT /translation="MAKKNQEDRVIASNRKARHDFEILDTFEAGMVLTGTEVKSLREGK FT ASLVDGFCQFYRDELYIENVYIPEYLNGSWTNHAARRRRKLLLHRQELIKIERKISEAG FT LTVVPLSLYFKSGRAKVEIGVARGKREFDKRQTLREKQDNREALRAMRERNRGNA" FT CDS 1360987..1362117 FT /transl_table=11 FT /locus_tag="AARI_12220" FT /product="putative phage integrase" FT /function="4.4 Phage-related function" FT /note="match to protein family PF00589" FT /db_xref="GOA:E1VUX8" FT /db_xref="InterPro:IPR002104" FT /db_xref="InterPro:IPR011010" FT /db_xref="InterPro:IPR013762" FT /db_xref="InterPro:IPR023109" FT /db_xref="UniProtKB/TrEMBL:E1VUX8" FT /protein_id="CBT75431.1" FT /translation="MAVIQTIERKKDTGYRVVYRNKDTGKMASRIFDDEVKARTFKDFL FT EANGSSLKAATEVKRIHDKRMPRVHEIVTSHIDQLTKPQTGTIKRYRNHNAGHIIGSTL FT GNMAIDKVTKQHVIDWMAGLRAVKGSNKPIGSELSQRTKKNIHALLSSAFDTAVEEGKM FT AKNVAKGIGDPDKGEAREAVYLSLEDLQIIEDAMPDQYKLFIRVLAKTGLRYNEATALR FT KRDIRVEGKRCIIMITRAWKSTDDGEQIGPPKTEMAKRNVTCSLELSADLIEHMKDLRP FT GELIFTRPDGEFLRNSYFHKYTWQPVINKLVEDGDLDEKPWIHEIRKAHTTHLLQAGVP FT VSVVQARLGHEDPQTTLKIYARLANDDDQKAADALG" FT CDS complement(1362176..1362703) FT /transl_table=11 FT /locus_tag="AARI_12230" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.718 FT between position 29 and 30" FT /db_xref="GOA:E1VUX9" FT /db_xref="InterPro:IPR015250" FT /db_xref="InterPro:IPR021652" FT /db_xref="UniProtKB/TrEMBL:E1VUX9" FT /protein_id="CBT75432.1" FT /translation="MKKLAPLAAAAALALSLTACSGEIEKGGAEPAASSEATKESATTE FT QVETLQFGDKYTWTNGVSMAISKPKKFELSEVGKMVVTNEDANFVSFDVVVENGSEEDF FT DPVMIHFTASSDGEEAEAVFDTDNKLDGPPQTTIKPGKSAKFKIGFGVADPKDITMDAS FT AGMEYSTQTFAN" FT gene complement(1363039..1363413) FT /pseudo FT /locus_tag="AARI_34810" FT /product="transposase of IS256 family (pseudogene)" FT /function="4.5 Transposon and IS" FT gene complement(1363394..1363939) FT /pseudo FT /locus_tag="AARI_34820" FT /product="transposase of IS256 family (pseudogene)" FT /function="4.5 Transposon and IS" FT gene complement(1364070..1364246) FT /pseudo FT /locus_tag="AARI_34830" FT /product="transposase of IS256 family (pseudogene)" FT /function="4.5 Transposon and IS" FT CDS 1364784..1365257 FT /transl_table=11 FT /locus_tag="AARI_12240" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR021214" FT /db_xref="UniProtKB/TrEMBL:E1VUY0" FT /protein_id="CBT75433.1" FT /translation="MGKNSSQRVSPFLSAIYAVVAFLLEVGLLFAAALAAIAFIDLPTI FT PAILVVVIPLLVVWAIFFSPKAVVKLRLRTRLLLIHIIYLVGAYVLWLSVDHSFYDQSQ FT IWAIAMLALTAISAILVIATGGYVVPHDRTKKPPKQAPSRASSGAPKGRRAAR" FT CDS complement(1365306..1365686) FT /transl_table=11 FT /locus_tag="AARI_12250" FT /product="CrcB-like protein" FT /function="3.4 DNA packaging and segregation" FT /note="identified by match to protein family PF02537. CrcB FT is a putative integral membrane protein possibly involved FT in chromosome condensation. Overexpression in E. coli also FT leads to camphor resistance" FT /db_xref="GOA:E1VUY1" FT /db_xref="InterPro:IPR003691" FT /db_xref="UniProtKB/TrEMBL:E1VUY1" FT /protein_id="CBT75434.1" FT /translation="MLSPGLFLIVSLCGGVGACLRFVLDALIKLWLPSSLPWGTILINI FT SGSFALGLLTGLFAGGLLPEPWLVAAGTGLLGGYTTFSTASFETIRLLQAGQLAASLVN FT AAGTLLATVLAALLGFQVALLF" FT CDS complement(1365686..1366147) FT /transl_table=11 FT /locus_tag="AARI_12260" FT /product="CrcB-like protein" FT /function="3.4 DNA packaging and segregation" FT /note="identified by match to protein family PF02537. CrcB FT is a putative integral membrane protein possibly involved FT in chromosome condensation. Overexpression in E. coli also FT leads to camphor resistance" FT /db_xref="GOA:E1VUY2" FT /db_xref="InterPro:IPR003691" FT /db_xref="UniProtKB/TrEMBL:E1VUY2" FT /protein_id="CBT75435.1" FT /translation="MTLPPAPTSQNSAPRVYLRPGLLLLVFLGGALGTAARQALGMLFP FT EASVVPVSIFIANILGAFLLGMLLEALSRRGRDVGRRRSLRLLLGTGFMGGFTTYSALA FT TGTMQLLRSGAMPWALAYPLGTVILGALATWCGIAVGAKWAARSPGGRR" FT CDS complement(1366159..1366638) FT /transl_table=11 FT /locus_tag="AARI_12270" FT /product="universal stress family domain-containing FT protein" FT /function="4.1 Adaptation to atypical conditions" FT /note="identified by match to PF00582: universal stress FT protein family. The universal stress protein UspA is a FT small cytoplasmic bacterial protein whose expression is FT enhanced when the cell is exposed to stress agents. UspA FT enhances the rate of cell survival during prolonged FT exposure to such conditions, and may provide a general FT stress endurance activity" FT /db_xref="GOA:E1VUY3" FT /db_xref="InterPro:IPR006016" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VUY3" FT /protein_id="CBT75436.1" FT /translation="MVARPIILGVPDRVDAHVLATAAELAAKLRTTLLCIHVDATRYQL FT EELDDGSVRSAPLDPDSGEESLQDFPAELLQQIRAQLAGLDLHWQTQARAGGAGAQLAQ FT LAVAHDAALIVLGVRQRSVANRIREVLNGSVALHLAHRQCYPVLLVPPPASPRAE" FT CDS complement(1366710..1367339) FT /transl_table=11 FT /locus_tag="AARI_12280" FT /product="putative metal-dependent transcriptional FT regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF01325 and PF02742. The FT diphtheria toxin repressor protein (DTXR) is a member of FT this group. In Corynebacterium diphtheriae where it has FT been studied in some detail this protein acts as an iron- FT binding repressor of dipheteria toxin gene expression and FT may serve as a global regulator of gene expression. The N- FT terminus may be involved in iron binding and may associate FT with the Tox operator. Binding of DTXR to Tox operator FT requires a divalent metal ion such as cobalt, ferric, FT manganese and nickel whereas zinc shows weak activation" FT /db_xref="GOA:E1VUY4" FT /db_xref="InterPro:IPR001367" FT /db_xref="InterPro:IPR007167" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR022687" FT /db_xref="InterPro:IPR022689" FT /db_xref="UniProtKB/TrEMBL:E1VUY4" FT /protein_id="CBT75437.1" FT /translation="MKSARRGPSGLTTSEEDYLKALYLLTEWEETEVSTGALADQLGLS FT PASATAMVQKLAAKSLVHHVPRGAITLSSTGRREALRMVRRHRLLETFLRDELGYGWDE FT VHDEAEELEHTVTDRFVDALDARLGYPRHDPHGDAIPSAHGQLPASQAIRLDRFTGARA FT IIDRISDEDPQFLRRAAAQGLVPGAVIELPHQLDFIEASLIWVRRS" FT CDS complement(1367352..1368158) FT /transl_table=11 FT /locus_tag="AARI_12290" FT /product="putative histidinol-phosphatase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="3.1.3.15" FT /note="catalyses the following reaction: L-histidinol FT phosphate + H(2)O <=> L-histidinol + phosphate. Involved in FT histidine biosynthesis" FT /db_xref="GOA:E1VUY5" FT /db_xref="InterPro:IPR000760" FT /db_xref="InterPro:IPR020583" FT /db_xref="UniProtKB/TrEMBL:E1VUY5" FT /protein_id="CBT75438.1" FT /translation="MAEYTLQQDLDFALALADKVDAFTLARYGANDLVVESKPDMTPVS FT DADRGAEQLILAELAAHRPDDSVLGEEFGVHGSGSRRWVIDPIDGTKNFVRRVPVWATL FT IALLIDDEPVLGVVSAPAMVRRWHAATDLGAFVTEPGAAVGTTATRPLQVSSVASLADS FT SLGYASLNGWKDAGKLDGFLELLDTAWRTRGYGDFLSYALLAEGALDAAFEPELELYDM FT AALVPVVREAGGRFTSVAGVEGCHGGNALATNGKLHEAILPYLNRS" FT CDS complement(1368174..1369265) FT /transl_table=11 FT /locus_tag="AARI_12300" FT /product="putative ribosome-associated GTPase" FT /function="3.7.1 Ribosomal proteins" FT /note="identified by match to protein family PF03193" FT /db_xref="GOA:E1VUY6" FT /db_xref="InterPro:IPR004881" FT /db_xref="InterPro:IPR010914" FT /db_xref="UniProtKB/TrEMBL:E1VUY6" FT /protein_id="CBT75439.1" FT /translation="MRYSDYDESSVRIRPNKKGSRPRTKDRPAYEQAVIGRIITVDRGR FT YTAILDEDTANERIVIAARARELRRQAIVPGDLVGLVGDTSGKPDTLSRLIRIEERTTL FT LRRSADDTDATERVVVANVDKLVIVVAAANPEPRTGFVDRALVAAYDAGIQPVLCVTKA FT DVKDPADFLTHYEGLDFPVVISRTTAADASGVDARSADGASARLDAGALAELEQILSGC FT VSVVLGHSGVGKSTLVNALTGSTRATGHVNAVTGRGRHTSSNALALRLGDTPGSWLIDT FT PGIRSFGLGLVDPDNILAAFEDLAEIATGCPRGCTHAAGEAGCALEAWAENAEGTQAAD FT RLASYRRLVTTEETTHEKELGAL" FT CDS complement(1369265..1370668) FT /transl_table=11 FT /gene="aroA" FT /locus_tag="AARI_12310" FT /product="3-phosphoshikimate 1-carboxyvinyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.5.1.19" FT /note="sixth enzyme in the shikimate pathway, a seven-step FT biosynthetic pathway which converts erythrose-4-phosphate FT to chorismic acid. Chorismic acid is a important FT intermediate in the synthesis of aromatic compounds, such FT as aromatic amino acids (phenylalanine, tyrosine and FT tryptophan), p-aminobenzoic acid, folate and ubiquinone" FT /db_xref="GOA:E1VUY7" FT /db_xref="InterPro:IPR001986" FT /db_xref="InterPro:IPR006264" FT /db_xref="InterPro:IPR013792" FT /db_xref="InterPro:IPR023193" FT /db_xref="UniProtKB/TrEMBL:E1VUY7" FT /protein_id="CBT75440.1" FT /translation="MLLRTVKTCLEPKDLPISTASAPGSPTDKLHNAEKTWWAAPHAAT FT GLDAIVSVPASKSLTNRYLILAALASSPSTIHNTLISRDTELMLDALAAFGIGIERTTQ FT PDGSTTVAITPGKLATGPLSIDCGLAGTVMRFVPPLAAVAGASVAFDGDEAARVRPMAP FT VLDALETLGARIEYAGTTGMLPFTMDASALQERHEVLIDASGSSQFISALLLVGQALPG FT GLKLRAAAGHIASPDHIAMTVQTLRELGVEVAVGEDARSWSIAPGQLSGFTITVEPDLS FT NAGPFLAAALATNGTVRVPFWPASTTQVGGKWVQILSRMGAEISHDEDGVLTVRGTGVI FT RGIDYADASELAPTLAALCTLADSPSKLTGIGHLRGHETDRLAALETELAKVGATVTST FT DDALEIIPGTLQAADLDSYEDHRMATAGALLGLAIEGVRVENIATTAKTMPDFPQLWTD FT MAATAKGQG" FT CDS 1370727..1371530 FT /transl_table=11 FT /gene="rpoE" FT /locus_tag="AARI_12320" FT /product="RNA polymerase sigma factor RpoE" FT /function="3.5.1 Transcription initiation" FT /note="the sigma factor RpoE is involved in heat shock and FT oxidative stress response; it is believed to control FT protein processing in the extracytoplasmic compartment" FT /db_xref="GOA:E1VUY8" FT /db_xref="InterPro:IPR007627" FT /db_xref="InterPro:IPR013249" FT /db_xref="InterPro:IPR013324" FT /db_xref="InterPro:IPR013325" FT /db_xref="InterPro:IPR014284" FT /db_xref="InterPro:IPR014293" FT /db_xref="UniProtKB/TrEMBL:E1VUY8" FT /protein_id="CBT75441.1" FT /translation="MSRLVVPSVTIRQDTSNAGGTACAVAEEPRGLRSGAGTRLKPVER FT VDSAVMNNKSVDENLPDVAAESEEQRRERFERDAMQYVDQLYSAALRMARNPSDAEDLV FT QEAYTKAYSAFHQYKPGTNLKAWLYRILTNTYINLYRKRQREPQRTSTDTIEDWQMAQA FT MEHSPAGLRSAEAEALDHLPDSDVKAALQSIGEDFRMAVYFVDVEGFSYKEASEILGVP FT IGTVMSRLHRGRKNLRELLADYAADRGIANGTQSKRGAKAERGAK" FT CDS 1371532..1371792 FT /transl_table=11 FT /locus_tag="AARI_12330" FT /product="anti-sigma factor" FT /function="3.5.1 Transcription initiation" FT /note="may act on RpoE. Match to protein family TIGR02949. FT Anti-sigma factors bind to sigma factors and inhibit their FT transcriptional activity" FT /db_xref="InterPro:IPR014295" FT /db_xref="InterPro:IPR024020" FT /db_xref="UniProtKB/TrEMBL:E1VUY9" FT /protein_id="CBT75442.1" FT /translation="MDCNSLGDCADDRIVRIYEYLDGALTLADLKEVKSHLDGCPECTE FT QYDLECIIRSVVRRSCQEHAPQTLKANIIARISQIRVESGH" FT CDS complement(1372039..1372728) FT /transl_table=11 FT /locus_tag="AARI_12340" FT /product="putative lipase/esterase" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.1.-" FT /note="match to protein family SSF52266" FT /db_xref="GOA:E1VUZ0" FT /db_xref="InterPro:IPR013830" FT /db_xref="InterPro:IPR013831" FT /db_xref="UniProtKB/TrEMBL:E1VUZ0" FT /protein_id="CBT75443.1" FT /translation="MATSPVAVAMTAKVGIDSSFWSQRKVAQLELRTIRITAIGDELLA FT GHGDPRGLGWFGRVMARTQDPALRLQSFVLASPAEGSEALAERWLGEASRRFSDQYENR FT LVIALSDRDVDLDVSTARSRLNLANILDSASQMNIKALLVGPAPGLDDARNQRVAELNR FT VYSDVALRRNHHYVDTFTPLRAHAQWRADLNASGGVPGQAGYGLMAWLVLHRGWYSWLD FT LPEPGEG" FT CDS complement(1372861..1376613) FT /transl_table=11 FT /gene="sucA" FT /locus_tag="AARI_12350" FT /product="oxoglutarate dehydrogenase FT (succinyl-transferring)" FT /function="2.1.3 TCA cycle" FT /EC_number="1.2.4.2" FT /note="it is a component of the multienzyme 2-oxoglutarate FT dehydrogenase complex in which multiple copies of it are FT bound to a core of molecules of EC 2.3.1.61 FT (Dihydrolipoyllysine-residue succinyltransferase), which FT also binds multiple copies of EC 1.8.1.4 (Dihydrolipoyl FT dehydrogenase). Involved in the TCA cycle" FT /db_xref="GOA:E1VUZ1" FT /db_xref="InterPro:IPR001017" FT /db_xref="InterPro:IPR001078" FT /db_xref="InterPro:IPR005475" FT /db_xref="InterPro:IPR011603" FT /db_xref="InterPro:IPR023213" FT /db_xref="UniProtKB/TrEMBL:E1VUZ1" FT /protein_id="CBT75444.1" FT /translation="MPEQAHHRLTEEFGGNEWLVDELFEQYLVDKNSVDKKWWDIFESL FT AAEKTAPAAPAAQPAPAAAASAAAPAANGQGAPRAAAQARATEPAPAAKAAPAAEAKKA FT EPAPKTAPIPAQAPKATPSTELFGEEKRTPLRGPMKAIATNMDASLTVPTATTVRAVPA FT KVMIDNRIVINNHLKRARGGKISFTHLIGFAVIRALKQIPSMNVTYDVIDKKPTAIQPA FT HVNFGIAIDMPKPDGTRMLAVPNIKAAETLSFNEFWATYEDLIKRARGNKLTADDYAGT FT TVSLTNPGGIGTVHSVPRLSKGQAAIIGVGALEYPAEYRGSSEKTVAALGIGKHITLTS FT TYDHRVIQGAGSGEFLKLVESLLLGEQNFYDEIFEQLRIPYEPVRWAVDNQVDIDLQVN FT KVARIQHLINSYRVRGHLMADINPLEYVQRKHPDLDINNYGLTLWDLDREWLAGGLGGK FT DRALLRDILGVLRDAYCRTIGTEYMHLQNPEEREWFQAKLESGYAKPSREEQLRILSKL FT NSAEAFETFLQTKFVGQKRFSLEGGESLIPLLDAIISDAADEQLDEVAIGMAHRGRLNV FT LTNIAGKTYAQVFREFEGTATPGSVQGSGDVKYHLGTEGSYTSDAGNQTKIYLAANPSH FT LEAVDPVLEGITRAKLDRLNSKNTVLPILVHGDAAFAGQGVVSEVLAMSQLPGYKTGGT FT VHVIVNNQIGFTTAPSSSRSSVYATDVARTVQAPIFHVNGDDPEAVVHVGQLAFEYRQK FT FGKDVVIDLVCYRRRGHNEGDDPSMTQPIMYNLIEAKRSTRKLYTEALVGRGDITQEEA FT ENVLAEYKENLERIFAETHAAQTSPIPIITPGSTINDLEKPFAQAADENTVDGARGSAI FT SAQVLAKIGAAHLEIPEGFTMHTKLKSLLERREKMSREGGIDWGFAEIAALGSLSMEGV FT PVRLAGQDSRRGTFVQRHSVFHDRENDNEWYPVHHLSDDQAPLWIYDSLLSEYAALGFE FT YGYSVERPDALVMWEAQFGDFVNGAQTVIDEFISSAEQKWSQSSSLVMLLPHGYEGQGP FT DHSSARIERFLQLCAENNMVVAQPSTGANHFHLLRRQAYARPRKPLIVFTPKQLLRLKA FT AASQVEDFTSGSFREVIGDASITDTNAVDKVLLCSGRVYYDLLAARTKANDTKTALVRV FT EQLYPAPAEQIAAELAKYPNASVSWVQDEPANQGPWPFFGLYVAPSLDQKITLVSRPAS FT AATSAGNAKRHEAENAVLIQQAFAR" FT CDS 1377043..1378365 FT /transl_table=11 FT /locus_tag="AARI_12360" FT /product="putatve CBS domain-containing transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="possible transporter. Match to PF00571 (CBS domain FT pair)" FT /db_xref="GOA:E1VUZ2" 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:E1VUZ2" FT /protein_id="CBT75445.1" FT /translation="MEWLSILFGLLLILGTGFFVAVEFSMVALDKSTVQRAVDNGERGA FT KPLLQCLTSLSTQLSSCQLGITLTTLLTGYVLEPAMSALLEPLMEQFGVPAASALAIAV FT VVSMVVATLLSMLIGELVPKNMAIAQAMKVGKLLARPQLVFTAIFKPAIIVLNGFSNAV FT LRKFFGLEAKEEISAARSSQELASLVRRSAQLGTLDLQTARFVESTIEFSERTAADVMT FT PRTSMSTIDSEAALSELIEVSADTGFSRFPVTTGSTDEIQGICHVKAIVSVPRERREAL FT QVGEFARDALYVPETIHLDVLLEQLRAAEFQVAIVMDEYGGTAGLVTLEDLVEEIVGEV FT SDEHDEDEEEAVTQPDGNWLFPGMYRPDQINENFDNDVIPEESSYETIGGFMLAELGRL FT AELNDRVETEHGVFTVTELDGRRISQVRFEPAAPAQEADDE" FT CDS 1378370..1379431 FT /transl_table=11 FT /locus_tag="AARI_12370" FT /product="CBS domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF00571 (CBS domain pair)" FT /db_xref="InterPro:IPR000644" FT /db_xref="InterPro:IPR002550" FT /db_xref="UniProtKB/TrEMBL:E1VUZ3" FT /protein_id="CBT75446.1" FT /translation="MGLIWLVVLLAGNAFFVAGEFAVMSARRSQIEPLADEGNKRAKVA FT LYAMEHVSIMLAVCQLGITVCSLLILNISEPAIHHLLAEPLTMIGMASSVADTVAFLIA FT LVLVTFLHVTFGEMVPKNISVSVADKAVLLLAMPLVGLSKVLTPITASLNGIANLVLHA FT FGIEPKDEVASSYTAAEVRSIIDTSSEEGALDEDDAARLTKALEFSSVTARSCMVKIDD FT LFTLEYGQTTAREFEKKVGKTGFSRMVITKNEVPVGYWHVKDVMLIDDAHSTQPLLDLP FT LHPLGRLGQDTEIEAALEAMRQEGNHLSAVVDESGSTIGVVFLEDVIEVLVGEITDTTR FT KRVNPPRSEKQAK" FT CDS 1379562..1380395 FT /transl_table=11 FT /locus_tag="AARI_12380" FT /product="iron/manganese/zinc ABC transporter, ATP-binding FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT Manganese/Zinc/Iron Chelate Uptake Transporter (MZT) Family FT (TC 3.A.1.15.z). ABCISSE: ABC transporter, ATP- binding FT protein (ABC), MET-family. This family is comprised of FT systems involved in the uptake of various metallic cations FT such as iron, manganese and zinc" FT /db_xref="GOA:E1VUZ4" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:E1VUZ4" FT /protein_id="CBT75447.1" FT /translation="MTQSPIVRFEDARLAYGSRVLWEELNLSIAAGEFLAVLGPNGSGK FT TSFINTMLGTTALNRGSVSIAGEPVRRGSSVVGLIPQQRPFGDNVPLRARDLVALGLDG FT TKLGVRLAHKSVRGKVDELLEMVGATAYANRAVSDLSGGEQQRLRAAQALASNPRVLLC FT DEPLLSLDLNHQQAISEVIHRQAVERGSAVVFVTHEINPILPYVDRVLYLAEGRFHLGS FT VDEVMQSSVLTKLYGAPVEVLRVNGRIVVVSGDGNRALPADGHDHAEDIDLAAGK" FT CDS 1380405..1381262 FT /transl_table=11 FT /locus_tag="AARI_12390" FT /product="iron/manganese/zinc ABC transporter, inner FT membrane subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT Manganese/Zinc/Iron Chelate Uptake Transporter (MZT) Family FT (TC 3.A.1.15.z). ABCISSE: ABC transporter, permease (IM), FT MET-family. This family is comprised of systems involved in FT the uptake of various metallic cations such as iron, FT manganese and zinc" FT /db_xref="GOA:E1VUZ6" FT /db_xref="InterPro:IPR001626" FT /db_xref="UniProtKB/TrEMBL:E1VUZ6" FT /protein_id="CBT75448.1" FT /translation="MNFSDLVEKAFNFQDYALLLPLVSNSLIAGAVLGVVGGLIGIFIM FT MRDMAFAVHGIAELSFAGAAFALLIGADVVTGSVLGSLIAALILGFLGTRARDRNSITG FT VLMPFGLGLGILFISLYEGRSANKFGLLTGQIVAVDDVQLNGMLALSAVVVIALLLVWR FT PLTFASVDPVVANARGVRTSGLSIIFMMILALAVAVTIQVVGALLVLALLITPAAAAMR FT VSSNPIITVVLSIVFAELAVVGGILLALAGSLPISPYVTTISFVIYVICRGVEAMRSPR FT RHQV" FT CDS 1381338..1381976 FT /transl_table=11 FT /locus_tag="AARI_12400" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VUZ5" FT /db_xref="InterPro:IPR017517" FT /db_xref="InterPro:IPR024344" FT /db_xref="UniProtKB/TrEMBL:E1VUZ5" FT /protein_id="CBT75449.1" FT /translation="MRKIPAHEIWPMVHAERLALIDDLETLDAASWEVPSLCAGWSVHD FT VAAHLADNARTTFFRLFIAMAKAGFSLDRQNDNGVAEMKASAPEGTLQKLVEVAALRCT FT PPVPVASRLVEEIAHGEDIRRAVGLQRSYPKKALEPAIRYQAATPQGVGGAKELASKVQ FT LCSQDGTFRLGIGPQIVGSRLELLMLLSGRGEHATGLSGPGMALVRQGA" FT CDS complement(1382044..1383504) FT /transl_table=11 FT /locus_tag="AARI_12410" FT /product="HNH endonuclease domain-containing protein" FT /function="3 Information pathways" FT /note="identified by match to SM00507" FT /db_xref="GOA:E1VUZ7" FT /db_xref="InterPro:IPR003615" FT /db_xref="UniProtKB/TrEMBL:E1VUZ7" FT /protein_id="CBT75450.1" FT /translation="MSAAKVHGNGLAPASDQEELDSHLIQLENDLSRIQDHGSKTQCAQ FT AIASIEERISSLRYQQAGLAHQLEKEVLRENEERGTNIDDQVRGAASQVAIARKRPQRG FT SRSFLSNCRILFEDTPNIASAYSRGEFTEAQIQAMLTPLQDVRPLRRSQFDEIFGQNPD FT MFESMGPKRIKETVTNFTVKYTSDREDKKLKEANAERYVRFHKDREAGCVFLHARLPIV FT GGTGLQMTLREQSLRIKRKGDPRTRTQIQADLLSRYMFFDENAEQKINVQLGLIMTDKS FT LFMGDREPAYLEGYGFIPAQTARELIGGHQIPNELTFEEMEAKITPENIERIEVMTEIT FT RLYTAPGDQELITMDSKARIFPEKLKKFIRIRDRHCRTPFCDGLVEETDHVTQFARGGK FT TSVSNSAGRCEICNKAKQAPGWYEYTAFRDNYSMMICPGSTMSYRSTAPPATGYMHKPF FT PQLMRDSKWFKDFKERLKNPDPPQIDDS" FT CDS complement(1383616..1384041) FT /transl_table=11 FT /locus_tag="AARI_12420" FT /product="putative metal uptake regulation protein" FT /function="3.5.2 Transcription regulation" FT /note="match to protein family PF01475" FT /db_xref="GOA:E1VUZ8" FT /db_xref="InterPro:IPR002481" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VUZ8" FT /protein_id="CBT75451.1" FT /translation="MSQPETRVTKQRLAVTEALTEVDDFATAQQLHRWLQDSEKKVSLA FT TVYRLLQSMADDGLVDVLRSGDGEARFRRCVTEVHHHHLVCRVCSKTVEVLAPSVERWA FT ARVAAEHDFSDPEHTVEIYGLCADCRAISKTDSTPAS" FT CDS 1384194..1384895 FT /transl_table=11 FT /locus_tag="AARI_12430" FT /product="metallo-beta-lactamase superfamily protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00753: metallo-beta- FT lactamase superfamily. Apart from the beta-lactamases, a FT number of other proteins contain this domain. These FT proteins include thiolesterases, members of the glyoxalase FT II family, that catalyse the hydrolysis of S-D-lactoyl- FT glutathione to form glutathione and D-lactic acid and a FT competence protein that is essential for natural FT transformation in Neisseria gonorrhoeae and could be a FT transporter involved in DNA uptake" FT /db_xref="GOA:E1VUZ9" FT /db_xref="InterPro:IPR001279" FT /db_xref="UniProtKB/TrEMBL:E1VUZ9" FT /protein_id="CBT75452.1" FT /translation="MRITPRGHSCIELATIDGKVLLDPGGFSQLENAFDGINAVLITHE FT HADHADQPAIIEALETNSVLELYAPAALAKALREQLPPAAQSQVVVVKAGSDFIVGGIR FT VRTFGGTHATIHHTIPRIANVGYLLGDRAVGQLEVFHPGDSYEVPFGAQPDVLMLPVMA FT PWGKMAEAADFAVSVNARCWMPIHDGLLNEQGLGLFDRQLGAIAARQGCTYLRVEQGIE FT HDLQKMVGGKQ" FT CDS 1384895..1385731 FT /transl_table=11 FT /locus_tag="AARI_12440" FT /product="thiosulfate sulfurtransferase-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /EC_number="2.8.1.-" FT /db_xref="GOA:E1VV00" FT /db_xref="InterPro:IPR001307" FT /db_xref="InterPro:IPR001763" FT /db_xref="UniProtKB/TrEMBL:E1VV00" FT /protein_id="CBT75453.1" FT /translation="MNPLISASQLREALAAGQKPVLLDVRWVLGRDDGAQSYAAGHIPG FT AVFVDLEKELSSAPGEHTGRHPLPLPADFEAAARSWGINAESHVVVYDNSGALAAARAW FT WVLRHAGFDAVQVLDGGLAAWSDAGGELALGYQQPAAGTVSLSWGRMPVVEFDELDALE FT GTLIDSRATARYLGIEEPVDPVAGHIPGALNRPTTDNLDAQMRFRNPEVLHDSFLKLDA FT QRSGSAAYCGSGITAAHQVLAAASAGIELALYPGSWSEYCSYTDAPVATSDEKHRR" FT CDS 1385761..1386189 FT /transl_table=11 FT /locus_tag="AARI_12450" FT /product="putative histidine triad family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF01230: histidine triad motif. The FT histidine triad motif (HIT) is related to the sequence H- FT phi-H-phi-H-phi-phi (where phi is a hydrophobic amino FT acid). Proteins containing HIT domains form a superfamily FT of nucleotide hydrolases and transferases that act on the FT alpha-phosphate of ribonucleotides" FT /db_xref="GOA:E1VV01" FT /db_xref="InterPro:IPR001310" FT /db_xref="InterPro:IPR011146" FT /db_xref="InterPro:IPR011151" FT /db_xref="UniProtKB/TrEMBL:E1VV01" FT /protein_id="CBT75454.1" FT /translation="MSTLFTKIINGEIPGHFVWKDETCVGFLSIGPLSDGHTLVVPREE FT VDEFTDASDELVAHLTLVATKIGRTQKRVFTSQRAGLMIAGFEVPHLHVHVWPTNSLAD FT FDLSNAADNPDPAAMDNNAEALRAGLREDGHGEFVPEA" FT CDS 1386192..1386608 FT /transl_table=11 FT /locus_tag="AARI_12460" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VV02" FT /protein_id="CBT75455.1" FT /translation="MKFIRYQSPVPNLRGVHLGIFALANGLGHGGNLTVAEHAIWRAGN FT DWYDAAYPNPSDCQPAVYDHARNPGAVAWFKDSAQHLLERVEPYLRLLDAHQIGWEKLE FT SDAPGIIIYEDDVQVIATPVAGRGTGATVAPARP" FT CDS complement(1386583..1390542) FT /transl_table=11 FT /gene="hrpA" FT /locus_tag="AARI_12470" FT /product="ATP-dependent helicase HrpA" FT /function="3 Information pathways" FT /EC_number="3.6.1.-" FT /note="identified by similarity to protein SP:P43329 FT (Escherichia coli)" FT /db_xref="GOA:E1VV03" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR002464" 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:E1VV03" FT /protein_id="CBT75456.1" FT /translation="MALSITYPEALPVSARREDILAAVRENQVVVIAGETGSGKTTQLP FT KMLIELGLAEKGMIGHTQPRRLAARTVAERIAEEMGTEIGEEVGFHVRFTGEVSRKTKL FT KVMTDGILLAEIKRDKLLKKYSAIIIDEAHERSLNIDFLLGYLKQIMPKRPELKIIITS FT ATIDPQRFAEHFGKALPSGEIEPAPILEVSGRTFPVELRYRPLQAEPALEEDEAAENSL FT EEERDPLDAVTDAVKELSREAPGDILIFFSGEREIRDAAEALRAMVTANKRLPRYEVLP FT LFARLSLAEQHRVFHPGGAPRIILATNVAETSLTVPGIKYVIDTGTARISRYSHRTKVQ FT RLPIERVSQASANQRSGRCGRVSEGIAIRLYAESDYESRPQFTDPEILRTNLASVILQM FT ISMGVVASATEVSSFPFVQPPEAKAITDGVNLLRELGALEQNKAAKLTETGRALAVLPL FT DVRLGRMIVESAQRGVAKEVMVLAAGLSIQDPRERPSEETGQRDRAVELHKRFADDKSD FT FIALLNLWAYLQEQQKELSSSAFRRLCKSEFINYLRVREWQDLFTQLRQLAKPLGITIP FT AAPIDPAANEDAVHKSLLSGLLGHIGLYDERKRDYLGARGTRFAIFPGSGLFKKSPTWV FT MSAELVETSRLWARTNAAIDPAWVEELAPHLLKRTHSEPHWSKRTGSVMGYEKVTLFGL FT PIIPRRQFHYWRVDKDLARELFIRHALVEGDWRTHHKFFAKNRALLEEVEELETRMRRH FT DLRISDEDLFAFYDARVGAEVYSERHFDRWWKQARATDPTLLDFDPEALLVEGDSVDER FT AFPTTWQLGSIHLPLSYEYNPAAAAGEGDGVSLSVPVVFLNQLDPARFAWLIPGLRHEL FT LTALIRSMPKAIRKNFVPAPDVAGKALAMLEADFDPATDDLAESLALVLRRLRGMVVDP FT SVFDFSTLPAHLRFGFTVTDGAGKVLGSGDDLAALQYKFAAANRAALASGVNSPGAATG FT KPAVPGKPAAASKGQSKKKGAAATASAASGAWDQKSLDHWPQLASAGETLGDTLPAKVT FT TTVMGQQITAYPGLMDTGEKVDLSVFRTESERDAAHRTGVIRLLMLRLPPAGKFVISHL FT KNAEKLVFTQNPHGSIEKLIADCTMAAVDQLVPEKLPMNRAEFEALFEAVRAEQIDTVF FT TITAIVAKVFGSSTRINKDLKSTNSLAMFAAVTDIRSQLEQLIYPGFIAATGAAHLMRL FT PRYVQGIETRLEKLRGGAVTRDSQALVVIQKLEDEYDAALDRVPAGARVPAGLAQVKWM FT LEEMRISLFAQELGTAYSVSEKRIRKAIKDGLEQL" FT CDS 1390941..1391936 FT /transl_table=11 FT /locus_tag="AARI_12480" FT /product="putative sugar ABC transporter, substrate-binding FT protein" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-2 (CUT2) family (TC 3.A.1. FT 2.z). ABCISSE: ABCISSE: ABC transporter, binding protein FT (BP), MOS-family (monosaccharides: pentoses and hexoses)" FT /db_xref="InterPro:IPR007487" FT /db_xref="UniProtKB/TrEMBL:E1VV04" FT /protein_id="CBT75457.1" FT /translation="MKSFTAMKFAAIAAAGALALTACGGSEPEGSAAGGDDAVKIGISQ FT FVSHPSLDAVVTGFKAGMEEAGYTGDKISYDENNAETDQATNTSIAGKLAADSDIDLVL FT AVATPSAQAAAQAITNIPVLFSAVTDPVDAKLVASNEAPGANVTGTSDMNPVDEQLQLL FT KELAPDAKKVGIVYSSGEANSAVQVKMAKEAAKSLGLTIEEAAVSASSEVQQAASSLDV FT DAYYVPTDNAVVSALEGLLQVAQKNGVPVISADGESVKRGATATYGINYEKLGEQTAAM FT AVKLLKGEAEPATLPVETISEVDLYLNEDAAKKVGIEFTDEMKAEAVEVY" FT CDS 1392036..1392956 FT /transl_table=11 FT /locus_tag="AARI_12490" FT /product="putative sugar ABC transporter, inner membrane FT subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-2 (CUT2) family (TC 3.A.1. FT 2.z). ABCISSE: ABCISSE: ABC transporter, permease (IM), FT MOS-family (monosaccharides: pentoses and hexoses)" FT /db_xref="GOA:E1VV05" FT /db_xref="InterPro:IPR001851" FT /db_xref="UniProtKB/TrEMBL:E1VV05" FT /protein_id="CBT75458.1" FT /translation="MITAVELGLIYAIMALGVYLTFRILDFPDLTVDGSFTTGAAVASV FT GIVNGMNPWLATVLAFFAGMVAGVITGLLHTKGKIDGLLAGILTMIALYSINLRIMGKA FT NTPLLGEDTLISPMRASGILGSWASVSILFAVCLVFVAAIVWFLHTELGMAMRATGDNQ FT EMIRSFGVSTDNQKILGLALSNGLVALSGAVIAQYQGFADIGMGIGLILIGLASVIVGQ FT AIFTQRYIWLAAIAVVFGAVIYRLVIQMALSAGLEVNDMKLISAVLVVLALLLPKWKGF FT QKVLKSVKKRPQPVTESKEEVRTNA" FT CDS 1392949..1393740 FT /transl_table=11 FT /locus_tag="AARI_12500" FT /product="putative sugar ABC transporter, ATP-binding FT subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily (TC 3. FT A.1.y.z). ABCISSE: ABC transporter, ATP-binding protein FT (ABC), NO family (NO family systems represent few ABC FT proteins with unknown function and which are apparently FT unrelated to existent families)" FT /db_xref="GOA:E1VV06" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VV06" FT /protein_id="CBT75459.1" FT /translation="MLEIKNLSRTFFPGTVNERKALRNINLNLADGEFVTVIGSNGAGK FT STVLNMVAGKLQPDVGSVTIAGKNVTKLADYKRAKYIGRVFQDPMAGTAPTMSIEENMA FT LAYARGRFRGLGLGVGSKRRELFVEELKSLELGLENRLKTKVGLLSGGQRQALSLLMAT FT FSKPKILLLDEHTAALDPQRAALVSRLTKEIVERHQLTTLMVTHNMEQALQLGTRLIMM FT HDGQIILDLNQEEKSKMTVQDLLDEFGKIKGAQLDDKTMLQ" FT gene complement(1394121..1394615) FT /pseudo FT /locus_tag="AARI_12510" FT /product="truncated hydrolase" FT /note="similarity with haloacid dehalogenase-like proteins. FT Absence of the corresponding N-terminal section" FT CDS complement(1394688..1395167) FT /transl_table=11 FT /locus_tag="AARI_12520" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VV07" FT /protein_id="CBT75460.1" FT /translation="MDLVIATHRGVDIRFEGANLTSDLPYSRYVTDGDTGLEFHLRGVT FT NDETRRLDTQFYSALELWSSKIKEQGADQADPAPQMPSNSIIEPVKANITDDVGTSYIC FT VGGRIGGTGTDWDATWIYYPAPPPDTQQLILEFTISGVPTDQSCIIEWQAPANER" FT CDS complement(1395348..1396544) FT /transl_table=11 FT /locus_tag="AARI_12530" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VV08" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VV08" FT /protein_id="CBT75461.1" FT /translation="MATQRGFAVLWAASSLSNLADGVAFIAVPLIAASLTQDPRLIAGL FT SLCYAVVRLLFALPVGVWVDRLDRRTLFSAANVLRGIALLFLALAFHFSGPNLLVLYLA FT MAFIAILEGTADTVAIALLPQLVGDKKLDQANSQITATQLITDEFAGPPLGGVLFAFAA FT AIPLYSMGGLWAVAGLIALALPRSAPPTVDSDERQRIWAEAREGIRWLLKHRLVGALSM FT ISGLASVGYMMAFSILVLFANEKLGLDSTGYGLLLSFSALGGLAGSAITPKLRRSLGYR FT NVILGSLALGSLSLGVLAFSTTALLAGIMLALYIMHAVIWNICSLSLRQRLVPEHLMGR FT VSAASRVLGLAGLALGSTLGGFVGHVSLILAVASGAAVFVLCVGLAWIGVEKEPDSTC" FT CDS complement(1396681..1397034) FT /transl_table=11 FT /locus_tag="AARI_12540" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VV09" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VV09" FT /protein_id="CBT75462.1" FT /translation="MAGIHRRLALPEARLVVASKATVPAGFTISSPHDGYLEIYYVAVA FT PNFWGQGVARELLADVDRHAQNAGVQELRLWVIAETSRATDLYQANGYRDSGQELADET FT TGRIELLLSKTMG" FT CDS complement(1397180..1397683) FT /transl_table=11 FT /locus_tag="AARI_12550" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VV10" FT /protein_id="CBT75463.1" FT /translation="MARIEFAPLDLVVAVHQGIDVCFAGLKLSTVPPPWQEYSEDYDAV FT DSSGFEFKLRSLANDVTRELDAGFNKNLEIWNAQVKEFGASVAGRAPSLPSDIFFEHIC FT AQVEDDLGTEYVWIGGEMASFDAPWEATWIYSPAPPEDAEHLVLKFVVDGLETGHSCTM FT DLRS" FT CDS complement(1397781..1398503) FT /transl_table=11 FT /locus_tag="AARI_12560" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="5 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR008217" FT /db_xref="UniProtKB/TrEMBL:E1VV11" FT /protein_id="CBT75464.1" FT /translation="MTDSLNSHPGEPHDLNFAERLNWLRAGVLGANDGIVSVAATVVGV FT AGVTNHTAPIITAGMAAVIGGAISMALGEYVSVSSQRDSQRALVEKERQELREDPEAEL FT TELAGIYQAKGLSKHTAMQVATELTEHDALAAHLSAELNIDEEEVVNPWHAAYASAVAF FT IVGAILPMLAILLPPEEIRIPVTFVAVLAALALTGTLSAYIGGSSKHVAALRLVIGGAL FT ALAATFIIGSLLGSSGII" FT tRNA complement(1398627..1398702) FT /locus_tag="AARI_36730" FT /product="transfer RNA-Arg" FT /anticodon=(pos:1398667..1398669,aa:Arg) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 1398869..1400512 FT /transl_table=11 FT /gene="argS" FT /locus_tag="AARI_12570" FT /product="arginine--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.19" FT /note="activates arginine and transfers it to tRNA(Arg) as FT the first step in protein biosynthesis" FT /db_xref="GOA:E1VV12" 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/TrEMBL:E1VV12" FT /protein_id="CBT75465.1" FT /translation="MTPEELSAAISACLTEAVAAGEISVEVPETVRVDRPKSREHGDWA FT TNIALQLGKKAGMAPRDFAQILATRLASVPGVGAVDIAGPGFLNITLEAGAAGELARTI FT VEAGSAYGSNEALAGHVVNMEFVSANPTGPLHIGHTRWAALGDAISRVLRASGASVTSE FT YYINDAGNQMNVFARSVYNRIHGLPVPEGGYPGEYIKELGDAVLAENPELKDLEEAEAI FT PALRDAAYKAQLADIKSTLADFGVSFDVFFSETTLHERGAVADAVARLREQGHIFDLEG FT AVWLRTTDFGDDKDRVLIRANGEPTYFAADAAYYLSKKDRGFEEKIYLLGADHHGYVNR FT LKAIAACAGDDKDKNIEVLIGQLISVNGAKLSKRAGNIIELRDLINWIGADALRYSLAR FT FPADSPIALDPEQLKKNTNDNPVFYVQYAHARSAAAARNAAAKGVTRNDFDAALLTDPT FT ENELLAVLGQFPSVVAGSAEFREPHRIARYLEQVAGAYHSWYAATRITPMGEDEAIAPV FT HGTRLWLNDAATTVLANGLELLGVSAPERM" FT CDS 1400519..1401940 FT /transl_table=11 FT /gene="lysA" FT /locus_tag="AARI_12580" FT /product="diaminopimelate decarboxylase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.1.1.20" FT /note="catalyzes the conversion of diaminopimelic acid into FT lysine, the last step in the biosynthesis of lysine" FT /db_xref="GOA:E1VV13" FT /db_xref="InterPro:IPR000183" FT /db_xref="InterPro:IPR002986" FT /db_xref="InterPro:IPR009006" FT /db_xref="InterPro:IPR022643" FT /db_xref="InterPro:IPR022644" FT /db_xref="InterPro:IPR022653" FT /db_xref="InterPro:IPR022657" FT /db_xref="UniProtKB/TrEMBL:E1VV13" FT /protein_id="CBT75466.1" FT /translation="MAVSPLAPQWLQFPENINALRDIEWASGVSREAGGELSVQGISVS FT KLAEEFGTPLFVLDENDFRARAAGFKTAFDEAFKDLCGGVDVYYAGKAFLCTEVARWVT FT AEGLRLDTCSGGELAVASAAKVPAANLSLHGNNKSAAEITRAIEMGVGRLVIDSLDELE FT RVISIADAMGQTAQVMLRITPGVHASTHEAIATAHEDQKFGLSILEDGTGSSPALRAVA FT GALAAKNINLLGLHAHIGSQIFEAEGFAMVARTMLGLLHKIREIHGVQLPELDLGGGYG FT IAYTSEDQPSTPAKLAGQMAQVVSETCKELELECPRISIEPGRAIAGPSTFTLYEAGVR FT KDVQVEDASGTLHPRRYISVDGGMSDNPRPVLYDAQYTAVLASRMTQNDAIISRVVGKH FT CESGDIVVKDVYLPEDVAAGDLLAVPATGAYCWALSSNYNYLTRPAVVAVRDGQARLIV FT RRETETDLLARDMGV" FT CDS 1401941..1403227 FT /transl_table=11 FT /gene="thrA" FT /locus_tag="AARI_12590" FT /product="homoserine dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.1.1.3" FT /note="catalyzes NAD-dependent reduction of aspartate 4- FT semialdehyde into homoserine. This reaction is the third FT step in a pathway leading from aspartate to homoserine. The FT latter participates in the biosynthesis of threonine and FT then isoleucine as well as in that of methionine" FT /db_xref="GOA:E1VV14" FT /db_xref="InterPro:IPR001342" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR005106" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR016204" FT /db_xref="InterPro:IPR019811" FT /db_xref="UniProtKB/TrEMBL:E1VV14" FT /protein_id="CBT75467.1" FT /translation="MSGEKNLKVALLGCGTVGAQVARILLEDANELASRSGAGLQLIGI FT AVRNLDAKRDVALPQELFTTDAHGLIAQADVVIELLGGLEPAGEYIAAALSKGASVITG FT NKALIALEGAKLNEIAAANGAQLRYEAAVAGAIPILRPIADSLAGDRITKVMGIVNGTT FT NFILDAMDTTGAAFDDVLAEAQALGYAEADPTADVGGHDAAAKAAILASLAFHTNVSSD FT QVSTEGITEVTAADVSAAAAAGYVIKLLAIAEQAEAGISVRVYPALVRRSHPLATVHGA FT FNAVFVEAENAGDLMFYGAGAGGNATASAVMGDVVSVARQIAAGAPLPNGSINQAPTLL FT DFEAITTRYWIGLSVKDQSGVLAAIATVFGEHGVSIESMSQQVDAEAGAQLRILTHQGT FT EAALASTVEALKALDAVHSVLSVMRVEGN" FT CDS 1403229..1404329 FT /transl_table=11 FT /gene="thrC" FT /locus_tag="AARI_12600" FT /product="threonine synthase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.3.1" FT /note="catalyzes the formation of threonine from FT homoserine-phosphate" FT /db_xref="GOA:E1VV15" FT /db_xref="InterPro:IPR000634" FT /db_xref="InterPro:IPR001926" FT /db_xref="InterPro:IPR004450" FT /db_xref="UniProtKB/TrEMBL:E1VV15" FT /protein_id="CBT75468.1" FT /translation="MAHQWRGVIREYADRLPVNENTKVITLGEGGTPLVYAPALSAHTG FT NEVYLKVEGMNPTGSFKDRGMTMAMTAAVAAGAKAVVCASTGNTSASAAAYATQAGLKC FT AVLVPDGKISMGKMSQAIAHGADIIQIDGNFDNCLEVARKLSENYPVFLVNSVNPARIQ FT GQKTGAFEVVDFLGDAPDYHLLPVGNAGNITAYWKGYKEYSTEWTNEAGKVLEPVSTKN FT PIMWGFQAAGAAPIVAGHPITEPDTIATAIRIGNPASWEQAEVARDESGGQIDSVTDEQ FT ILEAHRWLSSREGVFVEPASAAGVAGLLKHHAAGNVPTGKKIVITVTGHGLKDPDWALK FT QSDGSDVAPKKVALDVVEVAGALGLA" FT CDS 1404461..1405393 FT /transl_table=11 FT /gene="thrB" FT /locus_tag="AARI_12610" FT /product="homoserine kinase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.7.1.39" FT /note="catalyses the formation of O-phospho-L-homoserine FT from homoserine. Involved in the biosynthesis of threonine" FT /db_xref="GOA:E1VV16" FT /db_xref="InterPro:IPR000870" FT /db_xref="InterPro:IPR006203" FT /db_xref="InterPro:IPR006204" FT /db_xref="InterPro:IPR013750" FT /db_xref="InterPro:IPR014721" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/TrEMBL:E1VV16" FT /protein_id="CBT75469.1" FT /translation="MTQQIALGQKLIVSPPATSANLGPGFDSLGLALEYRDRLEVGTAR FT SSSVEIFGDGADELPRDESHLIIKEMHRYWKDAGFAPVGVDLVAHNRIPHARGMGSSAA FT AIVAAYAAADALLPAEARRGTESIFQAAAAWEGHPDNVAPAVFGGLSISATNPDGSFSS FT VQVPLHPDLRAVLAIPSNGLSTEVARGALPSHIEHAVAAANSASAALLIHALSNDPSQL FT LGGTKDYLHQDYRAAAMPQSAALIAKLRDAGLAAVVSGAGPTVMTLVSSEDQVAAVQAV FT INEFSASSSVSWRAEVPKLASNGVTVEVL" FT CDS 1405728..1407995 FT /transl_table=11 FT /gene="rho" FT /locus_tag="AARI_12620" FT /product="transcription termination factor Rho" FT /function="3.5.4 Transcription termination" FT /EC_number="3.6.1.-" FT /note="facilitates transcription termination by a mechanism FT that involves Rho binding to the nascent RNA, activation of FT Rho RNA-dependent ATPase activity, and release of the mRNA FT from the DNA template" FT /db_xref="GOA:E1VV17" 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="UniProtKB/TrEMBL:E1VV17" FT /protein_id="CBT75470.1" FT /translation="MTETTSLTEGVDTKTSENKSAGLASLKMTQLQQLASQLGITGGSR FT MRKADLVKAIGDHQRGGSVAAKDDKAAQEAKAAKAEAPAEKAEAEAPAKATKARARREP FT KAAATQQAETAAPEASATEQAPAEKPVRARRTSRRVTDSGKINAPAENAEAAAQAPAEA FT PATEQAPAAEAKAPRQRRNSRNNKPVDQPAEQAAEPTEAEAENAENNGEAREERRERGN FT RRERGNRRERNNDRTAERGERAEAGEGENAEERTDRREERRERGNRRERNNDRNERNND FT RNERNNDRNDRNDRNERNNDRNDRNNDGVDSENTEDRNDRSDRNDRRERRERNNDRNDR FT NNDRNDRNNRRERNNDRNNRNRRNRRDDDEPQLSEDDVVLPIAGILDVLENYAFVRTSG FT YLPGPNDVYVTLGQVKKYNLRKGDAIVGAIRQPREGETPNPRQKFNALVQLTSVNGKKP FT EDNRERVEFNKLVPLYPTERLRLETDPKLVGPRVIDLVAPIGKGQRGLIVSPPKAGKTL FT ILQAIANAITINNPEVHLMMVLVDERPEEVTDMQRTVKGEVIASTFDRPADDHTTVAEL FT AIERAKRLVEMGMDVVVLLDSMTRLGRAYNLAAPASGRILSGGVDSAALYPPKRFFGAA FT RNIENGGSLTILATALVETGSKMDEVIFEEFKGTGNMELRLSRQLAEKRIFPAVDVNAS FT STRREEQLMSAEEVRIMWRLRRMLSGIDPQQALEVLTGKIRETGSNAEFLMLVNKTTPN FT KD" FT CDS 1408184..1409257 FT /transl_table=11 FT /gene="prfA" FT /locus_tag="AARI_12630" FT /product="peptide chain release factor 1" FT /function="3.7.5 Translation termination" FT /note="directs the termination of translation in response FT to the peptide chain termination codons UGA and UAA" FT /db_xref="GOA:E1VV18" FT /db_xref="InterPro:IPR000352" FT /db_xref="InterPro:IPR004373" FT /db_xref="InterPro:IPR005139" FT /db_xref="UniProtKB/TrEMBL:E1VV18" FT /protein_id="CBT75471.1" FT /translation="MFESVKSLLEEHAAIQAQLSDPAVYADQALARKLGRRSAQLNGIV FT EAYNKWQTATDDLEAAQEMADEDPDFAEEVQALTEELPQLEEKLRRLLIPRDENDGRNV FT ILEVKGGEGGDEAALFAADLLRMYTRFAEHKGWKVEMISFNESDLGGYKDAQVAIKGNS FT NDPAEGVYAQLKFEGGVHRVQRVPVTESQGRIHTSAAGVLVLPEVDEPEEVDIHQNDLK FT IDVYRSSGPGGQSVNTTDSAVRITHLPTGIVVAMQNEKSQIQNREAAMRVLRSRLLAHQ FT QEIIDKENSAQRASQIRTMDRSERIRTYNYPENRIADHRTGYKAYNLDAVMDGDLQPVV FT ESCIQMDEEERLAALGE" FT CDS 1409265..1410122 FT /transl_table=11 FT /gene="hemK" FT /locus_tag="AARI_12640" FT /product="putative methylase of peptide chain release FT factors" FT /function="3.7.5 Translation termination" FT /EC_number="2.1.1.-" FT /note="HemK methylates the translation termination release FT factors RF1 and RF2, which plays a pivotal role in the FT termination of translation" FT /db_xref="GOA:E1VV19" FT /db_xref="InterPro:IPR002052" FT /db_xref="InterPro:IPR004556" FT /db_xref="InterPro:IPR019874" FT /db_xref="UniProtKB/TrEMBL:E1VV19" FT /protein_id="CBT75472.1" FT /translation="MEELTAVRRQAIAALADAGVPSPGVDADLLLCHVLGISRSELKLR FT QMRGDAFDPAYRQQFTELVAARRTRIPLQHLTGVAHFRYLELKVGPGVFIPRPETETVV FT QQGIDYLHAQGIDNPRCIDLCSGSGAIAAALASEVPGSSVWAVELSEQAIGYTRANCQP FT HQVNVLHQDASQLPAELHGTMDLVISNPPYIPPNAIPREAEVREHDPQMALYGLGEDGL FT QIPRAITAQAMALLRPGGYYVMEHAEVQRESAAAMLREAGFTHVAGHEDLSGRARATSG FT YAPQ" FT CDS 1410157..1410840 FT /transl_table=11 FT /locus_tag="AARI_12650" FT /product="putative Sua5 family translation factor" FT /function="3.7.3 Translation initiation" FT /db_xref="InterPro:IPR004388" FT /db_xref="InterPro:IPR006070" FT /db_xref="InterPro:IPR017945" FT /db_xref="UniProtKB/TrEMBL:E1VV20" FT /protein_id="CBT75473.1" FT /translation="MSTTFSVSNEQEHVEGIAAAKAALAEKRCIVLPTDTVYGIGADAF FT SAQGVAMLLAAKGRNRTMPPPVLIAQSATMDGLARDIPDEARKLAEAFWPGGLTLILHA FT QPSLTWDLGETRGTVALRVPNDETALELLGQTGPLAVSSANRTGNPAALNIEQALEQLG FT DSVDVYLDGGPRGEEGDDVLPSTIIDCTGQHLSVVRSGAISIEELRVVVPGILDLGQDA FT PETSA" FT CDS 1410837..1411958 FT /transl_table=11 FT /locus_tag="AARI_12660" FT /product="putative FT phospho-N-acetylmuramoyl-pentapeptide-transferase" FT /function="1.1 Cell wall" FT /EC_number="2.7.8.13" FT /note="match to protein family PF00953. Catalyzes the FT formation of undecaprenyl-pyrophosphoryl-N-acetylmuramoyl- FT pentapeptide from UDP-MurNAc-pentapeptide and undecaprenyl- FT phosphate. Involved in peptidoglycan biosynthesis" FT /db_xref="GOA:E1VV21" FT /db_xref="InterPro:IPR000715" FT /db_xref="InterPro:IPR018480" FT /db_xref="UniProtKB/TrEMBL:E1VV21" FT /protein_id="CBT75474.1" FT /translation="MRTYVLLIAFSFTVSFLLTPIIRTLGNRFTGNQLVRERDQHQKPI FT VKFGGLAIIAAFAAGLWMASNLHFFRGVFGNDEAIRGIAYALGVIVVMGLADDMLDLKW FT WIKLAGQILIGWLAATHGIIIKSLPVGSWQIDEQWLQIVVTIFLIVLTMNAINFSDGLD FT GLAAGLAAIGAATFFVYSYVLATHVSADDYANIGALLCALLLGACLGFLPHNFNPANIF FT MGETGVLAIGMILSVAAIAVTGDVQGLEARRFRNIPAYMPMLLPMVIVFLPVLDLVLSV FT FRRLANKRSPFSPDAKHIHHRMLAQGHSVRHSVILLYLWAAVIAVSVVSIAFIPVVLVV FT PTALLFFLVAAIATWRPLVLKRVQGLRKRLGNS" FT CDS 1412128..1412562 FT /transl_table=11 FT /locus_tag="AARI_12670" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VV22" FT /protein_id="CBT75475.1" FT /translation="MNSGSARVSASSAPKSIWLPILGLSLVYSAIATAIFFLISWLVAD FT LRYALSGALAAGIVIGFFAIGILIAEAAGRIRHSWAMPAFLGVFVIKVFGIAFVLLNLG FT LPGWVNRQGFVLAAAISLVAWQVGEVRAFMKARLAIYNEE" FT CDS 1412828..1413640 FT /transl_table=11 FT /gene="atpB" FT /locus_tag="AARI_12680" FT /product="H(+)-transporting two-sector ATPase, chain A" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="3.6.3.14" FT /note="H(+)-transporting two-sector ATPase (also named ATP FT synthase or ATPase) is composed of two linked complexes: FT the F1 ATPase complex is the catalytic core and is composed FT of 5 subunits (alpha, beta, gamma, delta, epsilon), while FT the F0 ATPase complex is the membrane- embedded proton FT channel that is composed of at least 3 subunits (A-C). It FT uses a proton gradient to drive ATP synthesis and FT hydrolyzes ATP to build the proton gradient" FT /db_xref="GOA:E1VV23" FT /db_xref="InterPro:IPR000568" FT /db_xref="UniProtKB/TrEMBL:E1VV23" FT /protein_id="CBT75476.1" FT /translation="MFAFALPMASEEGGFVPPSVSDTHLPDIFPWMAEYGTGFGKQMLM FT IVLSIVLITWFFTKAIKNPKLVPGKMQYIAESGYAFVRNGIGRDIIGEKNFRPWIPLLF FT ATFFFVLLNNLFGAIPFLQLPSFSHAGSAYAMAIIIYGTWIAVGLKNHGIRYFKLAVVP FT SGVPGWIMPLMIPLEIISNFIVRPLTHSLRLMATMLAGHMIVMLAAAGARHLIVVQDSL FT AMNGLGILVIVGSVAMYFLELLIMVLQAFVFALLTAIYLQGAIEADAH" FT CDS 1413748..1413960 FT /transl_table=11 FT /gene="atpE" FT /locus_tag="AARI_12690" FT /product="H(+)-transporting two-sector ATPase, chain C" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="3.6.3.14" FT /note="H(+)-transporting two-sector ATPase (also named ATP FT synthase or ATPase) is composed of two linked complexes: FT the F1 ATPase complex is the catalytic core and is composed FT of 5 subunits (alpha, beta, gamma, delta, epsilon), while FT the F0 ATPase complex is the membrane- embedded proton FT channel that is composed of at least 3 subunits (A-C). It FT uses a proton gradient to drive ATP synthesis and FT hydrolyzes ATP to build the proton gradient" FT /db_xref="GOA:E1VV24" FT /db_xref="InterPro:IPR000454" FT /db_xref="InterPro:IPR002379" FT /db_xref="InterPro:IPR020537" FT /db_xref="UniProtKB/TrEMBL:E1VV24" FT /protein_id="CBT75477.1" FT /translation="MLHGSLNMIGYGLAAIGSAIGVGLIFAAYINGVARQPEAQRILQP FT IAMLGFALAEALAILGLVFAFVIGA" FT CDS 1414041..1414595 FT /transl_table=11 FT /gene="atpF" FT /locus_tag="AARI_12700" FT /product="H(+)-transporting two-sector ATPase, chain B" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="3.6.3.14" FT /note="H(+)-transporting two-sector ATPase (also named ATP FT synthase or ATPase) is composed of two linked complexes: FT the F1 ATPase complex is the catalytic core and is composed FT of 5 subunits (alpha, beta, gamma, delta, epsilon), while FT the F0 ATPase complex is the membrane- embedded proton FT channel that is composed of at least 3 subunits (A-C). It FT uses a proton gradient to drive ATP synthesis and FT hydrolyzes ATP to build the proton gradient" FT /db_xref="GOA:E1VV25" FT /db_xref="InterPro:IPR002146" FT /db_xref="InterPro:IPR005864" FT /db_xref="UniProtKB/TrEMBL:E1VV25" FT /protein_id="CBT75478.1" FT /translation="MNSTDFILAASESVNPLLPNPWEILVTGVGFAVLLFIVIKVIAPK FT FEQSYEDRVTAIEGGLEKAEAAQKEAEETLAQYKAQLLEARTEANRIREEARSEGAQIL FT ADLKTKATDEAARITEQSHRQIEAERVSALASLRTDVGALATELASKVVDEALQDDARA FT QRVVDKFLTDLEAQQNAGASN" FT CDS 1414595..1415407 FT /transl_table=11 FT /gene="atpH" FT /locus_tag="AARI_12710" FT /product="H(+)-transporting two-sector ATPase, delta chain" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="3.6.3.14" FT /note="H(+)-transporting two-sector ATPase (also named ATP FT synthase or ATPase) is composed of two linked complexes: FT the F1 ATPase complex is the catalytic core and is composed FT of 5 subunits (alpha, beta, gamma, delta, epsilon), while FT the F0 ATPase complex is the membrane- embedded proton FT channel that is composed of at least 3 subunits (A-C). It FT uses a proton gradient to drive ATP synthesis and FT hydrolyzes ATP to build the proton gradient" FT /db_xref="GOA:E1VV26" FT /db_xref="InterPro:IPR000711" FT /db_xref="InterPro:IPR020781" FT /db_xref="UniProtKB/TrEMBL:E1VV26" FT /protein_id="CBT75479.1" FT /translation="MASVSSESLAKALAFLEPKLALASIELPKELFAVLEVLDANAGLR FT RALTDPARDAAEKAGLLAQLLHGKVSADAEDTVAQLASTRWSSERDISDALETLAVTAV FT TAVAEQQDGASGLNKLEQDLFSFIEVVRGNHELQRALDDAQAPVEAKRALALKLVPNAS FT QTSQVLISQAVSNPRGLKPAALLERFVELVAKRQQRWIASVTSSVELSATQLSRLETSL FT NKLYGRQLKLNATIDPSLVGGLVVKVGDEVVDASVASRVADLRRALAS" FT CDS 1415534..1417171 FT /transl_table=11 FT /gene="atpA" FT /locus_tag="AARI_12720" FT /product="H(+)-transporting two-sector ATPase, alpha chain" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="3.6.3.14" FT /note="H(+)-transporting two-sector ATPase (also named ATP FT synthase or ATPase) is composed of two linked complexes: FT the F1 ATPase complex is the catalytic core and is composed FT of 5 subunits (alpha, beta, gamma, delta, epsilon), while FT the F0 ATPase complex is the membrane- embedded proton FT channel that is composed of at least 3 subunits (A-C). It FT uses a proton gradient to drive ATP synthesis and FT hydrolyzes ATP to build the proton gradient" FT /db_xref="GOA:E1VV27" 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/TrEMBL:E1VV27" FT /protein_id="CBT75480.1" FT /translation="MADLTINANDVRNALNEFASSYEPGKAERTEVGRVVAASDGIARV FT EGLPSVMANELLKFEDGTLGLAQNLDTREIGVVVLGDFTGIEAGQKVERTGEILSVPVG FT DGYLGRVVDPLGEPLDNLGPIASEGRRALELQAPGVTQRKSVHEPMQTGLKAIDAMIPI FT GRGQRQLIIGDRQTGKTAIAVDTILNQRANWESGDQTKQVRCVYVAIGQKASTIAAVRQ FT TLEEQGALEYTTIVASPASDPAGFKYLAPYAGSAIGQHWMYGGKHVLIVFDDLSKQAEA FT YRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAGSMTGLPIIETKANDVGA FT FIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGSAQVKAMKKVSGTLKLELA FT QYRDMQAFAMFASDLDAASKQQLTRGARLMELLKQGQYTPYPVEDQVVSIWAGTNGYLD FT DVPVEDVRRFEGEFIDYLRHRTDVLTVIGQTGKLENETLEAMKTAVADFKAGFFGEGDD FT KLVAAGHEEHDALDSESVDQEQIVKQKR" FT CDS 1417247..1418140 FT /transl_table=11 FT /gene="atpG" FT /locus_tag="AARI_12730" FT /product="H(+)-transporting two-sector ATPase, gamma chain" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="3.6.3.14" FT /note="H(+)-transporting two-sector ATPase (also named ATP FT synthase or ATPase) is composed of two linked complexes: FT the F1 ATPase complex is the catalytic core and is composed FT of 5 subunits (alpha, beta, gamma, delta, epsilon), while FT the F0 ATPase complex is the membrane- embedded proton FT channel that is composed of at least 3 subunits (A-C). It FT uses a proton gradient to drive ATP synthesis and FT hydrolyzes ATP to build the proton gradient" FT /db_xref="GOA:E1VV28" FT /db_xref="InterPro:IPR000131" FT /db_xref="InterPro:IPR023632" FT /db_xref="InterPro:IPR023633" FT /db_xref="UniProtKB/TrEMBL:E1VV28" FT /protein_id="CBT75481.1" FT /translation="MGAQIRVYRQKIGSTKSMRKIFKAMELIAASRIGKARTRVSASLP FT YANAITRAVTAVASQADVEHPLTTEPAQVRRAAVLVMTSDRGLAGSYSASVLKQAEHLV FT ELLREEGKEVKTYLVGRKAQAYFDFRSREYARVWTGETDSPRFETARELRDVLLEDFDT FT DFEQGGVDEIHVVYTQFKSMVTQEPTVIRLLPLEVVEDESETPTDELLPLYEFEPSPEE FT VLDSLLPRYIDSRLFNCQLQSAASELAARQRAMKAAGDNAGELIKKYTRLLNNARQAEI FT TQELSEIIAGADALNS" FT CDS 1418177..1419622 FT /transl_table=11 FT /gene="atpD" FT /locus_tag="AARI_12740" FT /product="H(+)-transporting two-sector ATPase, beta chain" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="3.6.3.14" FT /note="H(+)-transporting two-sector ATPase (also named ATP FT synthase or ATPase) is composed of two linked complexes: FT the F1 ATPase complex is the catalytic core and is composed FT of 5 subunits (alpha, beta, gamma, delta, epsilon), while FT the F0 ATPase complex is the membrane- embedded proton FT channel that is composed of at least 3 subunits (A-C). It FT uses a proton gradient to drive ATP synthesis and FT hydrolyzes ATP to build the proton gradient" FT /db_xref="GOA:E1VV29" 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/TrEMBL:E1VV29" FT /protein_id="CBT75482.1" FT /translation="MTAQLNEQVTAGAIGRIARVTGPVVDVEFPADALPAIYNALTAEL FT TLNGETKKITFETSQHLGEGLVRAVSLQATDGLVRGAEVQDTGAAISVPVGDGVKGHIF FT NVLGDALDVDNSEIQVTERWPIHRQPPKFSELEGSTEMLETGIKSIDLLTPYIKGGKIG FT LFGGAGVGKTVLIQEMITRVARNFGGTSVFAGVGERTREGNDLWVEMDEANVLKDTALV FT FGQMDEPPGTRLRVALSALTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPS FT AVGYQPNLADEMGLLQERITSTKGRSITSMQAVYVPADDYTDPAPAATFAHLDATTELS FT REIASRGLYPAIDPLTSTSRILDPQYIGQDHYDVAIRVKAILQKNKELQDIIAILGIDE FT LGEEDKIVVARARRIQQFLSQNTYTAKQFTGVEGSTVSIKDTIEGFKAICDGELDHIAE FT QAFFNIGGLDDVERQWAEIQKAS" FT CDS 1419625..1419894 FT /transl_table=11 FT /gene="atpC" FT /locus_tag="AARI_12750" FT /product="H(+)-transporting two-sector ATPase, epsilon FT chain" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="3.6.3.14" FT /note="H(+)-transporting two-sector ATPase (also named ATP FT synthase or ATPase) is composed of two linked complexes: FT the F1 ATPase complex is the catalytic core and is composed FT of 5 subunits (alpha, beta, gamma, delta, epsilon), while FT the F0 ATPase complex is the membrane- embedded proton FT channel that is composed of at least 3 subunits (A-C). It FT uses a proton gradient to drive ATP synthesis and FT hydrolyzes ATP to build the proton gradient" FT /db_xref="GOA:E1VV30" FT /db_xref="InterPro:IPR001469" FT /db_xref="InterPro:IPR020546" FT /db_xref="UniProtKB/TrEMBL:E1VV30" FT /protein_id="CBT75483.1" FT /translation="MAELQVEIVAADHFVWSGAAKLVKARSVDGEIGVLPGHVPMLSVL FT AAGDLEIEPISESRFSVQIDGGFFSVDSDRVVIVADNAVLGTAA" FT CDS 1419903..1420331 FT /transl_table=11 FT /locus_tag="AARI_12760" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="InterPro:IPR019675" FT /db_xref="UniProtKB/TrEMBL:E1VV31" FT /protein_id="CBT75484.1" FT /translation="MFEITAPVLIALLILIGIAMFFGAMAVRRIQLRRTLGTFDASILA FT PNGKWIMAIGRYGGAHLDLLRFFSVSPIPSFVIERRGLDITGRREPTDEEASRIPPGFI FT IVMLDRNGEELLLAMDYRDYTGFSAWLEAGPIAGSWQI" FT CDS 1420473..1421594 FT /transl_table=11 FT /locus_tag="AARI_12770" FT /product="NAD dependent epimerase/dehydratase family FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF01370: NAD FT dependent epimerase/dehydratase family. This family of FT proteins utilise NAD as a cofactor. The proteins in this FT family use nucleotide-sugar substrates for a variety of FT chemical reactions" FT /db_xref="GOA:E1VV32" FT /db_xref="InterPro:IPR005913" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VV32" FT /protein_id="CBT75485.1" FT /translation="MLRTLILGGTGWLGSELAQQLVEAGHEVTALARGVAGTVPDGVRL FT VRADRSLPGAYDTVSRSEWDEVIELSYEPAFVEEALAALSAHAAHWTLVSTVSVYANQQ FT QPAANEDAAVYEPRDLGDYGQAKVAAERTSEQVLGERLLIARPGLITGPKDPTDRFSYW FT VSRLALAGAAQVLTPAVQGRYVQVIDVRDVAAWIIDAGQRELQGVVNVVGTPRPLADVL FT DTAAQVAGFTGELVAAEDQWLQDHQVSYWPGERSLPLWLPREDFGFLQRGNQRYKSAAG FT PERDMTDLLADILADERARALDRERRAGLDRGKNWNCWQSLPAGARRPRGIRPCGSSGP FT AAGQRPGPAHRRRIHSAATLPHRPGRSARPGWQ" FT CDS complement(1421458..1422666) FT /transl_table=11 FT /gene="nagA" FT /locus_tag="AARI_12780" FT /product="N-acetylglucosamine-6-phosphate deacetylase" FT /function="1.1 Cell wall" FT /EC_number="3.5.1.25" FT /note="catalyzes the hydrolysis of N-acetylglucosamine-6- FT phosphate to glucosamine-6-phosphate and acetate" FT /db_xref="GOA:E1VV33" FT /db_xref="InterPro:IPR003764" FT /db_xref="InterPro:IPR006680" FT /db_xref="UniProtKB/TrEMBL:E1VV33" FT /protein_id="CBT75486.1" FT /translation="MTTTRYALYATLISDGLKVTDGVLAVDGDRIRFAGNRDDFNALAD FT ADQYPVREVAPGSIIIPGLIDLHCHGALGADFSAPDHSSAAKAIAHLHRSGTTTLLASL FT VTAEPTAMIEAAELLAELAEAGQIAGIHAEGPFLSEARCGAQDPRYLQAPDPDFVSELV FT AASRGQLRTMTYAPELAGSEELIEQLVSQGVVPSLGHTNASAQCTADSLRFAREQLRSA FT GVDGFTERPTVTHLFNGMPPLHHREPGPVAACLEEAVNRNAFVELIADGVHLSPDTVRL FT VYRLVGAENILLVSDSMAATGLADGQYTLGPQEVNVAMGQARLASDNSLAGGTCTLLEV FT LQRAVQAGVSPVQAVTSATAIPASLIGLADEVGSLHYGFAADALVLDADLQLVQTIRKG FT EYL" FT CDS complement(1422846..1423592) FT /transl_table=11 FT /locus_tag="AARI_12790" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VV34" FT /protein_id="CBT75487.1" FT /translation="MDPLTASLMAIGSGSAAGLRPYFTVLALGIAGLAIPDTAPEMISS FT AARQIPESITNPWVLGICAVLAIGEAGVDKIPFLNLSMESISVWLRPIFGALVGIGLGA FT NSGVEVAILTGLLGAGSALSVSLGKSSVTAATNVVPEPITQWIRSLIEDFGALILVFAA FT VLLPVLAAALGLAAVLIGFFLYRMFRKVYRAMKNRFGSVKEHQAAAQAARQAQAQAGEK FT NSATQTLRRLAAGADPSRQPPSGTSS" FT CDS complement(1423756..1424451) FT /transl_table=11 FT /locus_tag="AARI_12800" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR002793" FT /db_xref="UniProtKB/TrEMBL:E1VV35" FT /protein_id="CBT75488.1" FT /translation="MRLVVAKCSVDYEGRLRAHLPLATRLIMVKADGSVLIHSDGGSYK FT PLNWMNPPLTLHEVEPGEDAAAMGATATWTVSSAKTDDKLTINFHSFEHDSAHILGTDP FT GLIKDGVEADLQRLLAEQIELLGTGHQLIRREYMTAIGPVDILARDAKGATVAVELKRR FT GDIDGVEQLTRYLELLNRDPLLKPVTGVFAAQQIKPQARTLAEDRGIRCLTLDYDAMRG FT VDDSAGRLF" FT CDS 1424511..1424882 FT /transl_table=11 FT /locus_tag="AARI_12810" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VV36" FT /protein_id="CBT75489.1" FT /translation="MPRSNRPRRSNNSRPAKGRNQGSGSGFRDGGQDDGSDQEEWMQRA FT RFGVVLRQDAPDGQWHVRKIAPLNANKTYTCPGCHRPIGIGVAHVVAWRADHWSGDDAA FT ANARRHWHPHCWETRSYRY" FT CDS complement(1424905..1426275) FT /transl_table=11 FT /locus_tag="AARI_12820" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="9 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR002549" FT /db_xref="UniProtKB/TrEMBL:E1VV37" FT /protein_id="CBT75490.1" FT /translation="MEQDQPRPHRNKHAPEKSLDGSEHAAKPVASGQESPAHSQPHEAN FT SQPASPASPAAQVPRSPASTPTSNDDVREGWTKKIAGKVGKILNNPQHAPAPGEESAAL FT LEGSPEPIPALHPIAMGFLGTIGVGIALGGFYLLTNVGSLMTWIAIALFIALGLDPIVR FT FLMRRGLSRPLAVAATMVSLLAIFGGFMALIIPTLVNQITAFITRAPEIVDDFLKSEWV FT VEIDRQYAVSERIMTEVDRFFGDSGAVTNVFGGVLGVSQTVAQSMFGVLIVLVLAIYFL FT ASLPGMMSFSLRLTPRSKRERVAELTVRITRSVGNYVMGQATVAILNCLLALILMSILG FT VPFTALLTLLVALLAFIPLVGGVIAGVLVTLVTLSLGWQTALIYAICYFGYLQIEAYFV FT SPRIMRRAVALPGAVAVISVIAGGSLAGVTGALMAIPVAASAMILLHEVFVARQDRR" FT CDS 1426455..1428167 FT /transl_table=11 FT /locus_tag="AARI_12830" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VV38" FT /protein_id="CBT75491.1" FT /translation="MIAMLLGAAALVVGIGQKTFWAPPETVTANMPQLTDEAPLTLIES FT SVNSPKLDPVELVITAKGEFTASLGRDYDVAAWIGDAAHVSVTGIDTENHKMIAEYTKG FT KGEVPNPAGADIFFDSQTADKTMTYRWTAPDTGDWSLLLAAGGKDAAPVDISVTYANDD FT AMPFAVPLIIAGSVLLVFGLALLIMRPAKPKTGTNTQHSVAVAAVLALAISGVSLPMAP FT SDDSSASPSESAQKSDEAKKSDDSKKPEDEKASEEAPSSASASSSVEETASFPVITEEQ FT LKRVLADAQEQISKADDKTSSKALDSRSAGAFKYLRNKRYEMLKEKFKVDKPLALTTQV FT IRSAAVPNASEAKFPRVISVVTAKNNDADTLPQALTLVQENARDNFKVVFAGQMLPNST FT FPGIAVGDPSTTQLKADSKGLQMTPEKALEALAKVLSDDGAKEKSKFAKSDFIAAVHSA FT QKDEAKAANEAKVTYKRSVTEGDTKVVSTPDGGAIVTGKLNNKARFIRTEDADPLESKD FT KLTEQLLGSSSSNGDVESTYAEPVMFYLPADGSKDKIQLISASQVLLDVKEVD" FT CDS 1428173..1429084 FT /transl_table=11 FT /locus_tag="AARI_12840" FT /product="putative thioredoxin" FT /function="4.6 Miscellaneous" FT /db_xref="GOA:E1VV39" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:E1VV39" FT /protein_id="CBT75492.1" FT /translation="MTDQNIPSTRGAVDLSALAHQGSEATQSAPAAAASWTTNLDQGAF FT EQFVGMSQQVPAIVSLGSPRVQVSVDLDATLRKLVDAKGGKFILGLVDAETYPQIAQAF FT QAQQIPMVVALIKGQPVPLFQGPAAEEQIVQVFAQLEQLAVQQGMSGTAPAFSGEAQQG FT EPELPPLHQKAVDAIDAGDYAAAEAAYLEALNEKPNDKDAQIGVYQVRLLSRTHNLDLA FT KSRDKAAQNPDDIAAQLDVADLDVVGGHVEDAFGRLVSLISRLADEDRERVRRRLIELY FT AVIGNNDPRVAASRQKLARVLF" FT CDS 1429220..1429978 FT /transl_table=11 FT /locus_tag="AARI_12850" FT /product="putative drug resistance ATP-binding protein" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TC 3.A.1.y.z. ABCISSE: ABC transporter, ATP-binding FT protein (ABC), DRI-family, DRB-subfamily (drug resistance, FT putative). Possible function in drug efflux" FT /db_xref="GOA:E1VV40" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:E1VV40" FT /protein_id="CBT75493.1" FT /translation="MNQIALDIRGLAKQFGAKIAVNNVSLQVPAGSFYGLVGPNGAGKT FT TMLSMATGLLRPDSGQALVNGVDIWADPQTAKATLGVLADGVRQFDRLTGRQLVTYSGL FT LRGMDRAEVAQRTEDLLRVMDLVSDGDKLVVDYSAGMTKKISLATAMIHSPKLLVLDEP FT FEAVDPVSAANIRDILNNYVEFGGTVIVSSHVMDLVQRMCTHVAVISDGVLKAQGTVDE FT VRGSKSLEDRFVDLVGGRANNEGLSWLRTS" FT CDS 1429960..1431525 FT /transl_table=11 FT /locus_tag="AARI_12860" FT /product="putative drug ABC transporter, inner membrane FT subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TC 3.A.1.y.z. ABCISSE: ABC transporter, permease FT (IM), DRI-family, DRB-subfamily (drug resistance, FT putative). Possible function in drug efflux" FT /db_xref="UniProtKB/TrEMBL:E1VV41" FT /protein_id="CBT75494.1" FT /translation="MVAHVLSLKLRLLANGFKRSIGQLIGVIIGGLYALGMIVMLTLAV FT WFTAGEIPFQADIFTLIGSAVVLGWAIIPPLLTGVDLTLEPSRFVHFGIPEKTLGPALV FT LAGFISIPAALTIVGLIGASLMWRLDAAALTLALVAAIATAVMAILLCQYLVIMATALR FT AKRRFRELTFVLLFVVLVGLGPILSSVFSAALSLGDWVSPIAAVLGYTPLGAFAAVPGA FT FAAGLYGQMAIHLLLGVIYLGGLYLLLARATAKATVTPPPEQRAATAKGLGFFKLLPAT FT PTGAVAARALTYWLKDPRYAIGVLIVPMLPLLFWFTGNQTGSYAMMYVLGPMIGILMGF FT SISADISYDNTAFALHALTGISGRADRAGRALSCLLVAIIPVLAAAILPGLITGSFWRI FT PGDLGLSLAALFIALGVSSVASARYTYSVPLPGDNPMKTPPGNGLRVALTQILTMLVMG FT LLLIPVLIPYVIGWVQQSQSLGFITLGAGLVLGVLLLLGGIALGGKWYEKRTPELMQAV FT MLNK" FT CDS 1431827..1432078 FT /transl_table=11 FT /locus_tag="AARI_12870" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021400" FT /db_xref="UniProtKB/TrEMBL:E1VV42" FT /protein_id="CBT75495.1" FT /translation="MVEQSEETRGGTATIERTETTQSVEAGDHERFAHYVQKEKIMESA FT LSGDPVIALCGKVWTPGRDPKKFPVCPECKEVYESLMG" FT CDS 1432134..1433900 FT /transl_table=11 FT /locus_tag="AARI_12880" FT /product="putative ATP-dependent helicase" FT /function="3 Information pathways" FT /note="possible DNA or RNA helicase" FT /db_xref="GOA:E1VV43" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR006935" FT /db_xref="InterPro:IPR014001" FT /db_xref="UniProtKB/TrEMBL:E1VV43" FT /protein_id="CBT75496.1" FT /translation="MTETLFDFGDKLPLEDKLPVAYPERAAWGTGPKLRAWQAEALALY FT FDTEPRDFMAVATPGAGKTTFALRLAKVLIDSGKINRLIVVAPTDHLKKQWADAAARVG FT ISLDPNYKNSDGRHGSHYMGVVVTYAQVALKPAVHRAKTEDARTLVIMDEVHHAGDALS FT WGDGIREAFEPATRRLALTGTPFRSDAAPIPFVQYVDEGDGIRRSKADYTYGYGSALAD FT HVVRPVLFMAYSGNMRWRTSAGEEMEANLGEGFTKDVTAHAWRTALDPHGDWIPSVLQA FT ADRRLSEVRRTVKDAGGLIIATDHEDARGYAAQLEAICGEKVTTILSDDPKASQKIDDF FT SESEARWMVAVRMVSEGVDVPRLCVGVYATSTSTPLFFAQAVGRFVRSRKRGEVASVFL FT PSVPILMALANEMEVERDHALDREGSKDEDGLDDSLLEAANKEDKASDELTRNKFEALN FT SQASFDRVLFDGGEFGTGADIGSEEELGFLGIPGLLDTEQVSELLRKQQNKQISKGATK FT PAPVSDHRLMMELRTKLSKNVSAWAARTGTPHGQIHNKLRSVCGGPAVPQATVDQLQAR FT IDKLQDWFVGRK" FT CDS complement(1434152..1434745) FT /transl_table=11 FT /gene="pncA" FT /locus_tag="AARI_12890" FT /product="putative nicotinamidase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="3.5.1.19" FT /note="nicotinamidase converts nicotinamide to nicotinic FT acid (niacin) and ammonia, which in turn can be recycled to FT make nicotinamide adenine dinucleotide (NAD)" FT /db_xref="GOA:E1VV44" FT /db_xref="InterPro:IPR000868" FT /db_xref="UniProtKB/TrEMBL:E1VV44" FT /protein_id="CBT75497.1" FT /translation="MSTALLIIDVQPDFCEDGALAVAGGNAVAAAIAADVAERKGSYSA FT IVTTQDWHIEPGDHFSENPDFIDSWPVHCVAGTPGAALHPHIAGLAVDAHFAKGRFTAA FT YSGFEARQLDPTADKADESGELLGLWLKAKGITAVDLVGLAADHCVKATALDAVQAGFA FT TTVISPLTAAVSPQGLPAVHDQLRAAGVTVLSLG" FT CDS complement(1434850..1436148) FT /transl_table=11 FT /gene="pncB" FT /locus_tag="AARI_12900" FT /product="putative nicotinate phosphoribosyltransferase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="nicotinate phosphoribosyltransferase catalyses the FT formation of nicotinate D-ribonucleotide and PPi from 5- FT phospho-alpha-D-ribose 1-diphosphate and nicotinic acid, FT this is the first, and also rate limiting, reaction in the FT NAD salvage synthesis. This salvage pathway serves to FT recycle NAD degradation products" FT /db_xref="GOA:E1VV45" FT /db_xref="InterPro:IPR002638" FT /db_xref="InterPro:IPR006405" FT /db_xref="InterPro:IPR007229" FT /db_xref="InterPro:IPR015977" FT /db_xref="UniProtKB/TrEMBL:E1VV45" FT /protein_id="CBT75498.1" FT /translation="MRTSLFTDHYELTMLQAALGSGAAHRPSVFEAFARRLPDGRRYGV FT VAGTGRMLEGLADFRFDDQQLRYLSDNKVVNAETIKYLENFRFTGNISGYAEGELYFPN FT SPLLTVESTFAEACVIETYLLSIMNHDSAIASAASRMIASAGERPCIEMGSRRTHEESA FT VAAARAAMIAGFSSTSNLEAGARYGLKTVGTSAHSFTLLHDTERAAFEAQIASLGKDTI FT LLVDTYDVEQGVRTAVEVAGPELGGVRLDSGDLVQQAGWVRELLDDLGNWNTKITVTSD FT LDEYAIAALASAPVDSYGVGTALVTGSGHPTASMVYKLVARQDDAGQWIPVAKAAANKA FT SVGGRKYAVRQLNDRNRAMAEVISTSEHTTGGPERDLVVPLVRNGEIDQSYVGAAGVKR FT ATERHYASIQELPGVARKMQRGEPVIPTVMIQG" FT CDS 1436291..1436575 FT /transl_table=11 FT /gene="clpS" FT /locus_tag="AARI_12910" FT /product="ATP-dependent Clp protease adaptor protein ClpS" FT /function="3.10 Protein degradation" FT /note="involved in the modulation of the specificity of the FT clpAP-mediated ATP-dependent protein degradation" FT /db_xref="GOA:E1VV46" FT /db_xref="InterPro:IPR003769" FT /db_xref="InterPro:IPR014719" FT /db_xref="InterPro:IPR022935" FT /db_xref="UniProtKB/TrEMBL:E1VV46" FT /protein_id="CBT75499.1" FT /translation="MTAMPDVISEFETLESQDKPWRLIVWNDPVNLMSYVAYVFRSYFG FT VSPEKAEKLMLQVHHDGFCTVRSGSREAIESDVQAMHGFGLNATMTQGA" FT CDS 1436578..1437156 FT /transl_table=11 FT /locus_tag="AARI_12920" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR018561" FT /db_xref="UniProtKB/TrEMBL:E1VV47" FT /protein_id="CBT75500.1" FT /translation="MAKAFKNGSKGITGTLHSAERKLIRELFNDVIAMLDERAQLHQLP FT EDLDPLYALTGMRPESMDLPEISDPALAKLLPNASDDAAVAAEHRRLSEADLIAQKIGR FT LREAQLLLETDKLVLDQHSATRFAQALNDVRLVLAERLEIRDEADSARVAQVLDASEVQ FT TPEEYMSLVYNLISWVLDTLMSALMDAEF" FT CDS 1437161..1438084 FT /transl_table=11 FT /gene="murI" FT /locus_tag="AARI_12930" FT /product="glutamate racemase" FT /function="1.1 Cell wall" FT /EC_number="5.1.1.3" FT /note="converts L-glutamate to D-glutamate, a component of FT peptidoglycan" FT /db_xref="GOA:E1VV48" FT /db_xref="InterPro:IPR001920" FT /db_xref="InterPro:IPR004391" FT /db_xref="InterPro:IPR015942" FT /db_xref="InterPro:IPR018187" FT /db_xref="UniProtKB/TrEMBL:E1VV48" FT /protein_id="CBT75501.1" FT /translation="MNSYFATGQVSAPEANTPIGIFDSGVGGLTVARAIIDQLPGESLV FT YVGDTANSPYGPLPIAQVRANALGVMDELVDGGVKLLVIACNSASAAVLRDARERYTAR FT YGIPVVEVIQPAVRRAVAGTKNGKIGIIGTQATVGSRAYEDAFAAAPNLQVSTVACPRF FT VEFVESGITAGAELLEIAQEYLAPLQAAQVDTLVLGCTHYPLLTGVISYVMGDSVTLVS FT SAEETAKDVFRALTRHSLVRNDGAAARHEFLATGNADSFGVLARRFLGPEVLQVRHVDH FT VAAHYPTGAIARITPQMIAASKASNE" FT CDS 1438081..1439022 FT /transl_table=11 FT /locus_tag="AARI_12940" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VV49" FT /db_xref="InterPro:IPR001279" FT /db_xref="UniProtKB/TrEMBL:E1VV49" FT /protein_id="CBT75502.1" FT /translation="MKLTIIGCTGSFPGPGSPASCYLVTAFDGTRDWKILLDLGSGALG FT VLQRYTDLKDIDGIMISHLHPDHCMDLCGLHVAIRWDPTGWGRDRMLVHGPEDTAERIE FT TAYSLPDGDTMAKDYDFQVWKSLKPVNIGPFTITPYPVRHPIKEAYALRVEAHEPGPDG FT ELLTSVLTYSGDTDSCDSLVEAARGADMFLCEAAFEEGRDDHIDGVHLTGKRAGEAAAA FT AGAERMLLTHIPVWTDINKVVEEAKEVYDGGIAVAVSGVTYGVYSGSLKDEKDPALFKG FT ERGSDYLKTLTGTMPTIKYEKTRKFPLLKRKR" FT gene 1439143..1439592 FT /pseudo FT /locus_tag="AARI_12950" FT /product="truncated protein" FT /note="C-terminal section of a conserved protein" FT CDS 1439682..1440416 FT /transl_table=11 FT /gene="rph" FT /locus_tag="AARI_12960" FT /product="tRNA nucleotidyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.7.7.56" FT /note="removes nucleotide residues following the -CCA FT terminus of tRNA and adds nucleotides to the ends of RNA FT molecules by using nucleoside diphosphates as substrates" FT /db_xref="GOA:E1VV50" FT /db_xref="InterPro:IPR001247" FT /db_xref="InterPro:IPR002381" FT /db_xref="InterPro:IPR015847" FT /db_xref="InterPro:IPR018336" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/TrEMBL:E1VV50" FT /protein_id="CBT75503.1" FT /translation="MTLRADGRGAAQLRDITITRGWSAQAEGSALIEFGNTRVLCTASF FT TEGVPRWLKGQGTGWVTAEYAMLPRATNTRNSRESVKGKLSGRTHEISRLIGRSLRAVV FT DTKALGENTIVLDCDVLQADGGTRTAAITGAYVALAEAIAWATSQGIVKQNAKVLTDSV FT AAISVGIIDGTPMLDLPYEEDVRAETDMNVVVTGSGDFVEVQGTAEGVPFKRAELDALL FT DLALGGTSELAEIQRETLGSTK" FT CDS 1440413..1441045 FT /transl_table=11 FT /gene="rdgB" FT /locus_tag="AARI_12970" FT /product="nucleoside-triphosphatase" FT /function="2.3 Metabolism of nucleotides and nucleic acids" FT /EC_number="3.6.1.15" FT /note="hydrolyzes non-standard nucleotides such as XTP and FT dITP/ITP. Might exclude non-standard purines from DNA FT precursor pool, preventing thus incorporation into DNA and FT avoiding chromosomal lesions" FT /db_xref="GOA:E1VV51" FT /db_xref="InterPro:IPR002637" FT /db_xref="InterPro:IPR020922" FT /db_xref="UniProtKB/TrEMBL:E1VV51" FT /protein_id="CBT75504.1" FT /translation="MSKPVLVLASRNQGKLRELRELLRGQVPGLDVDTQVVDAATAGAG FT DPVEDQVTFQGNALKKAREISASTGLVALADDSGLSVDVLGGAPGIFSARWSGVHGNDE FT ANIDLLLGQLGDIAAEHRGAQFVCAAALATPQGEEHVELGKVQGVLRTERSGEHGFGYD FT PIFEPAGAGKTMAEHTAEEKNAISHRARAFAALLPAIIDAVGKALAK" FT CDS complement(1441126..1442031) FT /transl_table=11 FT /locus_tag="AARI_12980" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VV53" FT /protein_id="CBT75505.1" FT /translation="MRRRHPQVINPGLFAGSNDHAVYWCRQQNPLASAAALARGDEDFE FT WSLRHPLKPGDLIVTALESSPPLIVSLEVIEEDENEEITYRNLAIFSDPISVIDAQHLI FT GAQLPRRSQYLKQPLAEKLLESMGALIADPRPIFITAGPCDALQSAQANEVLSVLAVLQ FT KGSPWEQLECRICDREILDEPEAHLPHVDQHGLRWEIQEHVDEAVLMCSDCHDMAHQPT FT LQQLRNYARPACPKCGERNPRQIIWGMPAFIPDPDDFVVAGCVLPMGPMAQWECRACSS FT RYLVADAGELAYPELMVHHE" FT CDS 1442625..1442984 FT /transl_table=11 FT /locus_tag="AARI_12990" FT /product="putative GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF00392. This FT family of regulatory proteins consists of the N-terminal FT HTH region of GntR-like bacterial transcription factors. At FT the C-terminus there is usually an effector- FT binding/oligomerisation domain. The GntR-like proteins can FT be divided into six sub-families: MocR, YtrR, FadR, AraR, FT HutC and PlmA. Many of these proteins have been shown FT experimentally to be autoregulatory, enabling the FT prediction of operator sites and the discovery of cis/trans FT relationships" FT /db_xref="GOA:E1VV52" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VV52" FT /protein_id="CBT75506.1" FT /translation="MIDDSKPIFLQIAELIENDIISGVLAEEAQVPSTNEFAAFYRINP FT ATAAKGINRLVEDGLLYKKRGIGMFVTKDAPRRLREQRRQKFQQQFITPLTAEATKLGI FT GLEELVTMIKTGSDS" FT CDS 1443014..1443931 FT /transl_table=11 FT /locus_tag="AARI_13000" FT /product="putative ABC transporter, ATP-binding subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily (TC 3. FT A.1.y.z). ABCISSE: ABC transporter, ATP-binding protein FT (ABC), NO family (NO family systems represent few ABC FT proteins with unknown function and which are apparently FT unrelated to existent families)" FT /db_xref="GOA:E1VV54" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:E1VV54" FT /protein_id="CBT75507.1" FT /translation="MSRTTAIAVRELSKTYKDVRALDNVTLDLEPDRIYGLLGRNGAGK FT TTLMSILTGQNYADHGTAEIFGHAPFEHDPTLSRICFIRESQKYPDDFKVFQAFKSAAL FT FFENWNEQLAQDLVQAFDLPTKRRIKKLSRGQLSAVGVIIGMASRADITFFDEPYLGLD FT AVARQIFYDRLVEDFAEYPRTIVLSSHLIDEVANLLEHVIVIDKGRIVIDSDAEQLRGT FT AVTVTGDAAKVQEFAGSAPVIHRDALGALSSVTIRATLDSDQREQAKLMGLDLSPVSLQ FT QLVVRSALSNTTERGLDERTEARK" FT CDS 1443928..1444623 FT /transl_table=11 FT /locus_tag="AARI_13010" FT /product="putative ABC transporter, inner membrane subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TC 3.1.y.z. ABCISSE: ABC transporter, permease (IM)" FT /db_xref="UniProtKB/TrEMBL:E1VV55" FT /protein_id="CBT75508.1" FT /translation="MNRIIKVARMQLINKATFIGIPLIILGASFLFTLIIWWLVRRNGA FT EGIMYGGGAQAPMWYFLALGIQALTLTFPFSMAMSISRRSFYLGTVALFSVCALVLSVF FT YYLMGLVEKATGGWGLDGRFFALQWVADNNWFIQIMFYFVLMLLLFMVGFLVATIYMRW FT RTTGMVVFFVALGVVVLGIIALFTFSDYWDQFWSWALTWTAAGVTLWGGLVALLMAGGS FT YLTLRRATA" FT CDS 1444814..1445311 FT /transl_table=11 FT /locus_tag="AARI_13020" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VV56" FT /db_xref="InterPro:IPR013538" FT /db_xref="InterPro:IPR023393" FT /db_xref="UniProtKB/TrEMBL:E1VV56" FT /protein_id="CBT75509.1" FT /translation="MSAIATGTRTAHGALELRREFTESPSKIWRYLADSEYLALWYGSW FT QGDPERGVVDVVLLAEDGAPAEEVQILHCDVRNHQLQVRLGTDQTAWQLELMVEAAGMG FT SRLVFQMLALDPQLAGSVGPGWDYYLDRLVAAVSGNDPASVEFEPDYYPALSPYYEELF FT RN" FT CDS 1445525..1446526 FT /transl_table=11 FT /locus_tag="AARI_13030" FT /product="putative DNA polymerase III subunit epsilon" FT /function="3.1 DNA replication" FT /EC_number="2.7.7.7" FT /note="DNA polymerase III is a complex, multichain enzyme FT responsible for most of the replicative synthesis in FT bacteria. The beta chain is required for initiation of FT replication once it is clamped onto DNA. DNA polymerase III FT contains a core (composed of alpha, epsilon and theta FT chains) that associates with a tau subunit. This core FT dimerizes to form the POLIII complex. PolIII associates FT with the gamma complex (composed of gamma, delta, delta, FT psi and chi chains) and with the beta chain to form the FT complete DNA polymerase III complex" FT /db_xref="GOA:E1VV57" FT /db_xref="InterPro:IPR001357" FT /db_xref="InterPro:IPR006055" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR013520" FT /db_xref="UniProtKB/TrEMBL:E1VV57" FT /protein_id="CBT75510.1" FT /translation="MALDFTAIDFETANGFIGSACSVGLVKVRSGQIVETEQWLMQPPA FT GFDHFDPRNISIHHITSDMVSDAPRVSQKLPDLLEFIGSDVLVAHNSSFDSGVIRAASE FT ASELPVPQIAHLCTVKLSRKAYDLPSYSLPFVAEEAGHPIENHHEALADSLACAWAMID FT IAQRSGRQSVLETADHYGVRLSLTQSWQPGDELSRATRDAQGWLAAGNQMPPQDAFNNW FT PQEGPNPDPNQNADPSHPLFGQTMVFTGNLSMPRPKAKELAAEHGAQTASRVTRATTAL FT VVGDGFVPQDLANGRLTNKAKHVLRLREKGQRVSIISEGEFMQMVGGFGLTA" FT CDS complement(1446607..1447542) FT /transl_table=11 FT /locus_tag="AARI_13040" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR005502" FT /db_xref="UniProtKB/TrEMBL:E1VV58" FT /protein_id="CBT75511.1" FT /translation="MNETGETALLPENYSDKVFAILLGLADGATHARDDIDLGATEILP FT LYLADGLLEALEWANDGVASDEAACMWLAALRGYNKITGSFPDRAPEPLGRWIDKEFAH FT VEIFEKIQDGDPQNLTGLDSADMGQPGRPTGPGTDTTGVLPRAAVAALLGRVPMGTTET FT LARAAAFLTHDAQAAKTTIAAAKIIRLAMERSEEAAGLWAELLADLEGPSADALREVVA FT KISENISLSSEDAYNAYFGENAPEQAEESDIEAAPAAIEEESARDPEVDAYAVALLAAV FT YGSEAVGERPASALDDIISELHDRWMALLV" FT CDS 1447594..1448760 FT /transl_table=11 FT /gene="sbcD" FT /locus_tag="AARI_13050" FT /product="putative nuclease SbcCD subunit D" FT /function="3.3 DNA recombination, and repair" FT /note="SbcCD cleaves DNA hairpin structures. These FT structures can inhibit DNA replication and are FT intermediates in certain DNA recombination reactions. The FT complex acts as a 3 ->5 double strand exonuclease that can FT open hairpins. It also has a 5 single-strand endonuclease FT activity" FT /db_xref="GOA:E1VV60" FT /db_xref="InterPro:IPR004593" FT /db_xref="InterPro:IPR024654" FT /db_xref="UniProtKB/TrEMBL:E1VV60" FT /protein_id="CBT75512.1" FT /translation="MRLLHTSDWHLGRTFHGASLIEAQRAVLQEIIDITINQQVDVVLI FT SGDIYDRALPHVDAVQLCNWVLRELRATGATVVITSGNHDSASRLGFGADLLDSAGVHI FT IADLERMLRPVICQAEDHQVAIYGIPYLEPRMVMERLGATHASHEAVVSAAITRIQENL FT EQQRQAGTPVVSIAMAHLFAAGGIGSDSERELSTGNLDVVSAELFENFDYSALGHLHGR FT QKVKDNVRYSGSPLAYSFSEAKQIKGVWVIDTSAQGIESIQEVLLAVPKDLAILKGNLE FT DLLDDEQFEYAVAAWCQVTLTDRERPADAMARVRTRFPDTVVLNFAPEGGDENEEPSTY FT AERMAKATSTEQVVGDFMEHVRERAADEAEREVITSVIRATREAKVSQ" FT CDS 1448757..1451828 FT /transl_table=11 FT /gene="sbcC" FT /locus_tag="AARI_13060" FT /product="putative nuclease SbcCD subunit C" FT /function="3.3 DNA recombination, and repair" FT /note="SbcCD cleaves DNA hairpin structures. These FT structures can inhibit DNA replication and are FT intermediates in certain DNA recombination reactions. The FT complex acts as a 3 ->5 double strand exonuclease that can FT open hairpins. It also has a 5 single-strand endonuclease FT activity" FT /db_xref="UniProtKB/TrEMBL:E1VV59" FT /protein_id="CBT75513.1" FT /translation="MRIHKLQIQAFGPFAGTEEINFDELAEGGLFLLDGPTGAGKSSIL FT DAICYALYGALPGSRTGSRQIRSDHAPTGLAPEVSCELTIGDRRFEVTRSPAWMRPSKR FT GKDKTTEQKASSLLREFTASGWNELSTRNDEVGHVLGSLLGLDREQFTKVVMLPQGGFA FT DFLRAKAKDREDLLANLFDTSDYAQIEEEFSARLAEERQKTESLEARLSASEEAIHAQA FT QSFLAGRESNAQDEASEDTEDSAQAAHATVAEQFADYQRRISVIHQRAASEAAALRAQR FT TGLREQVQSVEERQRIFARLAELRSKQAAYAQQHEAALSAGARLEKDAKAGAVRAYLTQ FT LNEAKATEQKIKDTWLASQQWLEKEQGLAPRIDIAGLESLRRPAHEAAEALAIAKAALE FT DEKRREVLAAQGEKAAELVGVHAKTRTEAEEEVLRLKTEREALEAQDLDQGAATEKVQQ FT AKDRVLGLETKIGHATERDGLEKKAMSAREKASAQELKIVDAANSLLDLRTEQLAQSAL FT RLSAALEDGKPCMVCGSEEHPAPAQADAGAPLIDDEQIQKLDAIVAAARVAGQQAAQTR FT DTLMAKLQAAQEAAGDQMVAELRVELEAAQAELEQARQKHNEISVRISKLDKVRRRVEE FT QNARAAQAVLEHSAAQHNAQTLQAQLEELDAKLVQLRQGKNSLSELVEQQTKTSNGLGN FT AFQNLRRLLEASQALERATATWDAERTAAGFAQLAEYEAALLEASQREQLRQLQRADAD FT LASAIATLESSEDCRKAQELSSQGIQAPGEDELVEARLLATAADERFEAAREQEVLALT FT QLTRHEQATGDLERQRADAGPVIETYRRLRGLAEVIRGGGENLYKMTLSTYVLAARLEE FT VAIAATQRLAVMSAGRYSLHHDDSKQGNAKSGLGLQILDSWTGKRRETQTLSGGETFMA FT SLALALGLADVISHHSGAVDMQTLFVDEGFGSLDAETLEEVMQALENLRAGGRTIGLVS FT HVAEMKQRITNRVSVIKTQHGSTIAREGTVILAG" FT CDS 1451941..1453215 FT /transl_table=11 FT /locus_tag="AARI_13070" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VV61" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VV61" FT /protein_id="CBT75514.1" FT /translation="MTQHTLSKEDHEGSEKMSGYSALVPLVGAPFLPLTFLARLPLAML FT TIGSMTLVTATTGSYALGGLAAAMVGLGSAVGGPSIGYLADRIGQRPVLTTVALIHTIL FT LVALTIFSNSSPEMSVAMLSVMCLAAGATGPQVGPMSRVRWIAMTRQQKKNPKVLSAAL FT SLESMFDELGFVFGPVAVGLLASLVDPVLPLYLAALLTLVLVPVFAAHHTVGAVKPVKT FT ATHAPKVAISRAQVAAISALVLGMMALGTVFGSSAAGTLAFAGAQGDSNQGGLLYGAMG FT FSSAIAAISVAAWPQAFRQINRWILCGAALTVLSFGLHVASNVPMMLVALFIAGFAVGP FT VIVTVMTLGGEVAPPQRLSTVMTMLSAGIVVGTAIGNGLAGVFAESLGYLGAFWVSTGG FT ALVIFLAAVAMKAIVAKAPSLARVR" FT CDS complement(1453321..1454016) FT /transl_table=11 FT /locus_tag="AARI_13080" FT /product="IclR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF09339: IclR helix-turn- FT helix domain. This family of bacterial transcriptional FT regulators groups several proteins, including gylR, a FT possible activator protein for the gylABX glycerol operon FT in Streptomyces, and iclR, the repressor of the acetate FT operon (also known as glyoxylate bypass operon) in FT Escherichia coli and Salmonella typhimurium" FT /db_xref="GOA:E1VV62" FT /db_xref="InterPro:IPR005471" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014757" FT /db_xref="UniProtKB/TrEMBL:E1VV62" FT /protein_id="CBT75515.1" FT /translation="MPTSQTLSRGIRVLEIVASSPVNLSIAEIAAKLEVHRSIAYRIIR FT TLEQHHLLNRDEAGHIRSASGLAVLARSVQRDLQAAATPELTALANELSMTTFVAVWEH FT DLCTTLQSVSPLNSQRAIVHRPGSVHGMDVGAAGIAIQSRYTKAEWDALDTRIQYREPA FT IAARQAGYATSADEVIQGVTSIAVPIQHAGQTPAALAVVFATSTVDSYERTIEELQHAA FT ARISEKLAH" FT CDS 1454280..1455620 FT /transl_table=11 FT /locus_tag="AARI_13090" FT /product="MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (MFS), metabolite:H+ FT symporter (MHS) family (TC 2.A.1.6.z)" FT /db_xref="GOA:E1VV63" FT /db_xref="InterPro:IPR005829" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VV63" FT /protein_id="CBT75516.1" FT /translation="MSSTASRTQEERRVLAGTLVGTTIEWYDFFIFAQLTATLLTPLFL FT EPLGEANPGVAQVLSFAMIGISFFFRPLGAVVAGHLGDRYGRKRILVLTLILMGVATAA FT IGLLPTYASIGIAAPILLVLLRVIQGFSAGGEWGGAALMAVEHAPEHRRGYFGAYPQIG FT VPIGMILATGLLYILRVALSPEAFTAWGWRIPFLLSIALIFVGYMIRRAVEESPVFKQL FT SLRKASEHTPLRELMTGHTKQVLQAALIFISNNAAGYLVIAFFISYTTKVLEMPLAPIL FT LATTIGSVGWLIFTLVGGWLSDKIGRRATFVIGYALVFVWMIPMFLLVDTGNIVLYGVA FT IFVLTVGLGLSYGPQSAMYAEMFPAHIRYSGISIGYAIGAILGGAFAATVAQILLETTG FT ASISIAIYIMVLTVISVAAVLWVGETRGRNLHVEEIEGEQAESRVAH" FT CDS 1456546..1457043 FT /transl_table=11 FT /locus_tag="AARI_13100" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VV64" FT /protein_id="CBT75517.1" FT /translation="MTVTPEEERAFIEQSAKEFAELDATGGVTLPDGSFYRMDVDQLVQ FT KLAMVEDGLSVSSSQIAAGGQIGRAAVSWDWNSFGSCVAKEMGIKAAVELAKVFAEPKV FT RKALKSKQWRKASSIAYARLKKISPKVAKLIIKKAANSVLPGGIVTVIAIPVGKCAIKE FT LF" FT CDS 1457063..1457314 FT /transl_table=11 FT /locus_tag="AARI_13110" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VV65" FT /protein_id="CBT75518.1" FT /translation="MTDFFRSLSKRATAILIAFVILVLIAVPTALLSGLLSGVFESPAE FT GMRVFFIMVGAGVLFLIVELFIENGRERRKKKASSAQK" FT CDS complement(1457507..1458514) FT /transl_table=11 FT /locus_tag="AARI_13120" FT /product="LacI-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to protein domain PF00356. Numerous bacterial FT transcription regulatory proteins bind DNA via a helix- FT turn-helix (HTH) motif. These proteins are very diverse, FT but for convenience may be grouped into subfamilies on the FT basis of sequence similarity. One such family groups FT together a range of proteins, including ascG, ccpA, cytR, FT ebgR, fruR, galR, galS, lacI, malI, opnR, purF, rafR, rbtR FT and scrR. Within this family, the HTH motif is situated FT towards the N-terminus" FT /db_xref="GOA:E1VV66" FT /db_xref="InterPro:IPR000843" FT /db_xref="InterPro:IPR001761" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VV66" FT /protein_id="CBT75519.1" FT /translation="MAGIKDVAQAAGVSIATVSRALSGRGSVSAAAQEAVQRAAAELGY FT VVSSSASGLASGRTRNIGVLVPVINHWFYACVLEGISSRLMDEGYDTTLYQLTQDSAQR FT EKVFSDFLLRQRVDAVIAVNVELADEEVQALLAVDKPLVGVGGPLPGVPTLHVNDEAIS FT ALATGHLISLGHERIGFIGGNAETDVDFMIPTHRRAGYEQALEQAGLPIDESLIVSADF FT SMTQGYAVAKQLLGNPASRPTAVFAASDEMAIGAILAARDLGLQLPRDLSVIGVDNHDL FT AELFGLTTVEQRPHEQGQLAVAMLLRAIRGEEPAQAHELGHRLIVRSSTTRPAQ" FT CDS complement(1458628..1460283) FT /transl_table=11 FT /locus_tag="AARI_13130" FT /product="glycosyl hydrolase, family 13" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="3.2.1.-" FT /note="enzymes of this family comprise mostly alpha- FT amylases (EC 3.2.1.1); pullulanases (EC 3.2.1.41); FT cyclomaltodextrin glucanotransferase (EC 2.4.1.19); FT cyclomaltodextrinase (EC 3.2.1.54); trehalose-6-phosphate FT hydrolase (EC 3.2.1.93); malto-oligosyltrehalose FT trehalohydrolase (EC 3.2.1.141)" FT /db_xref="GOA:E1VV67" FT /db_xref="InterPro:IPR006047" FT /db_xref="InterPro:IPR006589" FT /db_xref="InterPro:IPR013781" FT /db_xref="InterPro:IPR015902" FT /db_xref="InterPro:IPR017853" FT /db_xref="UniProtKB/TrEMBL:E1VV67" FT /protein_id="CBT75520.1" FT /translation="MQPEDSQWWRSSVIYQIYPRSFADSNGDGMGDLRGITQRLESIAQ FT LSVDAIWLSPFFTSPQKDGGYDVSNYCDIDPLFGTLEDFDTMVARAHELGLRVIIDLVP FT NHCSDQHPWFQAALKAAPGSPERDRFVFKDTPETGHPNNWESVFGGPMWTETKNADGST FT GQSYLHIFDSSQPDFNWHNEEVRAMFRDVLRFWLDRGTDGFRVDVAHGLIKADGLPDFT FT PDPTAASMGGTEELAPWWGQEGVHEIYRDWRKVMDEYEGNRVLCAEAWVNPLSLMAKWV FT RNDEMHQAFNFPYLSCDFDAQQIRHTIDESLGEFGKVGAPSTWVLSNHDVVRHATRLAL FT SADNPQGDGIGPRTPNLPEPEVGLRRARASSSLMLALPGGAYIYQGEELGLPEAIDLPN FT EARQDPTWFRTNGERYGRDGCRVPLPWENGKPAYGFSDSGESWLPQPANWDSYARDAQV FT DDKSSTLNLYRRLLQLRQDHALGTGSLNWVEGTEDDVLAFANGNVLVVANYAQNPLPLP FT AEAQAATELVRSQELDSAEAGMIPGETTIWFQLD" FT CDS 1460583..1461851 FT /transl_table=11 FT /locus_tag="AARI_13140" FT /product="maltooligosaccharides ABC transporter, FT substrate-binding protein" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family (TC 3.A.1. FT 1.z). ABCISSE: ABC transporter, binding protein (BP), FT OSP-family (oligosaccharides or polyols), FT maltooligosaccharides import" FT /db_xref="GOA:E1VV68" FT /db_xref="InterPro:IPR006059" FT /db_xref="InterPro:IPR006060" FT /db_xref="UniProtKB/TrEMBL:E1VV68" FT /protein_id="CBT75521.1" FT /translation="MKVNKNPWLLGGALTAIAALSLTACGGSGSNAPAASSSPAAAESS FT PAAASGGKLTVWVDANREPVLKEAAADFEKQSGVKVDLVIKDFSKIQEDFLRQVPTGKG FT PDITIGAHDWLGNLVNNGVVQPVELGDKAGEFQDVAVNAMSYEGNTYGVPYATENLALL FT RNADLVKEAPKTFDDMIAAGEKADTEFPFLVQVSDVGDPFHAYPFQTSFGAPVFGTDES FT GAYDPADLQIGNEGGIEFAKWLAEEGEEGNLKTSIDGDIAKEKFVSGDSPFFLTGPWNV FT EAAEDADINLEIDPIPSAGGEEAQPFVAVQGFFVSAKTENLLAATEFLTNYIGNEEVQT FT ELYEVGNRPPANKAAFEAAKSDEIIAAFGEVGANGVPMPNIPEMAAVWEFWGVAEAEII FT TGKADPAKRWKQMTEDIEKAISK" FT CDS 1461968..1463563 FT /transl_table=11 FT /locus_tag="AARI_13150" FT /product="maltooligosaccharides ABC transporter, inner FT membrane subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family (TC 3.A.1. FT 1.z). ABCISSE: ABC transporter, permease (IM), OSP- family FT (oligosaccharides or polyols), maltooligosaccharides FT import" FT /db_xref="GOA:E1VV69" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VV69" FT /protein_id="CBT75522.1" FT /translation="MTKTARQGAQSGTETQKPPLSPTARRFANSTNTSVGAMLAKIILV FT AIVDATAVFAIFTALGREAWVIASVIAVITVAINVVYFKRGWLPAKYLLPGTIFLLIFQ FT VFVIGYTGYIAFTNYGSGHNSDKDDAISALLQSNQNRVEGSAGYPVSILEGQDGLAMLI FT ERDGQQLLGDADEPFAPVDPAGLGDYSELAFADLLGRQQEVTSLTVPFTENPADGTLRT FT SDGRTAYQYTSSIKYDETADTMTDKATGVVYKDTGVGAYTAEDGSQLMPGWSINVGFDN FT FTRAITDSSIRNALFSVTVWTFAFAFLSVATTFFLGLFLAIVFNDMRMKGRKIYRVISI FT LPYAFPAFLGGLVWAGMLNRDFGFVNQVLFGGAEIPWLTDPWLAKFSVLWVNLWLGFPY FT MFLVCTGALQSIPNELSEAATIDGAKPFQIFRLIKLPLLLVSVAPLLISSFAFNFNNFN FT VIYMLTEGGPRLQDAGLNVGSTDILISMVYKVAFVGSQRDYGLASAFSIIIFVIVAIIS FT IISFKQTKALEELN" FT CDS 1463563..1464477 FT /transl_table=11 FT /locus_tag="AARI_13160" FT /product="maltooligosaccharides ABC transporter, inner FT membrane subunit" FT /function="1.2.4 Transport/binding of carbohydrates" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT carbohydrate uptake transporter-1 (CUT1) family (TC 3.A.1. FT 1.z). ABCISSE: ABC transporter, permease (IM), OSP- family FT (oligosaccharides or polyols), maltooligosaccharides FT import" FT /db_xref="GOA:E1VV70" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VV70" FT /protein_id="CBT75523.1" FT /translation="MSTEIIGKEAGSAPAPRAPRQSFGKWFTSTGWRHLIGVALCIYAA FT FPLLYVLSASLNPNGTLLSSNGFFSTIGFNSYVELFQNEQRPFGAWFVNTLVIGLTTAA FT ASVFLGALAAYSFSRMRFTGRRVGLVSLLIVQIFPQLLAVVAIFILLTSLGDVFPVLGI FT DNQIALIMVYLGGALGVNTYLMYGFFNTVPVEIDEAAKIDGAGHARIFFTMILRLVAPI FT LAVVGLLSFISSTSDFVIASVILVSPENQTLAVGLYSYVSEEFTSNWSVFAAGAVLAAI FT PVMALFLFLQKYIVGGLTAGAGK" FT CDS 1464579..1465568 FT /transl_table=11 FT /locus_tag="AARI_13170" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="8 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VV71" FT /protein_id="CBT75524.1" FT /translation="MKPHLPRAARNYLEQLRRALDFLSEQERREVLEATKQEIFRLPGG FT GRRKRDLIRLLGEPEARALKFERHEPQALEVGSGKHFLTRILAWPIFALALLTVMVVLF FT APPQAAQIDEQGFGYVAGSTGDLLAQLELLIGSQLIWIAFIPVVISLIPLWLPNIAGTI FT IQVIGALIMSVICVAGGGQLSLFFIPVTLLLWAQVFTPLLMMRGSMASPGPAWLICAAV FT LLIAVVGYATVRGLAHFSAEPWLILGPAVVLAVLALLLPFRWNSVHIALVAAGLLVMVA FT GFIASLPGTYSAALAWPWLAGGTSFAVGHLAVAAGMWHERARKLLALF" FT CDS 1465624..1466379 FT /transl_table=11 FT /locus_tag="AARI_13180" FT /product="TetR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein domains PF02909 and FT PF00440" FT /db_xref="GOA:E1VV72" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR004111" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011075" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR017956" FT /db_xref="UniProtKB/TrEMBL:E1VV72" FT /protein_id="CBT75525.1" FT /translation="MSENKETSTFEPVKRGRGRPRKDSEFVSLSKELIAQKALEIAGAE FT GYDALTMHRLAAEFKATPRALYNYVTDRQEVINLAVERFLSINPLIEFDCTDWERGVRE FT AYNATRNAYRAYPRASQMTIDEKLVVKPGPMRNRLIERILQFYVDIGLELKQAVALVRA FT LERDVLGFVMHVDYYYDRRSANAPDYISSPVPVQQLEAYPEVSTPLARQALELPQQDSD FT ELFEEVIELRLLAIERMREINGVAGQEQE" FT CDS 1466480..1468036 FT /transl_table=11 FT /locus_tag="AARI_13190" FT /product="putative MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (TC 2.A.1.y.z). FT Identified by match to protein family PF07690 (Major FT Facilitator Superfamily)" FT /db_xref="GOA:E1VV73" FT /db_xref="InterPro:IPR001411" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VV73" FT /protein_id="CBT75526.1" FT /translation="MSQSAPNTAPVAPELSASARWRLLGVLLAAMFMSLVSVSIVNVVL FT PAIGSTLHATEADLQWVLAGYALTFGVVLVAAGRAGDLLGRGVMFIAGVAIFTAASILA FT GVAADPLVLNIARFIMGIGSGLLNPQVMGMIQQHFRGAARGRAYGLLGTAVGFSVAIGP FT VLGGLLINWLGEDAGWRWTFLINVPVGVLAIVLALLWLPKPLFNKPTHKVDLDPVGGVL FT LAVGIFALLLPFVQGRETPWLWSLLALAAVVLVLWVWWEKKYKARGREPMVELALFKIR FT SFTNGTLIAGLYFMGVSSVWVLVAIYVQQSQGFSALQAGLICLPAALLSAFSSDIAGRY FT VMTLGRKLVIGGILSALFGLLSTIAVVILEDRGVLDIWWMLLSLAFIGVAQGFIISPNQ FT ALTLMEVPVANSGSAGGLMQTSQRVGTAVGIAVITAVFYGMNHVAGYSVAMSLSFVAIC FT VLVVATLLVGILDLRQGRRTPSKAGVEEIIPVAPGVQRTVTGAIDIVGPKEPTQPLDSQ FT L" FT CDS 1468080..1468496 FT /transl_table=11 FT /locus_tag="AARI_13200" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR005184" FT /db_xref="UniProtKB/TrEMBL:E1VV74" FT /protein_id="CBT75527.1" FT /translation="MERFLLRSAALATAFTAVSCAATSNDPGASKPIESETSVILQDPV FT GLWGSKEQGQPWLELAEDGKLTGSDGCNRLTGSWNASEDLQFDALASTKMFCEGVDDWL FT SRAATAKLEDGNTMLVLDADGKELGTLAFGGKGS" FT CDS complement(1468519..1469619) FT /transl_table=11 FT /locus_tag="AARI_13210" FT /product="putative fatty acid desaturase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.14.19.-" FT /note="identified by match to PF00487. Fatty acid FT desaturases catalyze the insertion of a double bond at the FT delta position of fatty acids" FT /db_xref="GOA:E1VV75" FT /db_xref="InterPro:IPR005804" FT /db_xref="UniProtKB/TrEMBL:E1VV75" FT /protein_id="CBT75528.1" FT /translation="MSSTATLDSQGPTVKPGDPKSFFHVKKLVTEAGLIGRRRGHYLGL FT GIVLTVLLAGTVTGFILLGDSWFQLLMAGALGLLLTQFAFLAHEAAHRQILASHKRNDK FT LGQFLANIVVGISYQWWMNKHNKHHATPNTVGKDPDIEWDTISFQTEDAKRQRGVLKWI FT TNRQGYLFFPLLSLEGLNLHMHSIKYLFKAGRVKNRKREMTGIFLRIAIYLAVIFYFLP FT VGMAFAFLGVQLAVFGIYMGASFAPNHKGMPMVPQNARIDFFSRQVLTGRNVMAKSSWG FT NRVLSHVYGGLNYQVEHHLFPSMPRANLAGVSAIVRQYCAEHQVPYTVASVRESYAQVI FT TYLNKVGLSARDPFECPMISGYRVSA" FT CDS complement(1469747..1471387) FT /transl_table=11 FT /locus_tag="AARI_13220" FT /product="putative drug resistance ATP-binding protein" FT /function="4.2 Detoxification" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT (putative) drug resistance ATPase-1 (Drug RA1) family (TC FT 3.A.1.120.z). ABCISSE: fused ATP-binding protein (ABC2), FT ART-family. Duplicated ATPase domains (PF00005)" FT /db_xref="GOA:E1VV76" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR007406" FT /db_xref="UniProtKB/TrEMBL:E1VV76" FT /protein_id="CBT75529.1" FT /translation="MTATLVAKDLAGGHAHRTLFSNLNFTAAPGDVYGVVGANGAGKST FT LLSLLAGAADPQAGSVSTAPDSAFIGWMPQEHDRIPGETITAYLARRTGCAAATTAMES FT TAEDLGGSKPGADDAYAAAFDHWMASGAMDLEDRIPEVLAKLGFTLPVDTEMTALSGGQ FT VARVALAALLLSRFDAVLLDEPTNDLDLEGLEHLENFINSLRAPVILVSHDREFLARCT FT TGIIELDLAQNQVATYEGGYDSYLAERAINRSHAREAYEQFENQKADLVSRARTQREWS FT SQGVRNAMRKAPDNDKIRRRANSESSEKQAAKVRQMESRIARLDEVAEPRKEWVLQFSI FT AAAPRGSSVICTLNEASVSHGDYTFGPVSVQVNAGDRIGITGPNGAGKSTLLNLLLGKL FT APHSGTASLGSSVNIGEIDQARTQLPGHLPLGEAFEHEVPEYSAAEVRTLLAKFGLKAD FT QSSALVDELSPGERTRASMALLQARGVNLLVLDEPTNHLDVPAIEQLEEALEAYTGALL FT LVTHDRRLLENVTLAARWEVEEGQLTTHF" FT CDS 1471471..1471836 FT /transl_table=11 FT /locus_tag="AARI_13230" FT /product="putative ArsR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF01022. ArsR-family FT transcriptional regulators include several proteins that FT appear to dissociate from DNA in the presence of metal FT ions" FT /db_xref="GOA:E1VV77" FT /db_xref="InterPro:IPR001845" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VV77" FT /protein_id="CBT75530.1" FT /translation="MHADNNIYAPDPSTEFVELAAEVFGLLSDATRIRIVLHLRRNGEL FT SVNALAELVEKSPSGVSQHLARLRMARMVTTRQDGTKVLYSLTDDHPARLVSEAIKQAE FT HSVSNGRLPLHHRAAQS" FT repeat_region complement(1472290..1472297) FT /rpt_type=DIRECT FT mobile_element complement(1472298..1473713) FT /mobile_element_type="insertion sequence:ISAar13" FT /rpt_family="ISL3" FT repeat_region complement(1472298..1472321) FT /rpt_type=INVERTED FT CDS complement(1472330..1473607) FT /transl_table=11 FT /locus_tag="AARI_34840" FT /product="transposase of ISAar13, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VSI7" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VSI7" FT /protein_id="CBT75531.1" FT /translation="MFKDTGGNDAASILLNLTDYRVIDATQEPAGRQVLIEPKATEAAC FT PTCGVITTRIHARPVHRVKDLPTGGNDIKVLVRKRRMACQETACERRSFVQTTEQLPLR FT ARITTRLSQKLVDEMSCELRAVSRVASAYQVSWPTVMARANMVGELVGNVDRMFIRRLG FT IDEHRFRKVRYARGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRCAAVKKWLKSRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKISVDHFHVIQRANLMITQVRRRRSHEVLQRR FT GRAADPAYKYRKLLTCNLENLSIRQVERLKLILEADPELGVIYGIKEHVRELLKTRDIH FT DFQSRWAVLEKSVKTTKMVEAKSLFRTLTAWRRELLVFIRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRVRILLYTAGLRPC" FT repeat_region complement(1473690..1473713) FT /rpt_type=INVERTED FT repeat_region complement(1473714..1473721) FT /rpt_type=DIRECT FT gene 1473731..1474510 FT /pseudo FT /locus_tag="AARI_13240" FT /product="truncated MFS superfamily transporter" FT /note="section of a MFS superfamily transporter. Disrupted FT by insertion of ISAar13, ISL3 family" FT CDS complement(1474555..1475217) FT /transl_table=11 FT /locus_tag="AARI_13250" FT /product="phosphoribosyl transferase domain-containing FT protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF00156. This family FT includes a range of diverse phosphoribosyl transferase FT enzymes" FT /db_xref="GOA:E1VV79" FT /db_xref="InterPro:IPR000836" FT /db_xref="UniProtKB/TrEMBL:E1VV79" FT /protein_id="CBT75532.1" FT /translation="MATDQSLKFDDRSHAGAALGMRLALELPAGSYTVLGLLRGGVPIA FT YEVAKILKARLGALAVRKLGVPSNPELAFGAIAHYASGNGRYINEEIYRRALRYFGADE FT LDSLEYGTHSELMLLADIFRAYSPGLTGQTVILCDDGIATGATMKASVELVRRLEAKSI FT VIAIPVAARESVEELESLTEHVYAVWTPENFGAVGAYYRDFTQINQARALQLLRLQD" FT gene 1475455..1475622 FT /pseudo FT /locus_tag="AARI_13260" FT /product="truncated protein" FT /note="N-terminal section of a conserved protein" FT gene 1475910..1476461 FT /pseudo FT /locus_tag="AARI_13270" FT /product="truncated protein" FT /note="C-terminal section of a conserved protein" FT CDS complement(1476668..1477777) FT /transl_table=11 FT /gene="hpaD" FT /locus_tag="AARI_13280" FT /product="3,4-dihydroxyphenylacetate 2,3-dioxygenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.13.11.15" FT /note="involved in the catabolism of tyrosine" FT /db_xref="GOA:E1VV80" FT /db_xref="InterPro:IPR004360" FT /db_xref="InterPro:IPR011981" FT /db_xref="UniProtKB/TrEMBL:E1VV80" FT /protein_id="CBT75533.1" FT /translation="MSKEIANPIPTPSVPAPDILRCAYAELVVTDLERSRNFYVDVLGL FT HVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRSTEEVDKAEAYYKELGCR FT TERRKEGFVKGIGDAVRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVRLDHFNQV FT TPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHDTALTGGNGPRLHHVAFS FT THEKHNIIQICDKMGALRISDRIERGPGRHGVSNAFYLYILDPDDHRIEIYTQDYYTGD FT PDNPTITWNVHDNQRRDWWGNPVVPSWYTEASKVLDLDGNVQEVIERTDDSELEVTIGA FT DGFSFTRAGDEDGSYHGQASKGFKLGNQV" FT CDS complement(1477829..1479322) FT /transl_table=11 FT /gene="hpaE" FT /locus_tag="AARI_13290" FT /product="putative FT 5-carboxymethyl-2-hydroxymuconic-semialdehyde FT dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.2.1.60" FT /note="5-carboxymethyl-2-hydroxymuconic-semialdehyde FT dehydrogenase catalyzes the formation of 5-carboxymethyl-2- FT hydroxymuconate from 5-carboxymethyl-2-hydroxymuconate FT semialdehyde" FT /db_xref="GOA:E1VV81" FT /db_xref="InterPro:IPR011985" 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:E1VV81" FT /protein_id="CBT75534.1" FT /translation="MSKHFVPENLPTHLQHYINGEFVDSIGGATFDVQEPVTNTNYATV FT ASAQPEDVDLAVASANKAFKEGPWSKMLPRERSRVLHKIADIVESRDEELSLLESYDSG FT LPITQAKGQARRAAENFRFFADLIVAQVDNTFRVPGRQMNYVNRKPIGVAALITPWNVP FT FMQESWKLAPAIATGNSVVLKPASYTPLSAGLWPEIFREAGLPEGVFNLVFGSGSVAGD FT YLVKHPDVPLVSFTGDSSTGATISTAAAPQFKGLSLELGGKSPAVVFADADLEAALDAT FT VFGVFSLNGERCTAGSRVLVQRDIYDDFVAKFAQRAKNIRVGLPSDPKTEVGALVHPNH FT FEKVMSYIEIGKTEGRLLAGGGRAEGFEEGNYVAPTVFADVAPDAQIFQDEIFGPVVAI FT TPFDTDEEALELANNTKYGLAAYVWTSNLKRAHNFAHQIDSGMVWLNSNNVRDLRTPFG FT GVKASGLGREGGYRSVDFYTTQQSIQITLNEAHSPKFGV" FT CDS complement(1479397..1480056) FT /transl_table=11 FT /locus_tag="AARI_13300" FT /product="GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF00392. This FT family of regulatory proteins consists of the N-terminal FT HTH region of GntR-like bacterial transcription factors. At FT the C-terminus there is usually an effector- FT binding/oligomerisation domain. The GntR-like proteins can FT be divided into six sub-families: MocR, YtrR, FadR, AraR, FT HutC and PlmA. Many of these proteins have been shown FT experimentally to be autoregulatory, enabling the FT prediction of operator sites and the discovery of cis/trans FT relationships" FT /db_xref="GOA:E1VV82" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VV82" FT /protein_id="CBT75535.1" FT /translation="MTASKSEAAYQLVSERIVNGAYSPGYRLVLGTIADELGCSVVPVR FT EAIRRLEAEGLVHFTRNVGATVAHVDSTLYLHTMQTLMVIEPAATALAADSMDAAWLAK FT ARALNEKMRQCLEDFDPVAFTRMNTEFHQLLYGQCPNPHILDLVQRGWRRLAAMRASSF FT THIPNRARASVQEHEKLLDLIGTHATPAQIEAAAREHRAHTLNAYLKAAGMAPSAI" FT CDS complement(1480056..1481558) FT /transl_table=11 FT /locus_tag="AARI_13310" FT /product="possible homoprotocatechuate catabolism FT bifunctional isomerase/decarboxylase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="5.3.3.10" FT /EC_number="4.1.1.68" FT /note="involved in the homoprotocatechuic acid pathway. EC FT 5.3.3.10 (5-carboxymethyl-2-hydroxymuconate Delta- FT isomerase ) catalyses the conversion of 5-carboxymethyl- FT 2hydroxymuconate to 5-carboxy-2-oxohept-3-enedioate. The FT latter is converted to 2-hydroxyhepta-2,4-dienediotae by EC FT 4.1.1.68 (5-oxopent-3-ene-1,2,5-tricarboxylate FT decarboxylase)" FT /db_xref="GOA:E1VV83" FT /db_xref="InterPro:IPR002529" FT /db_xref="InterPro:IPR005493" FT /db_xref="InterPro:IPR011234" FT /db_xref="UniProtKB/TrEMBL:E1VV83" FT /protein_id="CBT75536.1" FT /translation="MSNIVPVTEETFAQAGKILAVHLSYSSRAAQRGRTPKFPSYFMKA FT TSSLAASGSTVERPAGTELLAFEGEIALIIGKTARRVSVEDAWSYVGSVTASNDLGVHD FT MKYADKGSNIRSKSGDGYTPMGPKALEAATLDPAKLRVQTWVNGKITQDADTSELLFSF FT ATIVADLSQQMTLQPGDIILTGTPAGSTVFFPGDVVEVEVTDLVTGATTGKLKTTATEG FT TATFAAFGNQPKVTDKDKEDAYGDRETAGMAPILTGKDVLTDKVREQLASVATATLSAT FT LRKRGLNNVNIEVPGATKGMQRVIGTARTLRYIPNREDLFKAHGAGYNMQKQSIDSLGD FT GEILVMEARGETGSATLGDILALRSQQLGAAGIISDGGVRDLDAVSGLDIPVFYNGAHP FT AVLGRKHVAWDKDITVACGGVSVQPGDVIVADSDGIVVIPPAMVEQVAAEAMVTESNDE FT FIFAMVKRGHGIEGLFPMNAEWKTKYNAWKDAGSPDLDSWSL" FT CDS complement(1481933..1483168) FT /transl_table=11 FT /locus_tag="AARI_13320" FT /product="putative ABC transporter, inner membrane subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TC 3.A.1.y.z. ABCISSE: ABC transporter, permease FT (IM)" FT /db_xref="GOA:E1VV84" FT /db_xref="InterPro:IPR003838" FT /db_xref="UniProtKB/TrEMBL:E1VV84" FT /protein_id="CBT75537.1" FT /translation="MKSLTRLGTGFAAALLEAWQELRIHKLRVLLSLVGVTIAVASLTT FT ALAGAGMARQMMTENLESEGRPAMIVVYAFDPNSDGGPAGNAQIDEAFQKTSDRFKVEY FT TTMMGRNYEQTASAQGMSVDAEVMVVDPDYAPMHRLVVTEGRWLEAEDARNLAPAAVVD FT RNFMKELGLEGHRLPLTVDLMSNGKAVSVTVIGTTKGTSYGMGGRLWMLPATYEHWFGS FT QAPLNEVSYKLWVPIEGSEELAMHFGQQMQAELPGLTVDAHREDYLMWGADESLKMLTM FT VVAGIAIIILLLGSLSLLNVAMVTMKQRIREVGIRRSFGATTERVFFSVMMESVVATAV FT AGGIGVLISVALVSNETLLNMVMATELDQMPAFPIGAALLGMGVSIAVGALTGVLPALV FT AARVKIVDAIRV" FT CDS complement(1483165..1483872) FT /transl_table=11 FT /locus_tag="AARI_13330" FT /product="putative ABC transporter, ATP-binding subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TC 3.A.1.y.z. ABCISSE: ABC transporter, ATP-binding FT protein (ABC)" FT /db_xref="GOA:E1VV85" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VV85" FT /protein_id="CBT75538.1" FT /translation="MSGEPLLELENVTRSVLLPDDSELHILNGIDLSVSEGDHIAIVGR FT SGTGKSTLLNILGLLDRPTSGSLQWRGKDATRLSAKQAAHARGRDLGFVFQQFNLLPGR FT TALENVMAPLMYASGHEFWNRRKLATESLERVGLGKRLDSMPQTLSGGEQQRVAIARAL FT VRRPRVVLADEPTGALDVTTGRAVMDLLDSATVDSGAALITITHDSNVAALAREQLQLD FT GGRLHPLSEVAAR" FT CDS complement(1483862..1484872) FT /transl_table=11 FT /locus_tag="AARI_13340" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VV86" FT /protein_id="CBT75539.1" FT /translation="MKSLVKLAFAGGSAASDDDLYPTGEIPAETVFAEKATVENKLSIG FT GSIKLTESKELNAPVDGVVNWAFVKPGDNVSLGDRIFQIRVESQPDSAETDSAEDEEPQ FT DEQQPRAAAPVMKYHDVYAPATGKVGAFQIEVGDDTTKGTALGSIQPQEFLAVGSVDPL FT DRYRLLDENLEATITIDGGPEPFTCKNLNFGDSASKKASGSTEDQNMGSFSGPMVADES FT ADSDSSSEISCVVPTETVVFDGLNMTMEIDAGSAEDVLTVPVSAVRGLVGQGAVWKLDE FT NGKEIRTEVELGVTDGKVIEVISGLKDETEVLRFVPGSTPSPEDMMGMEYATDEW" FT repeat_region complement(1484863..1484886) FT /rpt_type=INVERTED FT mobile_element complement(1484863..1486311) FT /mobile_element_type="insertion sequence:ISAar19" FT /rpt_family="ISL3" FT CDS complement(1484869..1486176) FT /transl_table=11 FT /locus_tag="AARI_34850" FT /product="transposase of ISAar19, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRG4" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VRG4" FT /protein_id="CBT75540.1" FT /translation="MLNPTFTAPDLTTFTNLDGLGLTAIGQHLSAAKAEILCHVTNPIP FT WCQTCGAAGIPRDTVTRRLAHEPLGWRPTVLVIKHRRYRCANCQRVWREELSQAVAPRQ FT KISRTGLRWALVGLVCHHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFDGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLIDMVPGRSKAVFKTWLADQEEQW FT KQGIEVVAMDGFTGFKTAAVEELPHAVEVLDPFHVVKLGSEALDQTRQRIQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKTKLEDLFKEPEYEPVQLVWSVYQKMVDAYRQPKP FT EVGRWALEQLINEVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRRRLHPQS" FT repeat_region complement(1486288..1486311) FT /rpt_type=INVERTED FT repeat_region 1486937..1486940 FT /rpt_type=DIRECT FT mobile_element 1486941..1488542 FT /mobile_element_type="insertion sequence:ISAar10" FT /rpt_family="IS1380" FT repeat_region 1486941..1486960 FT /rpt_type=INVERTED FT CDS 1487062..1488360 FT /transl_table=11 FT /locus_tag="AARI_34860" FT /product="transposase of ISAar10, IS1380 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VV88" FT /db_xref="InterPro:IPR002559" FT /db_xref="UniProtKB/TrEMBL:E1VV88" FT /protein_id="CBT75541.1" FT /translation="MNHSTHVFPAFSTQLTGQALVSHAGLSVLTSFLNALDFRSLCENR FT FSQFVPATATHRPGKILGALALSLAAGGEQATDIDQLRTAPELFGSVASDATVSRFMGR FT IKEQPEAFSYGFATMTRNLRSKVWAAAGARNPARLATPANPLTIDIDASLVQVHSEKES FT SAGTYKGGYGFSPMIAMADYGKANGTGEVLAVQLHPGNRGANSAKSHIDVLNQALAQLP FT DDFYDEHGNLYREKILVRTDSAGSSREFLHYLDSLGIQFSTSYSLPVIKERFIRWIDEK FT KYWEPALTADGQERDDAWVIDASKVIELKDYPPGTRIYLRAEPLHPGAKATLFDTDGNR FT VTAFLTNSPRFNVAFLDARHRARGRCENRIKTLKSAGLGKLPYWSFAANQAWADLAMFA FT LNLVSWLQLAVLPGGHDASVWDLKRWRHGLLAA" FT repeat_region 1488523..1488542 FT /rpt_type=INVERTED FT repeat_region 1488543..1488546 FT /rpt_type=DIRECT FT gene 1488566..1489150 FT /pseudo FT /locus_tag="AARI_13350" FT /product="truncated peroxidase" FT /note="section of a peroxidase. Disrupted by insertion of FT ISAar10, IS1380 family" FT gene 1489193..1492672 FT /pseudo FT /locus_tag="AARI_13360" FT /product="truncated peroxidase" FT /note="section of a peroxidase. Disrupted by insertion of FT ISAar10, IS1380 family" FT gene complement(1492794..1494332) FT /pseudo FT /locus_tag="AARI_13370" FT /product="truncated glycosyl hydrolase" FT /note="section of a glycosyl hydrolase, group 1. Disrupted FT by insertion of ISAar22, IS481 family" FT repeat_region 1494626..1494640 FT /rpt_type=DIRECT FT mobile_element 1494641..1496362 FT /mobile_element_type="insertion sequence:ISAar22" FT /rpt_family="IS481" FT repeat_region 1494641..1494690 FT /rpt_type=INVERTED FT CDS 1494772..1496217 FT /transl_table=11 FT /locus_tag="AARI_34870" FT /product="transposase of ISAar22, IS481 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VV89" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VV89" FT /protein_id="CBT75542.1" FT /translation="MSNSLSASIRRQIIEFDPGLPDSLSISQFCKELGISRPSYYKVKE FT RFVAEGNKALNPHSRAPKTDRRIYSDQTKTTVLRIRKRLAKDGWDNGPLSIWFESLDTQ FT EFGELRPSVATIGRILAEAGATKRNPRKRPRKSWLRFARSHPMEMWQIDGLEYRLFDQD FT ATKAMIYQLIDDGSRFDVGTRCFEQMENAQDAMETLKAAFAEYGVPQQLLSDNGGAFNL FT SRQGLVNQTEIFLASVGCEAITGRFSHPQTQGKNERSHNTLTRFLDAHAPHNLAELSTL FT LEQYRNHYNHRRRHQALKVGHTYLTPAQAWEAGDHRGSDGVAIDIARIQAKAQSYLDKA FT LAVKADLVPEGVVDDGLQVLGRTKVENYTGSPSVLTDQRDDVIQIRRTNPQIYFRGRVF FT KVPAHLIGEYQLVLSKDAYTLYSTVDGEQSLSFPLPVRLHSSARLVPLWQVYGARIRDP FT KPAWTQKRIEYEDIYYSSDVAVS" FT repeat_region 1496313..1496362 FT /rpt_type=INVERTED FT repeat_region 1496363..1496377 FT /rpt_type=DIRECT FT CDS 1496480..1497772 FT /transl_table=11 FT /locus_tag="AARI_13380" FT /product="putative transferase" FT /function="1.1 Cell wall" FT /note="match to protein family PF04464. Possibly involved FT in teichoic acid biosynthesis" FT /db_xref="GOA:E1VV90" FT /db_xref="InterPro:IPR007554" FT /db_xref="UniProtKB/TrEMBL:E1VV90" FT /protein_id="CBT75543.1" FT /translation="MIGFLLELGTSLKSETRQLLSSLGRSIKIQETLGWIGIENGRTFN FT HEIENLPVPATVVVYFGDEPDKTYQLIQWLPVLEQLNQKHPVVLLFRRVESFRMMQRHT FT DLPRIFVRRFSSLMDLYEDNRYQLVIYVNNSRTNFQSLEHPRPVHVHVNHGESDKVSMV FT SNKAKAYDRVFVAGPAAIDRHRQRLIDFGLDKLLVTGRPQLDIEFDPLVEPSNRKTVMY FT APTWQGENEDNNYTSMDLYGREIVQALLADPGNRVIYKPHPRILDTRDLEVKAAHEAIC FT SLIAKANSVGADHEFFDSGNILAMFDSVDAMITDVSSVGLDFLYLCPEKPLILTDRRQN FT EDQLAIDAPISRSCPIINLVTKESLGSLLPVWIEDDEMARMRLESREFYFGNLKRGEST FT RKFFEQISSLIAERQDKISGYRAWHPTIESE" FT repeat_region 1497987..1497990 FT /rpt_type=DIRECT FT mobile_element 1497991..1499725 FT /mobile_element_type="insertion sequence:ISAar9" FT /rpt_family="IS1380" FT CDS 1498112..1499548 FT /transl_table=11 FT /locus_tag="AARI_34880" FT /product="transposase of ISAar9, IS1380 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VV91" FT /db_xref="InterPro:IPR002559" FT /db_xref="UniProtKB/TrEMBL:E1VV91" FT /protein_id="CBT75544.1" FT /translation="MNHSTQVFPAIPTQLTGQTLVSHAGLSVLTSFLNALDFRSLCEDR FT FSQFVPASATHRPGKILGALALSLAAGGEQATDIDQLRAAPDLFGPVASDATISRFMGR FT IKEQPEAFSYGFATMTRSLRSKVWAAAGPRNPARLATATNPLIIDIDASLVHVHSEKES FT SAGTYKGGYGFSPMIAMADYGKAHGTGEVLAVQLRPGNRGANSAKSHIEVLGQALAQLP FT DDFYDEHGNLVGEKILVRTDSAGSSREFLHHLDSLGIQFSTSYSLPVIKERFVRWIDEK FT KYWEPALTADGQQRDDAWVIDASKVLELKDYPPGTRIYLRAEPLHPGAKANLFDTDGNR FT VTAFLTNAPRFNVAFLDARHRARGRCENRIKTLKNAGLGKLPYWSFAANQAWADLAMFA FT VNLVAWLQLAVLPGGHKASVWDLKRWRYRLFSMAGKIVSGGRQRRLLISARAPEARLLR FT QLNEGVDVLFQRWRHDQLAT" FT repeat_region 1499726..1499729 FT /rpt_type=DIRECT FT CDS complement(1499903..1501831) FT /transl_table=11 FT /gene="ilvD" FT /locus_tag="AARI_13390" FT /product="dihydroxy-acid dehydratase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.1.9" FT /note="involved in the biosynthesis of isoleucine, leucine FT and valine. Catalyses the dehydratation of 2, FT 3-dihydroxy-3- methylpentanoate and 2, FT 3-dihydroxy-3-methylbutanoate into 3-methyl-2-oxopentanoate FT and 2-oxoisovalerate, respectively" FT /db_xref="GOA:E1VV92" FT /db_xref="InterPro:IPR000581" FT /db_xref="InterPro:IPR004404" FT /db_xref="InterPro:IPR015928" FT /db_xref="InterPro:IPR020558" FT /db_xref="UniProtKB/TrEMBL:E1VV92" FT /protein_id="CBT75545.1" FT /translation="MTTLRSHTVTHGRNMAGARALFRAAGVNGADLGRKPIIAVSNSFT FT EFVPGHTHLQPVGRIVSEAITAAGGIPREFNTIAVDDGIAMGHGGMLYSLPSRDLIADS FT VEYMVNAHCADALICISNCDKITPGMLMAALRLNIPTVFVSGGPMESGRATLVDGTVRT FT LDLVDAISEAVNENVSDADLLRIEESACPTCGSCSGMFTANSMNCLTEAMGLSLPGNGS FT TLATHTARKDLYQNAGKLVVDIANRYYGEDDETVLPRSIATKKAFGNAMALDIAMGGST FT NTILHLLAAASEAGVDFGLDEIDEVSRRVPCLAKVAPNAAGNGTIYYMEDVHRAGGIPA FT ILGELRRGGLLDETVHTVHSATLGEWLDDWDIRSGKAKEESFDLWHAAPGGVRSSTAFS FT QSERWAALDTDDAEGCIHSVENAYSKDGGLAVLRGNIAVDGAVVKTAGVDPSIWTFSGP FT AVVCESQDEAVEKILNKQVKEGDVVVIRYEGPKGGPGMQEMLYPTSFLKGRGLGKACAL FT ITDGRFSGGTSGLSIGHVSPEAASGGMIALVEDGDIISIDIPTRELTLNVSDEVLDERR FT ERLIATTGYRPKNRERVVSPALRAYAAMALSADKGAVRDVDRVERAMRESDERAAAALR FT AAGSAKA" FT CDS 1501917..1502696 FT /transl_table=11 FT /locus_tag="AARI_13400" FT /product="DNA binding domain-containing protein" FT /function="3 Information pathways" FT /note="identified by match to SM00530: Helix-turn-helix FT XRE-family like proteins. This is a large family of DNA FT binding helix-turn helix proteins that include a bacterial FT plasmid copy control protein, bacterial methylases, various FT bacteriophage transcription control proteins and a FT vegetative specific protein from Dictyostelium discoideum FT (Slime mould)" FT /db_xref="GOA:E1VV93" FT /db_xref="InterPro:IPR000014" FT /db_xref="InterPro:IPR001387" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VV93" FT /protein_id="CBT75546.1" FT /translation="MKPSQRRREELAAFLKDRRARADRSSHGLPEIGRSRVRGLRREEV FT ATLAGVSVTWYTWLEQARDINPSRQVLQSLARLFRLTSVESSYLFSLAGHGELEPIGNG FT GMTPALQRLLDALQFPAFLLSADWTILGWNTAYEELYPRVASLEREDRNLLWLVFTDAQ FT LREMLPDWEVQSRGFVGSFRAETRGWLSPSGESGIVARVSAASAEFAAIWNERDVAGFQ FT TGERVFRHPTKGLTRYEQHNLTPTEATDLTLLMYTPR" FT CDS complement(1502860..1503552) FT /transl_table=11 FT /locus_tag="AARI_13410" FT /product="hypothetical secreted protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.646 FT between position 58 and 59" FT /db_xref="UniProtKB/TrEMBL:E1VV94" FT /protein_id="CBT75547.1" FT /translation="MNRKASAALALGTIALLATACAATEDPAPGTSPAPSQSSPAAAES FT SSAQPSSPASVQAADIVPTLENAATDQDKTPEPVTDPEIDQDSIRALAQMSYAKQYAAV FT NDSGELCLIAWAYDGSQDANGTMSEEEVECEDPAEVKEEGLHLDVDATSSTPGVELYLL FT PPDLTEETVRTELLKIEGNHEDLRPLVEFAATDFGLVSVAMEAKTASDLGKISFPRSSG FT TEFTLDLD" FT CDS complement(1503817..1504566) FT /transl_table=11 FT /locus_tag="AARI_13420" FT /product="putative lipase/esterase" FT /function="2.4 Metabolism of lipids" FT /EC_number="3.1.1.-" FT /note="match to PS00120 pattern: lipases, serine active FT site" FT /db_xref="GOA:E1VV95" FT /db_xref="UniProtKB/TrEMBL:E1VV95" FT /protein_id="CBT75548.1" FT /translation="MTLDLNLRVISTDTETGAPPVLLIHGFASSADMNWMRSRWVQHFT FT THGRDAILLDLPGHGTDPYRNDGSWTPTRIRESIASALAEHGISKVDVLGYSLGARLGW FT EFAAHFPELVNKLVMGGAASIDPLAAFELDQARAFIDHGEEVHDEYTAKVITIAKAEGS FT NDFEALFRLIEAIKTDPYVPASKIPACPVLLVAGDHDDLATTMPELRRLLREAGTDSSI FT HWLPGRNHANAVTSREFKEKAVEFFSI" FT CDS complement(1504570..1505151) FT /transl_table=11 FT /locus_tag="AARI_13430" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VV96" FT /protein_id="CBT75549.1" FT /translation="MTVSQIQDAIEAGQPTEVASLALCLDPEAIYENFDFHRISDDAQP FT YWDFAKLWVQSAPALAKPLIARWVLDIATSEFAYLEIESEADKLLISSVQDAKNCLASL FT IEDVSVLSDNPDAGLAKAQILELGSASKTLKDRQSPNAGIWYQWIRQSAPAAGMEVTFC FT LRQHGFNRSLSAFICQCRDDRRESLKSPRI" FT CDS 1505358..1506086 FT /transl_table=11 FT /locus_tag="AARI_13440" FT /product="NUDIX domain-containing protein" FT /function="4.6 Miscellaneous" FT /note="identified by match to PF00293. Members of the Nudix FT hydrolase superfamily catalyze the hydrolysis of nucleoside FT diphosphates linked to other moieties. Substrates of nudix FT hydrolases include intact and oxidatively damaged FT nucleoside triphosphates, dinucleoside polyphosphates, FT nucleotide-sugars and dinucleotide enzymes. These FT substrates are metabolites or cell signaling molecules that FT require regulation during different stages of the cell FT cycle or during periods of stress. In general, the role of FT the nudix hydrolase is to sanitize the nucleotide pools and FT to maintain cell viability, thereby serving as surveillance FT and house- cleaning enzymes" FT /db_xref="GOA:E1VV97" FT /db_xref="InterPro:IPR000086" FT /db_xref="InterPro:IPR015797" FT /db_xref="UniProtKB/TrEMBL:E1VV97" FT /protein_id="CBT75550.1" FT /translation="MSSVPGWANVNERRNLPPALAVSTVILGIREGKDGGPDKLCLPLV FT RRIRQPHAGMWALPGGPVETRESLGQAASRNLAETTGLRPSYLEQLYTFGDIDRSPTHR FT LVTIAYFALLNADQVGATVQYENVAWFDIDDPQIAQMAFDHRKIVDYALWRLRNKTEYG FT QIAHRLLGERFTLAALRGVYEAILGRRLDPANFRRTLKSTASIEETDEYLAGGKHRPPR FT LYRYAGHGRDPLQVDTEQNN" FT CDS 1506138..1507427 FT /transl_table=11 FT /gene="nadA" FT /locus_tag="AARI_13450" FT /product="quinolinate synthetase A subunit" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="quinolinate synthetase A subunit. Quinolinate FT synthetase complex (A and B subunits) is involved in the de FT novo biosynthetic pathway of pyridine nucleotide formation. FT It catalyses the formation of quinolinic acid" FT /db_xref="GOA:E1VV98" FT /db_xref="InterPro:IPR003473" FT /db_xref="InterPro:IPR023515" FT /db_xref="UniProtKB/TrEMBL:E1VV98" FT /protein_id="CBT75551.1" FT /translation="MNSHHIQTAEATGSVAQNIAQLNLLAPESTCSTDLAASPWDTPAG FT YGPGASQEDQIPSGYPVQSSIPEEYLKASDEELDARIVAAKATLGDKAVILGHFYQRDE FT VVKYADFVGDSFQLANAALTRDKAEAIVFCGVHFMAETADILSREDQAVILPNLAAGCS FT MADMADGPSVQQCWEELTALYKDEEDDGRMPVIPVTYMNCSAELKAFVGRNGGLVCTSS FT NAATVLEWAFERGRRVLFFPDQHLGRNTAKAMGIALEQMPMWTPRKALGGNDEAIMHDA FT KVILWHGFCSVHKRFNPAQIAKARQEFPGVRVIVHPECPMEVVDAADEAGSTDYIQKAI FT AGATEPTTFAIGTEINMVNRLAAQYPQHTIFCLDPVICPCSTMYRIHPGYLAWVLEELV FT AGRVVNQITVPKDQQGDAKIALERMLAAKP" FT CDS 1507424..1509067 FT /transl_table=11 FT /gene="nadB" FT /locus_tag="AARI_13460" FT /product="L-aspartate oxidase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="1.4.3.16" FT /note="quinolinate synthetase B subunit. Quinolinate FT synthetase complex (A and B subunits) is involved in the de FT novo biosynthetic pathway of pyridine nucleotide formation. FT It catalyses the formation of quinolinic acid" FT /db_xref="GOA:E1VV99" FT /db_xref="InterPro:IPR000103" FT /db_xref="InterPro:IPR003953" FT /db_xref="InterPro:IPR004112" FT /db_xref="InterPro:IPR013027" FT /db_xref="InterPro:IPR015939" FT /db_xref="UniProtKB/TrEMBL:E1VV99" FT /protein_id="CBT75552.1" FT /translation="MNREENSSPQLVIVGSGVAGLCAALQGVELGLNPIVLSKDKLGDS FT NSKLAQGGLSAVTAASISHGDSVAKHVADTLSAGAGHCGVGPVQYMCSASDELVQALES FT YAVNFDRDEAGTYELGLEAAHSAHRILHIEGDATGAMMVHALVRAVRALEAEHKLRIVE FT DAVVTDLELQDGKVTGVKYLHHDGEQSLPAPAVLLATGGLGQLYAASTNPQGATADGIG FT LAVRAGAVIADAEFIQFHPTLVDPAQYPTAGMVSEAVRGEGAILVNETGQRFMKEIHPD FT AELAPRDVVARGIHGQIQAGHRVYLDARVVEESRGAGFLAKRFPSITARLAACAKDGTG FT LDMAHDLIPVVAAQHYFMGGIYTDTAGRTSVPGLYAAGECANTTVHGANRLASNSLLEA FT MVFARGAVTAMRGDSPAASCEVDPLSIQQIDTPNPAAPLGLEQLQTAASAKLGVHRTAN FT DLEEMAQLLAKGAPVAATAREQAELRNLWITARIITAGAIARTESLGAHHRVDAPENLS FT GNAGAGIRYGWTLHPSELNNENLLSKEMNA" FT CDS 1509064..1509930 FT /transl_table=11 FT /gene="nadC" FT /locus_tag="AARI_13470" FT /product="nicotinate-nucleotide diphosphorylase FT (carboxylating)" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.4.2.19" FT /note="involved in the de novo synthesis of NAD in both FT prokaryotes and eukaryotes. It catalyses the reaction of FT quinolinic acid with 5-phosphoribosyl-1-pyrophosphate in FT the presence of Mg2+ to produce nicotinic acid FT mononucleotide, pyrophosphate and carbon dioxide" FT /db_xref="GOA:E1VVA0" FT /db_xref="InterPro:IPR002638" FT /db_xref="InterPro:IPR004393" FT /db_xref="InterPro:IPR013785" FT /db_xref="InterPro:IPR022412" FT /db_xref="UniProtKB/TrEMBL:E1VVA0" FT /protein_id="CBT75553.1" FT /translation="MNTLIHPVPVAAMDRIIELALAEDNPRGDITALTIVAQDARATAV FT VKARQPGVLSGGDVFTRTMHLVDAQLEVEQLIPEGEKFEAGDDLLKVTGPAASLLTAER FT VGLNLLQRMSAIATATAQLVDLVAHTKARIVDTRKTTPGLRVLERYAVRCGGGVNHRDN FT LSDAFMAKDNHLALLDNGEQLTAALKSVRARLGHTTSMEVEVDSIEQIPPVLAAGVDII FT MLDNFDPADIPAAIELIDGQAVVEASGNINASTVVAVAEAGVDVISSGAITHSVKAIDL FT GLDMVIA" FT CDS 1509927..1511069 FT /transl_table=11 FT /locus_tag="AARI_13480" FT /product="putative cysteine desulfurase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.8.1.7" FT /note="identified by match to protein family PIRSF005572: FT cysteine desulfurase, NifS type. Cysteine desulfurase FT catalyses the following reaction: L-cysteine + [enzyme]- FT cysteine <=> L-alanine + [enzyme]-S-sulfanylcysteine. It is FT involved in the biosynthesis of iron-sulfur clusters, FT thio-nucleosides in tRNA, thiamine, biotin, lipoate and FT pyranopterin (molybdopterin) and functions by mobilizing FT sulfur" FT /db_xref="GOA:E1VVA1" 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="UniProtKB/TrEMBL:E1VVA1" FT /protein_id="CBT75554.1" FT /translation="MIYMDAAATAPPRQNVLDVINPLLTRDFGNPASLHESGQQAKRAN FT DWARTQVAGQLGVAAQEVYFTSGGTEGANAAVIGAALANPRGRVVVCSSVEHPAVMEAC FT KYLVEFHGFEHRIIPVTGTGLVDLKAAGELIDTDVAVVSVMAVNNEVGTIQPVAAVAEL FT VHEAGALMHTDAVQGAGWIDLKPLCAAVDALSISGHKIGGLKGSGAMYLSAKHRFVPLL FT QGGGQQGGMRSGTENPAAAVGIAVALQAATSQREGGLGANFGPYLIERILKELNAKHPG FT SVQLTGDPVHRVGGIVSFVFPQTAGETVLIELARKGILCSSGSACAAGSTEPSAVLTAM FT GYDEQLAHTALRLSFTRTTKENEISQVASAVVSCVSGLLG" FT CDS 1511315..1512127 FT /transl_table=11 FT /locus_tag="AARI_13490" FT /product="SH3 domain-containing protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="match to PF08239: bacterial SH3 domain. A homologue FT of the SH3 domain has been found in a number of different FT bacterial proteins including glycyl-glycine endopeptidase, FT bacteriocin and some hypothetical proteins. Signal peptide FT predicted by SignalP 3.0 HMM (probability: 1.000) with FT cleavage site probability 0.938 between position 26 and 27" FT /db_xref="InterPro:IPR003646" FT /db_xref="InterPro:IPR013247" FT /db_xref="UniProtKB/TrEMBL:E1VVA2" FT /protein_id="CBT75555.1" FT /translation="MKIPGRAAALALAMTMTVGTGGQAYAAPVAASQVPSALPATGPAI FT KSVKSSVAKRTTANLRLRAKSTLQSSTLRVIPNGAKVAVLDTKGSWDKVRYSGMTGWSH FT NSYLHALASASKTPSQTARYTTANLNLRAGAGTNHRSLGVIPQGGKVTLHRVSGNWAQV FT TSSKGSGWVSRLYLSSNAQPSIPKKQEKPSAPKQSQKYAYASAFLNLRAGAGTSHRSIG FT VISKGEKVAVLATSRGWSKVRSSKGTGGPAALIWFPRPPIRTSMRRPR" FT CDS 1512205..1512789 FT /transl_table=11 FT /locus_tag="AARI_13500" FT /product="SH3 domain-containing protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="match to PF08239: bacterial SH3 domain. A homologue FT of the SH3 domain has been found in a number of different FT bacterial proteins including glycyl-glycine endopeptidase, FT bacteriocin and some hypothetical proteins" FT /db_xref="InterPro:IPR013247" FT /db_xref="UniProtKB/TrEMBL:E1VVA3" FT /protein_id="CBT75556.1" FT /translation="MRSGAGVNHRSLGVISKGEKLTVHLSTSGWSKVTSSKGTGYVSST FT YLSVGKPTAEIKSVRPDTQRVMDTVRRLFSGDYTSFGTIRPGSVGHSSGWAVDVMISRY FT NSAGGVQAGDRIARFLIDNRSQLGVSYLIWQDQIWLGAQKGWEPYSTSGKYGTHLSKNW FT NDTSRHMDHIHVETHGSSARGGALDYSALND" FT CDS complement(1512873..1514300) FT /transl_table=11 FT /locus_tag="AARI_13510" FT /product="putative D-alanyl-D-alanine carboxypeptidase" FT /function="1.1 Cell wall" FT /note="N-terminal section of the protein: match to protein FT family PF02557 (VanY, D-alanyl-D-alanine carboxypeptidase). FT C-terminal section of the protein: match to PF08239 FT (bacterial SH3 domain) protein family PF02557" FT /db_xref="GOA:E1VVA4" FT /db_xref="InterPro:IPR001452" FT /db_xref="InterPro:IPR003646" FT /db_xref="InterPro:IPR003709" FT /db_xref="InterPro:IPR009045" FT /db_xref="InterPro:IPR013247" FT /db_xref="UniProtKB/TrEMBL:E1VVA4" FT /protein_id="CBT75557.1" FT /translation="MTKPSAFKLSLTATLSAALFATLLPATPAAAAAPAPVSIQVQAPA FT LSVDASVQIAAKKIQRNPAKDDVFVNKKYPLSPKKYAPKTVAIQGSNVRLRSSAAKAYN FT KMAKAAAKDGVKIRAVSGYRSYNRQAELFNYYTRIYGKSYASRISAVPGTSEHQTGLAI FT DVGNANGACGLQACFANTPVGKWVGKNAHKYGFIMRYQKGQESVTGYSYEPWHFRYLGT FT SLAKSVKNSGAKSLEAYYGVSGKKSDSAPKNSKGTAQTTANLNMRTGAGTGNRVLLTIP FT RGKSVQLTGSKKSGWYQVRYSSRTGWVSGKYLSSISMPSKPKKESKKSTPKQNTSNAKS FT AKTSANLNMRTGVGTSHRVVLTIPQGKKVAIRGAKKSGWYPVKYAGKNGWVSGTYLRSF FT SSSTYSPKSSDPKSSSSASKKTIANLNMRSGAGTSKRVILTIPKGKKVSIRGAKKSGWY FT PVKYAGKNGWVSGKYLR" FT CDS 1514739..1515254 FT /transl_table=11 FT /locus_tag="AARI_13520" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VVA6" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VVA6" FT /protein_id="CBT75558.1" FT /translation="MRIRPEVFDDRAAVYALTHAAFAGIDPMVEPEEVGLLQNLFNCEQ FT YDSRFSIVALDDTAVIGHVIATWGEVEGEALLGLGPLAVAPEYQHRGVGSILMQEIHDK FT AEEERVSGIVLLGAPAYYRRFGYGPAQAQGIIPTQSMWGEHFMVRVFDEARLPRGTFHY FT AKPFRSDR" FT CDS 1515319..1515795 FT /transl_table=11 FT /locus_tag="AARI_13530" FT /product="activator of Hsp90 ATPase 1-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF08327" FT /db_xref="GOA:E1VVA5" FT /db_xref="InterPro:IPR013538" FT /db_xref="InterPro:IPR023393" FT /db_xref="UniProtKB/TrEMBL:E1VVA5" FT /protein_id="CBT75559.1" FT /translation="MEPLEELNELSFSVKGFISKSVRQVYDAVADPEQLSHYFTTGGAQ FT GYLATGATVTWDFHDYPGAFPVHVLEAEVGKRIILRWGGQETLASDGMNTVTFEFTSES FT ESSRTKVVITESGWKPTAAGIQAAFGNCEGWTGMLAAMKAWLEHGINLREDFYK" FT CDS complement(1515808..1516401) FT /transl_table=11 FT /locus_tag="AARI_13540" FT /product="RibD domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF01872. This domain is FT found in the C-terminus of the bifunctional deaminase- FT reductase in combination with PF00383 as well as in FT isolation in some archaebacterial proteins" FT /db_xref="GOA:E1VVA7" FT /db_xref="InterPro:IPR002734" FT /db_xref="InterPro:IPR024072" FT /db_xref="UniProtKB/TrEMBL:E1VVA7" FT /protein_id="CBT75560.1" FT /translation="MGPVHCDVTVSLDGFCAGARQSMQHPLGDGGEDLHRWQFEQTEEN FT ATEIAAITEASAFVMGQNMFGPPSGDEQADWIGWWGDNPPYHSPVFVLTHHHKPTLCLE FT GGTSFQFITQGIEEALCQAQDAAGERPVAIAGGAQTIVQFLRAGLIDELRLHIAPIRLG FT QGEAITVEDIEMHMDRTNHRETTLATHVYYQRRR" FT CDS complement(1516513..1517202) FT /transl_table=11 FT /locus_tag="AARI_13550" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVA8" FT /protein_id="CBT75561.1" FT /translation="MKDEKLLGLDEAASTLGVETKDLRSYLRQHRPKGAVQKPPQPGGN FT WHVSESLLTQLQFAGAPGLNIELKAIDEQTIESLEWSEWNSFEQTVDSAPVAPGVYMFR FT FAGECERGQEPIYVGQAGERSGKGIKGRLKIYSSGKGATSGMGKYAFDLGLADPQWLRG FT LLDEAERGEPRTIQQVARQAIDRLNLEGRWVICIHRKAALLLEAALIQKHHASLWNTAG FT IPKDAQA" FT CDS complement(1517327..1517785) FT /transl_table=11 FT /locus_tag="AARI_13560" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VVA9" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VVA9" FT /protein_id="CBT75562.1" FT /translation="MTGTSNPAASLKVTTDAWEALFRAQVAVMREITAMPEFGKLSMRE FT YDVLFNLRTCPGGKSRMVDLNKQLLISQPSLSRMVNRLEDQELVVREADPDDHRAMQLS FT LTAKGRKLQQDIGREHVKHLHKLLGCALSEDEFHELERLSNKLRQAVQ" FT CDS complement(1517769..1518902) FT /transl_table=11 FT /locus_tag="AARI_13570" FT /product="putative luciferase-like monooxygenase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00296. Bacterial luciferase FT is a flavin monooxygenase that catalyses the oxidation of FT long-chain aldehydes and releases energy in the form of FT visible light, and which uses flavin as a substrate rather FT than a cofactor. There are structural similarities between FT bacterial luciferase and nonfluorescent flavoproteins FT (LuxF, FP390), alkanesulfonate monooxygenase (SsuD), and FT coenzyme F420- dependent terahydromethanopterin reductase, FT which make up clearly related families with somewhat FT different folds" FT /db_xref="GOA:E1VVB0" FT /db_xref="InterPro:IPR011251" FT /db_xref="InterPro:IPR023934" FT /db_xref="UniProtKB/TrEMBL:E1VVB0" FT /protein_id="CBT75563.1" FT /translation="MQFGVFSVSDITRDPTTGRIPTEKERIDAQVAIAKKVEEIGMDVY FT AIGEHHNRPFFSSSPTTTLAYIAAQTKRIILSTTTTLITTNDPVKIAEDFAMLQHLADG FT RVDLVLGRGNTGPVYPWFGKNMQDSVNLTVENYHLLRRLWDEDVVNWEGKFRTPLQNFT FT STPRPLDDVAPFVWHGSIRTPQVAEIAAYYGDGFFANNIFWPKEHYQQLINLYRERYEH FT YGHGRADQAVVGLGGQFYMAKDSQQAVKEFRPYFDNAPVYGHGPSLEDFTAQTPLTVGS FT PQQVLEKTLTFQEYFGSYQRQLFLIDHAGLPLKTVLNQLDMFGEYVLPELRKEMESRAP FT KDLTPAPTHQGLVAARNAKLEAEQANTKEPEVSDRDQ" FT CDS complement(1519019..1519687) FT /transl_table=11 FT /locus_tag="AARI_13580" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VVB1" 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:E1VVB1" FT /protein_id="CBT75564.1" FT /translation="MNIDSPVTVLLVDDDSLIRAGLGAILGSDQRICIVGEAENGHRAI FT ELSQRLDPAVILMDIRMPQLDGLSAMESILDQKPDAKVMILTTFGDESYIDRALSGGAA FT GFMLKSSGPDELISAVLAVAEGAAALSPRIAQRVIEKVRNLDSSGQSDAQTLVRKLTAR FT EHDVLALVGASLTNSEIAGRLFLTEATVKGHMTSIMLKINARNRVDAALIAYRAGIVDA FT " FT CDS 1519834..1520568 FT /transl_table=11 FT /locus_tag="AARI_13590" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="5 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR015414" FT /db_xref="UniProtKB/TrEMBL:E1VVB2" FT /protein_id="CBT75565.1" FT /translation="MNAEPAVPEFDPSSGLPDDPAKAPSLWENYLRNGLLIAVFLLMVW FT LAFNVHLPSIEEIRSRVDGTSWSARFGFIILYALVAITPIPISVMAICGGLLFGVFQGT FT AFSLIGVLLGSWAAYWLARALGRATVRKLMGKHAVRIEQRLESRGLLAVFMLRLMPGIP FT YWPVNYGSGAFGVSQRDYLVASALSVIPGQLSLVAIGSFIAVPNVFNGVVIGISWIVVG FT VLTIWAYLRWRRQPVPAAPVAS" FT CDS complement(1520653..1524030) FT /transl_table=11 FT /locus_tag="AARI_13600" FT /product="putative drug exporter of the RND superfamily" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="Resistance-Nodulation-Cell Division (RND) FT superfamily (TC 2.A.6.y.z). Match to protein family PF00873 FT (AcrB/AcrD/AcrF family). Some Members of this family are FT involved in drug resistance" FT /db_xref="GOA:E1VVB3" FT /db_xref="InterPro:IPR001036" FT /db_xref="UniProtKB/TrEMBL:E1VVB3" FT /protein_id="CBT75566.1" FT /translation="MQRLATLSLKNRALIALITVFAAIFGVISMGSLKQELIPALEFPQ FT ISVMATQMGSSPEVIDEQVAEPLETALQAVEGLESSSAVSQAGFTRIALTFEYGTDMDR FT ARTQVERAIANSKAQLPEDVEPTAFAGSIADFPVLALAVSSDQSLEQLNDAVERITLPK FT LQKIDGVREASVSGGSSQHIAVIPEDDQMQNAGLSVADLKDGIENAGSPMPIGNMDVDG FT LELPVIAGSTPDTLDAIKQIPLITDNGPVLLQDVAKVSVQADEATSITRTNGEETLSIQ FT VTKTPDGDTVAISHAVTAMIADLEAELGHKATITTVFDQAPFIEDSIKHLALEGALGLG FT FAVIIILVFLFSVRSTLVTAISIPLSLMATFIGMNVFGYTLNMLTLGALTISIGRVVDD FT SIVVIENIKRHLAHGESKAQSILLAVKEVAGAITAATLTTVAVFLPIALVGGMAGELFS FT PFALTMTIALLASLLVSLTIVPVLAYWFLPHRPGSGETKTVHVAEDKSWLQRAYVPVLK FT KTQKHPVITLLASVLILAGTVAMTPLLNTNLLGSTGENSISITAEMPSGTAMETTEKEA FT AKIEAKLAEIDGIEDVQMTVGSASGMAAMFSSGSDTASFTVITNADEDQESLTNTVREQ FT VEGLDLAKDLNLSFGSNSSAMMSSDVTVEVKAPDEDILREATSKMREALEGTEHVTELS FT DNLSAKREQVSIDIDAEKAAEAGLTETQLAGMVASQVSPVPAGTLRLDYTDMTVQIGQG FT LDLNSMDKLRELKIPTATGVKELQDLATVERANVVQQVTTSNGERIATLTLTPAENMLG FT AVSASVTERLESVQLPEGATAELGGAATEQAESFNQLYLALLAAIAIVYVIMVATFKSL FT IQPLVLLVSIPFAATGAIGLLLISGIPLGLPSLIGMLMLVGIVVTNAIVLIDLINQYRE FT DTPERPAMALEEAIMQGARQRLRPILMTALATIFALVPMGLGLTGQSGFISQPLAVVVI FT GGLVSSTLLTLILVPVLYRLVESRKEKNANARAARKHSAQQHTATQDLTRAMNSAHAKI FT TAPAASVAPEQQSPKPGKLRADEKASASGKPAAKRSAPAVASDAVVNPLTGQIPVSRKE FT RREFEEMMKKASNEKPEA" FT repeat_region 1524156..1524170 FT /rpt_type=DIRECT FT repeat_region 1524171..1524220 FT /rpt_type=INVERTED FT mobile_element 1524171..1525892 FT /mobile_element_type="insertion sequence:ISAar22" FT /rpt_family="IS481" FT CDS 1524302..1525747 FT /transl_table=11 FT /locus_tag="AARI_34890" FT /product="transposase of ISAar22, IS481 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVB4" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VVB4" FT /protein_id="CBT75567.1" FT /translation="MSNSLSASIRRQIIEFDPGLPDSLSISQFCKELGISRPSYYKVKE FT RFVAEGNKALNPHSRAPKTDRRIYSDQTKTTVLRIRKRLAKDGWDNGPLSIWFESLDTQ FT EFGELRPSVATIGRILAEAGATKRNPRKRPRKSWLRFARSHPMEMWQIDGLEYRLFDQD FT ATKAMIYQLIDDGSRFDVGTRCFEQMENAQDAMETLKAAFAEYGVPQQLLSDNGGAFNL FT SRQGLVNQTEIFLASVGCEAITGRFSHPQTQGKNERSHNTLTRFLDAHAPHNLAELSTL FT LEQYRNHYNHRRRHQALKVGHTYLTPAQAWEAGDHRGSDGVAIDIARIQAKAQSYLDKA FT LAVKADLVPEGVVDDGLQVLGRTKVENYTGSPRVLADQRDDVIQIRRTNPQIYFRGRVF FT KVPAHLIGEYQLVLSKDAYALYSTVDGEQSLSFPLPVRLHSSARLVPLWQVYGARIRDP FT KPAWTQKRIEYEDIYYSSDVAVS" FT repeat_region 1525843..1525892 FT /rpt_type=INVERTED FT repeat_region 1525893..1525907 FT /rpt_type=DIRECT FT gene 1526152..1526541 FT /pseudo FT /locus_tag="AARI_13610" FT /product="truncated OsmC-like protein" FT /note="N-terminal section of a OsmC-like protein. Disrupted FT by insertion of ISAar22, IS481 family. Match to protein FT family PF02566: OsmC, OsmC-like protein. Osmotically FT inducible protein C (OsmC) is a stress-induced protein FT found in Escherichia coli. This family also contains an FT organic hydroperoxide detoxification protein that has a FT novel pattern of oxidative stress regulation" FT CDS 1526694..1526972 FT /transl_table=11 FT /locus_tag="AARI_13620" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVB5" FT /protein_id="CBT75568.1" FT /translation="MTAQMPIAVQATAQQGIRRLTRIRYRYFSYALRFADGREVHGLGW FT AEADKLLQGYRYPADASCTHHGAERHCPAFGAGAWVDYPYGRPLAQQ" FT CDS complement(1527042..1528529) FT /transl_table=11 FT /gene="mqo" FT /locus_tag="AARI_13630" FT /product="malate dehydrogenase (acceptor)" FT /function="2.1.3 TCA cycle" FT /EC_number="1.1.5.4" FT /note="other name: malate:quinone oxidoreductase. Takes FT part in the citric acid cycle. It oxidises L-malate to FT oxaloacetate and donates electrons to ubiquinone-1 and FT other artificial acceptors or, via the electron transfer FT chain, to oxygen. NAD is not an acceptor and the natural FT direct acceptor for the enzyme is most likely a quinone" FT /db_xref="GOA:E1VVB6" FT /db_xref="InterPro:IPR006231" FT /db_xref="UniProtKB/TrEMBL:E1VVB6" FT /protein_id="CBT75569.1" FT /translation="MEILVPSETSTESFDVVLIGAGIMSATLGTMINQLEPTWSIGLFE FT NLDKAGQESSSPWNNAGTGHSALCELNYTAAKADGSVDPAKAIGINEQFQLSRQFYSWA FT VENKRVADNSFINALPHMSFVIGDDHSKYLQTRYEALKPNALFEELEITNDLDTINEWT FT PLVAKGRDASQKVAASRVVSGTDVDFGRLTSELTDSLGAAGASVNFGHKVQGIKRSGAG FT WELTVKDKASGALKNVKAKFVFVGAGGGALPLLQKAGIDEIKGFGGFPVSGQFLRCTDE FT NIINQHHAKVYGQASVGAPPMSVPHLDTRFVDGKRSLMFGPYAGFSMNFLKSTGQLDLP FT LSLRPHNIIPMLAVGKDNLDLTTYLIKEVLKSRAKKDESLAEYFPEADGSKWELITAGQ FT RVQVIKKDAKKGGVLQFGTEVITSSDGSISGLLGASPGASTATPIMIGLLSRCFPKQFA FT GWETKLKDMVPSYGQKLNENPALYAEVKAATDKTLGL" FT CDS complement(1528608..1530452) FT /transl_table=11 FT /locus_tag="AARI_13640" FT /product="putative dipeptide/oligopeptide ABC transporter, FT substrate-binding protein" FT /function="1.2.1 Transport/binding of proteins/peptides" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT peptide/opine/nickel uptake transporter (PepT) family (TC FT 3.A.1.5.z). ABCISSE: ABC transporter, binding protein (BP), FT OPN-family (oligopeptides and nickel), oligopeptides FT import" FT /db_xref="GOA:E1VVB7" FT /db_xref="InterPro:IPR000914" FT /db_xref="InterPro:IPR006311" FT /db_xref="UniProtKB/TrEMBL:E1VVB7" FT /protein_id="CBT75570.1" FT /translation="MPETPLNLVSRRALLTGTLATTALTLAACTGNSGTAGSASPAASA FT SATPVPRTLRLAAAAPPVKFDPAIVADNESFRVTRQVYETLIDIDPDTGGAVAGLAEAW FT TESPDGLRYTFTLRQGVLFHDGTELNAKAVVANFNRWENLSATLRADSTQGFTDVFHFG FT SDIPKLPTVKDLEKEFQGVEGPTEAELAAQQLRLKQLEELATQYKTDLFEGKSKGGTAS FT YFESVKATDTYLVTLNLRRRLPGLIEALTLPGMAIAAPSALTGGPKENPAQSLSTKPVG FT TGPYTFVSNKDGVVRLEIFKDYWNQSRLAENKTHPEVALISSVPSPYNREGALLADEID FT GFDMVSVDTMRTLVRNAKVVVQRDPFSVLYLGMDQRNKWLAKPEFRMAIAHAVNRTSLA FT EKLFLQGSKNASTLLPSALSIPAPDETPNHDTTKAKTLLADLGYNGEEIEFAYPLRVSR FT NYLPLPERTFAQIADDLAAAGIRVKPRPIAWTDGYVQTVQSKDFNGLHLLGFSGGYRSA FT DDFLSGILSSKENEFGYTSPLLDSQVMLARSIPAGEAQTAAYADILTILNADLPVLPLV FT FPISALAFNGNVTFYPPSPMLNECYADVQMTNSPSISS" FT CDS complement(1530604..1531536) FT /transl_table=11 FT /locus_tag="AARI_13650" FT /product="D-isomer specific 2-hydroxyacid dehydrogenase FT family protein" FT /function="2 Intermediary metabolism" FT /EC_number="1.1.1.-" FT /note="match to PF02826 (D-isomer specific 2-hydroxyacid FT dehydrogenase, NAD binding domain)" FT /db_xref="GOA:E1VVB8" FT /db_xref="InterPro:IPR006140" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VVB8" FT /protein_id="CBT75571.1" FT /translation="MSSQRTISFPTQELIDAVGPIPENLKAVLWDLENEPRTPLEDIEI FT AVLPYMASPQRLKNIRQAPNLKIVQTQNTGYDGMVDLIGDRADINTAAGVHAAATAEMA FT IGLAIASLRGYPQAVRDQQSGHWNPQQWPGLADRTVALVGVGGIGEEIRKRLEPFEVNL FT LRFGSTARTDDHGQVFATADLAARAAEIEVLILIVPLNESTHHLVDAELLAQLPDGATV FT VNVARGPVVQTEAIVAEVASGRLNMASDVFDPEPLPADHPLWQHPNALVIPHNGGNTKA FT FFPRMVKLLKKQVQSWAAGHDGENLVHRS" FT tRNA 1531710..1531785 FT /locus_tag="AARI_36740" FT /product="transfer RNA-Lys" FT /anticodon=(pos:1531743..1531745,aa:Lys) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 1531832..1531907 FT /locus_tag="AARI_36750" FT /product="transfer RNA-Lys" FT /anticodon=(pos:1531865..1531867,aa:Lys) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 1532292..1532364 FT /locus_tag="AARI_36760" FT /product="transfer RNA-Lys" FT /anticodon=(pos:1532325..1532327,aa:Lys) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 1532431..1532922 FT /transl_table=11 FT /gene="bcp" FT /locus_tag="AARI_13660" FT /product="putative peroxiredoxin" FT /function="4.2 Detoxification" FT /EC_number="1.11.1.15" FT /note="peroxiredoxin protects cells against toxicity from FT reactive oxygen species by reducing and detoxifying FT hydroperoxides. The Bcp protein shows substrate selectivity FT toward fatty acid hydroperoxides rather than hydrogen FT peroxide or alkyl hydroperoxides" FT /db_xref="GOA:E1VVB9" FT /db_xref="InterPro:IPR000866" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:E1VVB9" FT /protein_id="CBT75572.1" FT /translation="MSTPEKTSRLTAGDQAPDFTLQDAAGNSVAPADYRGKKTIVYFYP FT AASTPGCTKQACDFRDSLESLQGLGYAVVGISPDKIAKLEKFVAKEELNFPLLSDEDHS FT VAEAYGAWGEKKNYGKVYEGLIRSTIVVDEEGKVALAQYNVRATGHVAKLRRDLGIDPK FT " FT tRNA 1533015..1533099 FT /locus_tag="AARI_36770" FT /product="transfer RNA-Leu" FT /anticodon=(pos:1533049..1533051,aa:Leu) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 1533217..1533777 FT /transl_table=11 FT /locus_tag="AARI_13670" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VVC0" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VVC0" FT /protein_id="CBT75573.1" FT /translation="MAAKDLSTMYGLSESDPEQKLINRAGMSASDLEQIDRIMAEMGRM FT RQIERRIMRSSQEFMKLNETDMRALRKIISAKHAGRSVTPGELSQYLGISSASVTKMID FT RLEAHGHVLRTKHPTDRRSQCVEVTEETHLAARDQVGRHHAKRFEAASRLSSEERDVVI FT KFLAGTSDAMESSLGSPLDDDAR" FT CDS complement(1533802..1535265) FT /transl_table=11 FT /locus_tag="AARI_13680" FT /product="putative NAD dependent epimerase/dehydratase FT family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF01370: NAD FT dependent epimerase/dehydratase family. This family of FT proteins utilise NAD as a cofactor. The proteins in this FT family use nucleotide-sugar substrates for a variety of FT chemical reactions" FT /db_xref="GOA:E1VVC1" FT /db_xref="InterPro:IPR008030" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR021295" FT /db_xref="UniProtKB/TrEMBL:E1VVC1" FT /protein_id="CBT75574.1" FT /translation="MSLVAVTGASGYIGGRLVPLLLGKGHQVRVFTRDAQRLRDVPWRG FT QVEVVEGDLQDPAAVAKLCKDADLVYYLVHSMSSTRQFTAQEKACAQVMAQAAREQGVS FT QLVYLSGLHPAGALSEHLASRVAVGEILSTSANTLVLQAGLVIGSGSASFEMVRHLSEV FT LPVMPAPRWVLNRVQPIAIRDALHYLAACADLPRPVHKTYDIGGPSSYTYAQLMKIYAQ FT VAGLREPKIWALPLLTPRLASHWVNLVTPLPRTLASALVQSLQHDCVMGSREIDELIAP FT PAEGLCDYRRAVQLALEKMDADAVPTSWATAHPVTAPAEPLPSDPDWSGHKAYTDIRRA FT TTTATEAQLFSVLQRLGGESTYFAFPGLWKLRGLLDKLAGGVGSRRGRRSHSTLALGDV FT LDWWRVEALEENSLLRLRAEMRAPGRAWLDYRIQKGTDGQTELIQRAVFFPRGLAGRCY FT WWAVYPFHAAIFPATIANIVRAAQKHEAD" FT CDS complement(1535262..1536092) FT /transl_table=11 FT /locus_tag="AARI_13690" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="8 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VVC2" FT /protein_id="CBT75575.1" FT /translation="MSSSPDYPSTSPPTRAPSVSWTLPVITAIALVLAIAVSFIGSGAL FT GGTPIQQAAGGYLGADSTLLAPAGPAFSIWSVIYTGLAVYGIFQLTAAGRRSDWAASLR FT VPALLSALLNAAWITVVQLGLLGMSFAVIFILVAYLAWMLTIMVSRTPSSRTEYWIMWL FT TFGIYLGWVCVASIANTSAWLLSLGFGENASWAPGLAVALLAVAVAIGLGTSAYSGRIF FT TALAMAWGLAWIGQSRLAGSNQSELVGYAALACAALLLLGSIAIAWRKRGVPAP" FT CDS 1536208..1536693 FT /transl_table=11 FT /locus_tag="AARI_13700" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VVC3" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VVC3" FT /protein_id="CBT75576.1" FT /translation="MECSPPLNSSEVFRMLLSLHRSYELCETRLRHRLDLNDTDLRAVN FT LLRSMQTPSSGQLARELGVSSAGITSVLDRLEARGLIERKHHPADRRRTMVAAGPRFPE FT ATGPGQVLLRGVHKFYAQLDPPGRRNLAELLQQARTELDQSGTTSDENQATPDKSFQ" FT CDS 1536700..1537809 FT /transl_table=11 FT /gene="crtE" FT /locus_tag="AARI_13710" FT /product="farnesyltranstransferase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.5.1.29" FT /note="identified by similarity to protein SP:Q9KK76 FT (Brevibacterium linens). A variety of isoprenoid compounds FT are synthesized by various organisms. In bacteria this FT pathway leads to the synthesis of isopentenyl tRNA, FT isoprenoid quinones, and sugar carrier lipids. FT Farnesyltranstransferase catalyzes the sequential addition FT of the three molecules of isopentenyl pyrophosphate onto FT dimethylallyl pyrophosphate to form geranylgeranyl FT pyrophosphate" FT /db_xref="GOA:E1VVC4" FT /db_xref="InterPro:IPR000092" FT /db_xref="InterPro:IPR008949" FT /db_xref="InterPro:IPR017446" FT /db_xref="UniProtKB/TrEMBL:E1VVC4" FT /protein_id="CBT75577.1" FT /translation="MTMHTATHLAQPATAISAAIGSGLIDGPTRQKISDRLEEIAIQAQ FT RRSAAYSAQTALLWSRISKSLATGKLMRPSLVMLGYRAFGGGNEARAIDLGCAFELLHA FT ALLIHDDVVDRDFMRRGKATISALYRDQASASGRSLADAEHAGNSVGIIAGDLLISEAI FT KLAARAAAGSDSEAGVEQAFFEAIEQAGAGELEDLLYSLGSAAATTSQVLRMEQMKTAA FT YSFQLPLQAGALLAGAHPGQAEAIGAVGCQLGVAYQIIDDVLGTFGDPAQTGKSIESDL FT REFKSTILLALASEDKEFAALLSGFREGKVDAGRIRHELAAHGTERFARQLAKQLCSRA FT TGSSAFLDLPEEARTLLHQCSALILERSS" FT CDS 1537815..1538759 FT /transl_table=11 FT /gene="crtB" FT /locus_tag="AARI_13720" FT /product="phytoene synthase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.5.1.32" FT /note="identified by similarity to protein SP:Q93QX6 FT (Corynebacterium glutamicum), match to protein family FT PF00494. Phytoene synthase catalyzes the conversion of two FT molecules of geranylgeranyl diphosphate (GGPP) into FT phytoene. It is the second step in the biosynthesis of FT carotenoids from isopentenyl diphosphate. It is found in FT all organisms that synthesize carotenoids: plants and FT photosynthetic bacteria as well as some non- photosynthetic FT bacteria and fungi" FT /db_xref="GOA:E1VVC5" FT /db_xref="InterPro:IPR002060" FT /db_xref="InterPro:IPR008949" FT /db_xref="InterPro:IPR019845" FT /db_xref="UniProtKB/TrEMBL:E1VVC5" FT /protein_id="CBT75578.1" FT /translation="MTREFSSTDTTGTAALEHYSRAASRSARVVLGEYSTSFSLACRLL FT DASSAGHIANIYALVRLADEIVDGVAFQAGLDDPAIGACLDELEAETLRAMDRGYSTNM FT VVHAFAITARATGIKAELTTPFFASMRADLSTGEHDARSLQEYIYGSAEVIGLMCLQVF FT AAMPGAPQLNRAEEQRTKLAARSLGAAFQKVNFLRDLAQDSQELGRTYFPGMDPEGFDE FT QGKALLVAQINQDLAAARAGLPYLAPQAARAVCLAHDLFQELNVQLEKVPAAALLRTRI FT SVSAPRKAMIALRVLLGAGTPSHHKLRMEVSSR" FT CDS 1538756..1540348 FT /transl_table=11 FT /gene="crtI" FT /locus_tag="AARI_13730" FT /product="putative phytoene desaturase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="identified by similarity to protein SP:Q93QX5 FT (Corynebacterium glutamicum), match to protein family FT TIGR02734. Involved in carotenoid biosynthesis. Phytoene is FT converted to lycopene by desaturation at four (two FT symmetrical pairs of) sites. This is achieved by two FT enzymes (CrtP and CrtQ) in cyanobacteria (Gloeobacter being FT an exception) and plants, but by a single enzyme in most FT other bacteria and in fungi. This single enzyme is called FT the bacterial-type phytoene desaturase, or CrtI" FT /db_xref="GOA:E1VVC6" FT /db_xref="InterPro:IPR002937" FT /db_xref="InterPro:IPR014105" FT /db_xref="UniProtKB/TrEMBL:E1VVC6" FT /protein_id="CBT75579.1" FT /translation="MNHQDQEVVVIGGGFSGLASAGLLAARGCKVTLIEQQEHPGGRSG FT RLEREGFRFDTGPSWYLMPEVFDHWFRLMGTSTAEQLDLRELPTGYRVFFQNRQAPADF FT GIGAAASDLFETLEPGSAPALERYLRTAKEGYELALEHFLYDDFHSLKSLLDPRILRRA FT PQLAKLLSTSLQSHVARRFASNEIRQVLGYPAVFLGSSPEKTPALYQLMSHLDLADGVK FT YPMGGFAAVADAMAQLARKHGAQIQLGATATAIETSTGKNLAVSAVRWIDANGTLHRTP FT ATKVIGAADVRHLEGELLPESLQTHTAKSFARKDPGPSAVLLCLGIKGKLPQLEHHNLL FT FTEDWSENFSRIRQGRELEPETSIYVCKPSATDPGTAPEGCENLFILVPAPALPEWGIG FT AADGQGDAAVEAVAEAAIDQLSAWARIDDLRERIVVRQSIGPGDFAQQYGAYRGGALGL FT AHTLGQSAMLRPGNRSAKVEGLYYAGSTVRPGIGVPMCLISGELAAKAVLGIKDAGPMP FT ENRSVMRAQEAGA" FT CDS 1540345..1540707 FT /transl_table=11 FT /gene="crtYe" FT /locus_tag="AARI_13740" FT /product="putative C50 carotenoid epsilon cyclase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="identified by similarity to protein SP:Q93QX4 FT (Corynebacterium glutamicum). In Corynebacterium glutamicum FT MJ233C, CrtYe and CrtYf encode the proteins of a C50 FT carotenoid epsilon cyclase, which is involved in C50 FT carotenoid biosynthesis. It catalyzes the formation of FT flavuxanthin from lycopene" FT /db_xref="GOA:E1VVC7" FT /db_xref="InterPro:IPR017825" FT /db_xref="UniProtKB/TrEMBL:E1VVC7" FT /protein_id="CBT75580.1" FT /translation="MIYLGTLVFLLVCMGLLDAKGKLFIFRHPLRGFLALALGTGFFVF FT WDVLAIRAGIFLHKESQFMTGIMVGEQFPLEEVFFLVFLCYCSMIAFTGLPVAARALRN FT RRLDTVGRRQGGSHVS" FT CDS 1540697..1541053 FT /transl_table=11 FT /gene="crtYf" FT /locus_tag="AARI_13750" FT /product="putative C50 carotenoid epsilon cyclase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="identified by similarity to protein SP:Q93QX3 FT (Corynebacterium glutamicum). In Corynebacterium glutamicum FT MJ233C, CrtYe and CrtYf encode the proteins of a C50 FT carotenoid epsilon cyclase, which is involved in C50 FT carotenoid biosynthesis. It catalyzes the formation of FT flavuxanthin from lycopene" FT /db_xref="GOA:E1VVC8" FT /db_xref="InterPro:IPR017825" FT /db_xref="UniProtKB/TrEMBL:E1VVC8" FT /protein_id="CBT75581.1" FT /translation="MFLEMSLIFLIVAAAVFAAGMAVGKQSLRSVAKPLGAAMALMLAL FT TAVFDNLMIAAGLFGYGSGTLTGWRIGLAPIEDFLYAACAVLLIPGLWWLLGFGRTGST FT TSASEGSTSRKDGS" FT CDS 1541050..1541913 FT /transl_table=11 FT /gene="crtEb" FT /locus_tag="AARI_13760" FT /product="putative lycopene elongase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /note="identified by similarity to protein SP:Q93QX2 FT (Corynebacterium glutamicum). In Corynebacterium glutamicum FT MJ233C, CrtEb converts lycopene into the acyclic C50 FT carotenoid flaxuxanthin by the addition of two C5 FT isoprenoid groups" FT /db_xref="GOA:E1VVC9" FT /db_xref="InterPro:IPR000537" FT /db_xref="UniProtKB/TrEMBL:E1VVC9" FT /protein_id="CBT75582.1" FT /translation="MIRGIVASSRPISWVNTAYPFAAAYLLAGGGVDWKFILGTVFFLF FT PYNLLMYGVNDVFDYESDMRNPRKGGIEGAVLSKQSHKALLIACTVCSLPFLIVLAAGG FT DAASNITLAVSIFAVLAYSAPRLRFKERPGLDSLTSAVHFVSPAVYGWVLAGSAVQAEQ FT WMVFLAFLLWGMASHALGAIQDIIPDRQGGLGSIATVLSARKTIYLVLACYLLAGGLVA FT VGVSGIGRWAAVLSLPYVLNVLPHLGISDASSGTVNRGWKRFLWINYLCGFLLTMLLIF FT SAFFTY" FT CDS 1541940..1542455 FT /transl_table=11 FT /gene="idi" FT /locus_tag="AARI_13770" FT /product="isopentenyl-diphosphate Delta-isomerase" FT /function="2.4 Metabolism of lipids" FT /EC_number="5.3.3.2" FT /note="catalyses the interconversion of isopentenyl FT diphosphate and dimethylallyl diphosphate. Dimethylallyl FT phosphate is the initial substrate for the biosynthesis of FT carotenoids and other long chain isoprenoids" FT /db_xref="GOA:E1VVD0" FT /db_xref="InterPro:IPR000086" FT /db_xref="InterPro:IPR011876" FT /db_xref="InterPro:IPR015797" FT /db_xref="UniProtKB/TrEMBL:E1VVD0" FT /protein_id="CBT75583.1" FT /translation="MDVILLSEEGQRIGTCPKELVHTTDTVLHQAFSCHVRNEAGEVLV FT TRRALSKVTWPGVWTNSFCGHPQPGESFEEAIARHAMHELGFKVSTIEPALPDFRYRAV FT DASGIVENEICPVFTAVIDSEITANPDEVMDYCWVDPAKLGQALRATPWAFSPWLVMQA FT KGIALYAA" FT CDS complement(1542616..1543077) FT /transl_table=11 FT /locus_tag="AARI_13780" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVD1" FT /protein_id="CBT75584.1" FT /translation="MDNRPDENPTEQIKARLHAAFDSQIPNFASYNLVAGTGVAGSGGL FT KVIGYRRQPAELIIAPVNANSLESSEDAININNTNVNQLAELSDGGYEVAISSGRVFRF FT NIPEAPSVDFHVDDAVSIGATIDQKSDAEDFADFMDHFMNTIEGTENFV" FT repeat_region 1543126..1543133 FT /rpt_type=DIRECT FT repeat_region 1543134..1543157 FT /rpt_type=INVERTED FT mobile_element 1543134..1544350 FT /mobile_element_type="insertion sequence:ISAar1" FT /rpt_family="IS1595 group ISSod11" FT CDS 1543246..1544316 FT /transl_table=11 FT /locus_tag="AARI_34900" FT /product="transposase of ISAar1, IS1595 family, ISSod11 FT group" FT /function="4.5 Transposon and IS" FT /db_xref="InterPro:IPR024442" FT /db_xref="InterPro:IPR024445" FT /db_xref="UniProtKB/TrEMBL:E1VVD2" FT /protein_id="CBT75585.1" FT /translation="MTQPTPESTGNRPLAGRDYPADLAQLLAWFSDDESCVDYLQWLRW FT PEGICCPRCLSAFVNNEPDNRFRCKKCWYRFSATAGTIFDKTRTPLTVWFQTAWLMTAG FT KSGVCAAHLHRVLPISSYQTAWSMLGKLRSVMSTQDSSLLSGRVEVDESFFGGHRPGRT FT GRGAAGKTLVAGAIEIADDGWGRARLAIIPDASAASLREFITANIAPGSTIVSDGWRGY FT RNAVEGYAHEPVSVWKSGLEAHASLPAVHRLFALVKRMIEGTYQGSGSVGHLQEYLDEF FT VFRFNRRHSTHRGLVFMRLLERAVKRGPVTYRNLVRKPEPKAVHPRGVSGPHALPGSME FT REASERPWRSPRATLE" FT repeat_region 1544327..1544350 FT /rpt_type=INVERTED FT repeat_region 1544351..1544358 FT /rpt_type=DIRECT FT CDS 1544871..1546769 FT /transl_table=11 FT /gene="ilvB" FT /locus_tag="AARI_13790" FT /product="acetolactate synthase large subunit" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.2.1.6" FT /note="acetolactate synthase catalyses the first common FT step in the biosynthesis of the 3 branched-chain amino FT acids. The first step involves the condensation of either FT pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl FT fragment derived from another pyruvate molecule, covalently FT bound to the coenzyme thiamine diphosphate. The resulting FT products are 2-acetolactate and 2-aceto2-hydroxybutanoate" FT /db_xref="GOA:E1VVD3" 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:E1VVD3" FT /protein_id="CBT75586.1" FT /translation="MERIPMSNSTPANPASVAKSINRTKDAPAAVSSVVEASNPVQGPN FT NIVAPTQMTGSQAIVRSLEELGVKDVFGLPGGAILPTYDPLMDSTKINHVLVRHEQGAG FT HAAQGYAMVSGEVGVCIATSGPGATNLVTALADANMDSVPMVAITGQVNSAFIGSDAFQ FT EADIVGITMPITKHAFLVTNPEDIPQTLAAAFYLAQTGRPGPVLVDITKDAQTADMTFS FT WPPKVDLPGYRVVTRGHNKQLREATRLIASATRPVLYVGGGVIKANAHEQLKEFAEFIN FT APVVTTLTARGAFPDSHQQHVGMPGMHGAVSAVTALQQSDLLITLGARFDDRVTGVLSS FT FAPNAKVIHADIDPAEISKNRVADVPIVGSLDEIIPQLHEACATRFENEAPQDLTGWWG FT LLNRLRETYPIGYTETHDGLSAPQNVIGRIGELTGPEGVYVAGVGQHQMWAAQFVKYER FT PRSWLNSAGLGTMGYSVPAAMGAKVAQPDRVVWAIDGDGCFQMTNQELATCVINQIPIK FT VAIINNSSLGMVRQWQTLFYDGRYSNTDLNTGHGTARIPDFVKLADAYGCVGLRCERDE FT DIDATIQQALQINDRPVVIDFVVSADSMVWPMVPSGVSNDQIQIARGMTPEWEDED" FT CDS 1546773..1547291 FT /transl_table=11 FT /gene="ilvN" FT /locus_tag="AARI_13800" FT /product="acetolactate synthase small subunit" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.2.1.6" FT /note="acetolactate synthase catalyses the first common FT step in the biosynthesis of the 3 branched-chain amino FT acids. The first step involves the condensation of either FT pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl FT fragment derived from another pyruvate molecule, covalently FT bound to the coenzyme thiamine diphosphate. The resulting FT products are 2-acetolactate and 2-aceto2-hydroxybutanoate" FT /db_xref="GOA:E1VVD4" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR004789" FT /db_xref="InterPro:IPR019455" FT /db_xref="UniProtKB/TrEMBL:E1VVD4" FT /protein_id="CBT75587.1" FT /translation="MAKHTLSVLVEDVPGVLTRVASLFARRAFNIHSLAVGPTEIPGIS FT RMTVVVDVEGDSLEQVTKQLNKLVNVIKIVELLPETSVQRDHIMIKVRADAATRLQVTQ FT AAELFRASVIDVSTDSLVVEATGNAAKIDALLAVLEPFGIREIVQAGTLAVGRGSKSMS FT DRALKTLSA" FT CDS 1547416..1548447 FT /transl_table=11 FT /gene="ilvC" FT /locus_tag="AARI_13810" FT /product="ketol-acid reductoisomerase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.1.1.86" FT /note="catalyses the conversion of acetohydroxy acids into FT dihydroxy valerates. This reaction is the second in the FT synthetic pathway of the branched chain amino acids FT leucine, valine and isoleucine" FT /db_xref="GOA:E1VVD5" FT /db_xref="InterPro:IPR000506" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR013023" FT /db_xref="InterPro:IPR013116" FT /db_xref="InterPro:IPR013328" FT /db_xref="UniProtKB/TrEMBL:E1VVD5" FT /protein_id="CBT75588.1" FT /translation="MADLYYEDDADLSIIQGKKVAVIGYGSQGHAHALSLRDSGVEVIV FT GLAEGSKSRAKAEAEGLKVATVAEAAAWADVIMILTPDQVQAQVYTESIAEHLEEGNAL FT FFGHGFNIRFGFIQPPANVDVALVAPKAPGHTVRREFEAGRGIPDLIAVEQNFTGGAKE FT LALSYAAGIGGTRAGVIETTFTEETETDLFGEQAVLCGGTSQLVQYGFEVLTEAGYKPE FT IAYFEVLHELKLIVDLMWEGGIAKQRWSISDTAEYGDYVSGPRVITPEVKENMKAVLAD FT IQSGAFANRFMEDQKAGAPEFKELRAKGEAHPIETTGRELRSLFSWISDASSDDYVDGS FT VAR" FT CDS complement(1548637..1549293) FT /transl_table=11 FT /locus_tag="AARI_13820" FT /product="hypothetical secreted protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.464 FT between position 43 and 44" FT /db_xref="UniProtKB/TrEMBL:E1VVD6" FT /protein_id="CBT75589.1" FT /translation="MGRFGAHARSNFHGEKLNKLVQRSLAVIASGALVFSGVSAAAAAP FT LPASISSASVVAAKKKAPAVTIKKIGTKTVKGSAKATIKPSYSKAKNVKIKSALLKVVK FT GKKTIASKKKSVKLAAGTYKVTTTVKYQLKGKTSTVKKTQTLLVKKAAAKRSVKMNGKA FT KNCPAGYPVKGNRTGSQKEWKYHVKGQRFYDITKPEECFKTGSDARKAGYRASKI" FT CDS 1549493..1550194 FT /transl_table=11 FT /locus_tag="AARI_13830" FT /product="putative SAM-dependent methyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.1.1.-" FT /note="identified by match to protein domain PF08241" FT /db_xref="GOA:E1VVD7" FT /db_xref="InterPro:IPR013216" FT /db_xref="UniProtKB/TrEMBL:E1VVD7" FT /protein_id="CBT75590.1" FT /translation="MPQESNYDDFAKDYADENEFSMLNAYYERPATLELAGDVAGRKIL FT DIGCGAGPLAEQLTSRGATVSGFDTSQEMVELARQRLGGGSDIKVATLGEQLPYEDDSF FT DDAIASLVFHYLPDWSYALEEVRRVLKPGGRLIMSVNHPILYPFNHRGQDYFQLTRYTD FT EVTFNGKPAELTYWHRPLHDTMTALISAGFAIARVWEPPYAKDAPEGVIPEALRERDAF FT LSFLFFSLRAN" FT CDS 1550673..1553306 FT /transl_table=11 FT /locus_tag="AARI_13840" FT /product="DNA binding domain-containing protein" FT /function="3 Information pathways" FT /note="match to PF00196: Bacterial regulatory proteins, FT luxR family" FT /db_xref="GOA:E1VVD8" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR011990" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:E1VVD8" FT /protein_id="CBT75591.1" FT /translation="MEYSRFSSFNDASLGLGHWSELNYLKELSRIPELTMEKILSNQHV FT MGAVISGPPGSGRRAWVEAGMEKLENPPQLIRLNGSNFGTKVPLGALSYLLARLDLDDY FT TSRHELVHGLGRILCSENRPAAVMLGRPELIDEESSSLLAQLATMGKIKLFVICEQIQD FT LPGDLFALYRSGRIKHRLIHRMDNAETHQFVESELGGPASTFSSAVLRYLTSGSRELMS FT KLIQCWRDDGQLLQRNGSWILKLSGFGTGSATHGLYSLMTRGLDSREYDLMLAIALGGP FT VTLERIHLCELTESLDVLLNRGQVRYLPGASRRVGLCNPLLALLVRTDEQENKKESVKA FT LLKQLHADPLAAQVLAQVQALSDMNDHQAQIAVAKRYQATGYGPDAWPADPKTRMKIVD FT MHVKALAMTSQFQPAFEVIEVARTGAMAARDKNAPDEALDAALQELDLLAQFVSHLEDE FT MSRTKSDISSTQELVESANWMNESLRLRALSVQASVWAARQRQADALKLTLYVDSRLKD FT THLMSSQISTFDPEDAVDIEFELLQAELLSGHWNLALERSKKLASGFYSSPLSVTFSET FT VYGILLALDNDLDGAVAVLKKNREQLAAGQRPLLPAIINAITAYELARSGQRHEASAML FT ERNSLYHPTVDVPVNFYRWVQEIFTALTHAEIGATDLALDMLKNFTTQMRGESHTLLES FT LTLGYRVRLGDSEALTDFLRASALCQGTVGEGMSQVAKAIAAGNSSCTAAGLGDLAKLG FT HVLFSTASNNRIFANLEIRDQRKISRIINESKRSHATQFSGMAAELEESGEYRPAWMRE FT LTKREVQIAKLAIGGKSNAEIAKANGVSIRTIEGHLYQVYSKLQVRNRQELTALDRSSQ FT GTAGLR" FT CDS 1553303..1555969 FT /transl_table=11 FT /locus_tag="AARI_13850" FT /product="DNA binding domain-containing protein" FT /function="3 Information pathways" FT /note="match to PF00196: Bacterial regulatory proteins, FT luxR family" FT /db_xref="GOA:E1VVD9" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:E1VVD9" FT /protein_id="CBT75592.1" FT /translation="MTQELQVHRTHPSEYTELIQVLKRSEPSGAVILGALGMGKTTLVE FT SALQALGFPEPVMRLYCTRSLSEVPHGALSPYLGGLESIENPVTVLRELNRTLLASPSV FT SGTRIVVVEDAQYLDAQSCFILSLLVENGVVKVLALGGSSLEEGTPLASLGELPAFTRI FT QMQPLDREGIRQVAQSILGRQLSEGSIGIIERVSGGNPRFVEAYVASCMDQGTLFQDTS FT LLQDQAVHEPLWVVARALPEVDARLRALGREFFRFVTAEEERTLLLLALAGPQYKALLD FT ECALPYRRMLSSGDLEVRGETVSVRSKLLQRTFRELASVQQNAQLNELWARALSALGME FT PNAREILWCLELGVEVPSEQILACASGAAAEMNFRVALRLCLLGQLPQHHEEGGLLEAQ FT ALLGLGRHYAARAQLLRLIDQLTDLDLLGQAYALLLEVTSCIGVDVQEAAIIMDKWQDA FT AAGYEDKAAVERFLALHTDALRVLKFWVGINTPSGTLPEVQDMRDYLDDPDLNVQARII FT AMLALGDRLTSEGLCHDALDVLYPAMQLLKEHAVLGTLYEVRVFFRIGWNLLFSGEYGK FT AQAFIGQYRGDRLRIIHHYRGSVALLDGIHELLQGRVRKAIEKMAEAITELRTFDTAQV FT LALACNVYRMLLYRFGLPQPEALQQALNESQDKGASALSGQLGEESSEYRILARGFAAA FT LESPYEGESIRDFQLIHREILFSKVRQLSDDELSKNADHASLRMLAKQQQGTRARLLSR FT LAELRISEGTEALEHLADEALQCCENLVAVEALARAAERHAAAGDQRRCGALLRRATEL FT IEQHQMDPGKYLARVLAMTELTSREAEIVNLARRGLNNAQIARNLILSQRTVEGHLYRV FT FSKLGINERSELKKISS" FT CDS complement(1556150..1556389) FT /transl_table=11 FT /locus_tag="AARI_13860" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVE0" FT /protein_id="CBT75593.1" FT /translation="MAVHECLTPNWAWVFKYAYPKFTRIVLARCHLDLLSEHGKGSVPR FT GEYAYWYGACGQKEPATVLGAIREDQRAAGPVPG" FT mobile_element 1556441..1557889 FT /mobile_element_type="insertion sequence:ISAar20" FT /rpt_family="ISL3" FT repeat_region 1556441..1556467 FT /rpt_type=INVERTED FT CDS 1556576..1557883 FT /transl_table=11 FT /locus_tag="AARI_34910" FT /product="transposase of ISAar20, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVE1" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VVE1" FT /protein_id="CBT75594.1" FT /translation="MLNSTFTEPDLTTFTGLDGLGLTAIGQCLGAAKAEILCHVTTPNP FT WCRTCGGEGTPRDTVTRRLAHQPFGWRPTVLVIKHRRYRCGHCQRVWREDLSRAAPERQ FT KISRTGLAWALNGLVCQHLSVSRIAEGLGVTWNTANDAVLAEGQRLLIDDPARFSGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLLDMVPGRSKAVFKTWLAGQDDQW FT KQGIDVVAMDGFTGFKTAAAEELPHAVEVLDPFHVVKLGSEALDQTRQRVQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATDKQKAKLEDLFTAPEYEPVQLVWSVYQKMVDAYRQPKP FT EIGRWALEQLINGVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHVGSSNGPTEALNGR FT LEHLRGIALGFKNLTHYIARSLLETGGFRPWLHSQS" FT repeat_region 1557863..1557889 FT /rpt_type=INVERTED FT gene 1558384..1558656 FT /pseudo FT /locus_tag="AARI_34920" FT /product="N terminal part of transposase of IS110 family FT (disrupted by insertion of ISAar19, ISL3 family)" FT /function="4.5 Transposon and IS" FT repeat_region complement(1558614..1558621) FT /rpt_type=DIRECT FT mobile_element complement(1558622..1560070) FT /mobile_element_type="insertion sequence:ISAar19" FT /rpt_family="ISL3" FT repeat_region complement(1558622..1558645) FT /rpt_type=INVERTED FT CDS complement(1558628..1559935) FT /transl_table=11 FT /locus_tag="AARI_34930" FT /product="transposase of ISAar19, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRG4" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VRG4" FT /protein_id="CBT75595.1" FT /translation="MLNPTFTAPDLTTFTNLDGLGLTAIGQHLSAAKAEILCHVTNPIP FT WCQTCGAAGIPRDTVTRRLAHEPLGWRPTVLVIKHRRYRCANCQRVWREELSQAVAPRQ FT KISRTGLRWALVGLVCHHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFDGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLIDMVPGRSKAVFKTWLADQEEQW FT KQGIEVVAMDGFTGFKTAAVEELPHAVEVLDPFHVVKLGSEALDQTRQRIQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKTKLEDLFKEPEYEPVQLVWSVYQKMVDAYRQPKP FT EVGRWALEQLINEVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRRRLHPQS" FT gene 1560030..1560929 FT /pseudo FT /locus_tag="AARI_34940" FT /product="C-terminal part of transposase of IS110 family" FT /function="4.5 Transposon and IS" FT /note="disrupted by insertion of ISAar19, ISL3 family" FT repeat_region complement(1560047..1560070) FT /rpt_type=INVERTED FT repeat_region complement(1560071..1560078) FT /rpt_type=DIRECT FT CDS 1561047..1562405 FT /transl_table=11 FT /locus_tag="AARI_13870" FT /product="putative sugar transferase" FT /function="1 Cell envelope and cellular processes" FT /note="match to protein family PF02397. This entry FT represents a conserved region from a number of different FT bacterial sugar transferases, involved in diverse FT biosynthesis pathways. Examples include galactosyl-P-P- FT undecaprenol synthetase (EC:2.7.8.6), which transfers FT galatose-1-phosphate to the lipid precursor undecaprenol FT phosphate in the first steps of O-polysaccharide FT biosynthesis; UDP-galactose-lipid carrier transferase, FT which is involved in the biosynthesis of amylovoran; and FT galactosyl transferase CpsD, which is essential for FT assembly of the group B Streptococci (GBS) type III FT capsular polysaccharide" FT /db_xref="GOA:E1VVE3" FT /db_xref="InterPro:IPR003362" FT /db_xref="InterPro:IPR017475" FT /db_xref="UniProtKB/TrEMBL:E1VVE3" FT /protein_id="CBT75596.1" FT /translation="MPAVAVAQNSALGLLATGNTAYYAIAGLLLALAWMASLRLFKTQT FT IGTVAAGLQEYKFVLVAWAALAGGLGVTIGLTGQHSLRIFLIYSLPLGLGALLVSRWTW FT RQWLMRQSRNGYALSNVLLYGQAVDVPFALRQISKCTRQVYRVVGVVVDGQSEPEAQVD FT IRAADPTLPVIFGAESLHTEATRLNADSVIVAGPLTGGNEALQHLGWNLESTGTKLIVA FT SSLIGIADRRVRTSPLDGMALHHVEPARFTGVRYFLKRCFDVLFSSLVLLALAPIFALI FT ALLIRRDGPGKIFFLQERAGQDGRPFKMFKFRTMVEDAETQLATLQEQNEGSGPLFKLK FT NDPRVTRCGKWLRKHSLDELPQFLNVLRGEMSVVGPRPPLFTEVDKYQGHTNRRLLLKP FT GVTGLWQVSGRSNLSWQESIRLDLYYAENWTVCSDLRIIWRTLSVMLKPEGAY" FT CDS 1562949..1564556 FT /transl_table=11 FT /locus_tag="AARI_13880" FT /product="carbohydrate binding domain-containing protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="match to PF02018" FT /db_xref="GOA:E1VVE4" FT /db_xref="InterPro:IPR003305" FT /db_xref="InterPro:IPR008979" FT /db_xref="InterPro:IPR013781" FT /db_xref="InterPro:IPR017853" FT /db_xref="UniProtKB/TrEMBL:E1VVE4" FT /protein_id="CBT75597.1" FT /translation="MKEPTPSISRPKYQQAAPGASLLKKTFVTIASASLLTGLGAVPAA FT QAAKPDEAKNLVVNGKFDAGTEGWRTNDANTEKLSVRKYAQGAVAELRTTETKTAVLND FT ITNTIKSTEADASYTVSARVRTEHPGIWGQLRTRIVGNGETKIVGESFGLNDTSWTTVS FT FDLTVPTSGSTVDLNVLAWSLDPSKNLIIDDVKLVERDAASTQPVPAPVEEDPKGPATV FT EEDPKGPAPVEEDTQKPEQNTDTPAPIQPEPIDKCDVAPKTDRTLFGVSLGGSTTGAKE FT TFAQSMARQDANYDDTEVVRLFDPGMPVSWSKRAPYIEDKTISISFRPDPAEVLTGQHD FT AALLNWFNAAPSDQTIYWTYFHEPEPKIAAGEFTAAQYRAAWARIAKLADQACKPNMHA FT TLILTGWTANPRSNRDWRDYYAGDSVIDVLGWDPYNDATSQEGPKSYASPESIFGNVVE FT ISKNAGKPFAIGETGTRLIPTDPNGTQRAEWLKDVARYLDNEDALFVAYWDSKTFADFR FT LLDSASRDSWAGIIDGKY" FT CDS complement(1564632..1565600) FT /transl_table=11 FT /locus_tag="AARI_13890" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVE5" FT /db_xref="InterPro:IPR000863" FT /db_xref="UniProtKB/TrEMBL:E1VVE5" FT /protein_id="CBT75598.1" FT /translation="MANPDAISGSKPLVLYIAGSGRSGSTLLERLLGQLEGVQTLGEVH FT HMWLRAIGKNEQCGCSEIFTECEFWSQVGQEAFGGWDKVSVDEVERLKSQVDRQRHQPV FT TASPWTSKERTRKLLEYTDYYARVYHAVQKTTGARIIVDSGKHPSLALALTHRNDIDLR FT IVHLVRDSRGVSHSWGKAVQRPEATTDEDAMMQQYSPLISSVLWLSTNLAAEGIRLRGV FT PRYRMRYEDLVARPKPTLLKMFQSLGMPEDLELPIADDGTIDLLPNHSAAGNPMRFSVG FT TTKLRPDTAWRTQMGSKDRRLVSVLTASLRYCYGYAGKLGT" FT CDS complement(1565593..1566123) FT /transl_table=11 FT /locus_tag="AARI_13900" FT /product="putative transferase" FT /function="1.1 Cell wall" FT /note="match to PF00132: Bacterial transferase hexapeptide FT repeat. A number of different transferase protein families FT contain this repeat, such as galactoside acetyltransferase- FT like proteins, the gamma-class of carbonic anhydrases, and FT tetrahydrodipicolinate-N-succinlytransferases" FT /db_xref="GOA:E1VVE6" 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:E1VVE6" FT /protein_id="CBT75599.1" FT /translation="MKLLAILTEDLQANAGQPKGQLAVIGYRLAHAARKPLDQPPRIWA FT LPIGLVYRLLVEWVLGIEIPWGTKIGRRLRIYHGVGLVINDRAQLGDDVRLRQGITIGN FT SGHGVDCPVIEDGVDIGASAVLLGGITVGSHASIAAGALVTKDVPAGGQAKGNPAVIKE FT PRPVPVVEEGNRG" FT CDS complement(1566120..1567619) FT /transl_table=11 FT /locus_tag="AARI_13910" FT /product="possible lipopolysaccharide biosynthesis protein" FT /function="1.1 Cell wall" FT /note="match to protein family PF02706. This family FT includes proteins involved in lipopolysaccharide (lps) FT biosynthesis" FT /db_xref="GOA:E1VVE7" FT /db_xref="InterPro:IPR003856" FT /db_xref="UniProtKB/TrEMBL:E1VVE7" FT /protein_id="CBT75600.1" FT /translation="MSSEESVSLNIFWIIFKRYLPLILIITVLFTLAGVALAFALPKSY FT VASARVNITPIVSDPFNPTRSASGLLDVTTEEAMASSWIVAKRATEELGDDMHVMTMRQ FT NTEVRADINATTVSISYHAPSESEARAVADALATAYLDFRQEQADSRKARISDQLEDRI FT ESLRPVFNAASGEAKPVVQDQIATIERQLNQLALIDTNGGSVLNPASETGVFSEPSKKL FT FVAGGGVTGLFAGCVAAFACHRFSRKIRDHNDLQLVGFPALLPTITAPAASHDRVAAHE FT LDLFRTLRERVLNSSPTVRNLLLLDLGNLGLASRLGPQIAAAFAHTSQRVELLVLAPAA FT EDFPWGLEPYDFRIEQETTDAVFYSSAVLKELSLVVAKPDSNGLAPDPVVTNFVRERMV FT ETDETITRIVSLPRGSFESSKFSAARLADAVVILVPFKATLKSEVKRFGELVADLKKPV FT LAVFGVRMAKGSRARHMKAEAKQRASSGVERMDSMKEVSTR" FT CDS complement(1567733..1568680) FT /transl_table=11 FT /locus_tag="AARI_13920" FT /product="putative family 2 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00535: glycosyl transferase family 2. FT This domain is found in a diverse family of glycosyl FT transferases that transfer the sugar from UDP-glucose, UDP- FT N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to a FT range of substrates including cellulose, dolichol phosphate FT and teichoic acids" FT /db_xref="GOA:E1VVE8" FT /db_xref="InterPro:IPR001173" FT /db_xref="UniProtKB/TrEMBL:E1VVE8" FT /protein_id="CBT75601.1" FT /translation="MGNSLANSARSKARLSVGVVLATHNRPELMRKSLASISAQDYDGP FT IEVVIVFDKSPVDYSLERSTPLRTVRTIANTRAPGLAGARNTGILALSTELVAFCDDDD FT TWLEQKLARQVHALESSPDSEVASTAMKVIYNGTESVRCAGKQHVGYQDFLNSRMAMVH FT SSSLLFRRQKLIEGIGLVEEGLPNSMCEDWDLLLRASKRHPILHVDEPLIRVLWGGTSY FT FYHQWDVKNQAHQWMLEHYPDILTSKIGSSRVFGQLAFGHAALKNPHNALGWVRKSLKS FT NWREPRAYLALAVASGLVSDQTVIDRLQRKGRGI" FT CDS 1568822..1570147 FT /transl_table=11 FT /locus_tag="AARI_13930" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="10 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VVE9" FT /protein_id="CBT75602.1" FT /translation="MNNSFGDEEKSGLARAQLNSPALVTIDAVGRKSLPAWPFAVAFVG FT YPVLWVLGLGDTGWPMIAVYMVILLAKLVHGPKVPKAFGIWLLFMLWALCSALMLDSAG FT RIAGFAFRYSLYLAATVVFIYAYNARINLNAQRVLGILTAMWYFTVIGGIAGLLFPVFE FT LRTVLSYVLPQGLLSNEMIHEMAFRSLTQYNPNPDAYVISAPRPSAPFLYANSWGNVYS FT VLTPAVLVYLGMVRRTKRFWWIGASVLVSLIPAFLTLNRGMFLAMGIALAYVGVRAIMV FT GNMRVLGAMLGLGLVAAIAVTTLPVMERLDERTSKVSSVETRENLYIETFDRTLQSPAL FT GYGAPRPSIHPGAPSAGTQGQFWMVLFAHGFPGAILFVGWFAWIFGKTFKRTDKLGLLS FT NTVALITIIEIFYYGILTTGLVVVMTLAAIALREKPGGTPSE" FT CDS complement(1570218..1570901) FT /transl_table=11 FT /locus_tag="AARI_13940" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVF0" FT /protein_id="CBT75603.1" FT /translation="MAAIIIAVIWGLQMQNRTVNSSDPGSVPSTAATAEAESEEIPQGM FT DEVDPADDPVEQAAPKPSNIPSAETDPESEPENLPKQAENVSEELVETANTQLDEFLES FT YSEVLAAPEEADENLIEDLEKTLQDAALGQVQASAAEYAANGWVMTGAPEIVASSVREL FT DEEAAPPTMTVFACVDSSPVKITTTTGTRVPSNAGRAMNIFELQQNDDESWVLVNMSFP FT DDPSC" FT CDS 1571099..1572655 FT /transl_table=11 FT /locus_tag="AARI_13950" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="14 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VVF1" FT /db_xref="InterPro:IPR002797" FT /db_xref="UniProtKB/TrEMBL:E1VVF1" FT /protein_id="CBT75604.1" FT /translation="MNVGDGSSATSKSKNPHQQLGGVAKSGIISLTGSMTSAIMGFGLI FT LVLGRLLGESQAGIVLQSIAVFSIALAVARLGMDTTGVWLLPRLKLSEPALIRPAVFRL FT LVPTAALGMLGGLVLWFGAPLLASEQGGAAELVSSVRAMAWALPAGAVMMVALQITRGL FT GNINPFALIGNVFVPTLRPLFAVLVVAVGGTAVAVSISWAIPLLLGAIAALWVAGRRVK FT KASLLTADPQIQDPSAGKPIGHRIWGFAMPRWYASILEQSITWFDVVVVGFIAGASAAG FT VYGAASRFVTAGLIISTAMRIVVSPRFSSLLAQGKRTEVQHLYTTTITWVVLFGTPIFV FT VFGFFPQTILGWLGDGFETGAGVLLMLSAATVGCMMFGNADSLLMMSGRSGLLALNKSI FT VLALNIVGNLVLIPIWGIEGAAVVWSVSMLLNCLLAATQNKLTLGIGWESKPILYSVFV FT ALACSAIPCYVFTRFMGQSTLSLVIAVPVLLTFLAFWCFMDRRRLGLADLMRIRRATPI FT D" FT CDS 1572683..1573582 FT /transl_table=11 FT /locus_tag="AARI_13960" FT /product="sulfotransferase domain-containig protein" FT /function="2.7 Metabolism of sulfur" FT /note="identified by match to PF00686. This family includes FT a range of sulphotransferase proteins including flavonyl FT 3-sulphotransferase, aryl sulphotransferase, alcohol FT sulphotransferase, estrogen sulphotransferase and FT phenol-sulphating phenol sulphotransferase. These enzymes FT are responsible for the transfer of sulphate groups to FT specific compounds" FT /db_xref="GOA:E1VVF2" FT /db_xref="InterPro:IPR000863" FT /db_xref="UniProtKB/TrEMBL:E1VVF2" FT /protein_id="CBT75605.1" FT /translation="MNNLTLSKDSAPRWLKDAADIATRSYAQLTAPNRPAPDYLITGTK FT RGGTTSLFNYLLMHPGVMGLFPQVREKKSTDYFFKELERGDTWYRSHFQTEAYRKLKGS FT QLGYRPISGEASPYYMWDPRIATRIKASAPQVKSIILLRNPVERAWSHYQERVQNGVEP FT LDFVTALHLEDERMSSEYAAIEDGSEEYSEAFDFYAYRERGNYLPQLKNWFAKFDLDQV FT LVMRSEDMYQDVQGAVDQVCDFLEIPRHELPTKRTFNARKKSTPMPSEARDYLTNYFAD FT RNAELFDYLQVEPFWKIG" FT CDS 1573661..1574947 FT /transl_table=11 FT /locus_tag="AARI_13970" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVF3" FT /protein_id="CBT75606.1" FT /translation="MIENNLQSDKKKPASLGFALERLGQQIWAAGIEDGSLRLGVNPKP FT DNQYMQVESYWVIPSAKNPKFLVPDASSKLAAGALTSYRGLRNGTANAARFILGLVAKS FT GLPLSRDRLVVQLRTGTANCSPLSILKQKMDFEQLHAATGVRLGLNAKPTLHLFDETGN FT PVGFAKMSWNNASTTLVENETRVLGELDGGSAALRVPRVLDHGVIQGRSYLVTQPLPAG FT VRGLSQDDPAPTPVELQAIAPLSGESTLLEMKFFLGLQTKLDDLIVLDSGCGLCDPVQE FT LSRRLTQHDRKLPVATRWHGDLVPWNCARDRDGTLWCWDLETSDDGPAAGMDILHWHFN FT VRRRGKSQGAVADFEGAVQDSRLHHRALGLDDIAVSLVAAVYALKLVERAWTLASNSSG FT WDRSWISAEELSLLLGAARTQLDSPIGRR" FT CDS 1575228..1579541 FT /transl_table=11 FT /locus_tag="AARI_13980" FT /product="PDK domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF00801" FT /db_xref="GOA:E1VVF4" FT /db_xref="InterPro:IPR000601" FT /db_xref="InterPro:IPR001791" FT /db_xref="InterPro:IPR002181" FT /db_xref="InterPro:IPR003961" FT /db_xref="InterPro:IPR008979" FT /db_xref="InterPro:IPR008985" FT /db_xref="InterPro:IPR011047" FT /db_xref="InterPro:IPR012680" FT /db_xref="InterPro:IPR013320" FT /db_xref="InterPro:IPR013783" FT /db_xref="InterPro:IPR014716" FT /db_xref="InterPro:IPR022409" FT /db_xref="UniProtKB/TrEMBL:E1VVF4" FT /protein_id="CBT75607.1" FT /translation="MNLIPNVRKFLGVAAASSMVGMLLVAVPMSEAANAAPLDGLSEAT FT AAASCWEIKQEDSNAQDGSYWVMTPAMHAPQQVYCDMTTDGGGWVLVGKGRNGWATNYD FT GKGRESDLATAGVSPMSSHTTQYPSTLIDGLLNGQHVDTLEEGVRVKRAASSDGQSWQE FT VRLGMSKLDGWSWTFGALNEMNWYEFDGTRRSGGRTNDFGWDSGANHVTTTPIPSQGYS FT SGFAYGTSVPGSTSSTSYLFSRTENRGPAIPYAEVYVRPKVMTSSAEWERIGDSGTEEW FT TIPSGVRSLALNSPWGVAGLGHSAQREGDVEVQAFVESNGVVYVGGNFKYVQKSANSTG FT SDRVEQSYLAAFNRDNGELITSFTPSLNGTVMSLAALPDGNIVAGGTFSTANGEPSRMV FT ALDPDSGNTVSSWWVEIENNTSSGVTIRGMDIQGQWLYFGGSFTHIRGGSRTGNMLYSR FT NAARVSLSDGTPGTNWNPEFNGTVVDVDASEDGDRFYAGGFFTTSRRVPAENAAAVLTS FT SGASLATPTWSPTWSSSKSYQQAIAEVGDRVWSGGSEHSLFGFNTATFERERTYIEYNK FT GDLQTIATGNGNFYAGCHCNEYSYDGASTWPSLGNSWSRADSIGWIGEWDAETGDYNPH FT FTPNMAMRLGSGPWASQVDSNGTLWVGGDLTSAAAESSQGRWAGGFARFPKLDSTAPST FT PGSLSMSADSADTVRLAWGAASDAGGSVSYQVLRDDRVIATTSSRAMTVAKGGENRFFV FT RAVDANGNLSASTDAVKASGGNAAPVPEFEIEAAGKTVSFDASSSTDDGQIVRYAWDFG FT DGSEGQEAVAQHEYATFGSYEVTLEVEDEHAVVRSLTKTVDVIPGVPADAYGAEVYDDE FT PLIYWRLDESSGERADDSATGANSGTYFGSTTLGEPPLSDNVPGTSARFSGSENWVASS FT TRFDPVSVYSLELWFNSQSTSGGKLIGFGNTETGLSSSYDRHVFMQNDGTLKFGTYTGA FT ENVAVSPQSYNDGAWHHMVATQSDAGMKLYVDGALVAENPQTQAEGYSGYWRIGGDRVW FT GGASSNYFAGSIDEAAVYPKALTPEQVVEHYRIGSGAPEPANQDPVAEFTAEVQDLTVN FT VDASASTDLDGEITEYSWDFGDGSAGTGQSAEHAYADSGTYEVTLTVTDNRDGTATATH FT SVEVQAPANQDPVAEFNAGIVGFALQADASGSQDPDGQIVEYDWDFGDGSTATGETVQH FT DYAAAGSYQLVLTVTDDRGGTATKSQTIEAEVLADPQESEVIALDANWFWYFDLAAPPT FT DWMSAGFDASGWEEHPAPLGWGNSAIETDIRPDNWDEGNAVRGRAAYFVRDFQIADASK FT VVALQLESVADDGVVIYINGTEVARSNMPTGTISYLSFASSSRRYATAMQNPVTVDVPP FT DLLVDGINRASAETHVNYRNTPDATFHLQATLTSR" FT CDS 1579672..1581435 FT /transl_table=11 FT /locus_tag="AARI_13990" FT /product="DASS family symporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="divalent anion:Na+ symporter (DASS) family (TC 2.A. FT 47.y.z). Functionally characterized proteins of the DASS FT family transport (1) organic di- and tricarboxylates of the FT Krebs Cycle as well as dicarboxylate amino acid, (2) FT inorganic sulfate and (3) phosphate" FT /db_xref="GOA:E1VVF5" FT /db_xref="InterPro:IPR001898" FT /db_xref="InterPro:IPR004680" FT /db_xref="InterPro:IPR006037" FT /db_xref="UniProtKB/TrEMBL:E1VVF5" FT /protein_id="CBT75608.1" FT /translation="MEIDAIFTLIIVGLVLVLLAATRLTADLILLGACLVLMLLGILEP FT VEAFVGFSNPGVITVAVLYVVAAGLTETGAVQWITQYLLGRPRTIRGAYLRMLLPVGGM FT SGFLNNTTVVAMLMPAIQEWSAKLKISPSKLLMPLSYMAILGGTMTLIGTSTNLVVNGL FT LQSEKGISLGMFDIAAVGLPLTIAGALYLAFFGNRLMPDRQGALAQMESAREYAVEFEV FT AAGGPLAGKSIAVAGLRNLAHGYLVRLERGSQEVVEVAPETILEPFDVLTFIGAPECAG FT ELRGVRGLHPHAGDVGKLKVKHDYRRLVEAIVGPDFSGIGQSIKDSKFRSNYQAVILSI FT SRNGEMLHEKIGDVKLRVGDTLLLEAGAGFERRYRFRRDFMLVSGISQRAPANFRKAPW FT ALGILGAMILLNAFGVLEVIEAAMLAGVAMIVTGCLSLGNVRRHIDTQVIIVIAASFAL FT GAAMVKTGAAQYIALKLLGVGVGPWGALALVFLLTLCFTEMLTNNAAAVLVFPIAMSVA FT DTVGANFMPFAITVMVAASASFIIPIGYQTNLMVMGPGGYKVWDYVRAGVPMSMITAVV FT TLSVVPLVWPL" FT repeat_region 1581696..1581703 FT /rpt_type=DIRECT FT mobile_element 1581704..1583121 FT /mobile_element_type="insertion sequence:ISAar15" FT /rpt_family="ISL3" FT repeat_region 1581704..1581727 FT /rpt_type=INVERTED FT CDS 1581812..1583089 FT /transl_table=11 FT /locus_tag="AARI_34950" FT /product="transposase of ISAar15, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VTG2" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VTG2" FT /protein_id="CBT75609.1" FT /translation="MIKDTGRIDAASILLNLTDYRVITVTQELAGRQVLVEPIETEAAC FT PSCGVLTTRIQARPVHQVKDLPAGGDDLQVLVRKRRMACQEPACERRSFVQTTEQLPFR FT ARITTRLSQRLVDEMSCELRAVSRVAAAHGVSWPTVMARLTTVGELVGNVDRMFIRRLG FT IDEHRFRKVRYALGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRGTAVKKWLKNRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKVSVDHFHVIARANLMITQVRRRRSHEVHERR FT GRATDPAYKYRKLLTCNLENLSIKQVERLKLILESDPELGVIYGIKEHVRQLLKTADIH FT EFQSRWAVLEKSVKATKMTEAKTLFRTLTAWRRELLVFVRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRLRILLYTAGLRPC" FT repeat_region 1583098..1583121 FT /rpt_type=INVERTED FT repeat_region 1583122..1583129 FT /rpt_type=DIRECT FT CDS complement(1583191..1584342) FT /transl_table=11 FT /gene="cysC" FT /locus_tag="AARI_14000" FT /product="adenylyl-sulfate kinase" FT /function="2.7 Metabolism of sulfur" FT /EC_number="2.7.1.25" FT /note="identified by match to PF01583. Ultimate step in FT biosynthesis of 3-phosphoadenosine 5-phosphosulfate (PAPS), FT the primary biological sulfuryl donor" FT /db_xref="GOA:E1VVF7" FT /db_xref="InterPro:IPR002891" FT /db_xref="UniProtKB/TrEMBL:E1VVF7" FT /protein_id="CBT75610.1" FT /translation="MSKTHNFQGLETVLQLDGPALDLLELALGGLADQQDLARWLCAAG FT YVYPDSANSRRLLLADPDGTALASVEVRPSSTISDNSLDVAQLKPLARSEHGPGRASRL FT TSALTTQSAVLFSEAPTVSEIHKLSLSTVASQAFLVLVSSSKRASQTDYPNQLRELHDA FT ALLAGAQGAGHLIIPEEADMQQVVQRAVMEVLYDFRKPTDESLVQQGLVVLFSGLSGSG FT KSTLARSVMERIHLEMNREAVLLDGDDIRRFVSKGLGFSPEDRETNVVRIGWIASRISQ FT VGGIALCAPIAPFAQARAQMRALAEQAGRFVLVHVNTPLEVCEARDRKGLYAKARAGLV FT KDFTGIDSPYEVPEDASLTLDLSTLSIEAASDQVLELIRSTHH" FT CDS 1584535..1585293 FT /transl_table=11 FT /gene="cysQ" FT /locus_tag="AARI_14010" FT /product="3'-phosphoadenosine-5'-phosphosulfate FT 3'-phosphatase" FT /function="2.7 Metabolism of sulfur" FT /note="identified by similarity to protein SP:P65163 FT (Mycobacterium tuberculosis). This enzyme (PAPS 3- FT phosphatase) is considered as an important regulator of the FT sulfate assimilation pathway, by controlling the pools of FT PAP and PAPS" FT /db_xref="GOA:E1VVF8" FT /db_xref="InterPro:IPR000760" FT /db_xref="InterPro:IPR020583" FT /db_xref="UniProtKB/TrEMBL:E1VVF8" FT /protein_id="CBT75611.1" FT /translation="MSDVQFAAEIAKESGRVLLQLRAQARSKAMTESELKVAGDRASQE FT FLNRRLVESYPDDSILSEEATDDLTRLSNDRVWIIDPLDGTREYSEGRDDWVVHVALWK FT SGQLVVGAVALPGLDELLVSRSEPMGALNRGMRPVRIAVSRTRPPQIVAELSNHLDIEF FT VPMGSAGFKACAVARGEVDAYIHAGGQYEWDSAAPVAVAASRDLHVSRIDGSPLEYNQE FT NPYLPDLLICRKELRAALLGAMAGITLQTT" FT CDS 1585327..1586250 FT /transl_table=11 FT /gene="cysD" FT /locus_tag="AARI_14020" FT /product="sulfate adenylyltransferase small subunit" FT /function="2.7 Metabolism of sulfur" FT /EC_number="2.7.7.4" FT /note="catalyses the formation of diphosphate and adenylyl FT sulphate from ATP and sulphate. This enzyme participates in FT 3 metabolic pathways: purine metabolism, selenoamino acid FT metabolism, and sulfur metabolism" FT /db_xref="GOA:E1VVF9" FT /db_xref="InterPro:IPR002500" FT /db_xref="InterPro:IPR011784" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VVF9" FT /protein_id="CBT75612.1" FT /translation="MKLKQATSMRYQLDQLSALEAESIYIIREVVAELERPGLLFSGGK FT DSAVLLHLAAKAFAPAVIPFPVVHIDTGHNFQEVLDFRDAEVLRRGVRLIVGSVQEAID FT AGEVAEERNGSRNRIQTPVLLDTIEKHRLNALMGGARRDEEKARAKERVFSFRDEFGQW FT DPKNQRPELWGLYNSRLNLGESIRVFPLSNWTELDIWHYIARENIRIPSIYYAHERAVF FT DRNGMVFGVHEFCLPMEHEAVEIRTVRYRTVGDASLTAAVESTAGTTEQIVDEVALTRI FT TERGATRGDDQVSEAAMEDRKKEGYF" FT CDS 1586252..1587502 FT /transl_table=11 FT /gene="cysN" FT /locus_tag="AARI_14030" FT /product="sulfate adenylyltransferase large subunit" FT /function="2.7 Metabolism of sulfur" FT /EC_number="2.7.7.4" FT /note="catalyses the formation of diphosphate and adenylyl FT sulphate from ATP and sulphate. This enzyme participates in FT 3 metabolic pathways: purine metabolism, selenoamino acid FT metabolism, and sulfur metabolism" FT /db_xref="GOA:E1VVG0" FT /db_xref="InterPro:IPR000795" FT /db_xref="InterPro:IPR004161" FT /db_xref="InterPro:IPR005225" FT /db_xref="InterPro:IPR009000" FT /db_xref="InterPro:IPR009001" FT /db_xref="InterPro:IPR011779" FT /db_xref="UniProtKB/TrEMBL:E1VVG0" FT /protein_id="CBT75613.1" FT /translation="MDLLRIATAGSVDDGKSTLIGRLLFDSKAIFSDQLDAVEKTSTER FT GSEYTDLALLTDGLRAEREQGITIDVAYRYFATPKRKFIIADTPGHIQYTRNMVTGAST FT SDLSIVLVDARKGMVEQSRRHAFLVSLLKVPHLVVAVNKMDLVDWSEEAFEEIRNEFAD FT YASRLNIADVQVIPVSALTGDNVVSRSENMPWYQGSSLMHHLENVQIASDSNLVDVRFP FT VQYVIRPHSNDYHDYRGYAGQVASGVLKPGDEVVVLPSGLPSTIKEISTADGPVEAAYP FT PMSVTIRLNDDVDVSRGDMIVRPNNQPMVAQNFEAMVCWMSDRPMRVGQKLAIKQTTKS FT ARALVKGLRYGLNINTLHRDEEAGSLSLNEIGRITMRTTQPLLADAYQRNRTTGGFILI FT DEMTNDTVAAGMIIEGS" FT CDS 1587797..1588249 FT /transl_table=11 FT /locus_tag="AARI_14040" FT /product="oligosaccharide biosynthesis Alg14-like protein" FT /function="1.1 Cell wall" FT /note="match to protein family PF08660. Possibly involved FT in the biosynthesis of an exopolysaccharide" FT /db_xref="InterPro:IPR013969" FT /db_xref="UniProtKB/TrEMBL:E1VVG1" FT /protein_id="CBT75614.1" FT /translation="MSGLLFVGSSGGHLAQMLSMAAWWKERERSWVTFDTPDATSALAG FT EQVAWAYHPTTRNLWNTVRNLWLSFKVLHRQQPEAVISTGAGVALPFFLMARLRGIPTI FT YVEVYDRIDSRTLTGKLCRPLSSAFCVQWEEQLECYPGATVIGPLL" FT CDS 1588246..1588827 FT /transl_table=11 FT /locus_tag="AARI_14050" FT /product="putative family 28 glycosyl transferase" FT /function="1.1 Cell wall" FT /EC_number="2.4.-.-" FT /note="match to PF04101: Glycosyltransferase family 28 C- FT terminal domain. This family family comprises enzymes with FT a number of known activities; 1,2-diacylglycerol 3-beta- FT galactosyltransferase (EC 2.4.1.46); 1,2-diacylglycerol 3- FT beta-glucosyltransferase (EC 2.4.1.157); beta-N- FT acetylglucosamine transferase (EC 2.4.1)" FT /db_xref="GOA:E1VVG2" FT /db_xref="InterPro:IPR007235" FT /db_xref="UniProtKB/TrEMBL:E1VVG2" FT /protein_id="CBT75615.1" FT /translation="MNEKTAEFMILALVGTDHHPFDRMVELVDALQQAGEPGRNGRKCL FT IQFGTSSPPRYAQGMDYLPKSDVQRQIDLADLVICHGGPSTIVEILRSGKRPLVIARDP FT RKGEHVDGHQQRFARHMANQGHIDLADSAYDVEQLLSHAASTTISASNANVSLPSPDAS FT ALLLGALVDGLIAEGKSYRIWHSRRNESRA" FT CDS 1589185..1590780 FT /transl_table=11 FT /gene="serA" FT /locus_tag="AARI_14060" FT /product="phosphoglycerate dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.1.1.95" FT /note="catalyzes the oxidation of D-3-phosphoglycerate to FT 3- phosphohydroxypyruvate, which is the first step in the FT biosynthesis of L-serine, using NAD+ as the oxidizing FT agent" FT /db_xref="GOA:E1VVG3" FT /db_xref="InterPro:IPR002912" FT /db_xref="InterPro:IPR006139" FT /db_xref="InterPro:IPR006140" FT /db_xref="InterPro:IPR006236" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VVG3" FT /protein_id="CBT75616.1" FT /translation="MSDNKPIVLLAEQLSPATVAALGPDFEIRQTDGADRSQLLEAIAD FT VDAILVRSATQVDAEAIAAAKNLKVIARAGVGLDNVDIKAATQAGVMVVNAPTSNIISA FT AELTVGHIVSLARRIPAANASLKNGEWKRSSFTGVELFEKKAGIIGLGRIGALVAARLQ FT GFGMEIVAYDPYVTPARAAQLGVTLLTLDELLAEADFITIHMPKTPETLGMLGKDAFTK FT MKKSAYVVNVARGGLVDQDALYEALKDEEIAGAGIDVFVKEPSTDLPFFEFENVTVTPH FT LGASTDEAQEKAGVSVAKSVRLALAGELVPDAVNVAGGVIDENVRPGIPLIEKLGRIFN FT ALTSGSLTSIDVEVAGEIASLDVKALELSALKGVFMDVVSDQVSYVNAPVLAEQRGVAT FT RLITTPDSPEYRNQLTIKGSTNEGTQLAVAGTLTGPKQIEKLVGINGHEIEIPISDHMI FT VVRYADRPGVVGSLGNVLGEQGVNIAGMQVSRDEKKAEALAVINIDSALPQGVLDVVGA FT AIGASVAREINLAD" FT CDS complement(1591216..1591329) FT /transl_table=11 FT /locus_tag="AARI_14070" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVG4" FT /protein_id="CBT75617.1" FT /translation="MESIACTWVEWQSQDADRRTTTDQPGKLTRESEYRDR" FT CDS 1591807..1593528 FT /transl_table=11 FT /locus_tag="AARI_14080" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVG5" FT /db_xref="InterPro:IPR008397" FT /db_xref="InterPro:IPR008929" FT /db_xref="InterPro:IPR012480" FT /db_xref="UniProtKB/TrEMBL:E1VVG5" FT /protein_id="CBT75618.1" FT /translation="MMTAFNTDGQLFHTYSTVSTNDLSDQEFLGQLLTGSLKLLPHRSV FT NLGQTIVWDSDPLNDDNWRFQFHCLVWLDRLRSVSITEQSDRGLELYEKLLRSWIVSNP FT TSSPKDEYAWFDMAVGMRAIVLLMAAKHFDNPDWIVESIQTHATHLADPANYEGRGNHS FT LHQDMGLIALAQYLDRSDWIELAKSRILKMLDEAIDEQGVSREGSIDYQFRNYRWYEEA FT FTRMKAAKADPPREKYELLSKMTEFMAHATSPSGYYAMLGDTVYHKAPRIQDTPSDWTR FT DVSLAPADKSRIYDSGYVFARASWSHVDKRSNSYLTQRFGPGRSSAVHGHEDAGSITLD FT AFGERLLCDSGLFAYEAGEERLYFRGRESHNVIDVEGRKYYPSADSPLVHSHQTNDVMQ FT TTIRIQGLQGVVWYRTMAYFPNDDFILIDDRITNTLPGEIKQQWNLPKDSVIRSSKKDG FT YESVRTTSGSEIRIYCLNSEVSTEFVKGNRDPISGWISDEYRVKAPSPKLSYIQEGKSV FT RFTNLIEWSNTKSPFWSNKLYTKRSSKSFVISLMKTNELIEIDMESENISIKRTKK" FT CDS 1593811..1594026 FT /transl_table=11 FT /locus_tag="AARI_14090" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVG6" FT /protein_id="CBT75619.1" FT /translation="MTKDTGRIDAASILLNLIDYRVITVTQDSAGRQLLVEPVETEAAG FT PSCRVLTTRIHARPVHRVKDLPAGGP" FT repeat_region complement(1594169..1594182) FT /rpt_type=DIRECT FT mobile_element complement(1594183..1595851) FT /mobile_element_type="insertion sequence:ISAar27" FT /rpt_family="IS481" FT repeat_region complement(1594183..1594232) FT /rpt_type=INVERTED FT CDS complement(1594299..1595744) FT /transl_table=11 FT /locus_tag="AARI_34960" FT /product="transposase of ISAar27, IS481 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVG7" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VVG7" FT /protein_id="CBT75620.1" FT /translation="MPNALSPRLRAMIISFDPTQPEALSISEFCKTQKISRSIFYRIRE FT RATQESAGALHPRSRAPKLPSRRYGPDVINELVRIRKELKKDGWDYGPKTIHYEATILD FT EFPGGQIPSVATIARLLASVGHVERSPRKRPKSSYVPFARSAAMALWQLDAFEFRTHSD FT QVVTVYQLIDDATRFDVGSSAYARHENSGDAQQVLARAINDYGPPKEVLSDNSKAFNQL FT RGGTIGIVEAYLASQGTMPITGLPGRPTTQGKNERSHQTLQQFLKANRPQNLADVQKLL FT RRYREHYNQRRPHQSLNQATPQKAWELLEHTPATEPISMVVLEAKAAEYLMKRRIGSSA FT ANRADVVVSKTGDILKKLTEQHEPDMDRESHQLLVRVNKDNCQAYYRGKQISLPQTYAG FT RQFLRTITEDEFILSDPDTAEVVLSFPLPMVALRVHRRFVSSYSIRGIRLANPTKQWSR FT KVAEYQAQYEAREEDMPEVFDYR" FT repeat_region complement(1595802..1595851) FT /rpt_type=INVERTED FT repeat_region complement(1595852..1595865) FT /rpt_type=DIRECT FT gene 1595970..1596242 FT /pseudo FT /locus_tag="AARI_14100" FT /product="truncated protein" FT /note="N-terminal section of a protein. Disrupted by FT insertion of ISAar13, ISL3 family" FT CDS 1596324..1597601 FT /transl_table=11 FT /locus_tag="AARI_34970" FT /product="transposase of ISAar13, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVG8" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VVG8" FT /protein_id="CBT75621.1" FT /translation="MFKDTGGNDAASILLNLTDYRVIDATQEPAGRQVLIEPKATEAAC FT PTCGVITTRIHARPVHRVKDLPTGGNDIKVLVRKRRMACQETACERRSFVQTTEQLPLR FT ARITTRLSQKLVDEMSCELRAVSRVASAYQVSWPTVMARVNMVGELVGNVDRMFIRRLG FT IDEHRFRKVRYARGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRCAAVKKWLKSRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKISVDHFHVIQRANLMITQVRRRRSHEVLQRR FT GRAADPAYKYRKLLTCNLENLSIRQVERLKLILEADPELGVIYGIKEHVRELLKTRDIH FT DFQSRWAVLEKSVKTTKMVEAKSLFRTLTAWRRELLVFIRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRVRILLYTAGLRPC" FT CDS 1597733..1598140 FT /transl_table=11 FT /locus_tag="AARI_14110" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VVG9" FT /protein_id="CBT75622.1" FT /translation="MSRSSYVKIAAKLAPVAAVALFLTAGVVSLFSLRFALLALSVGLA FT ATVVSSLLRQKQSLHDTRTVVRQELRGVSLGAAPSADASTNEASKRLVDIADKLSREQS FT PVARELHIKTVEEIRFLQAQLDSYFKGGQQN" FT CDS 1598204..1600015 FT /transl_table=11 FT /locus_tag="AARI_14120" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVH0" FT /protein_id="CBT75623.1" FT /translation="MNAPIVRILDHEISRTITPQESGTSRGSRGIDNAAEITRALEAAS FT FLNTPGNFALDLSLGSADYSEISLNSWSVRHRFLALEIYLRASVIALVEKVGLDTFDDS FT IVFATEGPTAVRAAAEKYIVDIRSLSRARRFVTASTSHVFLSIESGLYEEIKSFRSRLS FT KDDSIRFNDLMATAPNLEIDWAQLVAESNALAVLYNFSPYTDTGAVVASKRIRASGDTY FT DVIACSFAHRKKIDSTIDRIAAPYVASKQFLPMVPSWATWSAFKAYALKSSRIAQKNID FT SGKKYEYLYTRAMWAPSHYAGLLLKKANPTLKWVAEFSDPLSLDVEGLPRGGAPLDDDF FT VTDLVKPIEESFGPIPMSERTIFALAELIAYAHADEIVFTNEHQKTTMLAHIYSDSLRA FT RVAAKSLVSNHPTLPSEFYEAEQVDYSVDNSKINLAYFGEFYATRGLTEITTAIRMLPA FT EYRHLIRLHVFTNYIPVSGSGSRPRGMSAKAYNDLVDRAINGVGAHGIENQVTLNGSLP FT YLKFLAITKNFDYLLVNDARSGEHHEVNPYLPSKWSDYAGSAAKSWAFVEDGSSLSHKP FT ATIHTPLGEVQAITRELHRIIIEKLGA" FT CDS 1600018..1600593 FT /transl_table=11 FT /locus_tag="AARI_14130" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVH1" FT /protein_id="CBT75624.1" FT /translation="MGLTPPSDNGLNEVLTKIGRASTPQVPHNSLGLTLPRALRCESWL FT NQKTDFFGVISGYLSESLQERDYTVVTATPGLSHHIMPENFAGVVVIDRLAFDEGTWFG FT AISETAATLREEVYELCRKARQNGIPVWFLDRPATTEPFGITRIKSASDVVMPIINPEE FT FEEGAKISESFTLIMSLVEARFASENYK" FT CDS 1600590..1605581 FT /transl_table=11 FT /locus_tag="AARI_14140" FT /product="hypothetical glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /note="match to PF00535 and PF00534" FT /db_xref="GOA:E1VVH2" FT /db_xref="InterPro:IPR001173" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VVH2" FT /protein_id="CBT75625.1" FT /translation="MSLNRNNMDESLSAKTILCVIDEESTNPQVYRRLVSTQLSSLRDM FT GAELVLLHVDGRAELLPAEYRSLDAELLVDKPIEGESDNQRSRKLAQRAVKHGKDSRYD FT IVIGFGWTLSRRVAGGQALSNKFWSVVDDPTESIDRSAWTNPTIVDALYRGSRKVFVFS FT DERRSILENTSNAANGRTYLPALHAYLDTSALKKKTYELGAATRVILPGLTQPAHYIDL FT LSELSELAKSGRSSYEFLFDGAEETWGELQNAPTTAVAAAIPGLKILRGHERFDGELTL FT GLVPNTAGEEWLSSFLIGEYLRHGVVPISLDRFLSLDHGNPAETISVADELSHLTIDVE FT RLEDANRVIAAANLDTVGGRSVDGNETAPRKVVLAGADFKFAGDLVELLNESPDFDLKI FT DLWANNSHPDPTQSTPFVEWADIVICEFASFNAIWYSQNKRRNQKLIVRMHGYELLQPW FT IDQLAIDNVDQIVFVSEFYRRKAIETKGWDESKTSVISNTVDFGDLSRQKLPGAEFHLG FT MAGYVPILKRPDRALDLLEELLKHDDRFVLHMRGHEPWNYQWEWKKPAHQAAYRDFYSR FT IATDENLRTHISFESFGPDMAGWFRKIGWMLSPSYRETFHLAPVEGMASGALPVVWERD FT GADEIFPADYVVSDVTEAAQLILSTIEDCGAYETRAFEIQSFAARYSRSTVKSEWIELI FT HSTADMEVEARGTSASPHSSLEALIERHESNSSATSLLNAVSEAWRIRDYATAISLLDA FT NIKLTANDTGELKQWEHWVRGTFQTAMNLESVLLKSVDGCVYHPRNDRAVVVSSEQAGA FT VILKSAVEGLDTKSIGIKLPVPGIELSHDNDLSNASAVSKDYLVKYDGTLRSNYYLVQA FT ASEIASIFRDTSARVAVANGGFFESLATLVAARRVGIPFIWAPSASTDAAEFFSAFDEI FT RNDDPVHEIYQAILENTDAILNSQDHNVVLASLKHKIPVFDSISVENLESVIAQKGIRP FT QGTQNKLSIAYAGDGTSVDTLSIVAHVEVCTSDNVLQVLDTAPDVFVLELASGNVAPPA FT YEKSANFADTTNLQQIQKSILHSRVMGARSVFISHNDPEALGLGKEIARKCDVVVSNDR FT KSLISYMRLNPNSNQMAANISGGRRTAIIPSIPSRNIKPITPCEDGSLYPASLEDGLVA FT GRPVVPAWTSGLSWVDSSQIGDHDAVLRYEATGKQEDGLASLWANCVELSQGRSGLDFA FT VSVLRTAGFPVIHPRGETSKPFGQRLTVNADTTTQFKPEIVVKDSVILDDGLKRDLVAL FT YRVSDAQRIVVETGADSAQSITITSANGHESVVSRARRTNQKSLKSASLSEFSDSGVSI FT VVATYNGAARLPRLLSTILKQRLPFSLLELVVVPNGPDDGTQDLLRAWSGEHPDISLKI FT LPVEEAGVAKARNLGIANASRQYITFVDDDDYLEPNYLLSLYSRADNNTVVLGRLSDVD FT EETNEIVRDTTTNRRVTELSGRLLPLAQRAGALGMNGAKLLPTWLTRECTYDSSLRSGE FT DVAFMAQLLRKPGIFVTSSADVGEADYMRVMRFNSISRREETFEFMVLERLDVLALLHR FT TWEQSEYKGGKGTIQYLATGQLGFMKRFVLESRSIADYERTLHAIEERNMDSLAILQPL FT LANLRSAISDPMSLNDGKRISLARE" FT CDS 1605868..1607610 FT /transl_table=11 FT /locus_tag="AARI_14150" FT /product="putative glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /note="match to PF00535: glycosyl transferase family 2. FT This domain is found in a diverse family of glycosyl FT transferases that transfer the sugar from UDP-glucose, UDP- FT N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to a FT range of substrates including cellulose, dolichol phosphate FT and teichoic acids" FT /db_xref="GOA:E1VVH3" FT /db_xref="InterPro:IPR001173" FT /db_xref="UniProtKB/TrEMBL:E1VVH3" FT /protein_id="CBT75626.1" FT /translation="MVSEDRHRPVPVTNVAVILDDFSAKAWAPEWNCTFITPESWKQDL FT KSQKFDLLFVESAWAGNKKSWQYHLTGPTAPRPAFVEMVEGFKQLSIPTVFWNKEDPPH FT FADFLETAKLFEHVFTSDSRLIPEYRKELGHDRVSALSFAAQPEFHNPVRPLNQERRDV FT AFAGMYFADKYPERKEQMDIVLGGASDISSRLSTGLDIFSRQHGGDKKYQFPAPYDKNV FT VGSLDYEKMLSAYKYYKVFLNVNSVVDSPSMCARRIFEITAAGTPVVSAPSAAIENFFS FT ASEVLQVSNRKEASDAIRSLVRSPELRDRMVHMGQRRIWQNHTYAHRAIQIEQQVGLQN FT SDNQPLRMTSTPNVTAIVSTIRPHQLHHIFKTVGKQRDVNVELILVTHKFTPDYNELAS FT YAREAGISEYRVLELGEQSTLGDCLNAAVSEASGDFITKMDDDDLYGEHYLFDQVASLR FT FSGASVVGKQAHYMYLADSNATLLRFAEREHRFTDLVMGPTMLGHASVFKETPFKTRNR FT GEDTRFLKDIVERGGTIYSSDRFNFTQMRGSDGQSHTWDLSDAELTATGSIQWFGRNEN FT HVFF" FT CDS 1607661..1608836 FT /transl_table=11 FT /locus_tag="AARI_14160" FT /product="putative group 1 glycosyl transferase" FT /function="1.1 Cell wall" FT /EC_number="2.4.-.-" FT /note="match to PF00534: Glycosyl transferases group 1. FT Proteins containing this domain transfer UDP, ADP, GDP or FT CMP linked sugars to a variety of substrates, including FT glycogen, fructose-6-phosphate and lipopolysaccharides. The FT bacterial enzymes are involved in various biosynthetic FT processes that include exopolysaccharide biosynthesis, FT lipopolysaccharide core biosynthesis and the biosynthesis FT of the slime polysaccaride colanic acid" FT /db_xref="GOA:E1VVH4" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VVH4" FT /protein_id="CBT75627.1" FT /translation="MRIMLLTHSFTPEISPPQRRWSIIADELAQLGHRVTVVTPKSDRI FT ATESQRLLLSNDRVKLQNYPSMRRSRTMLGKVVKHGVDAIISVPAAFLGQKPDVIVATV FT PAIPTLIVGYIASQLRRVPFVVDLRDAWPDLLSESQVLKLRWLEPLISKFISFVVNRSD FT MLITVTHGLAEKMQSNGAKNVATISNGVETERASLPITPRAHNDEFHILYLGNIGRSQG FT LETVIRAMTQVPDNVYLRVVGQGTEKNKLVEMAETLGINAEFLDPVYGREVLENYSWAD FT TCLVSLRSDWPSFKYTVPSKLYELLYLNQHVTGLVQGEAAGIIRASEAGIVVEQSVPAL FT VEYINQMAANPEFLRTERRGTAWVLENGSLRKSGREYASILSEVIESKSKR" FT CDS 1608847..1610592 FT /transl_table=11 FT /locus_tag="AARI_14170" FT /product="putative group 1 glycosyl transferase" FT /function="1.1 Cell wall" FT /EC_number="2.4.-.-" FT /note="match to PF00534: Glycosyl transferases group 1. FT Proteins containing this domain transfer UDP, ADP, GDP or FT CMP linked sugars to a variety of substrates, including FT glycogen, fructose-6-phosphate and lipopolysaccharides. The FT bacterial enzymes are involved in various biosynthetic FT processes that include exopolysaccharide biosynthesis, FT lipopolysaccharide core biosynthesis and the biosynthesis FT of the slime polysaccaride colanic acid" FT /db_xref="GOA:E1VVH5" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VVH5" FT /protein_id="CBT75628.1" FT /translation="MNLKVIPNAINTANLVISNIADDPTYFALQIGRRFRGNPVIRLVT FT SYLDRNSAPVEQRALGAMLNDDSSGLRAACGEWLGMETELPYSVFLANLCIASGEWHLA FT GMLLDGDSKSSRKIRAKARLMWSLGHMTNAIEILELIGRGRQLSHYRSELATFQGLAPT FT ISAQAQSKSTSSEFRSVLYVATNSLPHTGSGYAQRTQSILKSLSGKKWNVKALTRVNYP FT INIGKLTAGKSDVVSGITYERCLPFPAKHDFAGRVQQQADDLLARVLNDRPDVLHTTTD FT FSNALAVRAVAEATGTPWIYEVRGQLADTWLSTRPEDSRSSERYRLFVEREADVARHAD FT YVFTLGNEMKQNLVLAGVDESKISLLPNGIGEEFLQLPVNREDARGQLGLDSKAIYVGT FT VSSLVPYEGLSTVVEAIAKLASEHSNLRLLIVGDGTDRENLIRLAKTLGIESRCEFPGR FT VAREVAHLYHASLNAFVVPRVDSAVTRSVTPLKPVEAMASSVPVLASNLPALSELITDG FT ESGHLIAAEDVSEWAEAIEKLILNPENAELMGKSGREFVLANRTWDQNAHHIVEVYERV FT INKAL" FT CDS 1610724..1611956 FT /transl_table=11 FT /gene="wecC" FT /locus_tag="AARI_14180" FT /product="UDP-N-acetyl-D-mannosamine dehydrogenase" FT /function="1.1 Cell wall" FT /EC_number="1.1.1.-" FT /note="catalyzes the oxidation of UDP-N-acetyl-D- FT mannosamine to UDP-N-acetyl-D-mannosaminuronic acid. In FT Escherichia coli, UDP-N-acetyl-D-glucosamine 2-epimerase FT and UDP-N-acetyl-D-mannosamine dehydrogenase are FT responsible for the formation of UDP-N-acetyl-D- FT mannosaminuronic acid from UDP-N-acetyl-D-glucosamine" FT /db_xref="GOA:E1VVH6" 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="UniProtKB/TrEMBL:E1VVH6" FT /protein_id="CBT75629.1" FT /translation="MNNIKEVAVIGLGYIGLPTAAILASKGITVKGVDVTPRTVEAVNK FT GEVPFVEPALGEFVSAAVAAGTLSASFDTPEAEAYIVAVPTPFNDDYTADLSYIEAAAE FT GIAPKLKGGELVILESTSPPGATQHLFDYLLNKRPDLNKESLLVAHCPERVLPGYVMEE FT LVTNDRIVGGITPEAADKAKALYETFCQAAILTTDAVTAEMAKLVENSFRDVNIAFANE FT LSVISDKLGIDVWELISLANRHPRVNILQPGPGVGGHCIAVDPWFIVSAAPEESKLIRM FT ARNTNDAKPNWVIDKVVEATKAPSFNGKVAVLGLAFKANIDDMRESPSIAIARKLAESN FT PSIEFLAVEPHVDALPKNLAGIDNLKLVSTEEGLESASVITLLVDHDQFKAVPATALAG FT KEVIDTRGLWR" FT CDS 1611983..1613167 FT /transl_table=11 FT /gene="wecB" FT /locus_tag="AARI_14190" FT /product="UDP-N-acetylglucosamine 2-epimerase" FT /function="1.1 Cell wall" FT /EC_number="5.1.3.14" FT /note="catalyses the formation of UDP-N-acetyl-D- FT mannosamine from UDP-N-acetyl-D-glucosamine. The enzyme FT also hydrolyses the product to UDP and N-acetyl-D- FT mannosamine. In Escherichia coli, UDP-N-acetyl-D- FT glucosamine 2-epimerase and UDP-N-acetyl-D-mannosamine FT dehydrogenase are responsible for the formation of UDP-N- FT acetyl-D-mannosaminuronic acid from UDP-N-acetyl-D- FT glucosamine" FT /db_xref="GOA:E1VVH7" FT /db_xref="InterPro:IPR003331" FT /db_xref="UniProtKB/TrEMBL:E1VVH7" FT /protein_id="CBT75630.1" FT /translation="MKKIMPIYGTRPEAIKVAPIVKALKEADEFECVVVVTGQHREMLD FT QVNELFGITPDYDLDVIQPRQTLNGLLTKTIAGLDEIFEKEKPDAVVVQGDTTTSTAGA FT IAAFYRGIPVVHAEAGLRSYDIFSPFPEEANRKLTSQIASLHLAPTWLSKRNLERETFK FT SSDIVITGNSVIDALLTVVEKKVPFSDAKLEELVSSGKRIVLVTTHRRENQGEPMRGIG FT RALAKLSKAEPDVEFILPLHRNPAVREALLPEIDGLSNVTLTEPLAYGEFTRIIDASSV FT VLTDSGGVQEEAPSLGKPVLVMRLNTERPEAVTAGTVRLIGTDEKRIFDSVTELLHDEA FT AYNEMANAVNPYGDGKASERTVAAIAELLGVGSRIEEFDSKLSDPEDMMRATSI" FT CDS 1613291..1614298 FT /transl_table=11 FT /locus_tag="AARI_14200" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021139" FT /db_xref="UniProtKB/TrEMBL:E1VVH8" FT /protein_id="CBT75631.1" FT /translation="MMNQTAIFIDAGFLLSLGGHRAAGTTLRSAFTTHYESLVRGIVQT FT VKKNTGLNNLRVYWYDASKDGLFTEQHKRIGLIPGVKVRLGRISYNGEQKGVDLRLALD FT LVGVARNRSASIAYLVSGDDDLAEAVEEAQDLGMKVVLLGVAKSDSRLGVASVAEHLAL FT TADYIETISDQLLDSAFTKVLEWDKNHSAKTSLIANASTADQLKPTGKPLVPTPAVMAQ FT KPVSKPIPDRESEPSVVYSSGGEGSGYQGSAAYEQKELKVAEEIGAKVAESWLAFTTQS FT DVLDLVADKPQLPPEIDRTLLKDCAQVLGEWKTDQQTIRRTLRGAFWEYLDRIM" FT CDS 1614356..1615906 FT /transl_table=11 FT /gene="metG" FT /locus_tag="AARI_14210" FT /product="methionine--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.10" FT /note="activates methionine and transfers it to tRNA(Met) FT as the first step in protein biosynthesis" FT /db_xref="GOA:E1VVH9" FT /db_xref="InterPro:IPR001412" FT /db_xref="InterPro:IPR009080" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR014758" FT /db_xref="InterPro:IPR015413" FT /db_xref="InterPro:IPR023457" FT /db_xref="UniProtKB/TrEMBL:E1VVH9" FT /protein_id="CBT75632.1" FT /translation="MTSQQKPFYITTAISYPNGTPHIGHAYEVVATDVMARFKRLDGYD FT VFFMTGTDEHGQKMMQTAEKLEITPAQLAQRNSDAFQSMNDELGTSYDRFIRTTDADHH FT AAAQELWRRMEANDDIYLDKYAGWYSVRDEAFYTEEQTEVREDGIRYAAETDTEVTWTE FT EESYFFRLSKYQDKLLDYYRDNPEFGAPRSRFNEVVRFVESGLTDLSISRTTFDWGIPV FT PGNEKHVMYVWVDALTNYLTGVGFPDVDSASFKKYWPADVHVIGKDISRFHAIYWPAFL FT MSAKLPLPKRVMIHGFLHNNGVKMSKSLGNTVSPDDFVNRYGLDQVRYFFLREVPFGAD FT GNYNHETIVARINGDLANNFGNLAQRSLSMVAKNCGGVVPTPAELSEADNAILDAAGQL FT LEINREAYSRQEFSKALEAVWHVLGDTNAYFAEQEPWKLKKTDPERMATVLYVTIEIVR FT KVALLLQPVLPQAMTSMLNALAVGEGSARNFESFDSALVPGTELPVPSPVFPRYEEEK" FT CDS complement(1615976..1616668) FT /transl_table=11 FT /locus_tag="AARI_14220" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VVI0" 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:E1VVI0" FT /protein_id="CBT75633.1" FT /translation="MPNTETIKVALVDDQLLVRSGFRMLINSQDDMEVIVEAGNGRDAL FT AAPLMSQADVILMDVRMPEMDGIEATERLLDPEKKAADGPKIIVLTTFDMDEYALRAIQ FT AGASGFLLKDAPPEELLESVRTVNRGDAVIAPSTTRRLLDHMTPMLKKNAAQHDEHLIA FT AVESLTPREREVFGLIAVGLSNPEIAEKLFLSEATVKTHVGHILAKLEARDRVQAVVIA FT YQTGVVTA" FT CDS complement(1616675..1617907) FT /transl_table=11 FT /locus_tag="AARI_14230" FT /product="putative signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VVI1" FT /db_xref="InterPro:IPR003594" FT /db_xref="InterPro:IPR011712" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VVI1" FT /protein_id="CBT75634.1" FT /translation="MQEHLIFANPHRRIDGWIRENPGRVDFIAGLLYTLFCIPAALGLA FT SSMSTPAVLSILTLSLVQSAPLMARRRYPWAVTLVVALGHLLQLGFDGLILFSQVSVPI FT MVYTMAVYGKRWQSFFTLGLGLFGALLATFSMFSAAGNSPYPQSIFTFDMMISFVGLAL FT VVTLSWTFGDLARTRRLAMKSLREHAERLEKERLIERALAASDERNHIAREMHDIVAHS FT LSVIITQANGARYAAAKDPQIAIETLKTVSDTGRASLKEMRRLLGVLRKDEELDNRPLP FT SLANVSELVESAMVSGLNVQFEITGTPRKELPAGAELTIYRCVQESLTNVIKHAGPEAK FT AQVQLEWTSRGLNLSVIDDGRGAGSVVIEGAGQGLLGMRERVALYEGSCSALPQSGGGF FT AVSVSIPYSED" FT CDS 1618090..1619148 FT /transl_table=11 FT /gene="leuB" FT /locus_tag="AARI_14240" FT /product="3-isopropylmalate dehydrogenase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="1.1.1.85" FT /note="involved in leucine biosynthesis. Catalyzes the FT oxidative decarboxylation of 3-isopropylmalate into 2-oxo- FT 4-methylvalerate" FT /db_xref="GOA:E1VVI2" FT /db_xref="InterPro:IPR001804" FT /db_xref="InterPro:IPR019818" FT /db_xref="InterPro:IPR023698" FT /db_xref="InterPro:IPR024084" FT /db_xref="UniProtKB/TrEMBL:E1VVI2" FT /protein_id="CBT75635.1" FT /translation="MGNLIDIAVIPGDGIGPEVVAEAVKVLNFVTNGGKNEIKLTNYKL FT GAEHWLETGETLPEETLEAIKKHDAILFGAVGAAPGDTRIPSGIIEREMLLKLRFSLDH FT FVNLRPAKLYPGIESPLANPGEIDFVVVREGTEGPYVGNGGSVRTGTAHEIATEVSVNT FT AYGVERVVRDAFRRASERERKHVTLVHKHNVLVYAGHLWKRTVEMVAQEFPEVAHDYLH FT VDAATIFLTTDPSRFDVIVTDNLFGDILTDQAGAITGGIGLAASGNINMDRTYPSMFEP FT VHGSAPDIAGQQKADPTAAILSVALMLEHLGLTEEARTVEQAVEKEITSRQELTDNRTT FT SEIGDAIVALLA" FT CDS 1619263..1620357 FT /transl_table=11 FT /gene="ilvE" FT /locus_tag="AARI_14250" FT /product="branched-chain-amino-acid transaminase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.6.1.42" FT /note="last step in the biosynthesis of the branched-chain FT amino acids L-isoleucine, L-valine and L-leucine" FT /db_xref="GOA:E1VVI3" FT /db_xref="InterPro:IPR001544" FT /db_xref="InterPro:IPR005786" FT /db_xref="InterPro:IPR018300" FT /db_xref="UniProtKB/TrEMBL:E1VVI3" FT /protein_id="CBT75636.1" FT /translation="MEFTENLSTNRKSEQERAEILANPGFGDFFTDHTAVIDWSADASG FT RNGEWHDARIEPYGPIAMDPAASVLHYGQEIFEGLKAYRHADGSVWTFRPHANAARLNK FT SAQRLALPQLDEEVFVDSLRKVVATDIEWVPSGDGEALYLRPFMIATEAFLGVRAAREV FT SFRVIASPAGNYFGGELKPVAIWVSQNYARAGRGGTGSAKCGGNYAASLVAQLEAEENG FT CKQVLFLDSFNENAVEELGGMNVFFVTKDHKLITPALTGTILEGVTRSSVIQLAKDRGM FT VVEERKITLDEWREGIASGEIAEVFACGTAAVITPIGLLKNGDELIGDENAAAGEVTMS FT IREELLGIQLGTVEDRHGWLERLA" FT CDS 1620432..1621463 FT /transl_table=11 FT /gene="galE" FT /locus_tag="AARI_14260" FT /product="UDP-glucose 4-epimerase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="5.1.3.2" FT /note="catalyses the formation of UDP-glucose from UDP- FT galactose. Involved in the catabolism of galactose" FT /db_xref="GOA:E1VVI4" FT /db_xref="InterPro:IPR001509" FT /db_xref="InterPro:IPR005886" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VVI4" FT /protein_id="CBT75637.1" FT /translation="MHVLVTGGAGYIGSHTVLLLLNEGHTVSVLDNFSNSSPESLRRVQ FT NLTGREVAVYEMDLLDREPLMQLVSQLSPDAVVHFAGLKAVGESVSKPLQYYRNNVVGT FT LNLLDAMSATGCTSLVFSSSATVYGESTELPLVETTARSATNPYGRTKLHIEEMLEELA FT ASDPQWSIATLRYFNPVGAHESGQIGEDPQGIPNNLMPFVAQVAIGKRDKVNVFGADYA FT TADGTGVRDYIHVMDLAAGHLAALDYMSKHNGVGAWNLGTGQGTSVLEVVQAFSRVSKR FT DVPYTIVARRSGDVAESYAHPEKAMLELGWKAERGLEQMVEDMWRWQEQNPDGYIRATS FT DKD" FT CDS 1621743..1623059 FT /transl_table=11 FT /locus_tag="AARI_14270" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="InterPro:IPR015943" FT /db_xref="UniProtKB/TrEMBL:E1VVI5" FT /protein_id="CBT75638.1" FT /translation="MEPAPIPRAELTRPVPKDQRLIGRLNEGLPTRGYLEKHAHAFSTV FT RVLDVVELPGLGETAPWLAVAIVGTTNELQIVDPSDGKILHVLEIPSEYGTGLESLVWD FT PQRRRLYLSIDSTLIMWDSNNPKHVRKFAQIDGATALYSLDVDRSGNVFGGTYPLGAVF FT RVSNSDKSVRIYKRFADDSDYVRNIAVDEKGNVWAGTGASNPRLFYLDVTSDREPSQFD FT LPNRVHNGFVSSINLFGSKVVISASGVAPQMVFDRKLNAWIAPIDDMWTHRQISRVKDG FT HFFALSANKLIRISVDDFKEEMISPISTVTPFCISNLGNRVIVYSQEDELLNLEIYNVE FT SGELENRRGVNLSPSSFKIQSVVASQNNELYLGGYKAKGIASFSPSSGKIWNSPSGETL FT IQQIEGMIPFGDNRLYIGSYPGGDIIGSSSFSVVSPKNK" FT CDS 1623124..1624401 FT /transl_table=11 FT /locus_tag="AARI_34980" FT /product="transposase of ISAar13, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VSI7" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VSI7" FT /protein_id="CBT75639.1" FT /translation="MFKDTGGNDAASILLNLTDYRVIDATQEPAGRQVLIEPKATEAAC FT PTCGVITTRIHARPVHRVKDLPTGGNDIKVLVRKRRMACQETACERRSFVQTTEQLPLR FT ARITTRLSQKLVDEMSCELRAVSRVASAYQVSWPTVMARANMVGELVGNVDRMFIRRLG FT IDEHRFRKVRYARGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRCAAVKKWLKSRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKISVDHFHVIQRANLMITQVRRRRSHEVLQRR FT GRAADPAYKYRKLLTCNLENLSIRQVERLKLILEADPELGVIYGIKEHVRELLKTRDIH FT DFQSRWAVLEKSVKTTKMVEAKSLFRTLTAWRRELLVFIRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRVRILLYTAGLRPC" FT CDS 1624604..1624744 FT /transl_table=11 FT /locus_tag="AARI_14280" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVI7" FT /protein_id="CBT75640.1" FT /translation="MIDPVKDEIVWVIDAKASGIANGHSIVGLCADDEYLWLFRNKSVT FT T" FT repeat_region 1624705..1624712 FT /rpt_type=DIRECT FT mobile_element 1624713..1626161 FT /mobile_element_type="insertion sequence:ISAar19" FT /rpt_family="ISL3" FT repeat_region 1624713..1624736 FT /rpt_type=INVERTED FT CDS 1624848..1626155 FT /transl_table=11 FT /locus_tag="AARI_34990" FT /product="transposase of ISAar19, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRG4" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VRG4" FT /protein_id="CBT75641.1" FT /translation="MLNPTFTAPDLTTFTNLDGLGLTAIGQHLSAAKAEILCHVTNPIP FT WCQTCGAAGIPRDTVTRRLAHEPLGWRPTVLVIKHRRYRCANCQRVWREELSQAVAPRQ FT KISRTGLRWALVGLVCHHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFDGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLIDMVPGRSKAVFKTWLADQEEQW FT KQGIEVVAMDGFTGFKTAAVEELPHAVEVLDPFHVVKLGSEALDQTRQRIQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKTKLEDLFKEPEYEPVQLVWSVYQKMVDAYRQPKP FT EVGRWALEQLINEVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRRRLHPQS" FT repeat_region 1626138..1626161 FT /rpt_type=INVERTED FT repeat_region 1626162..1626169 FT /rpt_type=DIRECT FT CDS 1626714..1627478 FT /transl_table=11 FT /locus_tag="AARI_14290" FT /product="fumarylacetoacetate hydrolase family protein" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /note="match to PF01557. This domain is found in several FT enzymes, including EC 3.7.1.2, EC 5.3.3.10 and EC 4.1.1.68" FT /db_xref="GOA:E1VVI9" FT /db_xref="InterPro:IPR002529" FT /db_xref="InterPro:IPR011234" FT /db_xref="InterPro:IPR018833" FT /db_xref="UniProtKB/TrEMBL:E1VVI9" FT /protein_id="CBT75642.1" FT /translation="MRIARFVVDSDPMYGVVDGNDIHVLAGDPFFQGIKTTGTTHSLDD FT VRLVAPIIPRSKVVGFGRTYREHAKELGNEVPDEPLMFLKPNTAVVGHGDPVTLPAFSE FT EVSFEGELAVVIGRICKDVPADKAQDVIFGYTVANDLTARDAQRTDPQWARAKGFDGSC FT PLGPWIETEIADPDDLGIVSRVNGEVRQDGTTNDMIWPVNELVARASEAFTLLPGDVIM FT TGTPAGVGLVNAGDVVEVEVEGIGSLRTVFRR" FT CDS 1627581..1629086 FT /transl_table=11 FT /gene="gltX" FT /locus_tag="AARI_14300" FT /product="glutamate--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.17" FT /db_xref="GOA:E1VVJ0" FT /db_xref="InterPro:IPR000924" FT /db_xref="InterPro:IPR004527" FT /db_xref="InterPro:IPR008925" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR020058" FT /db_xref="InterPro:IPR020061" FT /db_xref="InterPro:IPR020751" FT /db_xref="UniProtKB/TrEMBL:E1VVJ0" FT /protein_id="CBT75643.1" FT /translation="MTDLSLIPVVTEDTPVRVRFCPSPTGTPHVGLIRTALFNWAYARH FT TGGKMVFRIEDTDAKRDSEESYNQLLDALAWLGIDWDEGVNAGGPHEPYRQSQRGDIYE FT DVIARLRAAGHLYESYSTPEEVEARHKAAGRDPKLGYDNFDRELTVEQKAEFKAEGREP FT VLRVRMPDHDITFNDLVRGEITFKAGSVPDYVVVRANGKPLYTLVNPIDDALMGITHVL FT RGEDLLSSTPRQVVLYALLHDIGVAQYMPRFGHLPYVMGQGNKKLSKRDPESSVFLHRD FT NGFIPEGLLNYLALLGWSLSADEDIFSREQLVEAFDVTDVLSNPARFDVKKAEAINGTH FT VRMLEAQDFRNRLVPYLKAAGLVGEELTERENDILDQAAPLVQERIALLGEATDMLEFL FT FKSDDKIVIDEKALKGMPANLVEVVDATVQGLETLTEWNAETIQAALRTKLVDELELKP FT RQAFGPARVAISGKRVSPPLFESMEILGRESSLKRLRAFGESR" FT tRNA 1629773..1629844 FT /locus_tag="AARI_36780" FT /product="transfer RNA-Gln" FT /anticodon=(pos:1629806..1629808,aa:Gln) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT tRNA 1629893..1629968 FT /locus_tag="AARI_36790" FT /product="transfer RNA-Glu" FT /anticodon=(pos:1629927..1629929,aa:Glu) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 1630068..1631834 FT /transl_table=11 FT /locus_tag="AARI_14310" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="GOA:E1VVJ1" FT /db_xref="InterPro:IPR001401" FT /db_xref="UniProtKB/TrEMBL:E1VVJ1" FT /protein_id="CBT75644.1" FT /translation="MESNSDLAKSSGQETASQTEIGSDSAARLSELQKLLEELSFVNGQ FT PREASAFEELRNKALHQISDYLIPRVSNLGAPLLVVVGGSTGSGKSTLVNSLLGEQVSL FT SGAVRPTTRTPVLAFNPVDQSFFESERILPELKRVAGRGFNADAGAASNHALLMTPREQ FT VPRGLAILDAPDIDSVSDENRELAGQLLNAADLWIFVTTANRYADALPWDMLTEAGARK FT ITVCVVLNRVPPGAEDDIVPDLKRLLSEKDLDPSLLHVLNETHLDDQKLIPSEHVEPLL FT AWLNSLAADSAKRQQIAAQTLDGALRRTTADVSELIAELQEQEKQLGELRALTNERFEQ FT SLARINDSLNDGSLLRGEILARWQDFVGAGELLRGIEGAIGRMRDRVGAFLTGRPPATH FT RVEQAIESGLHMVFIAEATKACHDVDRSWKNTPFGQALRSNLQSPRPPQDLNEQTSESI FT RLWQKDVLDMIRQEGAGKRKTARMAAFGVNGVAVILMVVVFASTAGLTGLEIGIAGGSA FT LVGQKLLEAIFGEDAVRRMATKARKMLDARARDLLDRTSSIYLDELAAKSQPELADRLG FT KITSALSSKGAH" FT CDS 1631834..1633477 FT /transl_table=11 FT /locus_tag="AARI_14320" FT /product="putative GTPase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF01926" FT /db_xref="GOA:E1VVJ2" FT /db_xref="InterPro:IPR001401" FT /db_xref="InterPro:IPR014743" FT /db_xref="UniProtKB/TrEMBL:E1VVJ2" FT /protein_id="CBT75645.1" FT /translation="MSERKILRAVSGLNSQINSVVEAMQLAEPYLEPETIDLAADVITR FT AESRRQFSSEHVVVGLFGATGSGKSTMFNALVGQELAATGVIRPTTTDTVAAIWEPEGS FT SELLDWLEVTTRHVMGDQDSRAQSGKKKKFDSGLLLLDLPDMDSTAVDHHKIAARLVGQ FT VDYLVWVLDPQKYADASIHHGYLNSLRSQQGNLLIVLNQIDKIAEQERKQVVDSLRGIL FT ATSGLENLPIVCASAATGEGVADVHAKITAAAKNKALSTRRLRADVDQVIHRLSEELQV FT EKVRLPSQLHQAELERVIAKAHGAQYIADAVETSYLLRGASRTGWPLTTWLVKMRNDPL FT KRMNLGRRHEDPELSLTSRPELSVAEASAIEHGIDQYVSEASNELPESWKEPLREKVHA FT NTEVLDDGIDAAIAGTPLGVERSSWWWPVVKVIQWVALVAALGGALWLAGYPVAGYFQF FT DLPQAPRVEGIAVPTLLVFIGILLGIVLGLACSFVNRIVAKVKRRKALKNIERSVSHLV FT RQAVIDPVDQHLDTFNSYSALITSAAKKAD" FT CDS 1633484..1634500 FT /transl_table=11 FT /gene="thiL" FT /locus_tag="AARI_14330" FT /product="thiamine-phosphate kinase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.4.16" FT /note="catalyses the following reaction: ATP + thiamine FT phosphate <=> ADP + thiamine diphosphate" FT /db_xref="GOA:E1VVJ3" 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:E1VVJ3" FT /protein_id="CBT75646.1" FT /translation="MTTNQPNVDATVGDLGEQGILDAMLPLLDSEQASLGPGDDAGALR FT VRGTEVLVSVDTLVENQDFRLIWPSGLEHRAYDIGWKSIAQNVSDINAMGGDATGAVIS FT LSLPKDTSLEWVRDFSRGVAEAIQGLGAQELTILGGDLGKSQEISVTTTVLGECEHGKV FT LRSGVQVGDRIAVAGRVGAAGAGLSVLEHDRNEQVWSRAVRRLVQAQCRPVPPLESGPR FT AAEAGATAMMDISDGLIRDAGRLAKASHVNLELESSVLQDYAVRLEAASELTGTDPMSW FT VLYGGEDFGLLAAFPEGLEIPEEFTVIGAAKPANGRRAVVKLDGKVAKPETGFDHFG" FT CDS complement(1634528..1635253) FT /transl_table=11 FT /locus_tag="AARI_14340" FT /product="IclR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF09339: IclR helix-turn- FT helix domain. This family of bacterial transcriptional FT regulators groups several proteins, including gylR, a FT possible activator protein for the gylABX glycerol operon FT in Streptomyces, and iclR, the repressor of the acetate FT operon (also known as glyoxylate bypass operon) in FT Escherichia coli and Salmonella typhimurium" FT /db_xref="GOA:E1VVJ4" FT /db_xref="InterPro:IPR005471" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR014757" FT /db_xref="UniProtKB/TrEMBL:E1VVJ4" FT /protein_id="CBT75647.1" FT /translation="MTIGSGVGVLDKAAAILNALENGPTSLSQLVELTEISRPTVHRIA FT QSLVHHGLVGRDMHGRFELGNRLVELASAAGEDRLVSAAGPVLIKLRDLTGESTQIFRK FT QGDYRVCIASAERPIGLRDTIPVGTQLSMKAGSAAQILLAWEDNERMVEGLHHARFTPT FT ILAGVRRRGWAQSLGEREPGVASVSAPVRGQSGRVIAALSLSGPIERLTRQPGKIHHEA FT VTSAAHELSELLRIQNDRA" FT CDS 1635367..1636815 FT /transl_table=11 FT /gene="leuC" FT /locus_tag="AARI_14350" FT /product="3-isopropylmalate dehydratase large subunit" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.1.33" FT /note="catalyzes the isomerization between (2R,3S)-3- FT isopropylmalate and (2S)-2-isopropylmalate, via the FT formation of (2S)-2-isopropylmaleate. Involved in leucine FT biosynthesis" FT /db_xref="GOA:E1VVJ5" 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/TrEMBL:E1VVJ5" FT /protein_id="CBT75648.1" FT /translation="MSAMQSPQTLAEKVWNAHVVRRGEGEGEARQPDLIYIDLHLLHEV FT TSPQAFEGLRLAGRPLRRPDLTIATEDHNTPTLDIDKPIADLTSRTQIHTLRDNCKEFG FT VRLHSLGDKEQGIVHVVGPQLGLTQPGMTVVCGDSHTSTHGAFGALALGIGTSEVEHVM FT ATQSLSLKPFKTMAINVEGTLKPGVTSKDIILAVIAKIGTGGGQGYVLEYRGSAIRSLS FT MDARMTICNMSIEAGARAGMIAPDETTFEYVKGRPHAPAGEDWDAAVEDWKQLHTDEGA FT RFDAEVFLNADELEPFVTWGTNPGQGVSLSENVPSPEDFEDENDRKACERALNYMGLTG FT GTPLKDIRVDTVFLGSCTNSRMEDLRAAAQVIKGKEKDPDVRMIVVPGSARVRLEAEAE FT GLDQIFKDFGAEWRFAGCSMCLGMNPDQLAEGERCASTSNRNFEGRQGKGGRTHLVSPL FT VAAATAIRGTLSSPSDLVNAPASV" FT CDS 1636830..1637435 FT /transl_table=11 FT /gene="leuD" FT /locus_tag="AARI_14360" FT /product="3-isopropylmalate dehydratase small subunit" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="4.2.1.33" FT /note="catalyzes the isomerization between (2R,3S)-3- FT isopropylmalate and (2S)-2-isopropylmalate, via the FT formation of (2S)-2-isopropylmaleate. Involved in leucine FT biosynthesis" FT /db_xref="GOA:E1VVJ6" 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/TrEMBL:E1VVJ6" FT /protein_id="CBT75649.1" FT /translation="MEKIVSHTGIGVPLRQSNVDTDQIIPAVYLKRITRTGFEDALFAG FT WRRDENFILNQEPFNTGSVLVAGPDFGTGSSREHAVWALKDYGFKAVISARFADIFRGN FT SGKQGLVAAEVAQSDIELIWKELENNPGTTVTVDLESRTVQCGSISAPFQIDDYTRWRL FT MEGLDDIGLTLQHEEDITAYEAKRPAHKPQTLPARTAG" FT CDS 1637693..1639012 FT /transl_table=11 FT /gene="murA" FT /locus_tag="AARI_14370" FT /product="UDP-N-acetylglucosamine FT 1-carboxyvinyltransferase" FT /function="1.1 Cell wall" FT /EC_number="2.5.1.7" FT /note="catalyzes enolpyruvyl transfer as part of the first FT step in the biosynthesis of peptidoglycan, a component of FT the bacterial cell wall. The reaction is FT phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = FT phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine" FT /db_xref="GOA:E1VVJ7" FT /db_xref="InterPro:IPR001986" FT /db_xref="InterPro:IPR005750" FT /db_xref="InterPro:IPR013792" FT /db_xref="UniProtKB/TrEMBL:E1VVJ7" FT /protein_id="CBT75650.1" FT /translation="MGKILTIHGGVPLKGTVRVGGAKNLVPKAMVAALLGDTPSVLRNV FT PEIKDVAVVRSLLEIHGVKVDQDPETGDLTMDPTQVKIASNQAIDAHAGDSRIPILFCG FT PLIHALGEAFIPDLGGCRIGDRPIDFHLEVLRDFGAIVDKAADGIRISAPNGLTGAKVE FT LQYPSVGTTEQVLLSAVRAKGVTEVSNAAIEPEILDLISLLQKMGAIISVHRDRVIRIQ FT GVEKLSGFDHSAMPDRNEAASWASAALVTKGDIFVQDATQRDLTAFLHVYRQIGGEFDV FT KSDGIRFYHPGGDLNPLILETDVHPGFMTDWQQPLVVALTQAKGVSVIHETVYENRFGF FT TDALVRMGSTVQVHTDCLGSTPCRFGQRNFKHSAVVVGPAKLTGADIDVPDLRGGFSHL FT IAALAAEGTSKVTGIEIINRGYEHFMEKLQALGANVELSN" FT CDS 1639030..1639794 FT /transl_table=11 FT /locus_tag="AARI_14380" FT /product="putative 1-acylglycerol-3-phosphate FT O-acyltransferase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.3.1.51" FT /note="1-acylglycerol-3-phosphate O-acyltransferase FT catalyzes the following reaction: Acyl-CoA + 1-acyl-sn- FT glycerol 3-phosphate <=> CoA + 1,2-diacyl-sn-glycerol 3- FT phosphate. It is involved in phospholipid biosynthesis" FT /db_xref="GOA:E1VVJ8" FT /db_xref="InterPro:IPR002123" FT /db_xref="UniProtKB/TrEMBL:E1VVJ8" FT /protein_id="CBT75651.1" FT /translation="MVKILAPGESAKTKRVFSVLAGIVRSAMNALIGKTWKGFEALPQG FT GYILCPNHLTEIDPLVVGHAIYSNGRLPRWLAKESLFKIPVLGWMLRETGQVPVARSAT FT SAGESLKAAKKVLDAGGVIVIYPEGTLTRDPNLWPMVGRTGAARLALQTGAPVVPMAHW FT GDQELLPRYSKKMNLFPRKHVTVLAGKPIDLEDLREVPRTRAVLEDATDRIMDAITDLT FT AELRQEDAPAERWDPSKHGQSKTGRNFDSPEN" FT CDS 1639861..1640862 FT /transl_table=11 FT /gene="gpsA" FT /locus_tag="AARI_14390" FT /product="glycerol-3-phosphate dehydrogenase (NAD(P)(+))" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.1.1.94" FT /note="catalyzes the following reaction: sn-glycerol 3- FT phosphate + NAD(P)(+) <=> glycerone phosphate + NAD(P)H. FT Involved in glycerophospholipid metabolism" FT /db_xref="GOA:E1VVJ9" FT /db_xref="InterPro:IPR006109" FT /db_xref="InterPro:IPR006168" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR011128" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VVJ9" FT /protein_id="CBT75652.1" FT /translation="MGAGSWGTTFAKVLADSVSDQGIPVQIWARREDAAKEINERHTNS FT RYLRETKLPANISASSDAQAVLTDADLVVLAIPAQSLREELAKFKELLEPDVVLLSLMK FT GLERGTDLRMSQVIAEVTGLPSAQIAVLSGPNLAMEIAREQPTASVVACTDSDIAQWIA FT ELCSASYFRPYTNDDVLGVELGGIVKNIIALAVGMCDGMGMGDNTKSTVITRGLAETTR FT LVLALGGRLDTLAGLSGLGDLVATCSSSLSRNNTAGRLLGQGLFLEEVNDRMSQTAEGI FT KSARAVFDLSRAHNVEMPITEAVVMVLEGTLSVENMAARLLSRELKSEGERH" FT CDS 1640862..1641974 FT /transl_table=11 FT /gene="ddl" FT /locus_tag="AARI_14400" FT /product="D-alanine--D-alanine ligase" FT /function="1.1 Cell wall" FT /EC_number="6.3.2.4" FT /note="participates in forming UDP-N-acetylmuramyl FT pentapeptide, the peptidoglycan precursor" FT /db_xref="GOA:E1VVK0" 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/TrEMBL:E1VVK0" FT /protein_id="CBT75653.1" FT /translation="MTERKLRVLLLFGGRSSEHSVSCVTAAGVMHAIDRERFEIVPVGI FT TRDGGWTLLDEDPEGWALNTGKLPEISSVDHPVHLSTDAQKTSLLSYSDSAVADLGEID FT VVFPLLHGPFGEDGSIQGMLEMAGVSYVGSGIAASAMGMDKHYMKVVFEGAGFNVGPYE FT VITNKQWLRDSEAAMKRCDNLQYPLFVKPARAGSSVGITKVDDPSELRAAIEIARAEDP FT KVIIEQGIVGREIECGVLEGRGSGPSRASLPGEIAVADNLHTFYDFEAKYVDGAAAELS FT CPANLSDEATLEIRELAVKAFDAIDAEGLSRVDFFYTPEGDWIINEINTMPGFTPSSMY FT PQMWAKTGIEYRELIDELIALATERNIGLR" FT CDS complement(1642049..1642498) FT /transl_table=11 FT /locus_tag="AARI_14410" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021903" FT /db_xref="UniProtKB/TrEMBL:E1VVK1" FT /protein_id="CBT75654.1" FT /translation="MSSTLLLPLLAGCASVASVDAAPDAANPLCAEMMVVLPEAIDDAE FT RRSTTSQATAAWGDPSKVVLRCGVEVPGPTTDPCVSVNEVDWVAHEDEATSIWTLTTYG FT RTPATEVVLDPNVIPSSTVLATLSDAAQKIPASKKCVSVDKSVNL" FT CDS 1642640..1643686 FT /transl_table=11 FT /locus_tag="AARI_14420" FT /product="putative cell envelope-related transcriptional FT attenuator" FT /function="3.5.2 Transcription regulation" FT /db_xref="InterPro:IPR004474" FT /db_xref="UniProtKB/TrEMBL:E1VVK2" FT /protein_id="CBT75655.1" FT /translation="MSFEEHPVRPRKKKKRTGRAIVLSVLALVVVAGLVAGGYLWNLGR FT TFDSESKTITNAFPAEETRPEVKEESKGAVNILLLGSDTRATRDADEDSDDFGTLPNGG FT RSDTMMLVHIPADRKNVFVTSVMRDTWLDIPGVGTAKINRAFASGGVPKAVETLEGLFG FT VRINHVASVDFEGFKGLTDAVGGVTVNNPRGFKQSIVNGMYFPEGVQTLNGEQALAFVR FT ERKSFPGSDYQRVKNQQLFVKALLGQLMSKETLSNPGKVSEVVSQIAPFIAVDETLDAA FT KVASYASSMLNLRSSDMEFFTLPNKGPGRSADGQSIVIPDMAVIEKFGKALQEDKMAEF FT VESTDLSR" FT CDS 1643710..1644678 FT /transl_table=11 FT /locus_tag="AARI_14430" FT /product="DAK2 phosphatase domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF2734 (DAK2; predicted phosphatase domain FT of the dihydroxyacetone kinase family) domain" FT /db_xref="GOA:E1VVK3" FT /db_xref="InterPro:IPR004007" FT /db_xref="UniProtKB/TrEMBL:E1VVK3" FT /protein_id="CBT75656.1" FT /translation="MTPQKLDTSVRAIREWLAQSVKSLGNHSDRLNAINVFPVADGDTG FT SNLYLTARAGHDAVSKLESDDIGGFLEVAARASMESARGNSGTLLAVFLSGLSEPWIGH FT DRLNASLLAAGLERAKVRSWSALSEPVEGTMLSVINAIALAAGSTLAHLKTDLDSRAAL FT DTVLTQMAQAARLAVKGTETELPSLVEAGVVDAGAVGMLVIIDELCAAIRNDSPDFESY FT EKFHGYQVQDPHVHLNKDTETGVEVMCTVSLDALGAATLRGQLDTMGNSVIMSPVNQVE FT DDTYRWRVHVHVPESERALELIKKYGDPVNISVTDLCTHDG" FT CDS 1644671..1646860 FT /transl_table=11 FT /gene="recG" FT /locus_tag="AARI_14440" FT /product="putative ATP-dependent DNA helicase RecG" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.6.1.-" FT /note="RecG protein is a junction-specific DNA helicase FT that drives branch migration of Holliday intermediates in FT genetic recombination and DNA repair" FT /db_xref="GOA:E1VVK4" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR014001" FT /db_xref="InterPro:IPR016027" FT /db_xref="UniProtKB/TrEMBL:E1VVK4" FT /protein_id="CBT75657.1" FT /translation="MAETTQTSFENAELSAYLGKKNSAALEKAFGYTTVGEFLWHFPRR FT YVEVGELTPIAELPFDEHVTVVAQVVNVSQRQMHSRRGFIFEVTVSDELSAGGQELKMT FT FFNGYQARTDLHIGTIAMFSGKVSWYQDYLQLSQPEYAILDEASQADPRPIPIYPASAK FT MPNKRIRDLMGLLLEQFTDQNIPEFLPTEVLSSRHYPVRHQAFLDRHFPKEIKYAYVAR FT QRFAFEEAFLLQLALGERGRQLGAQKAIARPPAPGRLAAKFDAQLPFRLTEDQVLVGQH FT ISADLEQSHPMHRLLQGEVGSGKTIVALRAILQVIDAGGQAALLAPTEVLAAQHYASIR FT KMLGNLAEPGLFGEGEGTGVALLTGSAKTAQRREALLGIASGETGLIIGTHALLSDQVQ FT FAELGLVVVDEQHRFGVEQRDALRAKAGDTVPHTLVMTATPIPRTVAMTVFGDLETSTI FT KRLPAGRAPIQTHIVPMQLSGFRDRLFSRITEEVQKGHQVYVVCPRISDTTAEQGVLLS FT TYDDSSVGQTMSVEAMQEMLAGMPEFAGIRTQTLHSQLDTTDKQETMDSFARGEIDVLI FT STTVIEVGVDVHNATLMVIMDAERFGISQLHQLRGRVGRGGLPGTCLMTTWLDADHPSV FT GRLKTIESTTDGFELAEADLAERREGNILGVQQSGSKSSLRELSIIKDRSLIEQARADV FT GLVLANGKWGTHHPMLLAAAGSWIDEPTKEFLNKN" FT CDS 1646880..1647464 FT /transl_table=11 FT /locus_tag="AARI_14450" FT /product="putative site-specific DNA-methyltransferase FT (adenine specific)" FT /function="3.2 DNA restriction and modification (and FT repair)" FT /note="match to PS00092 pattern: N-6 Adenine-specific DNA FT methylases signature. In prokaryotes, the major role of DNA FT methylation is to protect host DNA against degradation by FT restriction enzymes" FT /db_xref="GOA:E1VVK5" FT /db_xref="InterPro:IPR002052" FT /db_xref="InterPro:IPR004398" FT /db_xref="UniProtKB/TrEMBL:E1VVK5" FT /protein_id="CBT75658.1" FT /translation="MSRIIAGAAGGHPLKSVPGDATRPTTDRVKEALFSRLESWDILSG FT ARVLDLFAGSGSLGIETASRGARQVVLVEKAPKAVAVCQHNAALVNKVLKTNTVTVQRG FT NVDSVLDGYYNAISGVPSKTFDVVLMDPPYPLAEEELAITLEKISKILAEDATVIIERS FT ARSPEPVWPSSLEKFADKKYGETHLWFAEPV" FT CDS complement(1647441..1648223) FT /transl_table=11 FT /locus_tag="AARI_14460" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVK6" FT /protein_id="CBT75659.1" FT /translation="MTQKLAKRWLGFVQEHATIYDDDIVPGSMILAIGDAPQSHVNLSH FT PEEVFYEYLARIANHLTVLRPENRPLKMLHLGAGALTLARWASVIYPSSTHVAVDIERE FT LLDFVLTHLPLPLGCELSPIVADARSVLAEQLSDEKFDVIVLDIFSGPEAPEHLTTAGY FT YAELKNSLTNDGLLFVNIGDDPPLDFTCSQVEAARSSFETVMLSSSPEMFTKRFPGNMI FT LTASSQAFHEDQILQCQAAGPFPSEVRHAMDLDGFCKP" FT CDS complement(1648220..1649431) FT /transl_table=11 FT /locus_tag="AARI_14470" FT /product="putative aminotransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /note="identified by match to PF00155: aminotransferase FT class I and II" FT /db_xref="GOA:E1VVK7" 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:E1VVK7" FT /protein_id="CBT75660.1" FT /translation="MSNNFTPWQRTAYSVNLLDSTGQPGVTIFEEITALANHHGAINLG FT QGFPDTEGPTEIRQIAVEAIQNGANQYAPGSGTPILREAIAAHQERFYSLKIDPGSEVV FT VTTGATEAIAACLLAFLEPGDEVVTFEPYYDSYAAMIGLANAVHKVVQLKAPTFEPDLA FT ELRRTVTDKTRVILVNNPHNPTGTVLDESVLKEVIALAHQHNCIIIADEVYEHLTFGVQ FT HVPIATLPGGFERTITISSAGKSFSFTGWKVGWATGPRELITAVRTVKQFLTYSSGPAF FT QPAVAQALQLSDGFFSDFAASLGQAGEVLASGLEKAGIPVIRPKGTYFLVADVRSFDLN FT DAAEVARVMPERLGVAAIPMSVFVHPENQNDYQGLLRFAFCKQPDVISAAVERLQRLPE FT VLSK" FT CDS 1649544..1650011 FT /transl_table=11 FT /gene="coaD" FT /locus_tag="AARI_14480" FT /product="pantetheine-phosphate adenylyltransferase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.7.3" FT /note="reversibly transfers an adenylyl group from ATP to FT 4-phosphopantetheine, yielding dephospho-CoA (dPCoA) and FT pyrophosphate: ATP + pantetheine 4-phosphate = diphosphate FT + 3-dephospho-CoA" FT /db_xref="GOA:E1VVK8" FT /db_xref="InterPro:IPR001980" FT /db_xref="InterPro:IPR004820" FT /db_xref="InterPro:IPR004821" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VVK8" FT /protein_id="CBT75661.1" FT /translation="MRRAVCPGSFDPIHNGHVEIIARAASLFDEVIVAVSTNYSKKYRF FT SEDERVAMVEETVGGLRGVSAMPMGQGLLAYFCKEQGAEAIVKGLRSTVDYAYEIPMAT FT MNRHLTGVETVFLQADTRFTHLSSSLLKEVQALGGDVDDYFPRAVIKRLLT" FT CDS 1650104..1651003 FT /transl_table=11 FT /gene="galU" FT /locus_tag="AARI_14490" FT /product="UTP--glucose-1-phosphate uridylyltransferase" FT /function="1.1 Cell wall" FT /EC_number="2.7.7.9" FT /note="catalyses the formation of UDP-glucose from glucose- FT 1-phosphate" FT /db_xref="GOA:E1VVK9" FT /db_xref="InterPro:IPR005771" FT /db_xref="InterPro:IPR005835" FT /db_xref="UniProtKB/TrEMBL:E1VVK9" FT /protein_id="CBT75662.1" FT /translation="MPKSAITKAVIPAAGLGTRFLPATKAMPKEMLPVVDKPAIQYVVA FT EAVKSGFTDLLMVTGRNKRALEDHFDRVPSLEYSLEAKGDKKKLDAIHEATRLGDIHYV FT RQGDPRGLGHAVLCAKQHVGNEPFAVLLGDDLIDERDELLSVMAEVQRKTGGSVIALME FT VEPEQISAYGCADVSLVESEDFVKVNALVEKPEINEAPSNLAIIGRYLLHPRVFEVLEH FT TAPGRGNEIQLTDALQILAAAHGEGAGVHAVIFRGRRYDTGDKLSYLQANITLAVENDE FT LGPSLKSWLKGFVNQLAD" FT CDS 1651120..1652187 FT /transl_table=11 FT /locus_tag="AARI_14500" FT /product="putative cell envelope-related transcriptional FT attenuator" FT /function="3.5.2 Transcription regulation" FT /db_xref="InterPro:IPR004474" FT /db_xref="UniProtKB/TrEMBL:E1VVL0" FT /protein_id="CBT75663.1" FT /translation="MKKEQDQDLIFSSRSARNRLERKKKRTRSIVVSVVVVVLVAVLSA FT GYVLFDLQRQFNSKSNTVALSFSDAEEQARPIKDPDDKSMNILLLGVDHADEDTTQSAA FT LNEAVSQRSDSMMLVHIPEDRSQVYVMSMVRDMYVDIPGYGMNKLNAAISLGGVPLLMQ FT TVEGLFDTKLDHLAMIDFEGFRELSTALGGVTVDNEIPFTANDTDYFYPAGDITLQGDR FT ALRFVRERKSFTNGDYQRVANQRKFISAAANQVLSSNTLANPVKLYEIVDKVSPYLTFD FT QNFDAATLVGLGLQLKNVDTKNMKMFTMPTAGTSTSADGQSIELASELAIAQISDALQT FT DRMANYLQENPPETP" FT CDS 1652324..1653172 FT /transl_table=11 FT /locus_tag="AARI_14510" FT /product="capsular FT polysaccharide/lipopolysaccharide/teichoic acids ABC FT transporter, inner membrane subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="TC 3.A.1.y.z. ABCISSE: ABC transporter, permease FT (IM), CLS-family (capsular polysaccharide, FT lipopolysaccharide and teichoic acids). A typical system is FT made of a conserved permease (IM) and an ATP-binding FT subunit (ABC). In addition to these proteins, capsular FT polysaccharide exporter systems require two accessory FT proteins to perform their function: a periplasmic or a FT lipid-anchored outer membrane protein called OMA and a FT cytoplasmic membrane protein MPA2" FT /db_xref="GOA:E1VVL1" FT /db_xref="InterPro:IPR000412" FT /db_xref="InterPro:IPR013525" FT /db_xref="UniProtKB/TrEMBL:E1VVL1" FT /protein_id="CBT75664.1" FT /translation="MTVADEAEKYGLHRVGARPTLVNYLKETWQRREFIYELAKARVQS FT QNQRNRLGIVWIVLKPTFNALMYGFIFGILQGGSRGIDYPVFVVIGVFLFEFFSTSMTG FT GAKAITGNNALVQSLSFPRLALPVAQITQNVLTLMPMVVVMFIYALILGTTPKWSWLTI FT IPIIALFTVFNLGVALICARITVHVRDFTQILPLIGRVLFYTSGVLFSAERLLSHWPWM FT IAIFDVHPVYQTLQLARGMIMNVSEYDSWAWWVLTAWAVVTLLVGLLYFWKAEERYGRA FT N" FT CDS 1653183..1654049 FT /transl_table=11 FT /locus_tag="AARI_14520" FT /product="capsular FT polysaccharide/lipopolysaccharide/teichoic acids ABC FT transporter, ATP-binding subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TC 3.A.1.y.z. ABCISSE: ABC transporter, ATP-binding FT protein (ABC), CLS-family (capsular polysaccharide, FT lipopolysaccharide and teichoic acids). A typical system is FT made of a conserved permease (IM) and an ATP-binding FT subunit (ABC). In addition to these proteins, capsular FT polysaccharide exporter systems require two accessory FT proteins to perform their function: a periplasmic or a FT lipid-anchored outer membrane protein called OMA and a FT cytoplasmic membrane protein MPA2" FT /db_xref="GOA:E1VVL2" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VVL2" FT /protein_id="CBT75665.1" FT /translation="MINPELHPDYEPAPIFSDDTSFIDVVKPEEIKNSQLQVDESRQPV FT VIVDNLHVKYEVFSSGKAVGNAGARRLLQPKLKGVRTVHALKGITFVAYENESIGVIGS FT NGSGKSTLLKAITGLTPPSSGAVYARSRPSLLGVGAALIPDLSGDKNITLGGLALGYSR FT EQVEEMRTDITHFAELQEFIDLPMRTYSSGMSARLKFAIAASKKHDILIVDEALAVGDA FT KFKKRSEAKIREIRDSAGTIFNVSHSMGSIRETCNRVIWIEKGVQMMDGDPDTVIKEYQ FT KHLKAKK" FT CDS 1654057..1655100 FT /transl_table=11 FT /locus_tag="AARI_14530" FT /product="putative family 2 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00535: glycosyl transferase family 2. FT This domain is found in a diverse family of glycosyl FT transferases that transfer the sugar from UDP-glucose, UDP- FT N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to a FT range of substrates including cellulose, dolichol phosphate FT and teichoic acids" FT /db_xref="GOA:E1VVL3" FT /db_xref="InterPro:IPR001173" FT /db_xref="InterPro:IPR005829" FT /db_xref="UniProtKB/TrEMBL:E1VVL3" FT /protein_id="CBT75666.1" FT /translation="MTEFPGVSYVMPVLNESAYLEEAVTSILAQEYAGEKELVLALGPS FT HDSTNEVAKQLSAADSRIILVDNPLGRTPIGLNLAIRASTLPIVIRVDAHSELPKNYTQ FT RGIETLYRVNAHDVGGLMDAKGRTPIQRGIAAAYHSKFGFGGPAYHSGAPEGPSESAYL FT GIFRREVFEEVGYYNEELWRAQDWELCLRIRKAGHTVWFDPELRVGYYPRDSFKSLISQ FT SMASGTWRAEIARRFPEGKSLRHDVPPILLAGVATGFVAAVVEPLTRESAPTGLRVVLN FT VAKTIPAIYASIALVAGLSSNAKGLKDKLLAACAFPAIHLPWAVGYIKGRVCGAAGTVD FT KGRVKKS" FT CDS 1655097..1655915 FT /transl_table=11 FT /locus_tag="AARI_14540" FT /product="putative transferase" FT /function="1 Cell envelope and cellular processes" FT /note="match to protein family PF01066. Possibly involved FT in phospholipid biosynthesis" FT /db_xref="GOA:E1VVL4" FT /db_xref="InterPro:IPR000462" FT /db_xref="UniProtKB/TrEMBL:E1VVL4" FT /protein_id="CBT75667.1" FT /translation="MIVRPKNPTLDQLREVCQPPEVRARKNAEHWTAELYLRHISIYLT FT AVLVRTRISANGVTGLMILAGWCMSLALLIPGIWGPLLAVTLSQVQLYFDCSDGEVARW FT RATQSPRGIFIDMVGHHTTEALIPIALGYRVFKELSADNSPIEQAWPILFMSACLSVLL FT VLNRSQSLMVHAARGMAGLGKLPDTAAARSVPTTSLVGKLRSLARFLPFHKLLHAVELS FT LIILGCSIISLIVGTPGIAEKWMIWILLPACVLVNFGHFLSNMASSRLKA" FT CDS 1655955..1656845 FT /transl_table=11 FT /locus_tag="AARI_14550" FT /product="putative family 2 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00535: glycosyl transferase family 2. FT This domain is found in a diverse family of glycosyl FT transferases that transfer the sugar from UDP-glucose, UDP- FT N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to a FT range of substrates including cellulose, dolichol phosphate FT and teichoic acids" FT /db_xref="GOA:E1VVL5" FT /db_xref="InterPro:IPR001173" FT /db_xref="UniProtKB/TrEMBL:E1VVL5" FT /protein_id="CBT75668.1" FT /translation="MPAETKPTIGVVVLTMGNRPVELKRALESLLAQRSVAIDAVVVGN FT GWDPTDIPEGIKTHFLPENLGIPAGRNAGVKQIQGEYLCFLDDDSWFIDDDFLITAVER FT FRHYPRMGLLQPRITDPENEDQNPRRWIPRLKKRTALEPSKVFHVGETCLVTTRNIFDA FT TGGWAGGFWYAHEGIELAWRVWDTGTYVWYAGDMQIGHPIVDPRRHDEFYRLNARNRVW FT LARRNLPLPLRWVYPTTWMLIECLRLRRNKSAVAQYIAGWRAGWAGSPWYREPRPKLRW FT KTIVRMTLAGRLPII" FT CDS 1656910..1657371 FT /transl_table=11 FT /gene="tagD" FT /locus_tag="AARI_14560" FT /product="glycerol-3-phosphate cytidylyltransferase" FT /function="1.1 Cell wall" FT /EC_number="2.7.7.39" FT /note="involved in teichoic acid biosynthesis" FT /db_xref="GOA:E1VVL6" FT /db_xref="InterPro:IPR004820" FT /db_xref="InterPro:IPR004821" FT /db_xref="InterPro:IPR014729" FT /db_xref="UniProtKB/TrEMBL:E1VVL6" FT /protein_id="CBT75669.1" FT /translation="MTKTVLTYGTFDLFHIGHLNILKRLKAKGDRLVVGVSTDEFNAIK FT GKKPVVPFEQRLEIVQSIKYVDLAIPEENWAQKRSDIKKYDAKVFGIGEDWKGHFDDLG FT DEVEVIYLPRTAGISTTEMKRVLSEYDERHVESLKNTLDTLSQIVKELS" FT CDS 1657421..1658794 FT /transl_table=11 FT /locus_tag="AARI_14570" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVL7" FT /protein_id="CBT75670.1" FT /translation="MLAGWRGRIGRAVPESIISKVLERSLAASSTDVQRTAPDLRRSAE FT HKSIEIASRRKIDFSRASKDMPLCVAAKDWQSLRRDFEASGMIVRKLHGQHSFAASEAW FT SVGVQLPHSESIADLRGAGAIWQVFPGLIKEPVDVHDFGGTVDAVYTWVDAEDLQWASA FT YQDALGASGREMTDSSVNRARFQSHDELRYSLRSLELNLPWINKIHLVTAGQRPSWLVK FT EHPKLVLVDHQTIFNDPESDLPTFNSHAIESQLVNIPNLAEHFLYVNDDVFFGRYLYPN FT AFFGPAGQAKYSLSSSHFAQAEDPGLPVNQAAVNNRNVVVERFGRTSSHKFRHVAHPQR FT LSVHRQLHEELEESIARVAANRFRSENDLSIPSSLVHQFAAQMGMGYPSSTSYRYIDIG FT SKASVLELMRLSRDRGVDMFCINEVLASSDADRRSVLAREILASKFPLPSTFELSKPE" FT gene 1658966..1661197 FT /pseudo FT /locus_tag="AARI_14580" FT /product="truncated family 2 glycosyl transferase" FT /note="section of a family 2 glycosyl transferase. FT Insertion of ISAar44, IS3 family. Match to PF00535: FT glycosyl transferase family 2. This domain is found in a FT diverse family of glycosyl transferases that transfer the FT sugar from UDP-glucose, UDP-N-acetyl-galactosamine, GDP- FT mannose or CDP-abequose, to a range of substrates including FT cellulose, dolichol phosphate and teichoic acids" FT gene complement(1661327..1661425) FT /pseudo FT /locus_tag="AARI_35000" FT /product="C terminal part of transposase of ISAar22, IS481 FT family" FT /function="4.5 Transposon and IS" FT mobile_element complement(1661398..1662996) FT /mobile_element_type="insertion sequence:ISAar44" FT /rpt_family="IS3 group IS3" FT repeat_region complement(1661398..1661435) FT /rpt_type=INVERTED FT CDS complement(1661432..1662373) FT /transl_table=11 FT /locus_tag="AARI_35010" FT /product="transposase of ISAar44, IS3 family, IS3 group, FT orfB" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVL8" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VVL8" FT /protein_id="CBT75671.1" FT /translation="MNRRQNAARAGRALRATAPRPAPANKLTAQEETTILATLNSERFV FT DQAPEQIHATLLSEGTYLCSVSSMYRLLRRAKQVAERRRQARHPARKVPELVADQPGEV FT FTWDITKLAGPTKGVYFDAYVMIDIYSRYIVGCQVHTRESGELARDFIAGVFAKDQVPK FT VVHADRGTSMTSKPVAALLADLDVLKSHSRPKVSNDNPFSEAWFKTLKYLPTFPQRFGS FT LVDARAFMDRFVQSYNGHHRHSGIGFHTPADVHFGMTGHVDDQRLAALQRAWDEHPERF FT GRRRLPKKLQMPEAAWINEPVKRLEGQEMQAG" FT CDS complement(1662472..1662909) FT /transl_table=11 FT /locus_tag="AARI_35020" FT /product="transposase of ISAar44, IS3 family, IS3 group, FT orfA" FT /function="4.5 Transposon and IS" FT /db_xref="UniProtKB/TrEMBL:E1VS60" FT /protein_id="CBT75672.1" FT /translation="MSIDSIHPTPGNMPENGTMDSIDSRPEQPRRRSISPAQKLAYLDG FT YEQAIQTGEGRGYLRANALYSSQIVEWRRLRDAGVLGDSTSNSFPARSSSRLSKEQAEI FT ARLKKQLAANEQKLATTQTALEIMGKAHALLEQISKSADSK" FT repeat_region complement(1662959..1662996) FT /rpt_type=INVERTED FT mobile_element complement(1663164..1664689) FT /mobile_element_type="insertion sequence:ISAar46" FT /rpt_family="IS3 group IS3" FT repeat_region complement(1663164..1663182) FT /rpt_type=INVERTED FT CDS complement(1663196..1664188) FT /transl_table=11 FT /locus_tag="AARI_35030" FT /product="transposase of ISAar46, IS3 family, IS3 group, FT orfB" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVM0" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VVM0" FT /protein_id="CBT75673.1" FT /translation="MKAAYQRLLDIKIPQRKAAVIAGVSRTTMNRKPSKPQDTPRPAPP FT NKLSHVERAAILSALNSPEWVDMAPMQVYAKLLDEGQYLGSLSSFYRVLNENRLVKERR FT RLARHKPRAIPELEANAPGEVYSWDITKLAGPVKGKYFDCYLMVDIYSRYIVGAHVHAT FT ESGQLAVEMMKEIFGVHGIPLVVHADRGTSMTSKTVAALLSDLEVTRSHSRPRVSNDNP FT YSESLFKTLKYAPQFPERFSSLSDARLFISEFVQWYNHAHQHSGIGLHTPADVHFGLAN FT SVAAKRSQTLAAARARHPERFSTSQDPKILAMPEAAWINNPKDRAVQAA" FT CDS complement(1664185..1664577) FT /transl_table=11 FT /locus_tag="AARI_35040" FT /product="transposase of ISAar46, IS3 family, IS3 group, FT orfA" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVM1" FT /db_xref="InterPro:IPR002514" FT /db_xref="UniProtKB/TrEMBL:E1VVM1" FT /protein_id="CBT75674.1" FT /translation="MTNPGPRAGGPSRRRTFTPTEKLELLAGYDEAITEQKGGAYLREH FT GVYSSHITEWRKLRDAGVLEGKTAGTRLGKLSAEQAEIARLRRQLEVSEGKRKQTEEAL FT DIMGKLSAFFENAINESQDEAKSKKK" FT repeat_region complement(1664671..1664689) FT /rpt_type=INVERTED FT gene 1664805..1667654 FT /pseudo FT /locus_tag="AARI_14590" FT /product="truncated family 2 glycosyl transferase" FT /note="section of a family 2 glycosyl transferase. FT Insertion of ISAar44, IS3 family. Match to PF00535: FT glycosyl transferase family 2. This domain is found in a FT diverse family of glycosyl transferases that transfer the FT sugar from UDP-glucose, UDP-N-acetyl-galactosamine, GDP- FT mannose or CDP-abequose, to a range of substrates including FT cellulose, dolichol phosphate and teichoic acids" FT CDS 1667982..1668260 FT /transl_table=11 FT /locus_tag="AARI_35050" FT /product="transposase of ISAar3, IS3 family, IS407 group, FT orfA" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVM2" FT /db_xref="InterPro:IPR002514" FT /db_xref="UniProtKB/TrEMBL:E1VVM2" FT /protein_id="CBT75675.1" FT /translation="MARRHTPDQVIAKVRQGQKMLNDGHPMIEVIKELQITEATWYRWI FT NQYGSEKNAEASKRTKELEKENARLKKLLADQMLANDILTEVAKGKF" FT gene 1668300..1668449 FT /pseudo FT /locus_tag="AARI_35060" FT /product="N terminal part of transposase of ISAar3, IS3 FT family, IS407 group, orfB (disrupted by insertion of FT ISAar45, IS3 family, IS3 group)" FT /function="4.5 Transposon and IS" FT gene complement(1668471..1669277) FT /pseudo FT /locus_tag="AARI_35070" FT /product="C terminal part of transposase of ISAar45, IS3 FT family, IS3 group, orfB" FT /function="4.5 Transposon and IS" FT /note="disrupted by insertion of ISAar44, IS3 family, IS3 FT group. Second part of ISAar45. Second part of orfB" FT repeat_region complement(1669295..1669297) FT /rpt_type=DIRECT FT mobile_element complement(1669298..1670896) FT /mobile_element_type="insertion sequence:ISAar44" FT /rpt_family="IS3 group IS3" FT repeat_region complement(1669298..1669335) FT /rpt_type=INVERTED FT CDS complement(1669332..1670273) FT /transl_table=11 FT /locus_tag="AARI_35080" FT /product="transposase of ISAar44, IS3 family, IS3 group, FT orfB" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVL8" FT /db_xref="InterPro:IPR001584" FT /db_xref="InterPro:IPR012337" FT /db_xref="UniProtKB/TrEMBL:E1VVL8" FT /protein_id="CBT75676.1" FT /translation="MNRRQNAARAGRALRATAPRPAPANKLTAQEETTILATLNSERFV FT DQAPEQIHATLLSEGTYLCSVSSMYRLLRRAKQVAERRRQARHPARKVPELVADQPGEV FT FTWDITKLAGPTKGVYFDAYVMIDIYSRYIVGCQVHTRESGELARDFIAGVFAKDQVPK FT VVHADRGTSMTSKPVAALLADLDVLKSHSRPKVSNDNPFSEAWFKTLKYLPTFPQRFGS FT LVDARAFMDRFVQSYNGHHRHSGIGFHTPADVHFGMTGHVDDQRLAALQRAWDEHPERF FT GRRRLPKKLQMPEAAWINEPVKRLEGQEMQAG" FT CDS complement(1670372..1670809) FT /transl_table=11 FT /locus_tag="AARI_35090" FT /product="transposase of ISAar44, IS3 family, IS3 group, FT orfA" FT /function="4.5 Transposon and IS" FT /db_xref="UniProtKB/TrEMBL:E1VS60" FT /protein_id="CBT75677.1" FT /translation="MSIDSIHPTPGNMPENGTMDSIDSRPEQPRRRSISPAQKLAYLDG FT YEQAIQTGEGRGYLRANALYSSQIVEWRRLRDAGVLGDSTSNSFPARSSSRLSKEQAEI FT ARLKKQLAANEQKLATTQTALEIMGKAHALLEQISKSADSK" FT repeat_region complement(1670859..1670896) FT /rpt_type=INVERTED FT gene complement(1670874..1671071) FT /pseudo FT /locus_tag="AARI_35100" FT /product="N terminal part of transposase of ISAar45, IS3 FT family, IS3 group, orfB (disrupted by insertion of ISAar44, FT IS3 family, IS3 group)" FT /function="4.5 Transposon and IS" FT repeat_region complement(1670897..1670899) FT /rpt_type=DIRECT FT CDS complement(1670954..1671244) FT /transl_table=11 FT /locus_tag="AARI_35110" FT /product="transposase of ISAar46, IS3 family, IS3 group, FT orfA" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVM5" FT /db_xref="InterPro:IPR002514" FT /db_xref="UniProtKB/TrEMBL:E1VVM5" FT /protein_id="CBT75678.1" FT /translation="MPRIFTEEFKKDAVALVESGISQKQVSADLGVSKTALQTWVRDAR FT YQSHGMTPSSDADERKEMSQALKRIRELEMENEVLRKAAAYLSQSHIRSPK" FT gene 1671284..1672015 FT /pseudo FT /locus_tag="AARI_35120" FT /product="C terminal part of transposase of ISAar3, IS3 FT family, IS407 group, orfB" FT /function="4.5 Transposon and IS" FT /note="disrupted by insertion of ISAar45, IS3 family, IS3 FT group. Second part of ISAar3. Second part of orfB (66- FT 296)" FT CDS 1672311..1673984 FT /transl_table=11 FT /locus_tag="AARI_14600" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVM6" FT /db_xref="InterPro:IPR021520" FT /db_xref="UniProtKB/TrEMBL:E1VVM6" FT /protein_id="CBT75679.1" FT /translation="MQKQLPKPSLTNLKTAVKKTLPVDFYIKLRSAGLRGLESYGVAER FT RLKLFLHRDRNVNFICDVRSYKGLQWKVDTPVLPSTVAKESFDLVTKKLNDAGIQWWFI FT GVDQFQSGIVALRDDEKSRARKVLSGIDDGAPVYAAGEDGTTVLPVSTLASNSVWDDQN FT VISIFSPRCFNDSTLLFGAERNCQIEFWKFEPTEAGVRVTAPRENRASRLLSQSDVEFK FT EIETRFGKVPTPKVLTQTMIDDITFPIDAVYTWVDGEDPAWLETKRRRESELSGEEYHE FT EANHTARFRSRDELKYSLRSLQMFAPWFRKIFIVTAGQVPAWLDTSDPRIVVVDHRDIY FT PAGEYLPTFNSNSIISRLHHIDGLSEHYVYINDDVFFGRDLGPERFFTPTGIAKVSPSN FT NRRPFGEATLLDEPHFNLTRNIRRLLQERFNVTVSRAIKHTPHPQLKSVHFQMEEEFRD FT EYENTWASPFRDHRDIVADQLHHYYAQITGRAITTGLRYHYINIRDNNYRLVMENTLRL FT RDRDTFCINDAPVAGATPIDDEFVNDFLESYFPVKSDFEK" FT CDS 1674378..1674899 FT /transl_table=11 FT /locus_tag="AARI_14610" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR003772" FT /db_xref="UniProtKB/TrEMBL:E1VVM7" FT /protein_id="CBT75680.1" FT /translation="MHILNEQVPAPTDVGNALIGIRGGSELDLDLRLESVHEGILVSGT FT ATAQIAGECGRCLEPIEYDFEADIQELFYYEESEEFEDDDDVDQYWVVDDLIDIDPVLR FT GAVVTALPFQPVCKKDCLGLCSECGISLNDDPEHQHEILDPRWAALAQLSDNVASDATN FT DKTSFKREEK" FT CDS 1674902..1675105 FT /transl_table=11 FT /gene="rpmF" FT /locus_tag="AARI_14620" FT /product="50S ribosomal protein L32" FT /function="3.7.1 Ribosomal proteins" FT /note="ribosomal protein L32 is part of the 50S ribosomal FT subunit" FT /db_xref="GOA:E1VVM8" FT /db_xref="InterPro:IPR002677" FT /db_xref="InterPro:IPR011332" FT /db_xref="UniProtKB/TrEMBL:E1VVM8" FT /protein_id="CBT75681.1" FT /translation="MAVPKRKMSRANTRARRSQWKATAPNLVKTVENGRVTYSLPHQAK FT VVTDSAGTELFLEYKGRKVADV" FT CDS 1675130..1675807 FT /transl_table=11 FT /gene="rnc" FT /locus_tag="AARI_14630" FT /product="ribonuclease III" FT /function="3.6 RNA modification" FT /EC_number="3.1.26.3" FT /note="digests double-stranded RNA. Involved in the FT processing of ribosomal RNA precursors and of some mRNAs" FT /db_xref="GOA:E1VVM9" FT /db_xref="InterPro:IPR000999" FT /db_xref="InterPro:IPR001159" FT /db_xref="InterPro:IPR011907" FT /db_xref="InterPro:IPR014720" FT /db_xref="UniProtKB/TrEMBL:E1VVM9" FT /protein_id="CBT75682.1" FT /translation="MKRLGINIDSETFRLAFTHRSYSYEHGGIPTNERLEFLGDSILGF FT CVAEYLYASFPDLPEGDLAKRRAAIVSTRALAMIARDLEVGEHLFLGRGESQSNGANKS FT SILADTMEAILGATYLVQGMDEARALVLRFVTPLLEDPRLLGATTDWKTVIQEEVASQK FT LGEMCYEVTGSGPDHARTYVAKLCIGAKSYGEGHGPSKKEAEQEAAHNTWLLFHPGEVL FT PKG" FT CDS 1675819..1676742 FT /transl_table=11 FT /gene="mutM" FT /locus_tag="AARI_14640" FT /product="formamidopyrimidine-DNA glycosylase" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.2.2.23" FT /EC_number="4.2.99.18" FT /note="formamidopyrimidine-DNA glycosylases is a FT trifunctional DNA base excision repair enzyme that removes FT a wide range of oxidation-damaged bases (N-glycosylase FT activity; EC:3.2.2.23) and cleaves both the 3- and 5- FT phosphodiester bonds of the resulting apurinic/apyrimidinic FT site (AP lyase activity; EC:4.2.99. 18). It has a FT preference for oxidised purines, excising oxidized purine FT bases such as 7,8-dihydro-8- oxoguanine (8-oxoG). Its AP FT (apurinic/apyrimidinic) lyase activity introduces nicks in FT the DNA strand, cleaving the DNA backbone by beta-delta FT elimination to generate a single-strand break at the site FT of the removed base with both 3- and 5-phosphates" FT /db_xref="GOA:E1VVN0" FT /db_xref="InterPro:IPR000191" FT /db_xref="InterPro:IPR000214" FT /db_xref="InterPro:IPR010979" FT /db_xref="InterPro:IPR012319" FT /db_xref="InterPro:IPR015886" FT /db_xref="UniProtKB/TrEMBL:E1VVN0" FT /protein_id="CBT75683.1" FT /translation="MPELPEVEVVREGLDKWIRARTVQSVQVLDPRSVRRHIDGVDDFE FT QTLTGCTITSVVRRGKFLWMDLEGLETPTALVAHLGMSGQLLVEEPDAPDEKHLKVRLS FT LSQKSVFPRELRFVDQRIFGGMFLSPLVATADALPAGAGSIRATIPEAAAHIARDVMDP FT HRAPEDLYVSLRRRTTQLKRAILDQGIISGVGNIYADEALWQAGLSGLRNTATIRRPEV FT DRLNDALVDVMTRALAAGGTSFDSLYVNVNGASGYFARSLNAYGREGKACARCLENGRD FT SLIRRDPFMGRSSYSCPVCQPRPRKR" FT CDS complement(1676944..1677756) FT /transl_table=11 FT /locus_tag="AARI_14650" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF00144: beta-lactamase" FT /db_xref="InterPro:IPR001466" FT /db_xref="InterPro:IPR012338" FT /db_xref="UniProtKB/TrEMBL:E1VVN1" FT /protein_id="CBT75684.1" FT /translation="MSVLTQIDQWPSGHAVSVVVDVSGQIIDQHGDTQHAFPLASVTKL FT LSAYAFLVALEEEAISLDEPAGPEGSTVHHLLAHTAGYDFDSETIRFAVGTKRGYSNTG FT FDKLAEHLEAQTGISLPEYAQEAVFAPLGMNNTVIAGSCAKDGRSTAADLAKFAAELLN FT PTILAKETLADATRVHFENLAGILPGYGRQNPNDWGLGFEIRSTKSPHWTGASHPTDTF FT GHFGQSGTFLWVDPQHGLACVTLTDKNFGQWAVDAWAPFNEQVLQKHS" FT CDS 1677906..1681478 FT /transl_table=11 FT /gene="smc" FT /locus_tag="AARI_14660" FT /product="chromosome segregation protein Smc" FT /function="3.1 DNA replication" FT /note="identified by match to protein family TIGR02168. Smc FT participates in chromosomal partition during cell division. FT Component of a cohesin-like complex composed of scpA, scpB FT and smc" FT /db_xref="GOA:E1VVN2" FT /db_xref="InterPro:IPR003395" FT /db_xref="InterPro:IPR010935" FT /db_xref="InterPro:IPR011890" FT /db_xref="InterPro:IPR024704" FT /db_xref="UniProtKB/TrEMBL:E1VVN2" FT /protein_id="CBT75685.1" FT /translation="MHLKTLTVRGFKSFASATTFEFEPGVTAVVGPNGSGKSNVVDALS FT WVMGEQGAKTLRGGKMEDVIFAGTSGRAPLGRAHVSLTIDNTDGQLPIDYAEVTISRTL FT FRAGGSEYAINGSSCRLLDIQELLSDSGLGREMHVIVGQGQLDRILHATAEDRRGFIEE FT AAGVLKHRRRKEKTLRKLQAMQGNLDRLEDLSSEVRRQLAPLGRQAKIARRAKTVQLDV FT RDAKSRLLADDLVTLNNKLAQDIDDESRIQAQQDDANARLERGRKHLAELISKLELLSP FT RLGTVQEAWVSLSTQAERFRSLSALARERGKLLQSNETHFDSSRDPQRLEAQAERMSEE FT LEELEEALEDRHEILAEAVEAKEQAEEASRAEQQRMATMLRAAADRREGMSRLASQVAS FT ARSRVDVTRAEIGRLQENAQTFDSDVELDQRSYIQISADLETHMGAEAQLNSAFESAEN FT AFSVLDTAQRNDNQRERELSVRVSGLSARLEALKLNSKPNDQSAKLLESTSAQLMGRLG FT ELLTVRAGYEQAVASILRDNAEALVAENTSTALNLVAQLHSEQASAIFLHTDIQAPLNA FT MPVIPDAVFAREVVSAPAELDALLERLFSGQYIVEDLGQLQAILDQYPSAQLTTLEGIS FT VSAARSAVGDSASASLIAQQALVEQTTAELQSCREELGAIESQLAQRGPQLSIAQQARD FT EAAFALNESDATIEELSSYLARLGEKLRTTQASKQKLLLKLETLNEKFEIEQESLEEIT FT ERMELASTEQDDETVDDAGRAVLVDAAASARQQELEARLSLRSSEERAVALRSRIEGLR FT RTAAAERNHREVAARLAEQRKAQAANANRVEQAAERVLRFIEVSTSMASQERDELSVKK FT TELESMIGSQRTEAEQLSAELTRLADAVHRDEMARAELRMRIENLETKALEELGYTPDH FT LIAHFGPDQLIPEALDEDDKWGSLRQNVDEDGNPIGTKPYDRGEQEKRLKKAEKDLSAL FT GKVNPLALEEFAALEERHKFLSGQLEDLKKSRSDLQQIIVDVDSHVERVFTEAYEDTAV FT QFKRIFERLFPGGEGQLVLTDPGNMLATGIEVEARPAGKKIKRLSLLSGGERSLTAVAL FT LVAIFKARPSPFYVMDEVEAALDDMNLGRLITIFEELRESSQLIVITHQKKTMEVADAL FT YGVTMRGDGVSTVIGQKMDRAPAE" FT CDS complement(1681553..1682734) FT /transl_table=11 FT /locus_tag="AARI_14670" FT /product="putative multidrug efflux permease" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="drug:H+ antiporter-1 (12 Spanner) (DHA1) family FT transporter (TC 2.A.1.2.z). Match to PR01035 (Tetracycline FT resistance protein signature)" FT /db_xref="GOA:E1VVN3" FT /db_xref="InterPro:IPR001958" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VVN3" FT /protein_id="CBT75686.1" FT /translation="MLLVAAFIIALGFGLIAPILPQYAVSFNVGNAAATIIVSIFAFTR FT LIFAPVAGVLVGKLGEPKIYVTGVLLVAVSTLLCAVVQDYTQLLIARGLGGFGSTMFTI FT SAMALIARLAPDKSRGRISGLYAGSFLLGNVFGPVLGTLLAPLGMRIPFLIYGTALVIA FT AGVVYMALGRRRDLDSDAANPRTKHSDIEVVTTREALASPAYRAALFSGFSYGWLAFGV FT RNSMIPLFALAVFGQSMGATAAGISMTAFAIGNGCALVFSGRLTDSIGRKLPVIVGMSV FT LLLSIGAMGYSTSLVGFVVFSVLAGLGGGLLGPAQQATVADVIGSGRNGGKALAGFQMC FT TDLGSIIGPLFAGAMADLISFQLAFNISAIVGLVGVIAWLLVPKTIKPVTVND" FT CDS 1682962..1684143 FT /transl_table=11 FT /gene="ftsY" FT /locus_tag="AARI_14680" FT /product="signal recognition particle-docking protein FtsY" FT /function="1.6 Protein secretion" FT /note="identified by match to protein family TIGR00064. FT FtsY is a functional homolog of SRP receptor. Integral FT membrane proteins, are specifically recognized by a direct FT interaction between their noncleaved signal anchor FT sequences and the bacterial signal recognition particle FT (SRP) consisting of Ffh and 4.5S RNA. Recognition occurs FT during synthesis at the ribosome and leads to a FT cotranslational targeting to SecYE that is mediated by FtsY FT and the hydrolysis of GTP" FT /db_xref="GOA:E1VVN4" 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:E1VVN4" FT /protein_id="CBT75687.1" FT /translation="MTDLLITIIIAVAAVLIVAIGIIAFVAKGRKPKTPYTSERDLDDL FT PTGQSAEGDTDAAASEAGATDVAVAVEEPVAPAAPQLDVPEPVQSRLARLRARLTKSNN FT MFSKGLLALLSQDSIDEDVWEEIEENLLMADLGTEPALELVDALRERVKIEGSTDPARV FT KAMLREELLKLVDPTMDRSYLPAPHPDRPSIIMVVGVNGVGKTTTIGKLARVLVAEDKD FT VLLGAADTFRAAAAEQLATWGDRVGVPTVRSDIDGADPASVAFEAVSAGIDQEVDIVMI FT DTAGRLQNKVGLMDELGKIKRVVEKKAAIDEVLLVLDATTGQNGLQQAKVFSEVVNVSG FT IVLTKLDGTAKGGIVVAIQRQLGVPVKLVGLGEGPDDLAPFNAEDFVDALLEG" FT CDS complement(1684605..1685252) FT /transl_table=11 FT /locus_tag="AARI_14690" FT /product="putative 3-methyladenine DNA glycosylase" FT /function="3.3 DNA recombination, and repair" FT /EC_number="3.2.2.-" FT /note="3-methyladenine DNA glycosylase is a base excision- FT repair protein. It is responsible for the hydrolysis of the FT deoxyribose N-glycosidic bond, excising 3- methyladenine FT from damaged DNA" FT /db_xref="GOA:E1VVN5" FT /db_xref="InterPro:IPR003180" FT /db_xref="InterPro:IPR011034" FT /db_xref="UniProtKB/TrEMBL:E1VVN5" FT /protein_id="CBT75688.1" FT /translation="MDRSFFLPDAVDVAPQLLGAILEVDSPEGAVGVRITETEAYMGVG FT TAGRYDPGSHSKDRKTQRNASMFLEAGHAYVYFSYGMHFALNLVCSPADTASGVLVRAG FT QVVDGVALAAARRHAKRPQQEGASPLKEPQLARGPGNLATALGITREAHDGRDLFAAPF FT RIFRPEQPAQDIMAGPRVGVAGVAGGPEFPWRFWLPGEPSVSAFRPGRNAPR" FT CDS 1685591..1686811 FT /transl_table=11 FT /gene="amt" FT /locus_tag="AARI_14700" FT /product="ammonia transporter" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="involved in the uptake of ammonia. Ammonia channel FT transporter (Amt) family (TC 1.A.11.y.z). The generalized FT transport reactions catalyzed by members of the Amt family FT are suggested to be: NH4+ (out) <--> NH4+ (in)" FT /db_xref="GOA:E1VVN6" FT /db_xref="InterPro:IPR001905" FT /db_xref="InterPro:IPR024041" FT /db_xref="UniProtKB/TrEMBL:E1VVN6" FT /protein_id="CBT75689.1" FT /translation="MELDVANLWILIAAALVLLMTPALGLFYGGMTRATGVVNMMLMSF FT SAAAITAVVWVLWGYSFSAGEPAIAGIVGNPISDFAMHNTEQSELLAAGFAGTFAMISV FT AIISGAIADRARFAPWLFFVPLWVTLVYAPVAFWVWGGGLLSADGFLGSIFGEAIDFAG FT GAVVHTNAGIAALVLALKLGQRHNFHDRPQPHNTPLVMLGAGLLWFGWFGFNAGAATTV FT EQAGLIWVNTLAAPGAAVLGWILVEKLRGSRPSSLGVASGLVAGLVAITPSCADVAPWA FT AMLLGVLAGAGAAWAVNLKWKLGYDDSLDVVGVHLVAGLIGTLFLGFFALPTEESAGGL FT FYGGGVAQLIAQAATLIVVMVFSAVMTWVIATVIGKFSPWRVAADIEIAGIDEAEHNEN FT GYQLVSK" FT CDS 1687046..1689148 FT /transl_table=11 FT /locus_tag="AARI_14710" FT /product="catalase" FT /function="4.2 Detoxification" FT /EC_number="1.11.1.6" FT /note="decomposes hydrogen peroxide to molecular oxygen and FT water. Its main function is to protect cells from the toxic FT effects of hydrogen peroxide" FT /db_xref="GOA:E1VVN7" FT /db_xref="InterPro:IPR002226" FT /db_xref="InterPro:IPR010582" FT /db_xref="InterPro:IPR011614" FT /db_xref="InterPro:IPR018028" FT /db_xref="InterPro:IPR020835" FT /db_xref="InterPro:IPR024708" FT /db_xref="InterPro:IPR024712" FT /db_xref="UniProtKB/TrEMBL:E1VVN7" FT /protein_id="CBT75690.1" FT /translation="MASEPEQQASPGGEPVLSGPGQDSEFLTTNQGAPVSDTDHSLKAG FT ERGPTLLQDHHLREKIMHFDHERIPERVVHARGAGAHGSFISYGNASELCRADFLKPGK FT QTRVFVRFSTVVGSRGSMDTARDTRGFATKFYTEEGIFDLVGNNIPEFFIQDGIKFPDL FT VHAAKPHPDVEIPQAQSAHDTFWDFVSLHTPAQAHVMWQMSDRAIPRSLRMMEGFGVHT FT FRMVNEAGKASLVKFHWKPKLGVHSLAWEESQLAAGADPDFHRRDLAEAIDAGAYPEWE FT LGVQIFPDDGTAVFEGIDLLDPTKFVPEELAPVQPLGKMVLDRNPENYFAQTEQVAFHP FT GHLVPGIDISDDPLLQARLFSYLDTQLTRLGGPNFAQIPINAPVSPVNDMFRDGFHQHR FT VPKGIAPYKPNSLDGGCPYMSQVVSGQQPPLDFPQPVPESKKVRSEPASFSDHYSQARL FT FYISLSAVERAHVQQAYSFELGKCTDPVIRQRQVECLAKIDSQLAAGVAKALGLPQPAA FT MELADPIASPALSQIGKSWPVDGRKVGVVFNTGNHQHVPGIAQALAERGMSPLLVSASG FT GEVAPGLPIDRTYLTARSIEFDALVLIGPLPPAPDASVALDAKAGAAGAGGVPLDPRLA FT LLVTEAYRHNKAIITLEGLSDGLLQAVGLEDDAPGIELVQVDGVADSAQQLLSTHRAWE FT RFPVKD" FT CDS 1689246..1690376 FT /transl_table=11 FT /locus_tag="AARI_14720" FT /product="ribonuclease BN-like protein" FT /function="3.6 RNA modification" FT /note="identified by match to PF03631 (ribonuclease_BN, FT ribonuclease BN-like family): this family contains integral FT membrane proteins with 5 to 6 predicted transmembrane FT spans. The family includes ribonuclease BN, which is FT involved in tRNA maturation" FT /db_xref="GOA:E1VVN8" FT /db_xref="InterPro:IPR017039" FT /db_xref="UniProtKB/TrEMBL:E1VVN8" FT /protein_id="CBT75691.1" FT /translation="MTSESESHDGKGSAGATAAKARRAPAPDARSKPDSPPDMHPRSWK FT YAAGRSIREFSRKKCTDLAASLTYFAMLSIFPALLAVVSLLGVAGQAENMTRNILSLIQ FT ELASKEVVETLRQPIEQLASAPSAGLALVAGLLGALWSASGYVGAFGRAMNQIYEVYEG FT RPFYKLRPLMLALTLVLLVAVSVLGMLLIVSGPLAQAIGNVLGLGESAVAIWNIAKWPV FT IVLCAIVLVAVLYYGAPNVKQPKFRWVSLGSAIALLVLAVATVGFFFYVSNFGNYNKTY FT GAIGGVIVLLLWLWIANLSLLFGAVFDAEAERGRQLQAGIAAERSVQLPPRDIKASVKQ FT AEKEEQDISDGRALRFTSELQAEEQADPQPGRSPER" FT CDS 1690479..1690955 FT /transl_table=11 FT /locus_tag="AARI_14730" FT /product="FMN binding domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF01243: pyridoxamine 5- FT phosphate oxidase. This entry represents the FMN-binding FT domain present in pyridoxamine 5-phosphate oxidases, as FT well as in a number of proteins that have not been FT demonstrated to have enzymatic activity" FT /db_xref="GOA:E1VVN9" FT /db_xref="InterPro:IPR009002" FT /db_xref="InterPro:IPR011576" FT /db_xref="InterPro:IPR012349" FT /db_xref="UniProtKB/TrEMBL:E1VVN9" FT /protein_id="CBT75692.1" FT /translation="MANEEASKVIGIIKDLRIAMVSTHSAGKLASRPLTLIEASEQGEL FT WFFSTADSEIVHEIRAQGLVNAAFSGSKAWVSVSGQAQVVQDVAKKKELWNTAVETFAS FT EGPESAQTVLLRIDADSAEYWENPGGAASLVAGWVKQKLTGKPAEPGDSNTVEL" FT CDS complement(1691084..1691275) FT /transl_table=11 FT /locus_tag="AARI_14740" FT /product="putative CsbD-family protein" FT /function="4.1 Adaptation to atypical conditions" FT /note="identified by match to protein family PF05532. CsbD FT is a bacterial general stress response protein. Its FT expression is mediated by sigma-B, an alternative sigma FT factor. The role of CsbD in stress response is unclear" FT /db_xref="InterPro:IPR008462" FT /db_xref="UniProtKB/TrEMBL:E1VVP0" FT /protein_id="CBT75693.1" FT /translation="MGIGDKIQNKAQEASGKAKEAYGDATDNEKLQAEGMKDQAAAKAK FT QAGEHVKDAAKDVRDDLS" FT CDS complement(1691507..1693216) FT /transl_table=11 FT /locus_tag="AARI_14750" FT /product="putative EmrB/QacA subfamily drug resistance FT transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily, drug:H+ antiporter-2 FT (14 spanner) (DHA2) family (TC 2.A.1.3.z). Identified by FT match to protein family TIGR00711" FT /db_xref="GOA:E1VVP1" FT /db_xref="InterPro:IPR001411" FT /db_xref="InterPro:IPR004638" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VVP1" FT /protein_id="CBT75694.1" FT /translation="MTTSTSSRKTPADGPLVLTQRRIWIIFSALIAGMLLSSLDQTIVS FT TAMPTIVGQLGGVEHQAWITTAYLLATTIVMPIYGKFGDVLGRRNLFLIAIALFTLASV FT GAAFATSFWMFVVFRAMQGLGGGGLMILSQAIIADIVPASDRGKYMGPMGGIFGLAAVG FT GPLLGGYFVDHLTWQWAFYINIPVGIAAFAIAWFTLTLPSKKSQRKIDVFGVLLLSIAT FT TCLIFFTDFGGSANHGWSALETWAWGAGLVVAAMLFVLVEAKAEDPIIPLSLFKNKVFI FT NATAIGFTLGIGMFSAIAFVPTFLQMSSGTSAAVSGLLMLPMMVGMMGTSIYSGMAISK FT SGRYRGYPIAGTAITAVAMLAFTTLTAQTPLWLVCTYLFVLGAGMGLIMQVVVLVVQNA FT VAPEMVGTATSTNNYFREVGASLGVAIFGAMFTNRLSEKLMDVFSGAGASAADAGQATA FT TLDPETLSSLPQALQDGIVDAYASSLAPVFWYLIPFLVVAFALALLLKQVPLSDTAGMV FT ARGEAISGAEAEKIEKHQRLAATAPQGVQTQPEGSPVDAGDAVKAGTGDAAK" FT CDS complement(1693254..1693919) FT /transl_table=11 FT /locus_tag="AARI_14760" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="GOA:E1VVP2" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR015893" FT /db_xref="UniProtKB/TrEMBL:E1VVP2" FT /protein_id="CBT75695.1" FT /translation="MENSANKSDEPTASTPTLSGRMQKTRLSITRHCRDLTAEFGFNGF FT TIEQACERVGISRRTFFNYFPGKLDAVFGHGTEELPEGAIDRFMAARPEGIEGISPTLL FT ADLVALVLEQLSFDEKAIVSTHGFFAAARREPELLQHMVQSGPKKVAEFLERIASREGV FT EPDHPALPLVIHTLHFATIQAIERYVEGSGESSLGDLFLEHIAQGQQVLSQPLRRASE" FT CDS 1694274..1695335 FT /transl_table=11 FT /locus_tag="AARI_14770" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVP3" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR009075" FT /db_xref="InterPro:IPR009100" FT /db_xref="UniProtKB/TrEMBL:E1VVP3" FT /protein_id="CBT75696.1" FT /translation="MDQQPVSFSAANQRSGSKSAETWWNGEAAVRAAAVRCQGNPEAML FT RALQSAQGAPPAPAAGDTRRLWELLASVAATDLVAARTLEPHLDAAGILSQAGIGWEDG FT TTWGVFAAQSPTAKLEAARLPGGGWMLNGTKPWCSLAAQLSHALVTAGTPHGDRLFMLS FT LRQTGVEPATGCWVSRGMAQLPSGAVDFDAVPAQPVGEAGWYLTRPGFAVGGAGVAACW FT FGGAVGIYRHLLRSAQARTPDQLALAWLGEAERLLAGAAAILEHAAGLADAGQLDAIAA FT HQVRGQVAGACTRILQLSGQATGPGPLTADEEHARRAADLGIYLRQHHAARDDAALGQL FT VLDSAATAGRSPW" FT CDS 1695332..1696699 FT /transl_table=11 FT /locus_tag="AARI_14780" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF02585 and PF05401. FT Possibly involved in polysaccharide synthesis" FT /db_xref="GOA:E1VVP4" FT /db_xref="InterPro:IPR003737" FT /db_xref="InterPro:IPR008715" FT /db_xref="InterPro:IPR024078" FT /db_xref="UniProtKB/TrEMBL:E1VVP4" FT /protein_id="CBT75697.1" FT /translation="MSFTHREPGTCAARWQQAGLEQISALEPEKLFNATTSVIVLAAHP FT DDESLGAGGLISMALERGIKVHVIACSFGEASHPDSKTHTAAQLASLRKAELAQAMDRL FT QPQGTHAGKLHLHCLGLGDSQLETQQEQIRAALEQHAGEGCLIASTYRGDGHPDHEILG FT RIAAACAAAHGACHLEFPIWYWHWAQPGRQVGWKHWHRLALDAAGAKAKGRALEAHRSQ FT TLPLSDLPGDEVLLGAGFMQHFSQGAEIFRATWPGHKDAASAPATFDELYSQREDPWEY FT RSSRYEQRKQQILLASLPRVRYGAVLELGCSIGVQSAELARRCATLLAVDASATALAQA FT RDAVASMDHVTLLQATVPEQFPQLEPGSVELVVLSEIGYFLAADELDQVLADSADALAA FT GGELVLCHWLHPIEGWPLDGEAVHRMASGLGFERIVEHREADFLLEILRKPAGAHG" FT CDS 1696692..1697426 FT /transl_table=11 FT /locus_tag="AARI_14790" FT /product="putative family 2 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00535: glycosyl transferase family 2. FT This domain is found in a diverse family of glycosyl FT transferases that transfer the sugar from UDP-glucose, UDP- FT N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to a FT range of substrates including cellulose, dolichol phosphate FT and teichoic acids" FT /db_xref="GOA:E1VVP5" FT /db_xref="InterPro:IPR001173" FT /db_xref="UniProtKB/TrEMBL:E1VVP5" FT /protein_id="CBT75698.1" FT /translation="MGRGLAGMAVIIPAHDEQERLGCCLDSVRAAMDHLAGACPQVEAM FT AIVVADSCSDGTAQIARRHISEDPRISLQQVGYGNVGASRAAGARYALAGLGERMDPGS FT IWLASTDADTSVPENWLAGFAELHARGADAVVGTVQPDRGELDEDLFNLWQQAYHPVEG FT HGHIHGANFGVSAAAYLGVGGFEPLAAHEDVALVTSLRRAGYRVQATARMQVLTSGRLH FT GRLREGFADYLAGLDHQMLRAR" FT CDS complement(1697535..1697978) FT /transl_table=11 FT /locus_tag="AARI_14800" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VVP6" FT /protein_id="CBT75699.1" FT /translation="MPGRLVRSQTALRVAELLGSREGRRHLGNYGWTQGMPVVMTQPLE FT PLDDVMGLVSVHRRPVLVAMVETQTDELKFLHISEPSPVLEVVRPSAPRTKIKDLFDEA FT EQNGMTSFRVKYWQYSAVAHAVPAFNSELLAGKYAAQHPGSSS" FT CDS complement(1698304..1699731) FT /transl_table=11 FT /locus_tag="AARI_14810" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVP7" FT /db_xref="InterPro:IPR002937" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VVP7" FT /protein_id="CBT75700.1" FT /translation="MKTGKANIVGAGPNGLIAAAVLAEQGWDVQVFERNPHPGGAAASG FT STLGEGTIADLGAAAHPFAYGSRAFAHFDLAGHGLEWDFHDYPLAHPLDDADSVFLHQD FT LEATMEQFPSDARAWRLLHEPLVRNAQKILDNATSPLLGIPPHPILMARFGLRALPPAK FT VLGAAAFRTKQAAALFAGSSAHSMLPLSHPFTSGFGVLFGALGQSWGWPVARAGTGSII FT EALLRVLDDLGVQIHTGHQITSLAQLPEAQLTFLDLTPRQVLQLAGNQLPGNLRRRFER FT WRYGTAAYKVDYLLDGPIPWRDPRTSQAGTVHVIGDAARLAEAEHQVGSGRMPDRPFVM FT VVQPSSADASRAPAGQHVIWSYAHVPQGYGGDAGALIDAQIERFAPGFRDRIMHRVDTG FT PAQLQAWDPNLVGGDIGGGSLAGTQQFFRPTPSLNPYSLGVPGLYLCSSSTPPGGGVHG FT MAGWNAAHRALDDLRKN" FT CDS complement(1699728..1700258) FT /transl_table=11 FT /locus_tag="AARI_14820" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVP8" FT /protein_id="CBT75701.1" FT /translation="MPRTSIDQKTMHRYLSEHLLGSESGLNHFKAAHHTWADTAYAKRF FT ESLHQQVQADQDDLKRIMDQLGCTKRPMSRLLAPAAKLAGHVNPFNPLRMRKLAAAQVQ FT LDVLTGLLNAKLRMWQTMLLMLPHDPRLDQELLQDLSHRAESQISQLKALSDETWPERF FT APQVHHGRKEGRP" FT CDS complement(1700454..1701179) FT /transl_table=11 FT /locus_tag="AARI_14830" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVP9" FT /protein_id="CBT75702.1" FT /translation="MEKTALASTLARRTELAAAWAQDYLYAGAWQLRSMLPAASAKRLR FT TGGVSRLQPVVLIPGIWEPWKFMFPLAEVLRQAGHSVHVIPQLGYNRGSVPQMAEVVSD FT YLQQMQLEDAVLVAHSKGGLIGKYLMAASLQGYRVNKMIAISTPFSGSRYARYAPIRSL FT RSLSPNDLGLLKLSANLSVNAKIISIYSSFDPHIPGGCDLAGATNIKLPTLGHFRLLSD FT VRLHHAVLKHLAPPASLER" FT CDS 1701450..1703015 FT /transl_table=11 FT /gene="ffh" FT /locus_tag="AARI_14840" FT /product="signal recognition particle protein Ffh" FT /function="1.6 Protein secretion" FT /note="identified by match to protein family TIGR00959. FT Integral membrane proteins, are specifically recognized by FT a direct interaction between their noncleaved signal anchor FT sequences and the bacterial signal recognition particle FT (SRP) consisting of Ffh and 4.5S RNA. Recognition occurs FT during synthesis at the ribosome and leads to a FT cotranslational targeting to SecYE that is mediated by FtsY FT and the hydrolysis of GTP" FT /db_xref="GOA:E1VVQ0" FT /db_xref="InterPro:IPR000897" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR004125" FT /db_xref="InterPro:IPR004780" FT /db_xref="InterPro:IPR013822" FT /db_xref="UniProtKB/TrEMBL:E1VVQ0" FT /protein_id="CBT75703.1" FT /translation="MFNSLSDRLTATFKNLRGKGRLTEADIDGTAREIRRALLDADVAV FT PVVRGFVAQVKERALGAEVSESLNPGQQVVKIVNEELVGILGGETRRLNLAKNPPTVIM FT LAGLQGAGKTTLAGKLAKHLKAEGHTPMLVACDLQRPNAVKQLQINGERAGVPVYAPHP FT GVSSEFDTPTGDPVTVARDGVAEAKAKLHDIVIVDTAGRLGVDTEMMAQAANIRAAINP FT DEVLFVIDAMIGQDAVNTAQAFHEGVDFTGVVLSKLDGDARGGAALSVASVTGKPVMFA FT STGENLDDFEIFHPDRMASRILDMGDVMTLIEQAEKNWDKTEAERMAKKFADQEDFTLD FT DFLAQMAQIKKMGSMKKLLGMMPGAQISRQQLEQFDERQIDRVEAIVRSMTQHERVAPK FT IINGSRRARIAKGSGVSVSEVNQMLERFAEAQKMMKKMAAGGGIPGMPGAGKGAARKAK FT AKGKGKKQQKFGNPAKAAQAELEAKNKKAAAPTGASFGQGANQDFDPSSLNLPAGFEKY FT LGNK" FT CDS complement(1703369..1703851) FT /transl_table=11 FT /locus_tag="AARI_14850" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VVQ1" FT /protein_id="CBT75704.1" FT /translation="MPGRIVRTQTAIRVADFLATREGKAHLADYCWTPGMPIVMTQPAE FT SLNDAMGMVSIHGRAVLVAMLDPQTDELQLMHVTVPQPALQVAKPSSDRLTVGEFFDRL FT GTDLMIEFRMKFWKHTAVAHKIPACAAMQSQNTATARYSLPTKGVKPALATAASNR" FT CDS complement(1703983..1704432) FT /transl_table=11 FT /locus_tag="AARI_14860" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVQ2" FT /protein_id="CBT75705.1" FT /translation="MNKPLAVPLEKTTREAKAWQARIHKIAAFGSQQCQNKDTVHSAIC FT TITGSPDQLTVNLACTSKSEDSVSDLMQYANGTLLPQMEKDLGVRFEVRNLQFAVAGRE FT NLLASPEHADPAGLPKSWLDHPFTAEQASGPRMAVEDQPSILSMA" FT CDS 1704604..1705167 FT /transl_table=11 FT /locus_tag="AARI_14870" FT /product="putative MarR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01047. FT Regulators with the marR-type HTH domain are present in FT bacteria and archaea and control a variety of biological FT functions, including resistance to multiple antibiotics, FT household disinfectants, organic solvents, oxidative stress FT agents and regulation of the virulence factor synthesis in FT pathogens of humans and plants. Many of the marR-like FT regulators respond to aromatic compounds" FT /db_xref="GOA:E1VVQ3" FT /db_xref="InterPro:IPR000835" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VVQ3" FT /protein_id="CBT75706.1" FT /translation="MSSFRASGYWYDEGSSVPQAVDLLNLMRRYREAERSMRAQTRGSM FT GMNETDMSALRFLLAAHRKGKILRQRDFAEELCISNASVSALIDRLCRDGYADRVAHPA FT DRRSVGIVPTEYSDTEVRGTLHKMHERMIEAAGTLSESERLATAKFLNAMIRSVQITDE FT PGHSALRDSTMPQSTASSRQGHGT" FT CDS 1705394..1705669 FT /transl_table=11 FT /locus_tag="AARI_14880" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /db_xref="UniProtKB/TrEMBL:E1VVQ4" FT /protein_id="CBT75707.1" FT /translation="MPRKHIDVSVSHDEFEDLNNALEDHRDSFKQMAEEAIGGFGLEPE FT YWAGRAQEVERLRKTVHERSTEEREPQEGADPGSARGHDFESDSRE" FT CDS 1706002..1707195 FT /transl_table=11 FT /locus_tag="AARI_14890" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="match to the inorganic pyrophosphatase (PS00387) and FT Trp-Asp (WD) repeats (PS00678) signatures" FT /db_xref="UniProtKB/TrEMBL:E1VVQ5" FT /protein_id="CBT75708.1" FT /translation="MDSTEFNYLNLEFIFMGDKPEVAQLVRTALADRRLLGFIGGAVER FT ENSTQVTAEVATVSEARDAVLYRIDAKGKLREGSRVTKLVHELKNSTGASYVLVDGDEI FT DGPTPDDEVLGDFGSTNELLHGPKLKGSELVLAAGFADNEITVWDSASGLMAMLKEPVY FT APNISRSNRPFLSLTRMGNVISASIEAKGSRRDIFSSSLGIVLDLERTPILEPVAGSPA FT ALRLEELESLLYGYGEEDTELLEKLISDPAARAEAQQLLAHSADLKDLKRLLSLFGFDP FT RSVDYLTGRPLPEDRRVLATGNPIKTLRAALAEQEREAKGIERLLYRHSWNPKALIGSG FT IAVLASGLVAHQVLARSQKFEWLPKSARQVLMAAWYADGAFYLGKGIIDALKAKRSN" FT mobile_element 1707298..1708693 FT /mobile_element_type="insertion sequence:ISAar21" FT /rpt_family="IS4 group IS4" FT repeat_region 1707298..1707313 FT /rpt_type=INVERTED FT CDS 1707340..1708539 FT /transl_table=11 FT /locus_tag="AARI_35130" FT /product="transposase of ISAar21, IS4 family, IS4 group" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVQ6" FT /db_xref="InterPro:IPR002559" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR014736" FT /db_xref="InterPro:IPR024473" FT /db_xref="UniProtKB/TrEMBL:E1VVQ6" FT /protein_id="CBT75709.1" FT /translation="MARSGWMKPVEPTRLSDHVSLGVLAKVFPPSLVNEVVTKVGAGEQ FT RSRLLPAWMMVYYVMALALHAAASYEEVMRNLLGGLQWISHRTSEWSMPTKAAIFKART FT RLGAPVMIELFDQAAKPFGLQTPRGFLAGLRLVSVDGTTMDLADTPANERAYGRPGTNT FT EFKSAFPQARLLGLVECSTHAIIGAVTGPYTTAENDMYPGLHHKLDSSMLLMADRGFFS FT YRSFKDSAATGAQLLWRVRGNMVLPVHEEFEDGSYLSAVYEGTKERRNNVDPIRVRVVE FT YAVGDGEKTSEFRLLTTILDPGIASARELAEAYAKRWEIELCFKEMKTHQRGPSVVLRS FT KTPEGVLQEIYGYLCAHYALRTLIGEVAAEFDEDPLRISFTRTLRAARRSMATRPGFYP FT " FT repeat_region 1708678..1708693 FT /rpt_type=INVERTED FT repeat_region complement(1709188..1709195) FT /rpt_type=DIRECT FT mobile_element complement(1709196..1710644) FT /mobile_element_type="insertion sequence:ISAar19" FT /rpt_family="ISL3" FT repeat_region complement(1709196..1709219) FT /rpt_type=INVERTED FT CDS complement(1709202..1710509) FT /transl_table=11 FT /locus_tag="AARI_35140" FT /product="transposase of ISAar19, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VRG4" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VRG4" FT /protein_id="CBT75710.1" FT /translation="MLNPTFTAPDLTTFTNLDGLGLTAIGQHLSAAKAEILCHVTNPIP FT WCQTCGAAGIPRDTVTRRLAHEPLGWRPTVLVIKHRRYRCANCQRVWREELSQAVAPRQ FT KISRTGLRWALVGLVCHHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFDGVKV FT LGVDEHVWRHTRTGDKYVTVIVDLTAVRDGTGTARLIDMVPGRSKAVFKTWLADQEEQW FT KQGIEVVAMDGFTGFKTAAVEELPHAVEVLDPFHVVKLGSEALDQTRQRIQREQHGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKTKLEDLFKEPEYEPVQLVWSVYQKMVDAYRQPKP FT EVGRWALEQLINEVGTKVPKGLPELKKLGGTLRRRKTDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFKNLAHYIARSLLETGGFRRRLHPQS" FT repeat_region complement(1710621..1710644) FT /rpt_type=INVERTED FT repeat_region complement(1710645..1710652) FT /rpt_type=DIRECT FT CDS 1710732..1712102 FT /transl_table=11 FT /locus_tag="AARI_14900" FT /product="putative group 1 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00534: Glycosyl transferases group 1. FT Proteins containing this domain transfer UDP, ADP, GDP or FT CMP linked sugars to a variety of substrates, including FT glycogen, fructose-6-phosphate and lipopolysaccharides. The FT bacterial enzymes are involved in various biosynthetic FT processes that include exopolysaccharide biosynthesis, FT lipopolysaccharide core biosynthesis and the biosynthesis FT of the slime polysaccaride colanic acid" FT /db_xref="GOA:E1VVQ8" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VVQ8" FT /protein_id="CBT75711.1" FT /translation="MITWIIDEKFGGLTTACLQRASSFAKKDGKSNVVTFAYTQHLNST FT VERLRGIGLIASGVKVHNLYSDYASRVSHPPVKKLAAKAEGMKWSVEPVESQVNDAGIF FT KHVYAHTDDSASSRIIYSRPDGSKFMSDAKFVVGGESKREIAIFNGAGEVLKKFSSASS FT LYRHWLTEIVGYEESIAVFDSSFVASMMGPWRAPKTTKMFVFHSSHVVAGAEPETGPVV FT PKHQKIAANADNWDVFVFLTRQQADDFNARFGHESKSVVIPNIIKSSSLKKFSRRNDPR FT QIISVGSLDSRKQVDHAIRAVHELKELGVDCKLTIVGKGQKQQELQSLAKELGLSDRIE FT FAGHVDDVPRRLANSGILLFTSKLEGQGLVLLEAQFHGCVPISYDVRYGPASVIDSGVN FT GLLVGPNDIHALSSHVASLIDNPKEYKRLSKQAHSSAKRYARQDLTNLWIKAAKNAR" FT repeat_region 1712579..1712586 FT /rpt_type=DIRECT FT mobile_element 1712587..1714035 FT /mobile_element_type="insertion sequence:ISAar23" FT /rpt_family="ISL3" FT repeat_region 1712587..1712609 FT /rpt_type=INVERTED FT CDS 1712722..1714029 FT /transl_table=11 FT /locus_tag="AARI_35150" FT /product="transposase of ISAar23, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VS66" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VS66" FT /protein_id="CBT75712.1" FT /translation="MHHSIYTPANLTTFTNLDGLGLTAIGQRLTPKKAEILCQVTNPDP FT WCQTCGTPGNPRDTVTRRLAHEPFGWRPTVLVIKHRRYRCNHCQRVWREDLSQAVAPRQ FT KISRTGLRWALAGLVTQHLSVSRIAEGLGVTWNTANEAVLAEGQRLLIDDPTRFNGVKV FT LGVDEHVWRHTKSGDKYVTVIVDLTPVKAGTGTARLLDMIPGRSKAVFKTWLAERGEAW FT KNNVEVVAMDGFTGFKSAAAEELPQAVEVLDPFHVVKLGSEALDQARQRVQREQYGRRG FT RKDDPLYKCRRTLTTGLSLATEKQKQRVEDLFNVAKHEPVQLVWSVYQRMVDAYRQKKP FT EIGKWAMEQLINEIGTKVPKGLPELKKLGGTLRRRKPDILAYFDHIGSSNGPTEALNGR FT LEHLRGIALGFTNLTHYIARSLLETGGFRSRLHPES" FT repeat_region 1714013..1714035 FT /rpt_type=INVERTED FT repeat_region 1714036..1714043 FT /rpt_type=DIRECT FT gene 1714163..1715182 FT /pseudo FT /locus_tag="AARI_35160" FT /product="N terminal part of transposase of ISAar32, IS1380 FT family" FT /function="4.5 Transposon and IS" FT /note="disrupted by insertion of ISAar14, ISL3 family. FT First part of ISAar32" FT gene complement(1715153..1715464) FT /pseudo FT /locus_tag="AARI_35170" FT /product="N terminal part of transposase of ISAar14, ISL3 FT family" FT /function="4.5 Transposon and IS" FT /note="disrupted by insertion of ISAar14, ISL3 family" FT CDS 1715295..1715405 FT /transl_table=11 FT /locus_tag="AARI_14910" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVR0" FT /protein_id="CBT75713.1" FT /translation="MNTSNSRLHAVSVRNNDFASTIFVAFTDFSSTAHLD" FT repeat_region 1715458..1715465 FT /rpt_type=DIRECT FT mobile_element 1715466..1716881 FT /mobile_element_type="insertion sequence:ISAar14" FT /rpt_family="ISL3" FT repeat_region 1715466..1715489 FT /rpt_type=INVERTED FT CDS 1715572..1716849 FT /transl_table=11 FT /locus_tag="AARI_35180" FT /product="transposase of ISAar14, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVR1" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VVR1" FT /protein_id="CBT75714.1" FT /translation="MFKDTGGNDAASILLNLTDYRVIDATQEPAGRQVLIEPKATEAAC FT PTCGVITTRIHARPVHRVKDLPTGGNDIKVLVRKRRMACQETACERRSFVQTTEQLPLR FT ARITTRLSQKLVDEMSCELRAVSRVASAYQVSWPTVMARLNFEGELAGDIDRMFIGRLG FT IDEHRFRKVRYARGSSGKVVRIEPWSIVFTDLDTGKILDIVDGRRGAAVKKWLKSRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKISVDHFHVIARANLMITQVRRRRSHEVHERR FT GRVADPAYKYRKLLTCNLENLSIKQVERLKLILEADPELGVIYGIKEHVRELLKTRDIH FT DFQSRWAVLEKSVKATKMVEAKSLFRTLTAWRRELLVFIRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRVRILLYTAGLRPC" FT gene complement(1716820..1717854) FT /pseudo FT /locus_tag="AARI_35190" FT /product="C-terminal part of transposase of ISAar14, ISL3 FT family" FT /function="4.5 Transposon and IS" FT /note="disrupted by insertion of ISAar14, ISL3 family. FT First part of ISAar14. (AA 1-331)" FT repeat_region 1716858..1716881 FT /rpt_type=INVERTED FT repeat_region 1716882..1716889 FT /rpt_type=DIRECT FT gene 1718007..1718447 FT /pseudo FT /locus_tag="AARI_35200" FT /product="C-terminal part of transposase of ISAar32, IS1380 FT family" FT /function="4.5 Transposon and IS" FT /note="disrupted by insertion of ISAar14, ISL3 family. FT Second part of ISAar32" FT mobile_element 1718635..1720030 FT /mobile_element_type="insertion sequence:ISAar21" FT /rpt_family="IS4 group IS4" FT repeat_region 1718635..1718650 FT /rpt_type=INVERTED FT CDS 1718677..1719876 FT /transl_table=11 FT /locus_tag="AARI_35210" FT /product="transposase of ISAar21, IS4 family, IS4 group" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VVQ6" FT /db_xref="InterPro:IPR002559" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR014736" FT /db_xref="InterPro:IPR024473" FT /db_xref="UniProtKB/TrEMBL:E1VVQ6" FT /protein_id="CBT75715.1" FT /translation="MARSGWMKPVEPTRLSDHVSLGVLAKVFPPSLVNEVVTKVGAGEQ FT RSRLLPAWMMVYYVMALALHAAASYEEVMRNLLGGLQWISHRTSEWSMPTKAAIFKART FT RLGAPVMIELFDQAAKPFGLQTPRGFLAGLRLVSVDGTTMDLADTPANERAYGRPGTNT FT EFKSAFPQARLLGLVECSTHAIIGAVTGPYTTAENDMYPGLHHKLDSSMLLMADRGFFS FT YRSFKDSAATGAQLLWRVRGNMVLPVHEEFEDGSYLSAVYEGTKERRNNVDPIRVRVVE FT YAVGDGEKTSEFRLLTTILDPGIASARELAEAYAKRWEIELCFKEMKTHQRGPSVVLRS FT KTPEGVLQEIYGYLCAHYALRTLIGEVAAEFDEDPLRISFTRTLRAARRSMATRPGFYP FT " FT repeat_region 1720015..1720030 FT /rpt_type=INVERTED FT CDS complement(1720034..1721746) FT /transl_table=11 FT /locus_tag="AARI_14920" FT /product="putative fatty-acid--Co-A ligase" FT /function="2.4 Metabolism of lipids" FT /EC_number="6.2.1.-" FT /note="match to protein family PF00501. This family of FT enzymes includes luciferase, long chain fatty acid Co-A FT ligase, acetyl-CoA synthetase and various other closely- FT related synthetases" FT /db_xref="GOA:E1VVR3" FT /db_xref="InterPro:IPR000873" FT /db_xref="InterPro:IPR020845" FT /db_xref="UniProtKB/TrEMBL:E1VVR3" FT /protein_id="CBT75716.1" FT /translation="MSNTDKFRAARDLLLAARDDYDRARAEFTWPEFTDFNFAYDWFDA FT VAKDPKRADQPALILTEPDGSTARYSWAQLSHRSTQVARWLSDEGLQRGDTIILMLGNE FT VALWELMLAGMKLAAVIIPSTTQLVSADLADRIERGNANWVITSHEHVAKFDTVPGDYR FT IVQVRGEATEHTLDYAKSFDAPAEFSLQSPTLADENMLLYFTSGTTSLAKLVQHTHTSY FT TIGHLATMFWIGLEPGDVHLNVASPGWGKHAWSNFFGPWIAEATVFVYNYDRFDPLALM FT NQMDTENVTSFCAPPTVWRYLIQADLSALKTPPRKLVSAGEPLNAEVIDQVRTAWGQVI FT RDGYGQTETTVQIANSPGTEVKVGAMGRPMPGYVVELRNPTTGELAEVGEICLRLDPKP FT AGLMKGYFADPQKTEEALRGGVYHTGDIAERDEEGVLTYVGRADDVFKSSDYKLSPFEL FT ESVVLEHPAVAEVAVVPSPDPLKLSVPKAFVVLAANVEPSAAVAKDILGFCREQLAPYK FT RIRRLEFSQLPKTISGKIRRVELRLAEEEQQAKGAKPSGEYRDTDFPELKSLG" FT CDS complement(1721984..1723690) FT /transl_table=11 FT /locus_tag="AARI_14930" FT /product="putative fatty-acid--Co-A ligase" FT /function="2.4 Metabolism of lipids" FT /EC_number="6.2.1.-" FT /note="match to protein family PF00501. This family of FT enzymes includes luciferase, long chain fatty acid Co-A FT ligase, acetyl-CoA synthetase and various other closely- FT related synthetases" FT /db_xref="GOA:E1VVR4" FT /db_xref="InterPro:IPR000873" FT /db_xref="UniProtKB/TrEMBL:E1VVR4" FT /protein_id="CBT75717.1" FT /translation="MSVTEEFRAARDRLLELREDYTRARAEFTWPEFSEFNFGFDWFDH FT VAKDPQRRDQPALIIAELDGSSTQRTWAQLSRRSTQIARWLSDQGVKRGDSIAIMLGNQ FT VELWESMLAGIKLGAVLVPCTTQLTPTDLRDRIERGHIQWVITNESEIPKFESVPGTYT FT LIQIGGQPAPGILDYAQSAHAEAEFSLDSPTRADETLLRYFTSGTTSKAKLVEHTHTSY FT PVGHLSTMFWIGLEPGDIHLNVASPGWAKHAWSNFFTPWIAEATVFIYNYKRFDPAALM FT NQMDARHVTSFCAPPTVWRLLIQADLSELKNPPQKLVSAGEPLNAEVIDQVNKAWGQVI FT RDGFGQTETTVQIANPPGEQITIGAMGRPMPGYEIVLRDPATGEEGDLGEICLVTAQRP FT LGLMKRYFENEEKTNEVFRDGVYHTGDIAERDERGVLTYVGRADDVFKSSDYKISPFEL FT ESVLIEHPGVAEAAVVPAPDELRLTVPKAYIVASGGYEPGPELAESILAYCREHLSAFK FT RVRRIEFADLPKTISGKIRRVELRQAEEQRHGGSAPAGTEYKDTDFPNLMN" FT CDS complement(1723893..1724960) FT /transl_table=11 FT /locus_tag="AARI_14940" FT /product="putative thermonuclease" FT /function="3 Information pathways" FT /EC_number="3.1.31.1" FT /note="thermonuclease catalyzes the hydrolysis of both DNA FT and RNA at the 5-position of the phosphodiester" FT /db_xref="GOA:E1VVR5" FT /db_xref="InterPro:IPR002071" FT /db_xref="InterPro:IPR006021" FT /db_xref="InterPro:IPR016071" FT /db_xref="UniProtKB/TrEMBL:E1VVR5" FT /protein_id="CBT75718.1" FT /translation="MKKSSAWISIALTGSLITGGAVYATTYKSDKHGVITRVIDGDTVD FT MTIAGTQTRVRLLNIDTPETVDPSKAVECLGPEASEHLESLLQPGDKVELQYDVEREDR FT YGRTLAAVYKDDEFINRSIAAAGLGIAVKYEPNTKFYDEVLAGQLEAEAQTSGLFSPEV FT SCAIPSQVGNALTELDQVPSEAATTVEEAESMAADAAAAAAAGLLVSKSLKSLTPDTHP FT VTYALLAKKFPNALSKLDSSVQKAQDLEGQHSERHRELVKEGKERKKKEAEAKAKREAE FT KKAKREAQEAAERQAAQQAAERRATERRAAERRSTPQPRTTTPRRIEPKRPSVPKNYTG FT PRCYAPGGKTWKPCG" FT CDS complement(1725216..1726274) FT /transl_table=11 FT /locus_tag="AARI_14950" FT /product="putative thermonuclease" FT /function="3 Information pathways" FT /EC_number="3.1.31.1" FT /note="thermonuclease catalyzes the hydrolysis of both DNA FT and RNA at the 5-position of the phosphodiester" FT /db_xref="GOA:E1VVR6" FT /db_xref="InterPro:IPR006021" FT /db_xref="InterPro:IPR016071" FT /db_xref="UniProtKB/TrEMBL:E1VVR6" FT /protein_id="CBT75719.1" FT /translation="MTKKAIGVSLLVAGAMAVGATAFTSSSASEHRGTVIPVIDGDTVD FT IMVSGAKTRSQLLNVATPQTKQPQRSAECLGPEAAEFLERTLPAGQKVTLEHDAQRTDH FT EGQTLAVVYKADQLINSEIAAQGFGIAIKFDPNTKFHEQVSQAQREAESAERGLFSTKI FT ACTIPAQINDAMKAMHSVPVELGQTVEQADARAQQAAAGRAAADALQAQDRKEQLVSAA FT LAEDSLAPALEDLAETIEQTADLEIQHEQQVATPSKKVNAGRKAAGKQSPTQLPEESKA FT EEPRPKKSHTNSPRKSKKQSQPENQPKRVNPNRKPVNDNPLEQKPSREHLGSRVNPRAN FT CEAPNGQSSKNC" FT CDS 1726482..1727351 FT /transl_table=11 FT /locus_tag="AARI_14960" FT /product="putative ring-cleavage extradiol dioxygenase" FT /function="2 Intermediary metabolism" FT /db_xref="GOA:E1VVR7" FT /db_xref="InterPro:IPR004360" FT /db_xref="InterPro:IPR018146" FT /db_xref="UniProtKB/TrEMBL:E1VVR7" FT /protein_id="CBT75720.1" FT /translation="MTLLQQDKLAATTHMNAVQLKVGDMKTMSEYYQKALGLEILDESA FT AGIRLGRGTQELVNLRNAPGLKVPSRNEAGLFHTALLFDTKADLAATVLSAAQFDQTRF FT VGSSDHLVSEAFYFTDPEGNGIELYWDRPRDTWNWNDGQVAMDTVYLDPNQFLNTHLTE FT RAIAQQRNAAADVGHVHLQVGNVATARKFYVDTLGFDETTTLGEQALFVSAGGYHHHMA FT MNVWNSAGAGPRKDTLGLGEVLINVPSEEEVGKLAERLNFAKVGNHHTGAELRFKDPWN FT NELRVAVG" FT CDS complement(1727459..1728232) FT /transl_table=11 FT /locus_tag="AARI_14970" FT /product="putative transferase" FT /function="1.1 Cell wall" FT /note="match to PF00132: Bacterial transferase hexapeptide FT repeat. A number of different transferase protein families FT contain this repeat, such as galactoside acetyltransferase- FT like proteins, the gamma-class of carbonic anhydrases, and FT tetrahydrodipicolinate-N-succinlytransferases" FT /db_xref="GOA:E1VVR8" FT /db_xref="InterPro:IPR001451" FT /db_xref="InterPro:IPR011004" FT /db_xref="InterPro:IPR018357" FT /db_xref="UniProtKB/TrEMBL:E1VVR8" FT /protein_id="CBT75721.1" FT /translation="MRIQMSQLRPLLISHRILMTVPGMEDFEKTGTNYDPDAWISYEPD FT LALDPYTTFWGTSGTALPRMGAFSYTHSKLNKTITVGRFTSIAKGMKVMGAKHPLEWAS FT TSPVFYNQRLLMQTYSADHGVELNAADFSYKPGNISIGNDVWIGEKVTLGHGATIGDGA FT VIASNSVVSKDVPAYTVVGGLPAKKIRDRFETEVVQALQSSQWWQYAPKDLTHLDVANP FT AIFAQQVIGQAAAGNLQPFQTQPLTAKHIAEHLQA" FT CDS complement(1728312..1730120) FT /transl_table=11 FT /locus_tag="AARI_14980" FT /product="putative group 1 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00534: Glycosyl transferases group 1. FT Proteins containing this domain transfer UDP, ADP, GDP or FT CMP linked sugars to a variety of substrates, including FT glycogen, fructose-6-phosphate and lipopolysaccharides. The FT bacterial enzymes are involved in various biosynthetic FT processes that include exopolysaccharide biosynthesis, FT lipopolysaccharide core biosynthesis and the biosynthesis FT of the slime polysaccaride colanic acid" FT /db_xref="GOA:E1VVR9" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VVR9" FT /protein_id="CBT75722.1" FT /translation="MDSTQQHLNAYMVTWKLEREFGGMTTVCIQRAAAFAERYGSAAVV FT TFPPSPQLDQIAAELVQRGKLSPKVHVLNPYAFLAEHELDPQASIPEPASEPEHQDFTG FT TEQVYLPGDNGTLFCEHSTAGPDEQITRMTYYRGDGTVFLTDTSFEDTKPRRIVEAFDR FT SGILVARFPSAAAFYRHWLTQIVDHPDSLVVVDSKFTAKLLASWTPIHVPKIFAFHSVH FT VAKGQDLASGHLSKGHGPIIAERSTWDGFVFLTRAQRKAYVDRFGETDSTFVIPNPLNA FT PAVQPPVPQRSPLNLIAAGSLTPNKNVAAALEVIAELVRRGKQPTLHIVGEGNQSEALV FT QKVDELELGAHVVFHGYSDQLPRHFASCTAQLFTSTNEGQALVILEAQAQGCIPVSFDI FT NFGPSDSIIDGHNGFLVPHGDIQAMADRVQSLMDDPILAAELSENARTFASEYQSRDLV FT SRWEETLSLTKMLKNLGAKNRVPHFEAKLRGVDFLDGQRLHVRVEHQAQLEDLPEPAIF FT ELVFINRRSTEEIASVAASSVDEQLAAFDLEPSLLGETQEQDAAVDMNLRLRIGKAMQL FT KRLGLPESKILPYFTKHKNLSFNRRG" FT gene complement(1730401..1730586) FT /pseudo FT /locus_tag="AARI_14990" FT /product="truncated protein" FT /note="section of a conserved protein" FT gene complement(1730602..1730820) FT /pseudo FT /locus_tag="AARI_15000" FT /product="truncated protein" FT /note="section of a conserved protein" FT CDS 1730973..1731101 FT /transl_table=11 FT /locus_tag="AARI_15010" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVS0" FT /protein_id="CBT75723.1" FT /translation="MSSKSPRKGEAKKPGKSIKEKRAEKRLKHAESVIEPVRKTAR" FT CDS complement(1731224..1732234) FT /transl_table=11 FT /locus_tag="AARI_15020" FT /product="iron-siderophore ABC transporter, FT substrate-binding protein" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, binding protein (BP), ISVH- FT family (iron siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VVS1" FT /db_xref="InterPro:IPR002491" FT /db_xref="UniProtKB/TrEMBL:E1VVS1" FT /protein_id="CBT75724.1" FT /translation="MQSPRILALTAALAAASLALASCASSAPSTEPAPSAGTSAQEDAN FT FPASIKHFRGTTELAQRPLRVAALDPSYVDATILLGAELVAYTEYRKGTNPFPEYLGDT FT SKFTDEAVNVGTITEPDLEKLLAAEPDVIISADVRQGAMYDQLNKIAPTIFSESTGPTW FT KENVVLLGEALGKKEAAEEAVASYEARAAAVGKEILETKPETTYSLLRFAGEDTARLYA FT TDSFIGEIMVDMKIPRPKDAPDTTESIFVPLSPEEILKADAEVIFQSTWAPEGAEGDAS FT RAQEQKFTSNPLWEKLEGEVMQVDDSVFLSSVSLQGANEVITQVAEHFEVDAQLP" FT CDS 1732446..1733435 FT /transl_table=11 FT /locus_tag="AARI_15030" FT /product="iron-siderophore ABC transporter, inner membrane FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, permease (IM), ISVH-family (iron FT siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VVS2" FT /db_xref="InterPro:IPR000522" FT /db_xref="UniProtKB/TrEMBL:E1VVS2" FT /protein_id="CBT75725.1" FT /translation="MTPRISSLLILAAGVGAAIGISLWIGSTTSSFAELRHALLAPDGQ FT VSDIAIREIRWPRTVTALAAGAALGMAGTLIQGHTRNPIAEPGLLGINQGAALAIVSVV FT AFTGPLPAWTQALLALGGALAAALLVFGIGRIDGRGGSPITLLLVGAAVTALCAGVVSA FT IVLLSEAALETLRFWQVGSVVQGYESFLSLWPLLVAGTVLALANARGLNALTLGEDSAR FT SLGITALHARSLGLAAIVALSGLAVTLAGPIAFLGLLVPHISRRIFGADYRWIIPGSAL FT CGALLLCVADVLGRMLARPGELPVGVVIAMLGAPFFIYVARRRKAVTV" FT CDS 1733432..1734487 FT /transl_table=11 FT /locus_tag="AARI_15040" FT /product="iron-siderophore ABC transporter, inner membrane FT subunit" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, iron FT chelate uptake transporter (FeCT) family (TC 3.A.1.14.z). FT ABCISSE: ABC transporter, permease (IM), ISVH-family (iron FT siderophores, vitamin B12 and hemin)" FT /db_xref="GOA:E1VVS3" FT /db_xref="InterPro:IPR000522" FT /db_xref="UniProtKB/TrEMBL:E1VVS3" FT /protein_id="CBT75726.1" FT /translation="MSTQMMHPSASALRAKRTLATGVLLLTVAFAAFCVHLAIGGTPIP FT VGDVVATLFGAAPDARTELAILEFRLPRSVAAVLAGAGFGVAGALTQNVARNPLASPDV FT LGVTNGAALGAVSVLAIGVHTGGRSELLVHYGLPIAATLGGLMVSTLVFALVWRSSLES FT NRLVLVGLGFSGLCAALTSWMLTLGEIYNAQQALTWLAGTVNAISWADLAIAPAIIVPG FT LILAMLLRNQREVLALDSDTSRALGMNLGRDRVLMLALASLLAIAATVIAGPLAFVALA FT SGHAARLVARGTIPPVPHAALIGAIFVLLADLVAARAFPVILPAGVATAVIGAPYLIFL FT VIRQSKVRQRG" FT CDS 1734552..1736279 FT /transl_table=11 FT /locus_tag="AARI_15050" FT /product="HNH endonuclease domain-containing protein" FT /function="3 Information pathways" FT /note="identified by match to PF01844" FT /db_xref="GOA:E1VVS4" FT /db_xref="InterPro:IPR003615" FT /db_xref="InterPro:IPR003870" FT /db_xref="UniProtKB/TrEMBL:E1VVS4" FT /protein_id="CBT75727.1" FT /translation="MSIHQLVAASQTLREALTGSLPRAAAQMLLELMASCCALLVKLSV FT SLREIDDPRVAAAHARLVETIYRYTLREQLHSAIHLESTGAHMLEDEELVAVAESRSSF FT AVGARQHSGRAHYQNTGEFLATWLGLNSHEGQNRVRDAHLLIARRLMDGSTIAPRMNQL FT ATLYTQAPALDPRLVARVARALDKFEPADTCFQGQPLEPTASNEQGQLLEHLAAELLQE FT PDRATRESKLAALLATQRKARKKTRNPEPGIYPRGTVGDCDKYELYVAGTQREEFRSTL FT AQADNPRTNAGKAARSGESSDGVDMDYGAEESGSQGEAQPGQNAGDPAVDELFSSKEPP FT PPWAREDRGTFFGQQSAEEPEAEQPAHGAGEANPSRNLDSSLLGDGEVPVAQRRLNALM FT AALRRRSTGKAANGITPKIGMLIQLSDLQDLREASKLRATTGHGLNLDSVDTAQLICQG FT EIYRVVFGPDGQPLDVGRKERFFTDAMKRAIFARDRGCIVPGCTAPPEMIEYHHDNWWE FT RGGCTSVRNGSCLCRRHHHAIHAGLIGLVTVGGLAHIMLPKHLDPLQIPRRNSVPVAA" FT CDS complement(1736325..1736954) FT /transl_table=11 FT /locus_tag="AARI_15060" FT /product="RHBT family amino acid transporter" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="resistance to homoserine/threonine (RhtB) family FT protein (TC 2.A.76.y.z). The family includes homoserine, FT threonine and leucine efflux proteins. The transport FT reaction presumably catalyzed by members of the RhtB family FT is: amino acid (in) + nH+ (out) <--> amino acid (out) + nH+ FT (in)" FT /db_xref="GOA:E1VVS5" FT /db_xref="InterPro:IPR001123" FT /db_xref="UniProtKB/TrEMBL:E1VVS5" FT /protein_id="CBT75728.1" FT /translation="MTVPSAFLAFGVVAALMTLIPGVDTALILRSAITRGRGEAMLAAL FT GICTGVFVWGVAAAAGASAILAASNLAYQVLTYAGAAYLVFLGGQMIYRSLQKKRSPAA FT RIPMPQSSYRTYLTGLVTNVLNPKIGVFYIAAIPQFTPAGTNALLMGMGLSAVHVALTL FT VWAVALVYGVRIAGRWLGSAKSVSWMDRITGTVLIGFGLKVALSRP" FT CDS 1737205..1737615 FT /transl_table=11 FT /gene="rpsP" FT /locus_tag="AARI_15070" FT /product="30S ribosomal protein S16" FT /function="3.7.1 Ribosomal proteins" FT /db_xref="GOA:E1VVS6" FT /db_xref="InterPro:IPR000307" FT /db_xref="InterPro:IPR020592" FT /db_xref="InterPro:IPR023803" FT /db_xref="UniProtKB/TrEMBL:E1VVS6" FT /protein_id="CBT75729.1" FT /translation="MAVKIRLKRFGKMRAPFYRVVVMDSRAKRDGRAIEEIGKYHPTEN FT PSVIEINSDRAQYWLSVGAQPTEQVHALLKITGDWQKFKGIDGQEGTYKVAEPKPAFVA FT PDKGSVILPEAITKKAEKPAAEEAEAEATEAE" FT CDS 1737618..1737860 FT /transl_table=11 FT /locus_tag="AARI_15080" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVS7" FT /db_xref="InterPro:IPR004088" FT /db_xref="InterPro:IPR009019" FT /db_xref="InterPro:IPR020627" FT /db_xref="UniProtKB/TrEMBL:E1VVS7" FT /protein_id="CBT75730.1" FT /translation="MLVDALDHLVRGVVEEPEDVKVALKSTRRGDLLEVRVNPEDLGRV FT IGRQGRTARALRTVLAALAKEPVRVDVIDTDRRRG" FT CDS 1738015..1738557 FT /transl_table=11 FT /gene="rimM" FT /locus_tag="AARI_15090" FT /product="16S rRNA-processing protein RimM" FT /function="3.6 RNA modification" FT /note="essential for efficient processing of 16S rRNA. It FT is needed in a step prior to rbfA during the maturation of FT 16S rRNA" FT /db_xref="GOA:E1VVS8" FT /db_xref="InterPro:IPR002676" FT /db_xref="InterPro:IPR009000" FT /db_xref="InterPro:IPR011033" FT /db_xref="InterPro:IPR011961" FT /db_xref="UniProtKB/TrEMBL:E1VVS8" FT /protein_id="CBT75731.1" FT /translation="MRLQVARIGKPHGIRGEVTAQVMTDTPDERFTSGEELIVVDGPVK FT TLTVKSARWNKTILLLSFKEINDRNQAETLRGARLEIDVSEEPEDDSDEWYEHELLDLK FT VMLDGEQVGVITALRTNPAQDLLVFENSEGQEIYLPFVDEFVPEIDPEAGIVVITPPAG FT LLTLNSEESENDEEGSK" FT CDS 1738561..1739385 FT /transl_table=11 FT /gene="trmD" FT /locus_tag="AARI_15100" FT /product="tRNA (guanine-N(1)-)-methyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.31" FT /note="specifically methylates guanosine-37 in various FT tRNAs" FT /db_xref="GOA:E1VVS9" FT /db_xref="InterPro:IPR002649" FT /db_xref="InterPro:IPR016009" FT /db_xref="InterPro:IPR023148" FT /db_xref="UniProtKB/TrEMBL:E1VVS9" FT /protein_id="CBT75732.1" FT /translation="MRLDVISIFPEYLQPLSLSLIGRAAEDGILDLNVTNLRDFATDKH FT RKVDDTPYGGGAGMVMMPEPWGQALDSVRPANAAGAKPTLIVPSPAGTVFNQRMAYELA FT EEEHLVFACGRYEGIDERVIEYAHENFNVIPVSIGDYVLNGGEVAVMVMVEAIARLIPG FT VIGNPESLVEESHSDVLLEYPVYTKPASWRGRDVPEVLLGGNHQRVGRFRRDEQIKRTA FT VRRPDLITQLDAESLNRRDRDALWHSGFALVDGEITPKSKLDWATGAGTEKD" FT CDS 1739636..1739995 FT /transl_table=11 FT /gene="rplS" FT /locus_tag="AARI_15110" FT /product="50S ribosomal protein L19" FT /function="3.7.1 Ribosomal proteins" FT /note="this protein is located at the 30S-50S ribosomal FT subunit interface and may play a role in the structure and FT function of the aminoacyl-tRNA binding site" FT /db_xref="GOA:E1VVT0" FT /db_xref="InterPro:IPR001857" FT /db_xref="InterPro:IPR008991" FT /db_xref="InterPro:IPR018257" FT /db_xref="UniProtKB/TrEMBL:E1VVT0" FT /protein_id="CBT75733.1" FT /translation="MHILDSVDSASLRSDVPAFGAGDTLKVHVNIIEGKNSRVQVFQGY FT VLGRQGRGVGETFTVRKVSFGTGVERTFPVHSPIIDKIEVVSKGDVRRAKLYYMRDRHG FT KAARIREKRDFGAKK" FT CDS 1740009..1740656 FT /transl_table=11 FT /gene="lepB" FT /locus_tag="AARI_15120" FT /product="putative signal peptidase I" FT /function="1.6 Protein secretion" FT /EC_number="3.4.21.89" FT /note="signal peptidases remove the signal peptides from FT secretory proteins. In prokaryotes three types of signal FT peptidases are known: type I (gene lepB) which is FT responsible for the processing of the majority of exported FT pre-proteins; type II (gene lsp) which only process FT lipoproteins, and a third type involved in the processing FT of pili subunits" FT /db_xref="GOA:E1VVT1" FT /db_xref="InterPro:IPR000223" FT /db_xref="InterPro:IPR011056" FT /db_xref="InterPro:IPR015927" FT /db_xref="InterPro:IPR019533" FT /db_xref="InterPro:IPR019756" FT /db_xref="InterPro:IPR019758" FT /db_xref="InterPro:IPR019759" FT /db_xref="UniProtKB/TrEMBL:E1VVT1" FT /protein_id="CBT75734.1" FT /translation="MNQIARTERATSKRRAFSWVWRFAVLAIILGLLATILIRATVMDV FT FHIESNSMESTLNPGQSIAVDRRAYAESAPQRGDVIVFDGRGSFLPYAKASFADDLLNA FT FSLTGSNNKYVKRVIGVGGDTIECCSADGRLLVNGEPIDEPYIFAGDAPSEQKFSVAVP FT ENRLWVMGDHRSTSKDSRALLGASGGGMISIDRVTGKATHVVWPLDQRSEIE" FT CDS 1741080..1743521 FT /transl_table=11 FT /locus_tag="AARI_15130" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVT2" FT /db_xref="InterPro:IPR001254" FT /db_xref="InterPro:IPR009003" FT /db_xref="InterPro:IPR018114" FT /db_xref="InterPro:IPR019931" FT /db_xref="UniProtKB/TrEMBL:E1VVT2" FT /protein_id="CBT75735.1" FT /translation="MPHPKKKTAQRGIVAAAATALVVGSSFMPALAAPTASESPSAPAT FT ADDNVSDTSGSVDTTGLAEAIERDLGETPEEYLAEAKVSAKASDIKTALREAKIDSNVV FT VKDGVVVVQVGKGDLSASKKVIAEVEAAETTVAGEEVVQATATATAEAAEESVPAAVAP FT TEATKKAEKVEKKSVEPSATEKATESAAVEFETEEVSSIDEVLKKLKKTASPEALKELT FT SVTIDEHGQVIVRAGEASKTKSSEASESASKSNHPELSLTEAIERLDGAKLKLSKDGGP FT ATPAALEDVYGGMGYATTADGDYSGSFGICSVGLNAWNAEGEDAVITAGHCTTDGSMKD FT VNILEHDAINKPSAIGIDLGTFGFSQFGTAGNGGHPWNPEEAGDWEIGTDIAVIDAINP FT AANLHPAVTKWPAGVDEREATINITSAGAGVVGQSACNSGRTTGWQCSELLEEGVFFVG FT GYDENGEQTDQSVRTVWGYTGANPEGNTLLPGDSGGSVVQGTRAIGVNSAYGAGVALYT FT SLVDAQAKTPVKDYAVKLFISAPQITADNGTEVEAGDAITGTVANAADGTKVDIIVEGK FT VIDTVTVKAGKFSFTAPEELGEFSFTVQAKNGFDKSATTNANVVVIAAPTPTSTPTEEP FT TEEPTSTPTEEPTEEPTSTPTEEPTEEPTSTPTEEPTEEPTSTPTEEPTAEPTSTPTEE FT PTAEPTEEPTAEPTEEPTAEPTEEPTAEPSESTSPSPSEDETEKPSTSPSATEDDKSEA FT PKDQKDDEPTKSVTPKENPKDDDALADTGSNSVPLIAAGGAMALAGAAFLLFRRSARRQ FT G" FT CDS 1743695..1744282 FT /transl_table=11 FT /locus_tag="AARI_15140" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.703 FT between position 44 and 45" FT /db_xref="UniProtKB/TrEMBL:E1VVT3" FT /protein_id="CBT75736.1" FT /translation="MNFQFRTSRTPMVLASSATIAALMLTGCGQEPAPGAQTSTSAEAS FT ESAQQSDNTNGSTVDQDELLQINDQLSETLGDEYVQGWVKDGQLNVSTTNEKQLDAIEA FT AGAVGHLVQFSNEELRSAIQEIMKWQGKQENPVRSAIHAYTLNPETGGITLSVDKSQLE FT EVQKLIEADQPVGDIPVDYKSSGGIMTPAATQ" FT CDS 1744429..1745154 FT /transl_table=11 FT /locus_tag="AARI_15150" FT /product="signal peptidase I-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="non-secretory protein prediction by SignalP 3.0 HMM" FT /db_xref="GOA:E1VVT4" FT /db_xref="InterPro:IPR000223" FT /db_xref="InterPro:IPR011056" FT /db_xref="InterPro:IPR015927" FT /db_xref="InterPro:IPR019758" FT /db_xref="InterPro:IPR019759" FT /db_xref="UniProtKB/TrEMBL:E1VVT4" FT /protein_id="CBT75737.1" FT /translation="MEGTNRIVSAASAENPQSRGPLYKIWRFVREIVIIIAIALLLSFV FT IKTFFFRAYYIPSGSMEHTLEVDDRIFANLMVPGPFELERGDVVVFRDDQQWLPPLTEY FT PTAFQNVLSFVGVLPAADEQYLVKRIIGMPGDTVECCTAEGAITINGEPIDEPYIYDGD FT SPSDMEFKVTVPEGKLWVMGDHRGASADSRFHADRQGGFVDIESVQGRASVISWPTSRW FT GTIDSHEEVFANVPHAVAK" FT CDS 1745166..1745891 FT /transl_table=11 FT /gene="rnhB" FT /locus_tag="AARI_15160" FT /product="ribonuclease HII" FT /function="3.1 DNA replication" FT /EC_number="3.1.26.4" FT /note="recognizes and cleaves the RNA strand of RNA-DNA FT heteroduplexes" FT /db_xref="GOA:E1VVT5" FT /db_xref="InterPro:IPR001352" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR022898" FT /db_xref="InterPro:IPR024567" FT /db_xref="UniProtKB/TrEMBL:E1VVT5" FT /protein_id="CBT75738.1" FT /translation="MADSKSKATTLEHERALAAKHGVRYIAAVDEVGRGALAGPITVGM FT TVIDIQQVTEFPALRDSKLLSPDTRMALVDPVRQWAVGYGVGHASATEIDELGVTGALR FT LAGSRAMVQCAIQPEAALLDGSYDWLTAPEPDLFDILADDREPVGLRIPVATIVKGDMT FT CQAIAGASILAKVERDVIMVGLATEHPDFGWEINKGYATAAHRAAIVAQGPCDYHRKSW FT NLTSGADQAQGEATTKKAK" FT CDS 1745891..1746211 FT /transl_table=11 FT /locus_tag="AARI_15170" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR019592" FT /db_xref="UniProtKB/TrEMBL:E1VVT6" FT /protein_id="CBT75739.1" FT /translation="MAADDLENYESDMELQLYREYKTVAGLFNYVVETERRFYLANQVD FT VKTLSNAGEVYFELNLTDAWVWDIYRQGRFVKSVKVLTFKDVNVEELNRDELQIPKEGL FT DS" FT CDS complement(1746307..1747200) FT /transl_table=11 FT /locus_tag="AARI_15180" FT /product="osmoprotectant (glycine FT betaine/carnitine/choline/L-proline) ABC transporter, FT substrate-binding protein" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT quaternary amine uptake transporter (QAT) family (TC 3.A.1. FT 12.z). ABCISSE: ABC transporter, binding protein (BP), FT OTCN-family (osmoprotectants, taurine, cyanate and FT nitrate). Part of an uptake system of osmoprotrectants such FT as glycine betaine, carnitine, choline, proline betaine and FT L-proline" FT /db_xref="GOA:E1VVT7" FT /db_xref="InterPro:IPR007210" FT /db_xref="UniProtKB/TrEMBL:E1VVT7" FT /protein_id="CBT75740.1" FT /translation="MNRTIMKFGALAATAALGLTACSSSDAGGEGDAQASKEVTIAVFN FT GWDEGIATSELWKAVLEDKGYDVNLEYSDVAPLFSGLASGDYDLTTDVWLPVTHKDYLD FT KFGTDIEDLGAWNDESKLTVAVNKDAPIDSLEDLAANADKFNNKIVGIEAGAGLTRTME FT ESVIPDYGLEDMDFVTSSTSAMLTELKTATDAGENIVVTLWEPHWAYSSFPVKNLEDPK FT GSLGNTESIHNYSRAGFAKDFPEVADWMGGFKLSLDELYTLEKLLFVDNDTDDYEPLVR FT QWMEEHADIVERMTAS" FT CDS complement(1747309..1748205) FT /transl_table=11 FT /locus_tag="AARI_15190" FT /product="osmoprotectant (glycine FT betaine/carnitine/choline/L-proline) ABC transporter, inner FT membrane subunit" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT quaternary amine uptake transporter (QAT) family (TC 3.A.1. FT 12.z). ABCISSE: ABC transporter, permease (IM), OTCN- FT family (osmoprotectants, taurine, cyanate and nitrate). FT Part of an uptake system of osmoprotrectants such as FT glycine betaine, carnitine, choline, proline betaine and L- FT proline" FT /db_xref="GOA:E1VVT8" FT /db_xref="InterPro:IPR000515" FT /db_xref="UniProtKB/TrEMBL:E1VVT8" FT /protein_id="CBT75741.1" FT /translation="MDNFRIPIGDVSEDAIDWIIANLDGFFSVLRTIFIEMYDGLYLVL FT STPSFAVVTILIGLIALLARGWQFMLGAVLGLLVIVGVDQWENAMSTLALVIVAAFWAL FT LIALPLGIWAAKSDGFSQVVRPVLDFLQTMPAFVYLIPALMLFRVGVAPGIVATIIFAL FT APGVRFTELGIRSVDSEVVEAGQAFGSSPGRILRQIQLPLALPTIMAGVNQVIMLSLSM FT VVIAGMVGAGGLGGDVISSLSRLDTALGVEAGLAVVILAMILDRLTNAFGRQSGLFALF FT AKKRKAARTAREQQLAA" FT CDS complement(1748205..1749473) FT /transl_table=11 FT /locus_tag="AARI_15200" FT /product="osmoprotectant (glycine FT betaine/carnitine/choline/L-proline) ABC transporter, FT ATP-binding subunit" FT /function="1.2.5 Transport/binding of amino-acids" FT /EC_number="3.6.3.-" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT quaternary amine uptake transporter (QAT) family (TC 3.A.1. FT 12.z). ABCISSE: ABC transporter, ATP-binding protein (ABC), FT OTCN-family (osmoprotectants, taurine, cyanate and FT nitrate). Part of an uptake system of osmoprotrectants such FT as glycine betaine, carnitine, choline, proline betaine and FT L-proline" FT /db_xref="GOA:E1VVT9" FT /db_xref="InterPro:IPR000644" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005892" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VVT9" FT /protein_id="CBT75742.1" FT /translation="MTTNIALKVEGLYKVFGRKPKDAVKQLESGTPREKLPSGNTAAVI FT DASFEVKTGEIFVVMGLSGSGKSTLIRTLNGLWEASAGTVSLGEDIITGMQPAKLRAVR FT RKRVSMVFQHFALLPHRSVLENVAYPLEQQGVGRAERLATAAKTLKLVGLDGWGEKMPS FT ELSGGMQQRVGIARALSADTEILLMDEAFSALDPLIRREMQEQLVELQATLGKTIVFIT FT HDLNEAMFLGDRIAVMRDGRIVQIGTPEEILTDPANDYVEQFVQDVDRARVLTAASVMV FT PGRSVIQENAGPRAALRQMRDAVASAAIVTGRDRKVLGMITDRDALKLVRRGESSLSSK FT ISALSTVDADTALIDLFVPSVESPLPVTVTDAENRLLGVIPRVTLLAALASTTPQTEEI FT SVLDSPLPSDIVDAVLQIEPEKN" FT CDS complement(1749948..1751225) FT /transl_table=11 FT /locus_tag="AARI_35220" FT /product="transposase of ISAar13, ISL3 family" FT /function="4.5 Transposon and IS" FT /db_xref="GOA:E1VSI7" FT /db_xref="InterPro:IPR002560" FT /db_xref="UniProtKB/TrEMBL:E1VSI7" FT /protein_id="CBT75743.1" FT /translation="MFKDTGGNDAASILLNLTDYRVIDATQEPAGRQVLIEPKATEAAC FT PTCGVITTRIHARPVHRVKDLPTGGNDIKVLVRKRRMACQETACERRSFVQTTEQLPLR FT ARITTRLSQKLVDEMSCELRAVSRVASAYQVSWPTVMARANMVGELVGNVDRMFIRRLG FT IDEHRFRKVRYARGRTGKVVRIEPWSIVFTDLDTGKILDIVDGRRCAAVKKWLKSRPRY FT WRQRVQYVAIDMSAEFRKAVRENLPKAKISVDHFHVIQRANLMITQVRRRRSHEVLQRR FT GRAADPAYKYRKLLTCNLENLSIRQVERLKLILEADPELGVIYGIKEHVRELLKTRDIH FT DFQSRWAVLEKSVKTTKMVEAKSLFRTLTAWRRELLVFIRTRLTNARSEAANLTAKNLK FT RIGRGYRNHGHYRVRILLYTAGLRPC" FT CDS 1751494..1751856 FT /transl_table=11 FT /locus_tag="AARI_15210" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVU1" FT /db_xref="InterPro:IPR003509" FT /db_xref="InterPro:IPR011335" FT /db_xref="InterPro:IPR011856" FT /db_xref="UniProtKB/TrEMBL:E1VVU1" FT /protein_id="CBT75744.1" FT /translation="MRTASQRLGAAGELAAARFLRENNYEVLDRNWRCQAGELDLVARA FT GNGQLVAIEVKTRSSQRFGTGFDAINAAKYHRLQKLLIFWAQAHRMFMPQLRVDVVEVY FT PTAGGFECQLHQDVRS" FT CDS 1751853..1753406 FT /transl_table=11 FT /locus_tag="AARI_15220" FT /product="Mg chelatase-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family TIGR00368" FT /db_xref="GOA:E1VVU2" FT /db_xref="InterPro:IPR000523" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR004482" FT /db_xref="InterPro:IPR020568" FT /db_xref="UniProtKB/TrEMBL:E1VVU2" FT /protein_id="CBT75745.1" FT /translation="MSTARTSAVALHGVSASLVEVEADLGNGIPGFTILGLPDASLNEA FT RERIKAAARNTGIPLANRKLTVNLSPATLPKYGSGFDLAILVAALAADHQLLASPSTLY FT LAELGLDGTLRAVPGVLPAVQLAKEHGLDRVIVAEANGNEARLVEGIEVKSARHLGQVL FT EFCGAQKELITMHLHHPGPAVAPAQSTLASTSHDEADLQLVNGQQEARLALELAAAGGH FT HLIMVGPAGAGKTMLAKCLPTIIPPLDDSQALEATAVHSITSGAMHEVNQLQRTPPFVA FT PHHTSSLSALIGGGTAQLIPGAITRAHHGILFLDEAAQFNTGVLDALRQPIEEGYINLA FT RARSHQRLPARFQLILASNPCPCGRNFGTGTGCTCTPMARRRYFARLSGPILDRVDLQV FT RVNPVHQSQLLSTAQNESSAIVRERVRTTRERSQERLRPFSISCNAQIPTQILRHDLRY FT PAKTKAALEQLAARRGLSARGIHRLLRVAWTVADQQQHTAPTEDDLAVAAHLRQSLENS FT " FT CDS 1753415..1754659 FT /transl_table=11 FT /locus_tag="AARI_15230" FT /product="putative smf family protein" FT /function="3 Information pathways" FT /note="the SMF family (DNA processing chain A, dprA) are a FT group of bacterial proteins. In Helicobacter pylori, dprA FT is required for natural chromosomal and plasmid FT transformation" FT /db_xref="GOA:E1VVU3" FT /db_xref="InterPro:IPR003488" FT /db_xref="UniProtKB/TrEMBL:E1VVU3" FT /protein_id="CBT75746.1" FT /translation="MSINLNPVPVGDRTNQERLTYAHLNQLIEPNDYTASALLELMSPQ FT ELLALIRRADFVPWGLKPQVDDILGVKTTSNMAQDLKSALTRWRKRLPLSNPVAALDTA FT ARHNGGLLIPTDTMWPIQLDDLNLGRPLCLWWRASDPQLLAGAQVAKNVAIVGSRDASD FT YGDQVTFDLGRALATHGYTIVSGGAYGIDASAHRAALTVEDWAYSNPPTITVMAGGIDR FT LYPSGNSNLLNQIVARGVLLSEVPPGTTSARFRFLNRNRIIAALSRLVIVTEARHRSGA FT LNTASHAVELGREVAAVPGSVFAPNSAGCHRLIAEGSAALLASPQDALALVGADRSTQA FT SRVDQVPRRPTDQLGRDEGMVYDVMSFSKSLLVDEISARSGVPMIQTLQAVARLEALGL FT ASTDGLSWKLVYQGN" FT CDS 1754679..1755683 FT /transl_table=11 FT /gene="xerC" FT /locus_tag="AARI_15240" FT /product="tyrosine recombinase subunit XerC" FT /function="3.3 DNA recombination, and repair" FT /note="site-specific tyrosine recombinase, which acts by FT catalyzing the cutting and rejoining of the recombining DNA FT molecules. The XerC-XerD complex is essential to convert FT dimers of the bacterial chromosome into monomers to permit FT their segregation at cell division. It also contributes to FT the segregational stability of plasmids" FT /db_xref="GOA:E1VVU4" 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:E1VVU4" FT /protein_id="CBT75747.1" FT /translation="MVMKHDPVSKHSTGPSAKFSEPVADYLEYLQRERGRSENTLRAYD FT VDLRNLGQFLNEHAGDPALKQISVQMLRDWLAYLHESEVSRTTLARRISAVKNFFAWAL FT KNHLVENDPALRLAAPKKERRLPHILQPSQIDRLLSEHAGLTEENEAARQKGDGTDQDP FT KARAIQCRDRVIAELLYASGLRISELVALDISDIDFERRTLRVLGKGNKERMVPFGKPA FT ERVIIEWIRSYRRVVAAEQAEDALLVGVRGSRLNVRQAREVIASALRSLGDTSASGPHA FT LRHTVATHLLDGGADLRAVQEFLGHASLATTQLYTHVSVDRLRQSYRQAHPRA" FT CDS 1755826..1756329 FT /transl_table=11 FT /locus_tag="AARI_15250" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021491" FT /db_xref="UniProtKB/TrEMBL:E1VVU5" FT /protein_id="CBT75748.1" FT /translation="MSTPMTRGVIFVHSAPAALCPHLEWAIGAVLGTPVKMDWTEQHVA FT PGFCRAEIEWVGPQGTGALLTSEMHGWQHLRFEITEDPSPGADGSRWSVTPDLGIFHAT FT VDVAGNIMVGEERIRWAYEKGDGNPSIFYQEMSIALGEAWDEELEPFRHSGDEAPVRWL FT NQVV" FT CDS 1756624..1757004 FT /transl_table=11 FT /locus_tag="AARI_15260" FT /product="putative ring-cleavage extradiol dioxygenase" FT /function="2 Intermediary metabolism" FT /note="match to PS00082 extradiol ring-cleavage FT dioxygenases signature" FT /db_xref="GOA:E1VVU6" FT /db_xref="UniProtKB/TrEMBL:E1VVU6" FT /protein_id="CBT75749.1" FT /translation="MTAQFNHTIIASTDPQRMAEFYTDLLEAKPAPSWGPFCNISLDGG FT VLLQFATAPIDFPPQHYAFLLNEAHFDRAYQKICATEHEHWADPQRQHPGAINHEHGGR FT GVYLLDPSGHYLELITKEYIPR" FT CDS complement(1757007..1757582) FT /transl_table=11 FT /locus_tag="AARI_15270" FT /product="RibD domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF01872. This domain is FT found in the C-terminus of the bifunctional deaminase- FT reductase in combination with PF00383 as well as in FT isolation in some archaebacterial proteins" FT /db_xref="GOA:E1VVU7" FT /db_xref="InterPro:IPR002734" FT /db_xref="InterPro:IPR024072" FT /db_xref="UniProtKB/TrEMBL:E1VVU7" FT /protein_id="CBT75750.1" FT /translation="MRTLIATAFVSLDGVVEAPGGEPEYRNSGWTMNSVEFDPAAYELK FT GTEQAEASAMLLGRISYQAFSPIWPSMTEEFPHYNAMPKYVLSTTLAEKDPVDNWGETT FT ILRSISDVARLRAGEGGPISIHGSATLVRSLQEHQLIDRYNLLVFPVLLGAGKRLFSQE FT SMDAQKLKLVDSQTYSNGIQKNVFDVVR" FT CDS complement(1757774..1759021) FT /transl_table=11 FT /locus_tag="AARI_15280" FT /product="3-oxoacyl-[acyl-carrier-protein] synthase 2" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.3.1.41" FT /note="catalyzes the condensation reaction of fatty acid FT synthesis by the addition to an acyl acceptor of two FT carbons from malonyl-ACP" FT /db_xref="GOA:E1VVU8" 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="InterPro:IPR017568" FT /db_xref="InterPro:IPR018201" FT /db_xref="UniProtKB/TrEMBL:E1VVU8" FT /protein_id="CBT75751.1" FT /translation="MARKVVITGLGATTPIGGDVPTLWENALKGVSGAVTLEDDWVKEY FT DLPVTFAARAAVQPTEVLTRPETKRMDPSTQFAVVAAREAWADSGLVKEEMDQNKLAVA FT FATGIGGVWTLLNAWDTLREKGPRRVLPMTVPMLMPNGPAAAVSLDLGAAGGAHTPVSA FT CASGTEAMHVGLELIRSGKADVVMVGGAEAAIHPMPMAAFASMHALSRRNDDPTKASRP FT YDVDRDGFVMGEGAGALVLEAEEHAIARGARIYAELAGSSVTSDAHHITAPDPEGTGAT FT RALKAAMFDGRIQPEDVVHVNAHATSTPVGDKPEYAALKNALGDHLDNVWVSATKSQMG FT HLLGASGAVESVLCALAIYNRKAPVTINLDNQDPEIPLKVVTGEPAQLPAEGTIVALNN FT SFGFGGHNAVVAIRSV" FT CDS complement(1759142..1759387) FT /transl_table=11 FT /gene="acpP" FT /locus_tag="AARI_15290" FT /product="acyl carrier protein" FT /function="2.4 Metabolism of lipids" FT /note="also named fatty acid synthase acyl carrier protein. FT Carrier of the growing fatty acid chain in fatty acid FT biosynthesis" FT /db_xref="GOA:E1VVU9" FT /db_xref="InterPro:IPR003231" FT /db_xref="InterPro:IPR006163" FT /db_xref="InterPro:IPR009081" FT /db_xref="UniProtKB/TrEMBL:E1VVU9" FT /protein_id="CBT75752.1" FT /translation="MASNEEILAGLAEIVNSETGLDEADVQLDKSFTEDLDIDSISMMT FT IVVEAEEKFEVKIPDEEVKNLKTVGDAVTFIAGAQA" FT CDS complement(1759610..1760533) FT /transl_table=11 FT /gene="fabD" FT /locus_tag="AARI_15300" FT /product="malonyl CoA-acyl carrier protein transacylase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.3.1.39" FT /note="involved in the initiation of fatty-acid FT biosynthesis in bacteria" FT /db_xref="GOA:E1VVV0" FT /db_xref="InterPro:IPR001227" FT /db_xref="InterPro:IPR014043" FT /db_xref="InterPro:IPR016035" FT /db_xref="InterPro:IPR016036" FT /db_xref="UniProtKB/TrEMBL:E1VVV0" FT /protein_id="CBT75753.1" FT /translation="MLAIVCPGQGSQTPGFLTEWLNVDGVAEHLQALSSITERDLTAHG FT TTSDEETIKDTAVAQPLIVAAGLITARALFGQQLPANVIVAGHSVGEITASALAGALDE FT ADAMNFVKVRANAMAEAAAATPTGMAAVLGGDPEEVLAKLEELGLTPANANGGGQTVAA FT GTLEQLAALGENPPAKARVIPLKVAGAFHTAHMQPAVGTLQELANTLIAKDPAATLLSN FT FDGQAVANGQANLDSLVAQVSRPVRWDLCMESLAAAGVTGVLELAPAGTLVGLARRGLK FT GVKTLAVKSPADLEAAQAFIAEHTAS" FT CDS complement(1760710..1761921) FT /transl_table=11 FT /locus_tag="AARI_15310" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVV1" FT /protein_id="CBT75754.1" FT /translation="MSPEMDAAAAPKNRPSQSPAPSSATLKRLKNHIGVLSTTALKYLD FT QQLPWYRSLAPNERAALGLIAQKGISTFVSWYEDPSSTPSWVVTDVFGAAPTELTRSIS FT LQKALGLLRTIVEVVESQVPDIAPEAEQAALREAVLRYSREVAFAAADVYARAAETRGA FT WDSRLEAHVVDAVLHGEAHDSLASRIAAIGWKSQKNIRILVGTTPSSNAATFVSALRRM FT AIRYSRDSLVGVLGDRSVLMLSDTKFDEADLSRLTRFFGPGPVVYSPLAPTVKEMHQAA FT ASAVAGFSAAKAWPQAPNPIGADDLWPERACNGDELARTALIEQVYRPLQQASNGLAET FT LSSYLALGHSLEGTARELFVHANTVRYRLKRVSEVTGWDPLVPRDAFVLQTALLFGRLH FT ESNL" FT CDS complement(1762055..1764829) FT /transl_table=11 FT /gene="aceE" FT /locus_tag="AARI_15320" FT /product="pyruvate dehydrogenase E1 component subunit FT alpha" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.2.4.1" FT /note="the pyruvate dehydrogenase complex catalyzes the FT overall conversion of pyruvate to acetyl-CoA and CO2. It FT contains multiple copies of three enzymatic components: FT pyruvate dehydrogenase (E1), dihydrolipoamide FT acetyltransferase (E2) and lipoamide dehydrogenase (E3)" FT /db_xref="GOA:E1VVV2" FT /db_xref="InterPro:IPR004660" FT /db_xref="InterPro:IPR005474" FT /db_xref="InterPro:IPR009014" FT /db_xref="InterPro:IPR015941" FT /db_xref="UniProtKB/TrEMBL:E1VVV2" FT /protein_id="CBT75755.1" FT /translation="MEPQFNQGASVAVEEHISQIRSGLTYQLSDRDPEETQEWMDSFDS FT LVESQGTERAQFIIRSLLQRAGAKSVGVPHVTTTDYVNTIPVDQEPEFPGDEAIERRYR FT AFMRWNAAIMVHRAQNPAIGVGGHISTYAGAATLYEVGFNHFFRGKNHPGGGDQIFFQG FT HASPGMYARAFLEGRLSEEDMDGFRQEKSKEGHALPSYPHPRSLPDFWEFPTVSMGIGP FT ANAIYQAQLNRYLQNRGIKDTSDQQVWAFLGDGEMDEPESRGFLQLAANEKLDNLNFVI FT NCNLQRLDGPVRGNGKIMQELEAFFRGAGWNVIKVAWGREWDALLEADKTNALVDVMNQ FT TPDGDYQTYKAESGAFVREHFFGQRPETKELVADMTDDEIWNLKRGGHDYHKVYAAYKA FT AAEFKGKPTVILAKTVKGYGLGSHFEARNATHQMKKLTMEDLKKFRDHLRIPITDEQLE FT ADLYTPPYYRPSEDSAEYKYMMERRAALGGSVPTRRQEASKKLSLPGDKTYAIAKRGSG FT KQQAATTMAFVRLLKDLMRDKEFGHRIVPIVPDESRTFGMDSFFPTAKIYNPGGQNYLS FT VDRDLVLAYKESPQGQLIHPGINEAGAVAAFTAAGTSYSTHDEPLIPIYVFYSMFGFQR FT TGDQFWAAGDQMTRGFIIGATAGRTTLTGEGLQHADGHSPILASTNPAVITYDPAYGYE FT IGHIMRSGLERMYGGNHADPNVMYYLTVYNEPISQPAEPENVDVEGIIKGIHLLKEATT FT DGPRAQLLASGVAVPWALEAQAILADEWGVSADVWSVTSWNELARDGQRADAEVLVDPS FT KARRTPYVTSKLESTPGPVIATTDYMRAVPEQLRPYVPGEFHTLGADGFGFSDTRAAAR FT RFFKIDAHSLVVQTLQSLVERGEIPADTAVKAHAKYDLNNPNAGQSGNAGGDA" FT CDS 1765162..1765578 FT /transl_table=11 FT /locus_tag="AARI_15330" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR021412" FT /db_xref="UniProtKB/TrEMBL:E1VVV3" FT /protein_id="CBT75756.1" FT /translation="MSDAVSANLEPAKKLGFANEDLIQELGYDDDVDYDLRDSIEDLIG FT SELLTEEDHDVVDAVIFWWRDGDGDLVDALMDSLNCLDENGIIWLLTPKQGREGHVSPA FT LIQQEAPTAGLHVTTSEGVSEDWSAIRLAPRKKN" FT CDS 1765578..1766030 FT /transl_table=11 FT /locus_tag="AARI_15340" FT /product="putative thiol-specific antioxidant protein" FT /function="4.2 Detoxification" FT /note="thiol-specific antioxidant proteins confer a FT protective role in cells through their peroxidase activity FT in which hydrogen peroxide, peroxynitrate, and organic FT hydroperoxides are reduced and detoxified using reducing FT equivalents derived from either thioredoxin, glutathione, FT trypanothione and AhpF" FT /db_xref="GOA:E1VVV4" FT /db_xref="InterPro:IPR000866" FT /db_xref="InterPro:IPR012336" FT /db_xref="UniProtKB/TrEMBL:E1VVV4" FT /protein_id="CBT75757.1" FT /translation="MIQTGSRLFDFSLENQYGETITSTGLSSGRVLVVFYPWAFSRVCG FT SELATLQEHYEFFARHQVRIVAISVDHKFTLRNYAQSLGLDFELLADFWPHGAVAQQAD FT AFDRDRGVAARLSLYLVDGEVRDIFRSEMTQPRSIDDYKAAVERGV" FT tRNA 1766146..1766221 FT /locus_tag="AARI_36800" FT /product="transfer RNA-Val" FT /anticodon=(pos:1766179..1766181,aa:Val) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(1766464..1766721) FT /transl_table=11 FT /locus_tag="AARI_15350" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVV5" FT /protein_id="CBT75758.1" FT /translation="MNKRFAAAGLALCPLISSCTPGTIPSKAPARACAEEHEAPKSSGL FT AGSRKQSNSMSDLTHQETVVEDGVIIIRWAMDDGGAKSLH" FT tRNA 1766914..1766989 FT /locus_tag="AARI_36810" FT /product="transfer RNA-Val" FT /anticodon=(pos:1766947..1766949,aa:Val) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 1767101..1767709 FT /transl_table=11 FT /locus_tag="AARI_15360" FT /product="SAM-dependent methyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.1.1.-" FT /note="identified by match to protein domain PF08241" FT /db_xref="GOA:E1VVV6" FT /db_xref="UniProtKB/TrEMBL:E1VVV6" FT /protein_id="CBT75759.1" FT /translation="MTAPEENLWLATVRKNPDHSPNFAQRWRTLAAEGQDIFGEARTVD FT AMVARGSRILDAGCGTGRIGGWLSEQGHQVVGVDLDPHLIDVARVDYPKAQWQVGNLAD FT FTIAGAAGERQEFDLIVSAGNVVTFLSESERLPALQQLREQLAADGRMIIGFGSGRGYA FT FDDFEADAREAGLALQQRYSTWNFHLPADDFLVAVLGRK" FT CDS 1767969..1768631 FT /transl_table=11 FT /locus_tag="AARI_15370" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="5 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VVV7" FT /protein_id="CBT75760.1" FT /translation="MENGNSNEIDPARILRGIESDAQQAREGMSPNQQLLFSIWGVAWI FT IAFLGLYFALAPQGAPLLPAAVGIGTAVASFLIAIVISAVHSAKRGSGTRGPSMAQGAI FT YGNTFSLGMIITALLGWRLHAEGLSSMGMATFALAGLCLVIGVLVVAGSVLFNDRTQLI FT CGAWILAIALLSLAAPAPLNLLAGAVGGLGFIVLGLLHGSKPELVSGALIRGGHAGA" FT CDS 1768618..1768911 FT /transl_table=11 FT /locus_tag="AARI_15380" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VVV8" FT /protein_id="CBT75761.1" FT /translation="MQELDPLIHAQARLRTITVLDTLRAGDSISFPKLQGLLSMTSGNL FT ATHLRKLEEAEYVKVDKVLEGRSPVTYIALTRTGRTAYEEYKEQLRALLDTV" FT CDS 1769073..1769267 FT /transl_table=11 FT /locus_tag="AARI_15390" FT /product="putative CsbD-family protein" FT /function="4.1 Adaptation to atypical conditions" FT /note="identified by match to protein family PF05532. CsbD FT is a bacterial general stress response protein. Its FT expression is mediated by sigma-B, an alternative sigma FT factor. The role of CsbD in stress response is unclear" FT /db_xref="InterPro:IPR008462" FT /db_xref="UniProtKB/TrEMBL:E1VVV9" FT /protein_id="CBT75762.1" FT /translation="MGLGDKIQNKAQEVSGKVKKSVGDATDNERLQAEGVKDQAAAKAK FT QAGESVKDAAKDVRDGLDK" FT CDS complement(1769354..1770580) FT /transl_table=11 FT /locus_tag="AARI_15400" FT /product="putative methyltransferase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein domain PF05175. This domain is FT found in ribosomal RNA small subunit methyltransferase C as FT well as other methyltransferases" FT /db_xref="GOA:E1VVW0" FT /db_xref="InterPro:IPR002052" FT /db_xref="InterPro:IPR007848" FT /db_xref="UniProtKB/TrEMBL:E1VVW0" FT /protein_id="CBT75763.1" FT /translation="MRLSNADRQGHPIASHSATAPGTVSWDHEGTSTTAIWMSANSRRA FT PAQIVVADDRLSADAAMRHAARGTAMLWTGDFHNAKQLLAAMDRRMAAANAAKAGSSKA FT KKKVLDDAQKFYAIRQARAQRSRMLSLILVPLDFQAEDGLAVLDLPRAPIVGPAVAFGY FT EQAADLAGHRAVASLQELAGMLSAHQWFLKGVEVPALGAKIHPAYGTFMPTRQEYVDLV FT AVAPLEDLSLAFDIGTGTGVLSAVLAHRGVKQVIGTDIHQRAVDCANDNFARLGISAAA FT HAQLTSMFPEGRAPLVVCNPPWLPGSAPSTLDAAIYDPESKMLMQFLRGLPGHLTKNGE FT GWLIISDLAELLGLRTRALLLEAIEAAGLEVIDKIDTAPRHHRAQDAEDVLHAARSKEV FT TSLWRLKAK" FT CDS complement(1770656..1771879) FT /transl_table=11 FT /locus_tag="AARI_15410" FT /product="putative family 28 glycosyl transferase" FT /function="1.1 Cell wall" FT /EC_number="2.4.-.-" FT /note="match to PF04101: Glycosyltransferase family 28 N- FT terminal domain. This family family comprises enzymes with FT a number of known activities; 1,2-diacylglycerol 3-beta- FT galactosyltransferase (EC 2.4.1.46); 1,2-diacylglycerol 3- FT beta-glucosyltransferase (EC 2.4.1.157); beta-N- FT acetylglucosamine transferase (EC 2.4.1)" FT /db_xref="GOA:E1VVW1" FT /db_xref="InterPro:IPR001955" FT /db_xref="InterPro:IPR002213" FT /db_xref="InterPro:IPR004276" FT /db_xref="UniProtKB/TrEMBL:E1VVW1" FT /protein_id="CBT75764.1" FT /translation="MRLLMIAPGTHGDVAPMAGLGQNLAAHGFDVAIAANPAYQDVVVS FT AGCRFRELPGDMRALVNPAAPGAKASPKDLRRYLRELQDYFELAASGTMAAAEHGADII FT MANAVAPYAYDVAEAMGIPAIGGHLQPNEPSAAYSPMALGASRSFGPLGNKVLGQLFAA FT SKAPYDPPAKRVRQSLGLPARSRASSERLRRQHRNPILHGFSSAIVPRSADWHEGIVNC FT GYWWPAADPGWTPSQRLLDFLDDGQPPVFIGFGSTQALEPEFIVDVARRTGRRTIVQGE FT AEIDEPGILGIGAVPHHWLFPQMAAVVHHAGAGTTAAGLRAGVPAVPVPVFTDQPFWAQ FT RIHRLGSAAEPIAYKHLTAQRLASSITGVLANADLADGARRIARQLAAESDSSIPVIRI FT LEQLRARR" FT CDS 1771974..1772615 FT /transl_table=11 FT /locus_tag="AARI_15420" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00440: bacterial regulatory proteins, FT tetR family" FT /db_xref="GOA:E1VVW2" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR004111" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR011075" FT /db_xref="InterPro:IPR012287" FT /db_xref="InterPro:IPR015893" FT /db_xref="UniProtKB/TrEMBL:E1VVW2" FT /protein_id="CBT75765.1" FT /translation="MAGNQPRTGPRPRHSRAKIALAAIALADAEGIGAVSIRAVAAKIG FT AGAASLYRYVQSHEELTGLMVEQISAEYELESLAGSAAQQLLGLATQGLQIMRRHPWVP FT ALAMGKPPMGPNALAYLERGLAALEGSGLEAGAKLHCLAMLNAITAAFALNEQSEQQPQ FT DPAALFAQLETGRYPHLSAALGQAARPVDLQYAFENAIMNYLRGAGVIPD" FT CDS 1772732..1773877 FT /transl_table=11 FT /gene="argE" FT /locus_tag="AARI_15430" FT /product="acetylornithine deacetylase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="3.5.1.16" FT /note="removes the acetyl group from N-acetyl-ornithine. FT Involved in arginine biosynthesis" FT /db_xref="GOA:E1VVW4" FT /db_xref="InterPro:IPR001261" FT /db_xref="InterPro:IPR002933" FT /db_xref="InterPro:IPR010169" FT /db_xref="InterPro:IPR011650" FT /db_xref="UniProtKB/TrEMBL:E1VVW4" FT /protein_id="CBT75766.1" FT /translation="MKEIHELIAVDTTSRDSNLALIENVVKKLDAYGISSQLIHNEEGT FT KANLLATIPAADGSVQGGIVLSGHTDVVPVDGQNWSSDPFDAQVRGDKLYGRGTCDMKG FT YLGVILAKLDQLTSAELAEPIHLALSYDEEVGCVGAVSLVQKIVDDGLAPRGAFVGEPS FT SMRAIRGHKSMNVFRAEFNGVAAHSSLPSEGVNAISYALRFANFVEEVSAELRTSGPRD FT EAFIEPTTTMNVNKFDAGIAVNTIPSEAVVYFEYRSLAVVDRDALTARFREKAAELEAE FT MRAQNPACSVSVQQQAGAPGLDTAPGEEVVALAAACGAIATDEKVTYGTEAGLFSAAGI FT PTVVCGPGDIAQAHAPDEFIELEQIVACESFIDSLIAQLSS" FT CDS 1773928..1775148 FT /transl_table=11 FT /locus_tag="AARI_15440" FT /product="MFS superfamily transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="major facilitator superfamily (MFS), metabolite:H+ FT symporter (MHS) family (TC 2.A.1.6.z)" FT /db_xref="GOA:E1VVW3" FT /db_xref="InterPro:IPR011701" FT /db_xref="InterPro:IPR016196" FT /db_xref="InterPro:IPR020846" FT /db_xref="UniProtKB/TrEMBL:E1VVW3" FT /protein_id="CBT75767.1" FT /translation="MISSSIGAALEWFDIIVYATFATTIAKVFYPESDGTFALILTFAT FT FAISYLIRPLGGMVLGSYADRKGRKNALTLTLGLMMLGTLIMAVAPPYEMAGVAGALII FT LLSRMIQGFSAGGEFGTATAFLIETAPHKKAFYSSWQVASQGASMLLALAFGYFLTTGL FT SQEALESWGWRVPFFVGLLIGPVGLYIRAKLEETEEFISAPKEKSPLGTLFAQHYGRLL FT EAAATIGVATMSVYMILYMPTFAVTNLKIPADAAFLGGISAGIITLCGVPLVGHLADRV FT GPAKVMTYAAIAAFVLAYPLFKLMTSRPSVIVMVIVIAVLGIIMSFYFGPLPALLSNLF FT PAAIRGSGLSVAYNVGVTLLGGIAPLVLTWLLDVTGSLDAPSLYYMAISAISLIGLVVV FT RKRYGQR" FT CDS complement(1775229..1775918) FT /transl_table=11 FT /locus_tag="AARI_15450" FT /product="hemolysin III-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF03006: FT HlyIII, Haemolysin-III related" FT /db_xref="GOA:E1VVW5" FT /db_xref="InterPro:IPR004254" FT /db_xref="InterPro:IPR005744" FT /db_xref="UniProtKB/TrEMBL:E1VVW5" FT /protein_id="CBT75768.1" FT /translation="MATEPLNPNSQRRTAPAFSHIGTERTRWRGLIHAWSTPGVIVMNL FT VLIVLANGRLAEWTTAVFALCSILLFGTSALYHRGNWTDKVMGLFRRADHANIFLLIAG FT TYTPVAALTLPGKQAIIVLSVIWAGALAGIAIKSFWPGAPRWVGVSLYILLGWGALMQL FT PAFWAANPAVMILILAGGLAYTVGAVFYAAKRPNPLPKIFGFHELFHACTIVAFLCHWT FT AVLLVAL" FT CDS 1776032..1776964 FT /transl_table=11 FT /locus_tag="AARI_15460" FT /product="zeta toxin-like protein" FT /function="4.6 Miscellaneous" FT /note="match to protein family PF06414. This family FT consists of several bacterial zeta toxin proteins. Zeta FT toxin is thought to be part of a postregulational killing FT system in bacteria. It relies on antitoxin/toxin systems FT that secure stable inheritance of low and medium copy FT number plasmids during cell division and kill cells that FT have lost the plasmid" FT /db_xref="GOA:E1VVW6" FT /db_xref="InterPro:IPR010488" FT /db_xref="UniProtKB/TrEMBL:E1VVW6" FT /protein_id="CBT75769.1" FT /translation="MADEQEITEHLKTIADLNEPGQALANDSPHISVRNPQWFHELAPG FT KWEAIGQREQLHRKLISQQLREAHGAKAEYQAVVLAGAPGAGKSSLLRQVLGDQQDRYV FT VIDVDEFKELLLREAQEDGSYEQVFKPHEVRELEQQGEQFFPMDMASLVHEESSMLGDR FT LRAACLDKGLNVVIDKVLSSTESARKLAGQLEEAGYEISLIEAYAPQEVSEERIIERWE FT EQQEASLDGEDDLGARWVPEEFTEKVFDAPGQRSRPAVVAQMFARSCPAVVSFKLFHTA FT LDQGSKTDGSRLLFELRREAVGAQLLPVK" FT CDS complement(1777047..1777307) FT /transl_table=11 FT /locus_tag="AARI_15470" FT /product="hypothetical membrane protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VVW7" FT /db_xref="InterPro:IPR007341" FT /db_xref="UniProtKB/TrEMBL:E1VVW7" FT /protein_id="CBT75770.1" FT /translation="MGFIGWIVLGLIAGAIAKAILPGRQGGGWIATLVLGVVGALLGGW FT IGSAIFGEGVDEFFSISSWLLAIGGALIVLIIWGFITKRRA" FT CDS 1777627..1778133 FT /transl_table=11 FT /locus_tag="AARI_15480" FT /product="gluconokinase" FT /function="2.1.1 Specific carbohydrate metabolic pathway" FT /EC_number="2.7.1.12" FT /note="catalyzes the phosphoryl transfer from ATP to FT gluconate. The resulting product, gluconate-6-phoshate, is FT an important precursor of gluconate metabolism" FT /db_xref="GOA:E1VVW8" FT /db_xref="InterPro:IPR000623" FT /db_xref="InterPro:IPR006001" FT /db_xref="UniProtKB/TrEMBL:E1VVW8" FT /protein_id="CBT75771.1" FT /translation="MSEQVPPIVVMGVSGTGKSTIGQLLADRLDREFIDGDNLHPKANK FT DKMAAGHALDDADREPWLRVIGAKLAESNQRQAPLVIACSALKRSYRDLILTLEPATIF FT VHLAGVPTLIRDRMSARSHEYMPTSLLDSQLATLEAPDQDEPVLSADITDTPERIVRQL FT ISQLS" FT CDS 1778201..1779616 FT /transl_table=11 FT /gene="gntP" FT /locus_tag="AARI_15490" FT /product="gluconate permease" FT /function="1.2.4 Transport/binding of carbohydrates" FT /note="Gluconate:H+ Symporter (GntP) Family (TC 2.A.8.y.z). FT Match to protein family PF02447" FT /db_xref="GOA:E1VVX0" FT /db_xref="InterPro:IPR003474" FT /db_xref="UniProtKB/TrEMBL:E1VVX0" FT /protein_id="CBT75772.1" FT /translation="MTTELELNWTLGTPGLLMLAVAAVALLLVLIIRFRVHAFLALVLT FT SLLTAVASGIPAESVITTLTSGFGSTLASVALLVGLGAMLGRMLETSGGADVMTSWLIS FT KFGEKRAPLALSVASLLFGFPIFFDAGLVVMLPIIFTVARRLGGSLLLYAIPSATAFSV FT MHVFVPPHPGPVAASGLLEANVGLVLVLGLIVAVPTWYVAGHLFGKFVGKKFDIPVPNI FT LAAALGNGANKNDFKSSPSVGTVFSLLLLPLLLIFMNTGLNMLGSAGVVDPEVSWVRWL FT RLLGETPVALLITVLLGMFLLGFRKGKDKTLTETIVDSALGPVCSIILITGAGGMFGGV FT LRASGIGNAIASSLESVGMPLIVAGFLIAAIVRLAQGSATVALTTAAAIVQPAVLADAS FT LTVFQVATMVLALAAGSVFAGHVNDSGFWLISRFLDIDVPTTLKVWTVGQALVSVVGFA FT CVMVLYGLATALA" FT CDS 1779898..1780500 FT /transl_table=11 FT /locus_tag="AARI_15500" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVW9" FT /protein_id="CBT75773.1" FT /translation="MAPENNVARKGKKPLVIGSVIALVVGLAGGTGLGLAVADPTDSKQ FT YIEQSELLQATETELVEVKGNIDEREANVKTRGEELDVRSGELDSRSSDLDKREKSVEA FT ESAAVLEREKTVGLVEEEQKAKSIGDGVYTVGTDIEPGTYRAKEEVETNCFWGITKDGT FT NGENYIAAGNPLGGRPTVVVKKGQVLHLSYCGTFVRQ" FT CDS complement(1780601..1781335) FT /transl_table=11 FT /locus_tag="AARI_15510" FT /product="putative GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="match to PF00392: bacterial regulatory proteins, FT gntR family, and to PF07729: FCD domain" FT /db_xref="GOA:E1VVX1" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011711" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VVX1" FT /protein_id="CBT75774.1" FT /translation="MATSLHAHVVEHLGSRIVSGNIPRGSIILAAELEQKLQVSRSVIR FT EAIRVLAQCGLVTSTKRVGIRVLGAELWNPYDDHVIRWRLASDHKGAQLRSLTELRISV FT EPMAAELAAEVAPEAMRKELMMLSAQMNHYGRQGDLRRFLELDIRFHAVVLAASGNEMF FT ANLATPIGTILRGRTELGLMPERPHEEALLWHQSVADAISNSDSASARKNMESIMRRTH FT NEICSLWEGAPRLFVDPAKSAQ" FT CDS 1781545..1782984 FT /transl_table=11 FT /gene="gnd" FT /locus_tag="AARI_15520" FT /product="phosphogluconate dehydrogenase (decarboxylating)" FT /function="2.1 Metabolism of carbohydrates and related FT molecules" FT /EC_number="1.1.1.44" FT /note="involved in the pentose phosphate pathway. Catalyzes FT the oxidative decarboxylation of 6- phosphogluconate into FT ribulose 5-phosphate" FT /db_xref="GOA:E1VVX2" FT /db_xref="InterPro:IPR006113" FT /db_xref="InterPro:IPR006114" FT /db_xref="InterPro:IPR006115" FT /db_xref="InterPro:IPR006184" FT /db_xref="InterPro:IPR008927" FT /db_xref="InterPro:IPR012284" FT /db_xref="InterPro:IPR013328" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VVX2" FT /protein_id="CBT75775.1" FT /translation="MPAQIGVTGLAVMGANLARNFARNGYTVALHNRSVGKTDALLEAH FT GDEGDFIRTESLEELVANLETPRRVLIMVKAGGPVDSVIDQLVPLLEEGDVVIDGGNSH FT YTDTRRREAALAEKGLHFVGIGVSGGEEGALLGPSIMPGGSAESYKSLGPMLEKISAKA FT DDGAPCCAWISTDGAGHFVKMVHNGIEYADMQVIGEAYDLMRSAAGIEPAKQAQIFNEW FT NQGELSSFLIEITAEVLGHTDAATGKPLVDVIQDSAGQKGTGRWTVQSGLDMGSPVSAI FT AESVFARSLSSQRDIRAVGQEVLTGETAEVTLPENFVEDVRQALFASKLVSYAQGIDML FT TSAAGEYNWELKLDEIAGLWREGCIIRAALLKDITAAYSADEKPSNLLFAPAFAKAIND FT AVPAWRRVVSVAVQLGIPAPVFSSSLAYYDGLRRDRLPAALTQGLRDYFGAHTYRRTDK FT EGTFHTLWSGDRTEIAAEDTH" FT CDS complement(1783087..1783611) FT /transl_table=11 FT /locus_tag="AARI_15530" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVX3" FT /protein_id="CBT75776.1" FT /translation="MDRGRTRIAEDYHHDLQMLRSFLVAANASDLKRRSHGTRWTNEQL FT LFHMVFGYMVVRALLPLVHVLVRCPPSARSAFCRLLNAGTALSHPVNYLGSCAAAAVYN FT HRRMAFKLQRTIAALEAWLAAETTASLQRRTDFPDRWDPFFTPAMSVEQIYAYPSRHFA FT FHARQLALPAQ" FT CDS complement(1783691..1784281) FT /transl_table=11 FT /locus_tag="AARI_15540" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="GOA:E1VVX4" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR015893" FT /db_xref="InterPro:IPR023773" FT /db_xref="UniProtKB/TrEMBL:E1VVX4" FT /protein_id="CBT75777.1" FT /translation="MARTSAFDRAQVIQKARSIFWSKGYETSSIPELESATGLSRSSIY FT NSFGSKRGLFDAVVDSYLNEIVRPRLQPLLAGNVSPSALEEYLSSLAEVFAKPESLPAA FT HGCLLINTASAPLAADPEVASVISDYRDELHQALDRGLHAARPELAGERRGVLAEAITG FT LVVAAFALVRISPHEAVRLLHCAENLLGVEPGH" FT CDS 1784374..1784766 FT /transl_table=11 FT /locus_tag="AARI_15550" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR009732" FT /db_xref="UniProtKB/TrEMBL:E1VVX5" FT /protein_id="CBT75778.1" FT /translation="MIIAALIAASIAALLHVYIFSMESLTWTSKRTRAVFNATEEEAEA FT TREMAFNQGFYNLFLALASLIGVLLVALGNLAIGATLIFAGTGSMLAAAVVLAAGSPRK FT ATLAVRQGLFPLLAVVLLGLGVAMGR" FT CDS 1784819..1785829 FT /transl_table=11 FT /locus_tag="AARI_15560" FT /product="putative NADP-dependent oxidoreductase" FT /function="4.6 Miscellaneous" FT /db_xref="GOA:E1VVX6" FT /db_xref="InterPro:IPR002085" FT /db_xref="InterPro:IPR011032" FT /db_xref="InterPro:IPR013149" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VVX6" FT /protein_id="CBT75779.1" FT /translation="MTDAISTQILLASRPTGWPTQDNFTTVKRELADLKAGEVRVRNEF FT VSVDPYMRGRMNDTRSYIPSFQIGEQILGGAIGRVVLSADEALPEGTLVSHQHGWSDLV FT QAEAASFKAVPDLPGVPSSLRLHILGMTGLTAYVGLSHIANLEAGDTVFISGAAGAVGT FT AAGQIAKLMGAKRVIGSAGSAEKVELLTSKYGYDTAFNYKDGDVRGQLAAAAPEGIDVY FT FDNVGGDHLEAALASFNDGGRAALCGAISSYNTSEVPAGPNNMTNMVTRGLKMQGFTLS FT NYLFLSPEFGERMGQWFAEGKIAYDETIVEGIENTVDAFLDMMRGANTGKMLVRI" FT CDS 1785886..1786419 FT /transl_table=11 FT /locus_tag="AARI_15570" FT /product="hypothetical membrane protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="1 transmembrane helice predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VVX8" FT /protein_id="CBT75780.1" FT /translation="MNGFAGGLGWWLAILGSLSPIFTVLIAAIGVILALRTLKLRSKVD FT IAGQWWVRVQYAMDRCLSPDLTEQNVGITMLDYLQGQSEPPEQLDEEQREAWLRAHRNS FT WRVQPEDLALIHEVVKELALGKSAKLAAAGIRAEHEHDREYDTLLRQAKLVQKLEAKLG FT IAQDPEISRILAQD" FT CDS complement(1786420..1786920) FT /transl_table=11 FT /locus_tag="AARI_15580" FT /product="putative GNAT-family acetyltransferase" FT /function="4.6 Miscellaneous" FT /EC_number="2.3.-.-" FT /note="identified by match to PF00583: acetyltransferase FT (GNAT) family" FT /db_xref="GOA:E1VVX7" FT /db_xref="InterPro:IPR000182" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:E1VVX7" FT /protein_id="CBT75781.1" FT /translation="MAQQLRTPTPADAHELAKLHVACWKETYSDLLPEGFFDSAHDEQR FT LQMWNKVLADPNPLFRISLAENADGKLVGFAFSAAPTGNTEGIPSSVSRQLYNLYVLQG FT FHGDGTGQALLDAVLGGEPAMLWVESQNPRAIRFYQRNGFALDGVTEDDPMAPKITDAR FT MVR" FT CDS complement(1786923..1789184) FT /transl_table=11 FT /gene="uvrA" FT /locus_tag="AARI_15590" FT /product="excinuclease ABC subunit A" FT /function="3.3 DNA recombination, and repair" FT /note="excinuclease ABC catalyses nucleotide excision FT repair in a multi-step process" FT /db_xref="GOA:E1VVX9" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VVX9" FT /protein_id="CBT75782.1" FT /translation="MSQHPADSHEKIRVRQARENNLRGVDVDIPKRRITAFTGVSGSGK FT SSLVFGTIAAESQRLINETYTTFIQSFMPSMPRPDVEVLENLSAAIVVDQERMGANSRS FT TVGTATDAYSLLRVLYSRYSTPSAGGAGAYSFNLGEGACPVCEGFGTEASIDLDELLDW FT DKTLNEGAITAPNFAPGAWLWQTLTAGTEPDLDLKLRDMPKPMLDRLLYEEAGKVKLNG FT ANMSYSGLITRIKSNYIHSGREIKQAHIREWIERISTTAPCSACDGSRLGEKARASKIN FT DRGIADMTALQVTELLDELEKVQHEDAAPLIANLKAVLKSMVDLGLGYLSLDRPAGTLS FT GGEAQRVKMIRHLGSALSDVTYVFDEPTVGLHPHDIQRMNGLLANLRDKGNTVLVVEHK FT PEVIKIADHVVDLGPGAGTHGGTVCYSGDVAGLLAGDTLTGKHFNTRATLKQNPRKAQG FT AMEIRGASLHNLKNVSVDIPTGVMCAITGVAGSGKSTLVHSTIAKREDVAVVDQSAIRG FT SRRSNPATYTGIMDPIRAAFAKANGVKPALFSANSAGACPGCNGVGFTYTDLASMAGVA FT LPCEQCGGKRYTAEVLEYTFDGLNIAEVLDLSMEEALAQLNVPKAKPVLARLNQVGLGY FT LKLGQRLNTLSGGERQRIKLAINLGQGAGTYILDEPTTGLHMADVQNMLRLLDEMVDEG FT NTVIVIEHHLAVVAHSDWVIDLGPGAGHEGGSIVFEGTPKDLAASGTLTGVHLAEYSKG FT " FT CDS 1789315..1789866 FT /transl_table=11 FT /locus_tag="AARI_15600" FT /product="hypothetical lipoprotein precursor" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="match to PS51257: prokaryotic membrane lipoprotein FT lipid attachment site profile" FT /db_xref="UniProtKB/TrEMBL:E1VVY0" FT /protein_id="CBT75783.1" FT /translation="MSNRPRKLVKLGPLTVLFGCLALAGCGSTTAGSASEEPSSPTQSA FT SLESSSPQASAPEASTSPTAAASSSAAGESEQTETIGGQELGKLPSNAIEYADALVVAW FT GNGNEAQMQQLATAQVITSLTGHSKEGGAHWSQTSSDAGAGSVFVSYENTEDGSVLNLR FT VQNQVVGQGHEQGVVEANFE" FT CDS 1790164..1791444 FT /transl_table=11 FT /locus_tag="AARI_15610" FT /product="putative dicarboxylate/amino acid transporter" FT /function="1.2.5 Transport/binding of amino-acids" FT /note="Dicarboxylate/Amino Acid:Cation (Na+ or H+) FT symporter (DAACS) family (TC 2.A.23.y.z). The members of FT the DAACS family catalyze Na+ and/or H+ symport together FT with (a) a Krebs cycle dicarboxylate (malate, succinate, or FT fumarate), (b) a dicarboxylic amino acid (glutamate or FT aspartate), (c) a small, semipolar, neutral amino acid FT (Ala, Ser, Cys, Thr), (d) both neutral and acidic amino FT acids or (e) most zwitterionic and dibasic amino acids" FT /db_xref="GOA:E1VVY1" FT /db_xref="InterPro:IPR001991" FT /db_xref="UniProtKB/TrEMBL:E1VVY1" FT /protein_id="CBT75784.1" FT /translation="MKLLKKIPLLGWVLVAIVLGILLGPVMPVWLGSLFLTYNSIFSGF FT LGFIVPLIIFGLVAPAIAELGKGAGKWLGITALIAYTSTLCAGLLAYFVSRWLFTKSLS FT GGGVEEVGGGEGSGFAPYISLVGEAGDGATEIVLTPLMGVMTALVLAFMLGLGLTAFRS FT TVLFRGTVEFRSIVEMVIRKIIVPALPLFIFGIFLDLSAAGDAVVVVQKFLFVAVVSFV FT LTLVVLLVQYTIAGAMNKRNPLSALWGMRNAYFTALGTSSSAATIPVTLESAKKNGVSD FT TVAGFVVPLCATIHLSGSMTKITCFSIAVLLLTGGDVSFTTYLPFILMLGVMMIAAPGV FT PGGAIAAAAGLLTQMLGFGEVEVGLMFAAYIALDSFGTATNVTGDGALAMIMHKLTKGK FT LGAQPQDPEDEVVELADGTEAADHKLA" FT CDS complement(1791629..1792213) FT /transl_table=11 FT /gene="cysE" FT /locus_tag="AARI_15620" FT /product="serine O-acetyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.3.1.30" FT /note="catalyses the first step of the synthesis of L- FT cysteine from L-serine" FT /db_xref="GOA:E1VVY2" FT /db_xref="InterPro:IPR001451" FT /db_xref="InterPro:IPR005881" FT /db_xref="InterPro:IPR011004" FT /db_xref="UniProtKB/TrEMBL:E1VVY2" FT /protein_id="CBT75785.1" FT /translation="MSFFSRLCEDLANARQHDPAARSDPENFFVYSGLHAIWMHRLAHK FT MWQNPSLKWPARLLSQANRALTGIEIHPGATIGRRFFIDHGMGIVIGETAEIGDDVMLY FT HGVTLGGRSLAKVKRHPTIGDRVVIGAGAKVLGPITIGADSAIGANAVVVKDAPEGSIV FT TGIPAQNRQRRPDERKPAVDPAEYIDPAMWI" FT CDS complement(1792357..1793292) FT /transl_table=11 FT /gene="cysK" FT /locus_tag="AARI_15630" FT /product="cysteine synthase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.5.1.47" FT /note="responsible for the formation of cysteine from O- FT acetyl-serine and hydrogen sulfide with the concomitant FT release of acetic acid" FT /db_xref="GOA:E1VVY3" FT /db_xref="InterPro:IPR001216" FT /db_xref="InterPro:IPR001926" FT /db_xref="InterPro:IPR005856" FT /db_xref="InterPro:IPR005859" FT /db_xref="UniProtKB/TrEMBL:E1VVY3" FT /protein_id="CBT75786.1" FT /translation="MGKIYNNVTEIVGNTPLVKLNRVGEGLPGNIAVKLEFYNPANSVK FT DRIGVAIVDAAEKSGALKPGGTIVEGTSGNTGIALAMVGAARGYKVILTMPETMSTERR FT VMLRAFGAEIVLTPGADGMRGAVEKAKEIVATSENAIWAQQFANTANPQVHADTTGPEI FT WADTEGKVDVLVAGIGTGGTITGAGRYLKEKNPDLKIVAVEPKDSPILNGGKPGPHKIQ FT GLGANFIPEVLDTELYDEVLDASIEDSVSTARALGVKEGILGGISAGAAVWGAVQIAAR FT EENAGKQIVAIIPDFGERYISTLLFDDIRG" FT CDS complement(1793419..1794039) FT /transl_table=11 FT /gene="msrA" FT /locus_tag="AARI_15640" FT /product="peptide-methionine (S)-S-oxide reductase" FT /function="3.8 Protein modification" FT /EC_number="1.8.4.11" FT /note="plays a role in preventing oxidative-stress damage FT caused by reactive oxygen species by reducing the oxidized FT form of methionine back to methionine and thereby FT reactivating peptides that had been damaged" FT /db_xref="GOA:E1VVY4" FT /db_xref="InterPro:IPR002569" FT /db_xref="UniProtKB/TrEMBL:E1VVY4" FT /protein_id="CBT75787.1" FT /translation="MQRRNVVNNVSILSLQSPHQFSPSLEVQGTKLTTFVLAGGCFWCL FT DAVYQRTRGVYAVISGYIGGHTADPQYREVCSGMTGHAEAVAVIFDAAVVPEEIILDMF FT FTVHDPTTLNRQGYDVGTQYRSAMFPLDDQQRELFEQSIQKFAGIYPNPIVTTMEESKD FT FYPAEQIHQDYYSANQEVGYCRVIIDPKLVKVRKYYAQWLNEA" FT CDS 1794078..1795031 FT /transl_table=11 FT /locus_tag="AARI_15650" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR002678" FT /db_xref="UniProtKB/TrEMBL:E1VVY5" FT /protein_id="CBT75788.1" FT /translation="MQSKANNSQDLGKNNDSAEAAKLKPVADEKVEQPVGETPAVETTL FT GNVLEAVEELWPKSLAEGWDAVGLVTGRTSQKISKIVMAVDPTLEVIEDAIKRGADLLI FT THHPLLLRGVTQVAGTSFKGEAIHRLIESGTALLTAHTNADSAIGGVNDALADAFGLKG FT CVPLVESKDGLPEEGLGRVGFLEKPMKLEDFAERVYTVLPAVAGGVRVAGDRTGIVRKI FT ALCGGAGDSLFDAVRSHQADVYVTADLRHHPASEAREAADGGFPYLIDVSHFASEWVWL FT SAGARALGNVLKDTGHEVEIEVSQINSDPWDFVLTP" FT CDS 1795044..1795427 FT /transl_table=11 FT /locus_tag="AARI_15660" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VVY6" FT /protein_id="CBT75789.1" FT /translation="MLHHLEIWVEDLVASTASLGWLLTRLGYRLESQWADGASYAQDKF FT YIVLESGPDVRKQAHDRLAPGLNHLAFSVATRGEAEMIVREALEHGFTLMFPEKHPYAG FT GPEHYAAYLEDAAGFEVELVATQ" FT CDS complement(1795481..1795699) FT /transl_table=11 FT /locus_tag="AARI_15670" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVY7" FT /protein_id="CBT75790.1" FT /translation="MSYQKSQGEAIEVQVEITQLPTSGLPTPAPEQLPLDLADTGADPW FT ILLIAVAVFALGAFATRFSRRKRMTGS" FT CDS complement(1795696..1796736) FT /transl_table=11 FT /locus_tag="AARI_15680" FT /product="conserved hypothetical protein precursor" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.987 FT between position 31 and 32" FT /db_xref="InterPro:IPR010317" FT /db_xref="UniProtKB/TrEMBL:E1VVY8" FT /protein_id="CBT75791.1" FT /translation="MSHTPRTFTRVALTTMLAAGLGFSTALPAAASPTPSDEQAPITWS FT MSPLPEENQSNTQWVELDMKPGESVQRELVVKNHSAQEATFGLQAADGYFTDTGRFNML FT ASDEPSEAAGTWISIQEEITVAPKASENVRFTVTVPENATPGDHAAGVASSTTSIGQSA FT DGASLGVESRIGFRVITRVEGELNPSLAVQELHTGYKQSWNPFAPGSITADFRLHNDGN FT LQLQPQSALFSFQNAEGQSLESGSLLPGDGAKVTMKLDQSWPTFLTPVTLEVTGTDNGG FT AEQVLRTEKVWVWTLPLPQLFVLLGATLCFLGLRRRKTKQTERMDELLDQARRDGAEQA FT RQESNA" FT CDS complement(1796805..1797431) FT /transl_table=11 FT /locus_tag="AARI_15690" FT /product="hypothetical protein precursor" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 1.000) with cleavage site probability 0.697 FT between position 29 and 30" FT /db_xref="UniProtKB/TrEMBL:E1VVY9" FT /protein_id="CBT75792.1" FT /translation="MSKNKVLPRAVALTAGCTLLLGVGAAAIANPVEHGSNEIDVNVKI FT AELEGPGALAMTVAGASSTSLVESGSDELIRQFTGTLPTVSVTDTRAAEDVAEGAYWYV FT LGTASAFSSETGETIGAEHLGWTPRLIDGGTSGGVTEGDSVDTVLDSGNNNVGLVDQEL FT LAMAWDSNELLEEGSWTANADLYLRTPADVERGSYSSKLTLSLFE" FT CDS complement(1797472..1799778) FT /transl_table=11 FT /locus_tag="AARI_15700" FT /product="metallophosphoesterase domain-containing protein" FT /function="4.6 Miscellaneous" FT /note="match to PF00149. The metallophosphoesterase motif FT is found in a large number of proteins invoved in FT phosphoryation. These include serine/threonine FT phosphatases, DNA polymerase, exonucleases, and other FT phosphatases" FT /db_xref="GOA:E1VVZ0" FT /db_xref="InterPro:IPR003961" FT /db_xref="InterPro:IPR004843" FT /db_xref="InterPro:IPR008963" FT /db_xref="InterPro:IPR008979" FT /db_xref="InterPro:IPR015914" FT /db_xref="UniProtKB/TrEMBL:E1VVZ0" FT /protein_id="CBT75793.1" FT /translation="MALALFGTTVITGQSALAAPETDIEDQTVITTADTEWKFLDDGSD FT PAAGLSSLNAWTENDFDDSTWKNAKGSFGAKNGSLGAVGPYTPKTLLNHYLPEQGKTTV FT PTYFFRTSFDLEAGQADQYVELSGEATYDDALVIWVNGTKVAGFLDDRLTGENNQEYAG FT SSNGDPVTSTFRIPADVLVDGENTVAVSLHQDREVSSDIYLDFPELSLHTTEHHEPPSR FT VILTPTETPETSQYVSWLGGIANEETGVVEIRETAGTEVRSIDARFVDRVNNNPLPHFS FT AELTGLTPATSYTYRVGNAGSYSPWYTFKTADPNAKNFQYIYFGDAQIGLDTTWPKVVK FT QAMAAAPNIVGSVHAGDLINTGSNETEWTNWFKGMKDSGATTNVMAAPGNHEYSGDNKL FT LAWKANFEYPGNNPSVETAGELAKLTVGDTPQAIQYRALFEHWTEFAKETVYFTDYQGV FT RFITINATRSTGFLVPDNLPACEGSDCPAGNVSSLWVQFQAAWLDHILEDSDSKWNVVT FT FHQPVYSASAGRNEPVLREHWVPVFQKHNIDLVQMGHDHVYARGYHNSNTTEHEGVTDG FT PVYVVSNSGAKHYDLAPAADNVWTQNDATQVLRGRGFTTYQIIDVTEDALTYKSYVAEK FT TSTSTTDLAVGDLWDEFTVTKDEAGTKWVTEAGVKAPEEAEPALAVDVNTSVRCLAGKA FT TLTVAATNGEAGPISLKIVSDFGTKQFNKVNSGKKGTAAFSTRQAELAEGTISVEASDG FT TTSSTQKVDFAATGC" FT CDS complement(1800122..1800901) FT /transl_table=11 FT /locus_tag="AARI_15710" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR005583" FT /db_xref="UniProtKB/TrEMBL:E1VVZ1" FT /protein_id="CBT75794.1" FT /translation="MLILLPPSEGKNAHTEGSPFEFEDLSFPELAEQRAQVLAALTEVS FT AREDAMEILGVGATLANEVARNISLHTEPAAKAHDIYSGVLFEALNYASLDEAAQQRAD FT ESILVISALWGAVRFADRIPPYRLSMSVKLEPLGKLASWWKKRLTPVLDAAAGDELIVD FT ARSSTYAAAYKPTNDNSVAVNVFQLRNGVPKVVSHFAKHTRGEVARFLVQQPVAPTNKD FT ELLALIQSKWEASLVEDKKGVALNILLSEGHKFTTAS" FT CDS 1801611..1803068 FT /transl_table=11 FT /gene="gap" FT /locus_tag="AARI_15720" FT /product="glyceraldehyde-3-phosphate dehydrogenase" FT /function="2.1.2 Main glycolytic pathways" FT /EC_number="1.2.1.12" FT /note="catalyses the reversible oxidation and FT phosphorylation of D-glyceraldehyde-3-phosphate to 1,3- FT diphospho-glycerate" FT /db_xref="GOA:E1VVZ2" FT /db_xref="InterPro:IPR006424" FT /db_xref="InterPro:IPR016040" FT /db_xref="InterPro:IPR020828" FT /db_xref="InterPro:IPR020829" FT /db_xref="InterPro:IPR020830" FT /db_xref="InterPro:IPR020831" FT /db_xref="UniProtKB/TrEMBL:E1VVZ2" FT /protein_id="CBT75795.1" FT /translation="MTQQSVVAQQEWSGREELAEAMIPLIGRLYRKNNVVTSVYGRKLI FT NQSAIDIIKAHRVVRRIDGEELDLNDTKAILDAIETLNVGSVAVDLGRVNKKFKESGSA FT DLNAFLTEELGEKVGQAGATDAEPQDVVLYGFGRIGRLLARILVERGGYGLRLRAIVVR FT KGSDDDIVKRASLLRRDSVHGRFEGSITVDEENSTILANGTLIKVIYSNDPTTVDYTAH FT GIDNAIVVDNTGRWRDEAGLSQHLQAKGVSRVLLTAPGKGDLKNIVHGINDSWITADDK FT IVTAASCTTNAITPVLKALNDKFGVIHGHVETVHSFTNDQNLIDNFHKGERRGRSAALN FT MVITETGAAKAVAKALPEFEGKLTGNAIRVPTPDVSMAILNLNLENETTKEELNAYLRE FT TSLTSSLHKQIDYIDSPEVVSTDFVGSRRAGIVDGLATIVTGKNAVVYVWYDNEFGYSC FT QVVRVIESMAGTHPAAVPALKAEAVTV" FT gene complement(1803149..1803352) FT /pseudo FT /locus_tag="AARI_15730" FT /product="truncated dehydrogenase" FT /note="C-terminal section of a dehydrogenase. Match to FT PF00890 (FAD binding domain): This family includes the FT flavoprotein subunits from succinate and fumarate FT dehydrogenase, aspartate oxidase and the alpha subunit of FT adenylylsulphate reductase" FT gene 1803372..1803527 FT /pseudo FT /locus_tag="AARI_15740" FT /product="truncated protein" FT /note="segment of a conserved protein" FT gene 1803531..1803638 FT /pseudo FT /locus_tag="AARI_15750" FT /product="truncated protein" FT /note="segment of a conserved protein" FT gene 1803645..1803875 FT /pseudo FT /locus_tag="AARI_15760" FT /product="truncated protein" FT /note="segment of a conserved protein" FT CDS complement(1803888..1804460) FT /transl_table=11 FT /gene="def" FT /locus_tag="AARI_15770" FT /product="peptide deformylase" FT /function="3.7 Protein synthesis" FT /EC_number="3.5.1.88" FT /note="involved in polypeptide synthesis by removal of the FT formyl-group from methionine in growing polypeptides" FT /db_xref="GOA:E1VVZ3" FT /db_xref="InterPro:IPR000181" FT /db_xref="InterPro:IPR023635" FT /db_xref="UniProtKB/TrEMBL:E1VVZ3" FT /protein_id="CBT75796.1" FT /translation="MPIRQITVYGEPVLHKRAVEVTEFDDALRALVADMHLTMDEAHGV FT GLAAPQIGLGLRMFTYVFADQDDAPERGVVINPKLTLSKVSQAPAHPDEDSEGCLSVPG FT LNYPLQRADYAKVEGFDEFGNPISFEAHGWFARIMQHEYDHLDGYLYVDKLQPRWEKRW FT KKAKKALGWGVPGNTWLPGTDEDPFGH" FT CDS complement(1804485..1805633) FT /transl_table=11 FT /locus_tag="AARI_15780" FT /product="putative acyl-CoA dehydrogenase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.3.99.-" FT /note="possibly involved in the metabolism of lipids. Match FT to protein domains PF08028, PF02771 and PF02770. Acyl-CoA FT dehydrogenases catalyze the alpha,beta- dehydrogenation of FT acyl-CoA thioesters to the corresponding trans 2,3-enoyl FT CoA-products with concommitant reduction of enzyme-bound FT FAD" FT /db_xref="GOA:E1VVZ4" 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:E1VVZ4" FT /protein_id="CBT75797.1" FT /translation="MKRALFEEDHEQFRELATEFNAREISGKYAQWEKDHQIPREVWQS FT AGENGLLGLAVPEEFGGMGIDDYRFRVVLDEEFVRSGHLAVALAFHLHDDLVLPYLLSY FT GSAELKAKWLPRMVDGSTITSCALTEPGAGSDLRAVRTKAVRDGDDWLISGQKTFIGNA FT AFGDASLVLARTDGESSRAGAHSFSLFMVERSEGYSNGKPFDKMGLRASDTAELFFDEV FT RVSATDLVGEVGQGLSYVKAQLPQARLALAVAASAICSASFEQALEHTKNRSTFGQVLT FT EYQNTRFELADLKTEAHVTQSFVDRAVLAFNEGELNASDAAEVKLWASESAKKLSDKAL FT QLHGGYGYIMEYPIAQSFTASRLLTIFGGTSEIMRETIGRAL" FT CDS complement(1806095..1808794) FT /transl_table=11 FT /locus_tag="AARI_15790" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VVZ5" FT /db_xref="InterPro:IPR000792" FT /db_xref="InterPro:IPR011991" FT /db_xref="InterPro:IPR016032" FT /db_xref="UniProtKB/TrEMBL:E1VVZ5" FT /protein_id="CBT75798.1" FT /translation="MTGSTWEFDINKMPGFQMERREVLPSRVKALNTALTAARTGGPIF FT IIGEVGTGRTTFSLQLMDRIESNFIWIIGSQALSSVPFSTLSVLATQLPHGSTGTSPTE FT LVTGIGRATSNRTQWIFLDQAEYVDQQSAAVLKQFATAGNIRLVVATTAVHAMPSELRS FT MISSPNFMRMELGPLTYDDAGVMLSEVLGGEVNSSAVTSLLEFSGGHALHLRELALDAQ FT STGALSKQQDYWTLNRSWTPHGKRTTDLINARLSNQPEDVREALELLAVTGPLPLPIAR FT KLMGQSIYDAIDAGLVRLDFVSENPVTGERTEHVRLGAGLSSQLVFSSFDSSTLRRHIN FT TIDEKLSWELFDAESRSRFTRHRLDMGLTVPIRELLSDVEQLTSARQFPQVIALTDLLD FT QQRVDSPDQLESLLIARADALYELGKPEAALALLQDHLPTGSPEIRFIAAKIAYASLGR FT LELAEQILEPRPGDPPGIAAYLLLIRSRANKVVDIASLRQYASMPELRSEGRASCLAHV FT LIEKSHSGSAEEAMAEYVRISSSPEWKTESASVRSELLFAFPAMAFALGMNPAQFAQLT FT VGDNLKEANVDHGNVIVGIGMGYLESGMASQALAALEQAIGLLSVGDPYLVKGFAAAFA FT AYAASLLGDRAKASYYLDMSRAEPEVSGQILRPIAERSLLSVVLDLEGEQAAEDLLHKL FT LAEAESFGRKNLVMRLLLEAWQCGLLADASRLSEAALQVQGPLAATLAGYQTALEDPAE FT LNVGQLVQAHIEGGQLLLAAQLAASASERARVLGRRTVASHLLGLSVDIAQPLEHVNTS FT ALGRARVDESLLTAREYATCIRAASGASNHEISQELFLSPRTVEGHLQRSYAKLGITDR FT RQLLAERVATDAGVLQAAEDTLALPVFE" FT CDS 1809160..1809381 FT /transl_table=11 FT /locus_tag="AARI_15800" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VVZ6" FT /protein_id="CBT75799.1" FT /translation="MIEVEMVVGERQRRCVFVNMRCIRCFRDGDGPAVSDGSGDQDLGN FT AGSKLLRDLEEFRASQKLVLCDGATKCQ" FT tRNA complement(1809551..1809626) FT /locus_tag="AARI_36820" FT /product="transfer RNA-His" FT /anticodon=(pos:1809591..1809593,aa:His) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS 1809995..1810411 FT /transl_table=11 FT /locus_tag="AARI_15810" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VTN1" FT /protein_id="CBT75800.1" FT /translation="MSTVGVTREEIRDYVHQYNLQPHGTRTAWLQQQPFSRATFYRWNQ FT LVFEGDLDRNLVPRDHGQMNTTPSQRSAFEQARAKEQAEHEDELKALRERVRQLEGTNE FT ALGKAIGLLHALNEQEPATSTTDERKNSSPRKTN" FT gene 1810663..1811427 FT /pseudo FT /locus_tag="AARI_35230" FT /product="partial transposase of IS3 family" FT /function="4.5 Transposon and IS" FT tRNA complement(1811776..1811851) FT /locus_tag="AARI_36830" FT /product="transfer RNA-His" FT /anticodon=(pos:1811816..1811818,aa:His) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(1812011..1812622) FT /transl_table=11 FT /gene="orn" FT /locus_tag="AARI_15820" FT /product="putative oligoribonuclease" FT /function="3.6 RNA modification" FT /EC_number="3.1.-.-" FT /note="exoribonuclease specific for small FT oligoribonucleotides. Belongs to the oligoribonuclease FT family" FT /db_xref="GOA:E1VVZ8" FT /db_xref="InterPro:IPR006055" FT /db_xref="InterPro:IPR012337" FT /db_xref="InterPro:IPR013520" FT /db_xref="UniProtKB/TrEMBL:E1VVZ8" FT /protein_id="CBT75801.1" FT /translation="MASNSEKIVWIDCEMTGLDLVNDALIEVAVLITDSDLQIVDEGIQ FT VVIKPEPAALAQMDDFVRNMHMVSGLLPELENGIAMDEAQRLVIDYIKKHVPEPNKALL FT GGNSVGTDKNFLARDMPEVIEHLHYRIIDVSTLKELSRRWFPKAHYSAPAKTGNHRALG FT DIQDSINELRYYRDAIMVPAPGPTSDEARKIATEISQNAG" FT CDS 1812835..1814358 FT /transl_table=11 FT /locus_tag="AARI_15830" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="11 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VVZ9" FT /protein_id="CBT75802.1" FT /translation="MSASKPAVSSPPYAGVNRTILSGVIGSSLILFGSFGTGWLASVSP FT LNRDPFFIMLRTEPAGVITCVVLLALGCWILFRSWWRLGQKLKGWGEGSLTVVRKAVWL FT WSIPMLVTLPIMSRDVFAYIGQGRLVDAGQDPYVDGISSLNNWFQLGTDTMWAQDGTPY FT GPLYLSIEWLVVNIVGGSTDVAILVFRAIAFIGVLLCLHFVPKLAELHAVPGAKATWMT FT VVNPLFLVNFVASAHNDSLMTGLAVWSVYLACKRYGFWAIVVLAASVGVKPITLVLLPF FT IGLLWAGPEAKWPRRILYWFYTGMLFLALMTFVGWLNGYWFGWLSVMLNYTGAGFSIYA FT PLGLATIGIQNIFNSFGLESGGVLDVVKTAGRLVGVAIAFILMFRGKYSHLVQRMAIAF FT AAIVVLSPVIQPWYLLWLLPFFAVTGLRDDWQMLWLHLTTIFFLAYQAADQIFVWQFLQ FT ESLVPRIQMISWCISIACAVYLVFFDPKTKNICPDLLSSTNWLKRTKEA" FT CDS 1814358..1815839 FT /transl_table=11 FT /locus_tag="AARI_15840" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="12 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VW00" FT /protein_id="CBT75803.1" FT /translation="MEVQERKLEANRLSLRSLAWQGFSASALVTIASWGVGWFPRNQLS FT PLARTGFFIEFRTDAIGVISCIVLMALGIVWLTRCWILARPWVQTAGEITGRQLARILA FT MWSAPLMLSFPILSRDVYSYLAQGRMLHADKSPYAEGISALPGWFDGGSDGLWAQSPSP FT YGPFFLVMARIIFFASNGIPEVGVGLLRIIAALGVWGCYHFTAKLAQKMGQSADWANWA FT IVGNPLFLLTMIGGVHNDALMIAGVFSAFAYAYDRRPIAATMALAIAVSVKPIVLLALP FT FIGLILLGKNPTMRQRWKIWAKVAAMSLTWLLLIGAVTNLWFGWLLAMFTAGDAAFPYA FT PVGLIGWLVSNLAGALGGDISLVNSIVVGIFQVIALIIIARLALAKDISNPVRLAAWAL FT SAAVLLAPIIQPWYILWLMALFAISHRVSWGSEKLMIHVSSVILVAVFVDQLSIEQWHS FT AWIMKSLAGVLALGLFIGLFTADRKTRHVLRGPKA" FT CDS 1815897..1817000 FT /transl_table=11 FT /locus_tag="AARI_15850" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="9 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR006976" FT /db_xref="InterPro:IPR010432" FT /db_xref="UniProtKB/TrEMBL:E1VW01" FT /protein_id="CBT75804.1" FT /translation="MQTMFWPATIAILGGALFLGAAGIFLLAVQYRRHGRLSWRRTITT FT SMAAVYGFGLFSYTMLPLPETRDAYCRPGVAIPQLVPGRFLDDFKATIVERGLTGFATS FT FTLWQVLFNIILFMPLGILAVRWLRSNIFTGLILGFAASLAIELTQYTGIWGLYTCAYR FT VADVDDLIVNTTGALMGAIIAYLPIFKFLSGPVEADAATAPARAVTRSRRILANIFDAA FT ITTGVLFGVTGAVELLERLGGPVLDAQWKNFWIPLIVVAFTFWLPSLAPGRASLGQRCA FT WLMLTDGQGNPASASRALLRSLLGFGGINFLFHISTNLGEITAYPLLNMLLVIYIALSA FT FYFIFEANHRGLAGKISSTGFIDRRAL" FT CDS 1817131..1817907 FT /transl_table=11 FT /locus_tag="AARI_15860" FT /product="putative phage excisionase" FT /function="4.4 Phage-related function" FT /note="similar to putative excisionases from Mycobacterium FT phages" FT /db_xref="InterPro:IPR021235" FT /db_xref="UniProtKB/TrEMBL:E1VW02" FT /protein_id="CBT75805.1" FT /translation="MEDKKPEIPAEPHRAVLGTAVGATVLIAVGAFVLSFAALTDLAER FT SGISPRLAWIWPIIIDGMIVAATVAIVALNGFNRKAMIYPWSLLFFGAIVSTAANSTHA FT ILTVDSIENGVPPLVSALVAAMPPIVLLAITHLTVHMYQKKSEAAKLRAELEYDEAQEN FT AEKYGVAYDDGYNAALTDTKTAEDERLSQLEQEHQDALARARAEGIAAGRSDSKVTPIK FT SSAQPAPAKPAKAATAQPGEDKAPLFDDMAKRLSRP" FT CDS 1817991..1819091 FT /transl_table=11 FT /locus_tag="AARI_15870" FT /product="RelA/SpoT domain-containing protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF04607. This region of unknown function is FT found in RelA and SpoT of Escherichia coli, and their FT homologues in plants and in other eubacteria" FT /db_xref="GOA:E1VW03" FT /db_xref="InterPro:IPR007685" FT /db_xref="UniProtKB/TrEMBL:E1VW03" FT /protein_id="CBT75806.1" FT /translation="MMDPAQGQEHDEFSEQIAAAVEQYKSVTGELNTVMSAMKAKIRRL FT FANSEVQPLFITGRVKSPQSFAAKASRQLKENSETAPVLEFPNPLREIHDMVGIRIIVM FT LPHEIQQVASLIKSHRDSFDCRSDREKDIGSVESGTYGYSSRHLLLKTRSEPIVRKFQE FT ALGKPVVASGNFVFEVQIRTVLQHAWSEMEHDIRFKHPGEAAWNPQIDRHFTATAAMLE FT TVEDYFTDIDELYHRLNGYHDQQGAGSEPLTGEKIGEIWQTLLPHVDRKRDDDWSWAAE FT LLGSHGIDQTWQLAQLLDANVVTDVRAALDHRYSPGPDRLLDDVLLWRFGKDHIDKTSG FT GDLRREASLRRRLIQMMDYRSQPSTK" FT CDS 1819284..1820885 FT /transl_table=11 FT /locus_tag="AARI_15880" FT /product="putative drug resistance ATP-binding protein" FT /function="4.2 Detoxification" FT /note="TCDB: ATP-binding cassette (ABC) superfamily, FT (putative) drug resistance ATPase-2 (Drug RA2) family (TC FT 3.A.1.121.z). ABCISSE: fused ATP-binding protein (ABC2), FT ART-family, ARE-subfamily (antibiotic resistance)" FT /db_xref="GOA:E1VW04" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR017871" FT /db_xref="UniProtKB/TrEMBL:E1VW04" FT /protein_id="CBT75807.1" FT /translation="MISVANLELRVGARLLMDEVNFRIDKGDKIGLVGRNGAGKTTMTK FT VLAGETQPAAGEVTFKGSIGYLPQDPKTPDMEQLARNRILGARGLDVVVTKLAQNREEM FT ASEDPAVSAKAMRRYDRLEAEFIAAGGYAAESEAAAICANLDLPDRILDQPLRTLSGGQ FT RRRVELARILYSDAETLLLDEPTNHLDVDSIMWLRDFIKNYAGGVLMISHDTGLMESTV FT NKVLNLDANRGVVDVYNMNWKRYKLQRETDERARKRERANIEKKASVLLTQANKMKARA FT SGASAAQSMLKRVDRMLSGLQEERASDKVAALRFPDPAPCGKTPLMAEGLSKAYGSLEI FT FNDVSLAIDRGSKVVILGLNGAGKTTLLRMLAGVSEPDTGKIIPGHGLKIGYFAQEHDT FT LDPEASVLDNMRRNAPDHLNDADVRSILGSFLFVGDDVTKPAGVLSGGEKTRLALATIV FT ASSANVLLLDEPTNNLDPASRAEVLGALSTFPGAVVMVSHDEGAVMSLQPERVVILPDG FT DEDLFSEDYLELVSLT" FT CDS 1820992..1821399 FT /transl_table=11 FT /locus_tag="AARI_15890" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VW05" FT /protein_id="CBT75808.1" FT /translation="MALLAASTLAGCSSQVPDEVNAQWTLIDPAGVNESSTSLQLGVMA FT IACTSGTTGEITATDVELSNDQIVIGIAVEPAEGDTHTCPGNETVPYTLELDEPVGDRT FT LIDASCLEGIGQKTTACQDGGIRWSPPAEQS" FT CDS complement(1821473..1822384) FT /transl_table=11 FT /locus_tag="AARI_15900" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0. FT Signal peptide predicted by SignalP 3.0 HMM (probability: FT 0.652) with cleavage site probability 0.343 between FT position 21 and 22" FT /db_xref="GOA:E1VW06" FT /db_xref="InterPro:IPR002994" FT /db_xref="UniProtKB/TrEMBL:E1VW06" FT /protein_id="CBT75809.1" FT /translation="MYRFLASTRWVGWLVLVAIFAAACISLGNWQSDRRTEVLEGIERV FT NRNYFAEPVTGKQALENFEHLDEQKIWITAELTGEYLAEDTMIVRNRIKAGRPGYEVLV FT PFKTEQGTTVIVDRGYLPIGNKEGGHPDTVPAPPTGKVNVDVRMKPAEIRLDRGAPEGQ FT LASIQLEDYAKHLDYPIAQGAYGLMYEEDPAPATSPLQLDAPDMDEGPHLSYEIQWYIF FT GVLAFVGFWYAARQQKKLNAEDAAERAEAEALGLEEPMHKVRKIRIKADKKVRRDGTLT FT DEAIEDALLDQAENTPGGHKQQ" FT CDS complement(1822385..1822630) FT /transl_table=11 FT /locus_tag="AARI_15910" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VW07" FT /protein_id="CBT75810.1" FT /translation="MDLLGSLGGSSAAPEIQCSRKGCRNAADYQLLWNNPKIHTPERRK FT IWLACQEHRDWLETYLKERLLYKETLPMAGNEGERN" FT CDS complement(1822630..1823085) FT /transl_table=11 FT /locus_tag="AARI_15920" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="2 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR021449" FT /db_xref="UniProtKB/TrEMBL:E1VW08" FT /protein_id="CBT75811.1" FT /translation="MGADPTVQSEVFYMSSQPTNHGSNRPEVHRITEARQSHTSERDIR FT VRKYTISMTVRLICFILAFFVDGWLRWVFLAGAIVLPYIAVVIANGGADLTKREPPAEF FT YKTPDARPIAAPEQTAPQEAQDPEVIDGNFIDDDASGPPTTSAPKED" FT CDS 1823263..1823985 FT /transl_table=11 FT /gene="fabG" FT /locus_tag="AARI_15930" FT /product="3-oxoacyl-[acyl-carrier-protein] reductase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.1.1.100" FT /note="catalyses the following reaction: (3R)-3- FT hydroxyacyl-[acyl-carrier-protein] + NADP(+) <=> 3-oxoacyl- FT [acyl-carrier-protein] + NADPH. Is involved in fatty acid FT biosynthesis" FT /db_xref="GOA:E1VW09" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VW09" FT /protein_id="CBT75812.1" FT /translation="MTTEPTTGRSVLVTGGNRGIGLAIARAFEANGDKVAITYRSGEVP FT AGLLGVKADVTDSESIDAAFKEVEAAHGPVEVLVANAGVTKDTLLLRMSEDDFTSVIDT FT NLTGAFRVIKRASKGMIRLKRGRVVLISSVVGLYGSPGQINYAASKAGLVGIARSLTRE FT LGSRGITANVVAPGFINTEMTAVLPEDTQKEYLSNIPANRFAEPEEVANVVRWISSNEA FT AYISGAVIPVDGGLGMGH" FT CDS 1824020..1824769 FT /transl_table=11 FT /locus_tag="AARI_15940" FT /product="short-chain dehydrogenases/reductases family FT protein" FT /function="2.4 Metabolism of lipids" FT /note="identified by match to PF00106. The short-chain FT dehydrogenases/reductases family (SDR) is a very large FT family of enzymes, most of which are known to be NAD- or FT NADP-dependent oxidoreductases. Possibly involved in the FT metabolism of lipid" FT /db_xref="GOA:E1VW10" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VW10" FT /protein_id="CBT75813.1" FT /translation="MSEFKGGIVTGSSRGIGAVTAQLLAEQGIGVVVNYRAKAPRANKI FT VASIEEKGGKAVAVGADLTTVEGPQALVDAAVENFGSLDVVVLNASGGMETSMGENYAL FT RLNRDAQVAMLEAALPKLSEGGRVVFVTSHQAHFINDVSTMDAYDAVAKSKRAGEDALR FT EMIPKLAEKNITFVVVSGDMIEGTITATLLNRMEPGAIDARREAAGKLYSVEEFGAEVA FT KMVFADVETGHTELVGGAGDFLKASGN" FT CDS 1825092..1825508 FT /transl_table=11 FT /locus_tag="AARI_15950" FT /product="hypothetical protein" FT /function="5.1 Protein of unknown function similar to other FT proteins from the same organism" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.997) with cleavage site probability 0.464 FT between position 32 and 33" FT /db_xref="UniProtKB/TrEMBL:E1VW11" FT /protein_id="CBT75814.1" FT /translation="MNLRRTCRIAAVSLVLPLALAAVGCSAVHEETCDGGWPVSDPQTA FT VQGLLEAAESSDYEKACSVISLKLDDEAIEEHLTPLKSEMDSKQVSSSNFKMHKYERGG FT SAHFYNVYAEQPEMAIDIVVVNVGKGYRVAFGEE" FT CDS complement(1825639..1827387) FT /transl_table=11 FT /locus_tag="AARI_15960" FT /product="VanW-like protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF04294: VanW, VanW like protein. Family FT members include vancomycin resistance protein W (VanW). FT Genes encoding members of this family have been found in FT vancomycin resistance gene clusters vanB and vanG. The FT function of VanW is unknown" FT /db_xref="InterPro:IPR007391" FT /db_xref="InterPro:IPR022029" FT /db_xref="UniProtKB/TrEMBL:E1VW12" FT /protein_id="CBT75815.1" FT /translation="MQTPSPDSSSTTPTHSPQDKKKPKSKAKPWIITGSCVAAIAAAYF FT GGAAYVSSQVPANASIAGVNIGSMNKDQARSELEREVLPLAEKDIDVTVNGEKYTLDPA FT KAGLALNVDETINDLTSYEINPVELYERLTGDVHVDPAVDVDQEMLSTQLEALAKKANA FT ELAEGAIEFKDGTAKLTKPIDGVVLKADEAASLITDEWEIAGPALTLPAEVTKPKISAE FT SLQAFYDKDIKALLKDDVTLSSDKKKATISVESIVAAASYTPKDGAPAITLDDKKLYKA FT ATKNSDLSSTAENAKIVLKDGKPSIVKSSKGVSLETEGLGAKVLAATADKKRTATVEMT FT ETEAEFTTADAKKLGIKEPIVTFSTPYPASDKVRTKNLYAGSARVNGDIIKPGERFSLL FT EALGPITVANGYFSSGVVESGFSTEAVGGGLSQISTQMYNVGFLAGYDDITHKPHSRWF FT ERYPAGREATLWEGQIDMIWENNTPYGVMIQAWVSGDKVNTRLWSTKYWDVSQKSSGKY FT NLTNPETKYNPAEKCVSESGGKKGFSIDITRYRETFDGSKKLPAETKSWTYSPWHKIVC FT GEKPKD" FT CDS complement(1827550..1828470) FT /transl_table=11 FT /gene="serB" FT /locus_tag="AARI_15970" FT /product="phosphoserine phosphatase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="3.1.3.3" FT /note="responsible for the third and final step of the L- FT serine biosynthetic pathway" FT /db_xref="GOA:E1VW13" FT /db_xref="InterPro:IPR004469" FT /db_xref="InterPro:IPR006383" FT /db_xref="InterPro:IPR023190" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:E1VW13" FT /protein_id="CBT75816.1" FT /translation="MASSLVFVSRPALSRTDFIAVLQQAAAQGLISKADENSIKTSGQR FT LVAKFQIEQANHPQLQQAAAEFVDALVAGGSLDYADLCLAAVPAELTNAPQLLLLMDVD FT STLIKQEVIELLAAHAGREKEVAAVTEAAMRGELDFAQSLIQRVATLKDLPDTVLVEVG FT KRIIFSEGAQSLVQRFHAAGHKVGVVSGGFQQILDPLAAQLDLDHALANTLGITDAVLD FT GTVHGQIVDREMKETMLRGWAEEHQIPLEATIAAGDGANDLAMVAASGLGIAFNAKPAL FT RNEADVRLDFAWLDVIADLVLDDLA" FT CDS 1828651..1829445 FT /transl_table=11 FT /locus_tag="AARI_15980" FT /product="putative ABC transporter, ATP-binding subunit" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /EC_number="3.6.3.-" FT /note="TC 3.A.1.y.z. ABCISSE: ABC transporter, ATP-binding FT protein (ABC), YLU-family (unclassified systems)" FT /db_xref="GOA:E1VW14" FT /db_xref="InterPro:IPR003439" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:E1VW14" FT /protein_id="CBT75817.1" FT /translation="MNTMSEVLTFKDVSVVRGRKDLLKDVSWEVKEGQRWIVIGPNGAG FT KSTLMNIAATRLHPTRGTADILGERLGKVSVFDLRPLIGLSSALVANSIPANETALNVV FT LTAAYGMTGRWREKYEKLDERRAFHLLHNWGMSTFMNQPFGKLSEGERKRVLIARALMT FT DPELLILDEPAAGLDLAGRESLVGKLAELAADEDAPALVLVTHHLEEVPAGFTHIMMMR FT DGQVVAAGEIESTLNEANLEATYGMALSLRHEGGRYSAFARS" FT CDS 1829475..1830272 FT /transl_table=11 FT /locus_tag="AARI_15990" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="8 transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VW15" FT /db_xref="InterPro:IPR002781" FT /db_xref="UniProtKB/TrEMBL:E1VW15" FT /protein_id="CBT75818.1" FT /translation="MIEFWREALVFLGGLWAGTINTVVGSGTLVTFPILVALGTAPVNA FT VVSNAMGLVAGGFSGAWGYRREAASVRKTLLKLVPVSLVGGLIGSLLLLNLPESVFGVV FT APVLLVCALVLVIFQPRLSKWAETRQAASGGTDPDDADRAKIPLILYILVFIIGVYGGY FT FTAAQGVLLMAVFGVFLHASLQQSNAIKVILSLIVNLVAAAMYLVIAPERIHWIIVLLI FT AVGSLIGGFVGAKIGRKLSPGLLRLVIVILGLVALGNMLYKLV" FT CDS 1830277..1831110 FT /transl_table=11 FT /locus_tag="AARI_16000" FT /product="putative RNA methyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.-" FT /note="identified by match to protein family PF00588: SpoU FT rRNA Methylase family. Possible role in rRNA modification" FT /db_xref="GOA:E1VW16" FT /db_xref="InterPro:IPR001537" FT /db_xref="UniProtKB/TrEMBL:E1VW16" FT /protein_id="CBT75819.1" FT /translation="MPEILNPERIMQVADLSDARLDEYLRLSEAHLRMRTDVENGLYIA FT ESTKVVQRAINAEHVPRSFLLAEKHLDQLVEEFNRFPDAPIFIGDDRQLEDLVGFHLHR FT GAMASMNRPEPLDLSQVLEASSRVAILEDIADHTNLGAIIRSASGLGVDAVLLTPKCVD FT PWYRRSARVSMGTVFDLPWVRMLSWPEDIRTLKQHGYQMLAMELTDDAIPLNEVQITAG FT QKVAMILGNEGRGVTAQALEAVDQTVIIPMHREVDSLNVGAASAIAFWHLCSAPR" FT CDS 1831257..1831514 FT /transl_table=11 FT /gene="rpmE2" FT /locus_tag="AARI_16010" FT /product="50S ribosomal protein L31 type B" FT /function="3.7.1 Ribosomal proteins" FT /note="part of the 50S ribosomal subunit" FT /db_xref="GOA:E1VW17" FT /db_xref="InterPro:IPR002150" FT /db_xref="UniProtKB/TrEMBL:E1VW17" FT /protein_id="CBT75820.1" FT /translation="MKADIHPQYGPVVFNDLASGEKILTRSTAKSDKTIEWEDGNTYPV FT IDVEISAASHPFYTGKQRIMDTAGRVERFNARFKGFGGKK" FT CDS 1831652..1832707 FT /transl_table=11 FT /gene="lplA" FT /locus_tag="AARI_16020" FT /product="putative lipoate--protein ligase" FT /function="2.5 Metabolism of coenzymes and prosthetic FT groups" FT /EC_number="2.7.7.63" FT /note="catalyses the formation of an amide linkage between FT lipoic acid and a specific lysine residue in lipoate FT dependent enzymes. Lipoylation is essential for the FT function of several key enzymes involved in oxidative FT metabolism, including pyruvate dehydrogenase (E(2) domain), FT 2-oxoglutarate dehydrogenase (E(2) domain), the FT branched-chain 2-oxoacid dehydrogenases and the glycine FT cleavage system (H protein)" FT /db_xref="GOA:E1VW18" FT /db_xref="InterPro:IPR004143" FT /db_xref="InterPro:IPR019491" FT /db_xref="UniProtKB/TrEMBL:E1VW18" FT /protein_id="CBT75821.1" FT /translation="MMHHGEYKVVGGKLVVVDLDTADGVITDVSLNGDFFLEPDDALED FT LNDALRGLPVDASNSTIRDAVNQNLREGAVMFGFDADAVARVVRRALGHATKWEDHEWE FT ILAPEIIPITEQVALDEVLTRQIAKGTRKPTIRFWDWNEGAVVIGSFQSLKNEVDMEQA FT NKHGIQVVRRISGGGAMFMEAGNCITYSLYAPESLVDGMSFADSYPFLDAWVMEALESI FT GLKAHYKPLNDIATPAGKIGGAAQKRLANGAMLHHVTMSYDIDAQKMTDVLRIGREKIS FT DKGIASAVKRVDPLKSQTELERMEIIEIMMDTFAKRTGATRTQLDEASRKDAQELAETK FT FATEKWTARVP" FT CDS complement(1832720..1833475) FT /transl_table=11 FT /locus_tag="AARI_16030" FT /product="metallo-beta-lactamase superfamily protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to PF00753: metallo-beta- FT lactamase superfamily. Apart from the beta-lactamases, a FT number of other proteins contain this domain. These FT proteins include thiolesterases, members of the glyoxalase FT II family, that catalyse the hydrolysis of S-D-lactoyl- FT glutathione to form glutathione and D-lactic acid and a FT competence protein that is essential for natural FT transformation in Neisseria gonorrhoeae and could be a FT transporter involved in DNA uptake" FT /db_xref="GOA:E1VW19" FT /db_xref="InterPro:IPR001279" FT /db_xref="UniProtKB/TrEMBL:E1VW19" FT /protein_id="CBT75822.1" FT /translation="MPHQFHITEHAQGTYMVEGPASNWIILEDNGVYTVIDGGYPGDVP FT LVLDSIRRLGLSVKDAAAMLITHGHVDHTGAAAYFASELCVPVLSSHAEHTQMTGEERF FT QVSPVQILVRAWQPRVFKWMRHVLTVGGTEGTKVLEAKIWTTQQLAALPGAPVAVPTPG FT HTPGHSAFHLPDAKVLISGDALISGHALSTTTGAQMLHPMFHHERQQAYQALTAFDGLD FT ADSILPGHGKALHCQPAEAVHAALARNPR" FT CDS complement(1833631..1836276) FT /transl_table=11 FT /gene="pepN" FT /locus_tag="AARI_16040" FT /product="membrane alanyl aminopeptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.11.2" FT /note="catalyzes the removal of single amino acids from the FT amino terminus of small peptides" FT /db_xref="GOA:E1VW20" FT /db_xref="InterPro:IPR001930" FT /db_xref="InterPro:IPR012778" FT /db_xref="InterPro:IPR014782" FT /db_xref="InterPro:IPR024571" FT /db_xref="UniProtKB/TrEMBL:E1VW20" FT /protein_id="CBT75823.1" FT /translation="MDTLERYAPNENLRRDEAAWRAQNIDWHFAEIQLDVSNATDSSAS FT GYSSITTLNFSSKRAETFIDFIHESVDEVLVNGTAVDLDSAVLDARIYLDNLRTDVPNT FT VKITGTALYSRSGEGLHRFVDPQDGQTYLYTQFEPSEARRVFACFEQPDLKTSYRFTLT FT GPAAWHLASNQPIVDEVLHDNGTKTVACAPTPPISSYITAVLAGPYHVVRGEHIQKLED FT GEELSIEMAATCRASLAKHFDGEEIIKLTSQGLDYYHLLFDYPYPWGKYDSAFVPEYNL FT GAMENPGLVTFTERYVFTSQATEAQHEQRANTLMHEMAHMWFGDLVTMKWWDDLWLKES FT FADYIGTLANDEATDFTTAWTTFAARRKAWAYVADQMPTTHPIVADIPDLLAADQNFDG FT ITYAKGASVLKQLAAFVGADAFRDAARAYFRKHAYSNTSLDDFLEALETASGRDMGAWA FT EAWLKTSGVPKLHVQYDTDEAGTITAASLIQSGTDPVTGEKIARPHVLSVGAYQLADGK FT LSRSDSARVELAGESAALDFLVGSKVPDLVLPNDGDETYALIEFDQVSRATLLAHLSGL FT TDSLPRATCWASLWDAVRSATLDAQSYVQAILDHAHTVTDAGVFGVLTDQLITSISKYA FT APELRAELRTRAAGVLTGWLTEFESGSDQQTTTARTLARLARAGVAGQVIDAFLGEQPN FT QYQVTVDEQLLWASYIALAAAGRLDEAAEARMHEAAKAKPTSVALNAVRTALAARPDAQ FT VKETAFDTVLMARDEQGELSNDALSATALGFTMGSAALLAPFEQRYWAAVLPVFETMGM FT EFATRVIEGLFPGHQDLDGAVEQNQALAASTNWLERHEGAPTALKRILLEERAELERSL FT KAQAYSRTRG" FT gene 1836357..1836530 FT /pseudo FT /locus_tag="AARI_16050" FT /product="putative N-acetylmannosamine-6-phosphate FT epimerase fragment" FT /note="possible C-terminal fragment of a N- FT acetylmannosamine-6-phosphate epimerase" FT CDS 1836605..1837165 FT /transl_table=11 FT /locus_tag="AARI_16060" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VW21" FT /protein_id="CBT75824.1" FT /translation="MDVFIKGPSKRDVAGMKAAFGEVAAGDVISVLYKTTRFGNFLITG FT AAHATVLDDVMVGGLNAAAAKKKAKDADGGETMARQPDKDVRAFPAVFEGEFAPEDIEV FT SELSHGDLVVASFSQEPYGDFVITGVVTEAENDRSYLMVGPWILQTAEEAAPRLLSVQR FT VAANGTHVAPVPTLRGLVEVDGL" FT CDS 1837411..1837902 FT /transl_table=11 FT /locus_tag="AARI_16070" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VW22" FT /protein_id="CBT75825.1" FT /translation="MDKVMDSIGQLRSSRKFNWFNATELDALLEEEVAPEEIWWGTSRH FT DELHKLESVAQIPSILRMVLEWGENYSFENDPMTKYAQGTKLVDGNYTLELAVVGHQAC FT NIRIGYGADPDCLSSHPDADVEFESPQSLSIAQVTEVLGQWLLGRGLPSGYGGSIHIYG FT " FT gene 1838080..1838496 FT /pseudo FT /locus_tag="AARI_16080" FT /product="truncated protein" FT /note="section of a conserved protein" FT gene 1838500..1838793 FT /pseudo FT /locus_tag="AARI_16090" FT /product="truncated protein" FT /note="section of a conserved protein" FT CDS 1838790..1839728 FT /transl_table=11 FT /locus_tag="AARI_16100" FT /product="putative dihydrodipicolinate synthase family FT protein" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /note="this family comprises several pyruvate-dependent FT class I aldolases that use the same catalytic step to FT catalyze different reactions in different pathways and FT includes such proteins as N-acetylneuraminate lyase, MosA FT protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o- FT hydroxybenzylidenepyruvate hydratase-aldolase, trans-2- FT carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3- FT deoxy- gluconate aldolase. The family is also referred to FT as the N-acetylneuraminate lyase family" FT /db_xref="GOA:E1VW23" FT /db_xref="InterPro:IPR002220" FT /db_xref="InterPro:IPR013785" FT /db_xref="UniProtKB/TrEMBL:E1VW23" FT /protein_id="CBT75826.1" FT /translation="MTLAAKSTAGPATAWTGLSAFPLTPLRDDRLDEAAFIGLVQRLAR FT AEVDSITVLGSTGSYMYLDRAERRRVIELAVQHADRIPVLAGVGALRTSRVLEHIDDAR FT IAGAVGVLLAPVGYQPLNDDEVFALFKAASEHSDVPVIVYDNPRTTHFSFSNRLYGRIA FT QLPGIVSIKIPGVPADPVKAKEHVAAIRAVLPEHVGIGVSGDALGAAGLIAGCNAWFTA FT VGGTIPGPMVGITRAVQEGDPKKALAISARLEPLWELMAQCGGSLRISAAIAEHFGWVA FT ENCLPLPVQAVSPKQRELVAKVVADLSLGAS" FT CDS 1839823..1840269 FT /transl_table=11 FT /locus_tag="AARI_16110" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF00903: FT Glyoxalase/Bleomycin resistance protein/Dioxygenase FT superfamily" FT /db_xref="UniProtKB/TrEMBL:E1VW24" FT /protein_id="CBT75827.1" FT /translation="MPRIIRFDHIGVTVSDLDLVTEFFTSLGLEIEGRANGLEGEFLET FT VCAVPDSRTNIVMLKAPGTDVGIELSSFEKPGHLPGNPKVMANELGLRSIAFEVDDLDA FT ILNQLAADGYGLVGGVGQYQGAWKMAYVRGPEGIIVALAQRLDD" FT CDS complement(1840328..1842343) FT /transl_table=11 FT /gene="aco" FT /locus_tag="AARI_16120" FT /product="acyl-CoA oxidase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.3.3.6" FT /note="identified by similarity to potein SP:Q33DR0 FT (Arthrobacter ureafaciens). Catalyzes the oxidation of FT acyl-coenzyme A (acyl-CoA) thioester to the corresponding FT trans-2-enoyl-CoA thioester: acyl-CoA + O2 --> trans-2- FT enoyl-CoA + H2O2. Probably involved in beta-oxidation of FT fatty acids" FT /db_xref="GOA:E1VW25" FT /db_xref="InterPro:IPR002655" 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:IPR012258" FT /db_xref="InterPro:IPR013786" FT /db_xref="UniProtKB/TrEMBL:E1VW25" FT /protein_id="CBT75828.1" FT /translation="MSENRINVNALSEQLFGPYAEIRKASRARAADPQLQRDPLLGMDE FT HRERVLGQLGILVQQEAVQRAFPTEFGGQNDHGGSIAAFEELVAADPSLQIKAGVQWGL FT FAGAILHLGSEEHHKAWLPGAMNLDTPGAFAMTEIGHGSDVAAVATTATYDEATDEFVI FT HTPFKAAWKEFLGNAALHGKAATVFAQLITKGVNHGVHCFYVPIRDEAGNFLEGIGGED FT DGLKGGLNGIDNGRLHFTNVRVPRTNLLNRYGNVDETGTYSSPIPSPGRRFFTMLGTLV FT QGRVSLDGAATNASKIALQIAITYGNQRRQFNSTSDTEETTLLDYQRHQRRLITRLART FT YAASFAHDGLLEKFDAVFSGREDTDTDRQDLETLAAALKPLSTWDALDTLQEAREACGG FT AGYIAKNRFTQLYADLDVYVTFEGDNNVLLQLVGKRLLTDYAAEFRKLDTGAMALYVAK FT QVGTTALHRSGLRSVGQAFADISDERKSANFFKDPDNQRALLTGRIKAKVAEVAGALRT FT AGKDKAKGAAAFNENQDLLISAARDHGQLLRWEAFTAALENTSDAATKEVLTWLRDVFA FT LSLIEDDLGWYLSNGLLSMQRARTLPGYLNRLLARLRPHAQDLVEAFAYTQDHLRADIS FT SGGEAERQDEAMEYFRKLRASDDAPISEKSLQKPKG" FT CDS complement(1842390..1843049) FT /transl_table=11 FT /locus_tag="AARI_16130" FT /product="TetR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF00440: bacterial regulatory FT proteins, tetR family" FT /db_xref="GOA:E1VW26" FT /db_xref="InterPro:IPR001647" FT /db_xref="InterPro:IPR009057" FT /db_xref="InterPro:IPR015893" FT /db_xref="UniProtKB/TrEMBL:E1VW26" FT /protein_id="CBT75829.1" FT /translation="MNKITEEIDRETDGRAARWEAHRTARHEELLKLARKAVHKLGPQV FT SMEDIAGHAKTSKPVYYRYFGDKEGLRQALSAMVINDFRKRVIAAGQAKEDEGSALHAM FT VSAYLELATNSPNLYFFVTSAPRSAEDEAAGALTTFFEEASALISERLLRLYDQQATTA FT TLDLWPRAALGMVRAAGERWLRQPDSEQKPSLESLAEELTNWLAYGIASTNAPTTR" FT CDS 1843125..1844420 FT /transl_table=11 FT /locus_tag="AARI_16140" FT /product="acetyl-CoA C-acyltransferase" FT /function="2.4 Metabolism of lipids" FT /EC_number="2.3.1.16" FT /note="acetyl-CoA C-acyltransferase (also named 3-ketoacyl- FT CoA thiolase or thiolase I) has a broad chain-length FT specificity for its substrates and is involved in FT degradative pathways such as fatty acid beta-oxidation" FT /db_xref="GOA:E1VW27" FT /db_xref="InterPro:IPR002155" FT /db_xref="InterPro:IPR016038" FT /db_xref="InterPro:IPR016039" FT /db_xref="InterPro:IPR020616" FT /db_xref="InterPro:IPR020617" FT /db_xref="UniProtKB/TrEMBL:E1VW27" FT /protein_id="CBT75830.1" FT /translation="MSQPSVRNAVIIGGNRIPFARSNTAYVNASNQDMFTAALEGLVAR FT YGLQGQRIGAVSGGAVLKHSKNFNLIRESVLGSSLDHATPAYDVQMACATGMEAIGSLA FT NKIKLGQLDSAIGGGVDTTSDAPIAVSDSLRAILMELSRARSTKAKLAALAKLRPGHLA FT PAAPGTGEPRTGLSMGDHQAITTKKWGISREAQDELALASHKNLAAAYDRGFFNDLITP FT FNGLAKDNNLRADSSMEKLGKLKPAFGKNLGEAATMTAGNSTPLTDGASAVLLGSEEYA FT QANDLPMLANFVDFEAAAVDFVHGEEGLLMAPAYATARMLKRNNLTLQDFDFYEIHEAF FT AGTVLSTLKAWEDEEFCREKLGLDAPLGAIDRSKLNVNGSSLAAGHPFAATGGRIIAST FT AKMLHEKGSGRALISVCAAGGQGVVAILEARN" FT CDS 1844420..1845757 FT /transl_table=11 FT /locus_tag="AARI_16150" FT /product="short-chain dehydrogenases/reductases family FT protein" FT /function="2.4 Metabolism of lipids" FT /note="identified by match to PF00106. The short-chain FT dehydrogenases/reductases family (SDR) is a very large FT family of enzymes, most of which are known to be NAD- or FT NADP-dependent oxidoreductases. Possible 3-hydroxyacyl-CoA FT dehydrogenase (EC 1.1.1.35)" FT /db_xref="GOA:E1VW28" FT /db_xref="InterPro:IPR002198" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VW28" FT /protein_id="CBT75831.1" FT /translation="MADKYMELVNTGLTKKLATMLGLPRPPRLRRYSPDAALLPGPVLI FT LGASAKAQDLSDTLVSWGLDVRRHDAGDAKLGALVLLLDELERPTDLSPLMLAAGQAVR FT KLLPGARVVAISRETTDEDAPALAAVRQGIDGAVRSLGREMRGGATANGIVLAEGTHVA FT SPSALAAVRFFFSGRSAYVDGQFLNVRTNDGVLPADFAKPLAGKVAVVTGAARGIGAAI FT AKTLSRDGAQVVVVDMPQAGEALAKVANSIGATTLQLDVTAPDAGQQIMDHAIGRHGSL FT DLVVHNAGITRDKLLANMDAGRWDSVIAVNIASQLRMNEAFLAAKLPGLRIVSLASTSG FT IAGNRGQTNYAASKGGVIGMVHSSAKLFAEIGGSITAVAPGFIETEMTAKIPLGTRTVA FT RMVLPSLMQGGLPVDVAEAISFLGSDAAAGLNGQVLRVCGQSLVGA" FT CDS 1845758..1846618 FT /transl_table=11 FT /locus_tag="AARI_16160" FT /product="possible enoyl-CoA hydratase" FT /function="2.4 Metabolism of lipids" FT /EC_number="4.2.1.17" FT /note="match to PF01575 (MaoC like domain). Enoyl-CoA FT hydratase is involved in fatty acid metabolism. It FT catalyzes the hydratation of 2-trans-enoyl-CoA into 3- FT hydroxyacyl-CoA" FT /db_xref="GOA:E1VW29" FT /db_xref="InterPro:IPR002539" FT /db_xref="InterPro:IPR003965" FT /db_xref="UniProtKB/TrEMBL:E1VW29" FT /protein_id="CBT75832.1" FT /translation="MGAQIVTAIPSMASVYAKAVKTLNRKPKNPVLPDTVLVFQGAVAD FT PVKLSEYRKAVGAPMTGVLPSLYVHSLAFPLAMSLMVQDDFPLPLLGMIHLTNQVDVVA FT PLAEDEVFDIEVHSENLVAHAKGVTCDLVVRIVVDGQDRMLLRSTFLAKGMKLAGEAPQ FT QRTQVPFSAPQRTASWKLDAGTGRRWAAVAGDYNPIHLSALSAKALGMPAAIAHGIYLA FT ARALAGIEPAQGNYSWNIEFKTPVVLPASVDLAFAAQAEGFTVNAWHARKGKPHFELEL FT VRTES" FT CDS complement(1846682..1847866) FT /transl_table=11 FT /locus_tag="AARI_16170" FT /product="putative group 1 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /EC_number="2.4.-.-" FT /note="match to PF00534: Glycosyl transferases group 1. FT Proteins containing this domain transfer UDP, ADP, GDP or FT CMP linked sugars to a variety of substrates, including FT glycogen, fructose-6-phosphate and lipopolysaccharides. The FT bacterial enzymes are involved in various biosynthetic FT processes that include exopolysaccharide biosynthesis, FT lipopolysaccharide core biosynthesis and the biosynthesis FT of the slime polysaccaride colanic acid" FT /db_xref="GOA:E1VW30" FT /db_xref="InterPro:IPR001296" FT /db_xref="UniProtKB/TrEMBL:E1VW30" FT /protein_id="CBT75833.1" FT /translation="MRIAMLSLHTSPMQQPGSGDAGGMNVYIQNLSYALGALGHEVHMI FT TRTANESESLQVSEGVWMHQVQVAAEQKLSKEDLAQIIDPAVQEINAHLQGLKIDIIHA FT HYWLSGMVGLQLSAQWNVPLLVSMHTSAAAKEHESGISEPAERKSAETLLLAEAARIIA FT NTPVEAKQLARFYSVPAGKLDVVMPGVNHRIFHPNQDKLRRPLGEDDLHLIYAGRMQPL FT KGAHLLLEAMGIARREAPELRITASLFGALSGSTEYDLPALASAEELTDVVRFYDPLSP FT EKLALVFSNADVVAVPSLSETFGLVAAEAQACGTPVLANAVGGLSYAVHDGKSGWLMPE FT PDPQLWAAKLIELAREPEQITLAGHGALEHSGEFTWERAAVETLASYRMAKSQL" FT CDS complement(1847933..1848910) FT /transl_table=11 FT /locus_tag="AARI_16180" FT /product="putative prolyl aminopeptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.11.5" FT /note="prolyl aminopeptidase releases N-terminal proline FT from a peptide" FT /db_xref="GOA:E1VW31" FT /db_xref="InterPro:IPR002410" FT /db_xref="InterPro:IPR005944" FT /db_xref="UniProtKB/TrEMBL:E1VW31" FT /protein_id="CBT75834.1" FT /translation="MTSPAPQNADALHGLLPVAGGHHVYWEESGVPDGIPALHLHGGPG FT STLGAGGYRNRWDLARTRLIGLEQRGCGRSIPSAADAETSIHSFTTQQLIADIEELRIS FT LGIEKWILNGISWGSTLALAYAQAHPQRVIGMVLFAVTSTSREEVTWITETVGAIFPEA FT WDRLAGFAREHAPGYAAGSLRLVEAYAQLLNSDDLSLRDAASQQWALWEDTHISLGSEQ FT VIRDPRWQDQRLRHSLTRLTTHFWAHDGFCDPPLLENMAGIAHLPAVLIHGRSDISGPV FT RTAWRLHQALPNSELVICENDGHGGQSMVEHWNSANSKMLDLAS" FT CDS 1849016..1849135 FT /transl_table=11 FT /locus_tag="AARI_16190" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VW32" FT /protein_id="CBT75835.1" FT /translation="MKFSIIERSAAYFIDLMEPAEREIWESNVPKGALDTELA" FT tRNA complement(1849918..1850002) FT /locus_tag="AARI_36840" FT /product="transfer RNA-Leu" FT /anticodon=(pos:1849966..1849968,aa:Leu) FT /inference="ab initio prediction:tRNAscan-SE:1.21" FT CDS complement(1850231..1850875) FT /transl_table=11 FT /locus_tag="AARI_16200" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to PF03807: NADP oxidoreductase coenzyme F420- FT dependent" FT /db_xref="GOA:E1VW33" FT /db_xref="InterPro:IPR004455" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:E1VW33" FT /protein_id="CBT75836.1" FT /translation="MSIKRIGILGAGRAGTALARAAASAGIEVHIAASRPPRMLKYHLA FT QYASHATGVLAEDIAHDVDLVVLMVPQEELDDIDVSSLAGTLLIDATNRWEDEPLPHWF FT ESALDAGLSSSEAIAAHFKSSHVVKALNHISHWDMDADRATKQAAQRALGVASDSSENA FT GTVCELTQALGFSPVALPSLAAGRGMEPGGAVFNEVLDAVELAERLGLNTD" FT CDS complement(1850956..1852236) FT /transl_table=11 FT /locus_tag="AARI_16210" FT /product="putative divalent metal ion transporter" FT /function="1.2.3 Transport/binding of inorganic ions" FT /note="metal ion (Mn2+-iron) transporter (Nramp) family FT protein (TC 2.A.55.y.z). The generalized transport reaction FT catalyzed by Nramp family proteins is: Me2+ (out) + H+ FT (out) --> Me2+ (in) + H+ (in)" FT /db_xref="GOA:E1VW34" FT /db_xref="InterPro:IPR001046" FT /db_xref="UniProtKB/TrEMBL:E1VW34" FT /protein_id="CBT75837.1" FT /translation="MSENTQAPRADLDGGGPPRWKVIGPGLVVAATGVGAADMVATLVA FT GSQYGYALLWAVIVGVILKIVLVEGAGRYTLATGKTIFEGWKTLGKWTTWYFGPYIILW FT GFVYGATAMSSAALPLAALMPAVDLKIWAVIMGLLGFVMVWFGKYSFFEKVTAVLVGIM FT FITVVGLAFIAVPNIPEMLKGLIPMIPEGGVVYTLALAGGVGGTITLAAYGYWLREKGW FT YTPKWMRVMRIDNSMAYVMTGIFVLAMLIVGAEVVRAAGVTISGGDKGLLELGDVLRAE FT YGTVVGNGFLIGFWAASFSSIIGVWNGVSLMFADFWGHMRKKPANHPDTLTGGKYFKFY FT VLWLTFPPMVLFLLDKPIALILAYGVLGALFMPFLAVTLLGLLNGKRIPKAWANRWHTN FT TALAITAVLFIVLGVQQLIKTLSPLWS" FT CDS 1852479..1853147 FT /transl_table=11 FT /locus_tag="AARI_16220" FT /product="two-component system response regulator" FT /function="1.3 Sensors (signal transduction)" FT /note="response regulators are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VW35" 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:E1VW35" FT /protein_id="CBT75838.1" FT /translation="MQLLIVEDDQAVAHALIDAVRSAGHQAEHVSRGADALLNHHNAQV FT ILLDLGLPDMDGLEVLRKLRQVSEVPVVILSARNDERSVVRGLRQGADDFLVKPIGLTV FT LLARLEAVARRAKVEVAERAGVFNTGGLSVDASKHEASLDGRDLKLTAKEFDLLALLAQ FT YAGSVVTREQILDHLWGDAFIAVSRSLDVHLTGLRAKLATPGLIVNVRGVGYRLETRNP FT " FT CDS 1853144..1854580 FT /transl_table=11 FT /locus_tag="AARI_16230" FT /product="signal transduction histidine kinase" FT /function="1.3 Sensors (signal transduction)" FT /EC_number="2.7.13.3" FT /note="protein-histidine kinases are key elements in two- FT component signal transduction systems, which enable FT bacteria to sense, respond, and adapt to a wide range of FT environments, stressors, and growth conditions" FT /db_xref="GOA:E1VW36" 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:E1VW36" FT /protein_id="CBT75839.1" FT /translation="MRLRVLGIVGTLLLVIVGIVSGVLLQSVSRDATADLQLNRLSSLN FT RFVHLASQADRRSDLSMLQLEMDTYSHLYGEGLLVTIGQQQLVSGPIDPANPEVAGTVR FT NAELNLGLNQIPAIDPFSNSSALLSQPFGNSAQVLGSVTMQVNLETARAKVLEKSSLLW FT LVVVAIGAGLLLLTNRVTSWVLRPVHRLNNAVNDIARHQAPVRLEEQGPPELRELARSL FT SEMARTLANSLKQQQELIAETSHQLRNPVAALRLRVDLLKIRLGESVDLDGVQAVENEL FT DRVETLLDGVMRLASAEHRLTEQSAGESMLPSVEHGRCIDVVQMLAEEVERQTEAARRF FT GNLLVLDLDEAPTAPVVAWCNGFDLQQMLAELLENAFKYAPASKIVLSVASTPKAIEIQ FT IQDHGAGMSEAELARAGERFWRAEHVRQSPGTGLGLAIVDRLARANNGELILASVAGAG FT LKASIILPRAVQHEAVSHDS" FT gene 1854570..1855328 FT /pseudo FT /locus_tag="AARI_16240" FT /product="truncated protein" FT /note="N-terminal section of a conserved protein" FT gene 1855355..1855543 FT /pseudo FT /locus_tag="AARI_16250" FT /product="truncated protein" FT /note="C-terminal section of a conserved protein" FT CDS 1855628..1856944 FT /transl_table=11 FT /locus_tag="AARI_16260" FT /product="putative zinc metallopeptidase" FT /function="3.10 Protein degradation" FT /EC_number="3.4.-.-" FT /note="identified by match to protein family PF01546: FT peptidase family M20/M25/M40. This family includes a range FT of zinc metallopeptidases belonging to several families in FT the peptidase classification" FT /db_xref="GOA:E1VW37" FT /db_xref="InterPro:IPR001261" FT /db_xref="InterPro:IPR002933" FT /db_xref="InterPro:IPR011650" FT /db_xref="UniProtKB/TrEMBL:E1VW37" FT /protein_id="CBT75840.1" FT /translation="MPTVDAIAVMENEAVEICRKLIQIDTTNYGGNKGAGELEAARYVA FT QLLQEVGLAAQIYESAPGRANVLVRIPGADRTLPALVVHGHLDVVPAIAEDWSVDPFGA FT EIIDGMIWGRGAVDMKNMDAMIIAAVRHLQRENITPPRDLIIAFFADEEAGGDYGSGWM FT VQNHPELFAGATEAISEVGGFSVEINGRRAYMLQTAEKGIAWLKLTAQGMAGHGSQLNP FT DNAVTALAGAVHRIGEHQWPLSYTKTTRALLEQVAELAGLDFDEANPAPLLTAMGNVSR FT FVGATLQNTANPTALEAGYKHNVIPGQAHALIDCRTLPDQHEATLQTLRELAGEHVEVS FT MMHEQDSLEVPFAGPLVESMVQSLLAEDPDAVVLPYMLSGGTDNKWLAKLDITGYGFAP FT LQLPAELDFTGMFHGVDERVPVDSIKFGVRVLHKLLQEY" FT CDS 1856994..1858133 FT /transl_table=11 FT /locus_tag="AARI_16270" FT /product="acyl-CoA dehydrogenase" FT /function="2.4 Metabolism of lipids" FT /EC_number="1.3.99.-" FT /note="Acyl-CoA dehydrogenases catalyze the alpha,beta- FT dehydrogenation of acyl-CoA thioesters to the corresponding FT trans 2,3-enoyl CoA-products with concommitant reduction of FT enzyme-bound FAD. They are involved in the metabolism of FT lipids" FT /db_xref="GOA:E1VW38" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR006092" FT /db_xref="InterPro:IPR009075" FT /db_xref="InterPro:IPR009100" FT /db_xref="InterPro:IPR013107" FT /db_xref="InterPro:IPR013786" FT /db_xref="UniProtKB/TrEMBL:E1VW38" FT /protein_id="CBT75841.1" FT /translation="MSIESVLTDQLLERFRTRAAGYDQENTFAIEDFKELVELGYLKAL FT VPVERGGLGWDFQMLALAQRRLATAAPGTALAINMHQVWAGVAYLLNARADDRLNMVTD FT WIADGEVMAFGISEPGNDAVLFDSKTKARTADDGSVAFDGVKIFTSLAPAFTRLGVFGK FT DEATGELVHGFVAKGPGVNSLNDWNTLGMRASQSHTTKLENAVAPSQWVHSRLPVGPNA FT DPLIFGIFASFLTLTASVYVGIADRAVTLGQEALNKRVHHDGSKYSQDIRARGLLAESA FT MRLLTLDALQRSVAGDLEAKVDHQSAWFPKLVTLRTVAGDTARENIQSAGQLLGGGGYF FT RGSEFERLYRDVQASWYHPSNAASAANTIASWLVGPLES" FT CDS complement(1858136..1858369) FT /transl_table=11 FT /locus_tag="AARI_16280" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VW39" FT /protein_id="CBT75842.1" FT /translation="MLEERIKPALHHEDDQRFEYLVITSFPGEPKHLARAALREHADNG FT KWELMRTCRYEGGAYKYWLRRRVMRIRSTLGT" FT CDS 1858414..1858623 FT /transl_table=11 FT /locus_tag="AARI_16290" FT /product="hypothetical protein" FT /function="6 Protein of unknown function, without FT similarity to other proteins" FT /db_xref="UniProtKB/TrEMBL:E1VW40" FT /protein_id="CBT75843.1" FT /translation="MSTEPSFALQALIARLEQHLAIVSQSRGAGEASIDAAFGALADAF FT EDYEDALYDQYSELLPFTIPSDDE" FT CDS 1858702..1859526 FT /transl_table=11 FT /gene="uppP" FT /locus_tag="AARI_16300" FT /product="undecaprenyl-diphosphatase" FT /function="1.1 Cell wall" FT /EC_number="3.6.1.27" FT /note="catalyses the formation of undecaprenyl phosphate FT from undecaprenyl diphosphate. Involved in peptidoglycan FT biosynthesis" FT /db_xref="GOA:E1VW41" FT /db_xref="InterPro:IPR003824" FT /db_xref="UniProtKB/TrEMBL:E1VW41" FT /protein_id="CBT75844.1" FT /translation="MNWFEAAFLGLIQGLTEFLPISSSAHLRIVGELLPNAQDPGAAFT FT AITQLGTETAVIVFFWRDIVRIIGAWCKALVGKIPHSDPDAKMGWLIIIGSIPIAVLGL FT LLEDYIDTNFRSLWIVATTLVVFGLILAIADHYGKQQRTLEKLTVKHGIFYGLAQAMAL FT IPGVSRSGGTITAGLLMGYTREAAARYSFLLAIPAVYASGLYKLVKSFDEPGVYTLAQT FT GVATAVAFVVGFLIVGWFLKFVSNHSYSFFVWYRILLGLALFVALGLGWMAA" FT CDS 1859654..1860916 FT /transl_table=11 FT /gene="cysS" FT /locus_tag="AARI_16310" FT /product="cysteine--tRNA ligase" FT /function="3.7.2 Aminoacyl-tRNA synthetases" FT /EC_number="6.1.1.16" FT /note="activates cysteine and transfers it to tRNA(Cys) as FT the first step in protein biosynthesis" FT /db_xref="GOA:E1VW42" FT /db_xref="InterPro:IPR014729" FT /db_xref="InterPro:IPR017812" FT /db_xref="InterPro:IPR024909" FT /db_xref="UniProtKB/TrEMBL:E1VW42" FT /protein_id="CBT75845.1" FT /translation="MHAWKDPEVPQVAGSAPTLELFNTATGTQQVTAPADQAAAPASMY FT VCGITPYDATHMGHAATYVTFDLVQRTWRDAGRSVAYTQNITDVDDPLLERAEATNVDW FT RELAESQIQLFRDDMEALNVIPPQNYIGAVESIHWLVPVVEQLLEADLAYVVPAGADGV FT EGDVYFDTMGAQNDAWKLGSVSNYDRETMLRFFAERGGDPQRAGKRDALDPLLWRAARE FT GEPSWDGGKLGEGRPGWHIECSVIARKTLPAPFTVQGGGSDLIFPHHEFSAAHAAAGDH FT AELAQTYVHTGMVGLDGEKMSKSLGNLVLVSKLRAAGVEPVAIRAVLLSQHYRTDWFWT FT DELLAGAQQRVATWRKALESASMQDAQQVIAGIREHMANDLDAPSALKAIDQWATQPAS FT SQGEGATALRDGINALLGLKL" FT CDS complement(1860950..1861858) FT /transl_table=11 FT /locus_tag="AARI_16320" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="InterPro:IPR008492" FT /db_xref="InterPro:IPR019151" FT /db_xref="UniProtKB/TrEMBL:E1VW43" FT /protein_id="CBT75846.1" FT /translation="MNEEYHAPTLNSYIAKTQHEIRPTIVLAAFEGWNDAGSAATDAVR FT LLLESNAYEHVATVGEDDFYDYQFTRPTTRRTETGREVQWPRTEIYKILLPNAAADLLV FT VLGVEPTFKWQAFCSRIIREAQTHNAHAVITLGALLADVPHTRPVPTSLASDDPRLQAH FT LKISASTYEGPTGIPSVLGVQFEQYGIPSLSLWAQLSHYVAQSPSPRVQLAIIELLEEI FT IPVSVPDQKLREDALAWKHGVDELAAADPDVAKYVALLEQATDTSELPEASGESIAREF FT ERYLRRRGKYRKDGSGSDFDI" FT CDS 1861943..1862656 FT /transl_table=11 FT /locus_tag="AARI_16330" FT /product="putative hydrolase" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family TIGR01509: FT HAD-superfamily hydrolase, subfamily IA, variant 3; match FT to protein family PF00702: haloacid dehalogenase-like FT hydrolase" FT /db_xref="GOA:E1VW45" FT /db_xref="InterPro:IPR005834" FT /db_xref="InterPro:IPR006402" FT /db_xref="InterPro:IPR023214" FT /db_xref="UniProtKB/TrEMBL:E1VW45" FT /protein_id="CBT75847.1" FT /translation="MPSTSFDFDAGSESPVPHAVLWDMDGTLIDTEPYWLAAEDQLVRS FT HGGTWSHEQGLALVGNALPDGARALQQAGVKLEIREIIDWLSAQVVAGIRREIPWRPGA FT RELLAACKEAGIPQALVTMSERSIVDELMLNIPAGTFQASVTGEEVEQGKPHPEPYLAG FT LELLSEYTGRDLVPAKCIGFEDSVPGIASASAAGLHAVLIPNATDPGAGNWRRIDSLES FT VDVQEMTRWLVQVSA" FT CDS 1862653..1863780 FT /transl_table=11 FT /locus_tag="AARI_16340" FT /product="zinc metallopeptidase" FT /function="3.10 Protein degradation" FT /note="match to protein family PF02163: Peptidase family FT M50. Match to PS00142 pattern: neutral zinc FT metallopeptidases, zinc-binding region signature. 6 FT transmembrane helices predicted by TMHMM2.0" FT /db_xref="GOA:E1VW44" FT /db_xref="InterPro:IPR008915" FT /db_xref="UniProtKB/TrEMBL:E1VW44" FT /protein_id="CBT75848.1" FT /translation="MSDTQEKSPGIKLGRIGGVPVYLSSSWFIITAVITFSVGMQLARG FT GVIPPLNAYLMGLSCAVAIAVAVLIHEVAHAMTARAFKWPDAHIVLTLMGGHTQFGSFK FT AKPGASLWVALSGPLSNFVLAGLGWLVMENIQLGVYPNLLLDFFVYANLLLGAFNALPG FT LPLDGGRLVESIVWKATGSQFKGTIASCWVGRVIAVGIVFYFVLLPFLRGQQPQIITVV FT VGIMVAMFMWQATTQLIGHSKMMLNLPTVIASDLMSPASAMVSHAMVSDVLSRKAARGG FT EIILVDPKGMPVGVIDAQALAKVDPRQGGNVPALAVSRALGQGAIVAEESDGRALIDYL FT ASVESAEYAVISASGHVVGLLHQREIIKAVTGRRK" FT CDS 1863823..1864884 FT /transl_table=11 FT /locus_tag="AARI_16350" FT /product="putative tRNA (adenine-N(1)-)-methyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.36" FT /note="identified by match to protein family PF08704: FT GCD14, tRNA methyltransferase complex GCD14 subunit. tRNA FT (adenine-N(1)-)-methyltransferase catalyses the following FT reaction: S-adenosyl-L-methionine + tRNA <=> S-adenosyl-L- FT homocysteine + tRNA containing N(1)-methyladenine. The FT enzymes from different sources are specific for different FT adenine residues in tRNA" FT /db_xref="GOA:E1VW46" FT /db_xref="InterPro:IPR014816" FT /db_xref="UniProtKB/TrEMBL:E1VW46" FT /protein_id="CBT75849.1" FT /translation="MSEAKSQAPHGAAARRGPFRVGDRVQLTDEKRRINTITLQRGGEF FT HTHKGVLPHEDIIGLPEGSVIENIDGFRYQALRPLAKDFVLSMPRGATVVYPKDAAQIV FT QFGDIFPGARVVEAGVGSGALSISLLRAVGDEGFLHSFERREEFADIARGNISTVFGGE FT HPSWKISIGDFQDRVVELEEPGSIDRVVLDMLSPWECLDAVATVLAPGGVWTNYVSSVT FT QMSRVVEAIRASGQFTEPECFETLVRGWHVDGLAVRPDHRMVAHTAFLITCRRLADSAD FT GIPKAKRIKEHSYSDEDLSAWTRDHSEEEWTAEALGERGLSDKKLRRAARDANQSVRVR FT AGEEGTEDAGAEA" FT CDS 1864985..1866742 FT /transl_table=11 FT /locus_tag="AARI_16360" FT /product="putative ATP-dependent 26S proteasome regulatory FT subunit" FT /function="3.10 Protein degradation" FT /note="COG1222: RPT1, ATP-dependent 26S proteasome FT regulatory subunit. Proteasomes are large protein FT complexes, which main function is to degrade unneeded or FT damaged proteins" FT /db_xref="GOA:E1VW47" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR003959" FT /db_xref="InterPro:IPR003960" FT /db_xref="InterPro:IPR022482" FT /db_xref="UniProtKB/TrEMBL:E1VW47" FT /protein_id="CBT75850.1" FT /translation="MRHAPQKTSSEQKPLSVTLDVGGWNVNENREAEELAQRLQMTERQ FT VNVLRDKNRNLDKQLAGISGNNQRLVALLETTREQIINLKSALEKDGDTPFSHGTIVAK FT HPRKHPEPGMGIESTGAQSLDVIYSGRKMRVSLSPLLDFDKLVIGQQVLLNEALVIVAA FT LGFEETGELVTVKEVLENHHAVVMARADDQRVIELAGPLREMHLRVGDQLSIDGRTGMA FT VSRVQLTDMQSLVLEEVPDIAYSDIGGLNSQIEAIKDSVELPFTHPELYREHGLSAPKG FT ILLYGPPGCGKTLIAKAVAHSLAQRVVERKEGTNNRSYFLNIKGPELLDKYVGETERHI FT RLIFARAREKALHGDPVVVFFDEMEALFRTRGTGVSSDVETTIVPQLLAEIDGVERLDN FT VIVIGASNREDMIDPAILRPGRLDVKIKIRRPDAEGAAEIFSKYLTTDLPLHPEELAAD FT GEDARATIERMIRGTVQAMYSTEKINEFLEVTYITGATEVLYFKDFASGAVIHNIVDRA FT KKHAIKALITEQQRGLKMEYLLRAVREEFAEHEDMPNTTNPDDWARISGRKGERISNIR FT SLVNQQASK" FT CDS 1866739..1868358 FT /transl_table=11 FT /locus_tag="AARI_16370" FT /product="putative proteasome component" FT /function="3.10 Protein degradation" FT /note="identified by match to protein family PF03136: FT DUF245, putative proteasome component. Proteasomes are FT large protein complexes, which main function is to degrade FT unneeded or damaged proteins" FT /db_xref="GOA:E1VW48" FT /db_xref="InterPro:IPR004347" FT /db_xref="InterPro:IPR022366" FT /db_xref="UniProtKB/TrEMBL:E1VW48" FT /protein_id="CBT75851.1" FT /translation="MSARRLVGLETEYGIIRPSMPKANSTVLSAQIVDAYAQLVAEQDS FT AAKAARWDYTDESPLQDARGFAMDRDQAHPSQLTDVEPGLEDEEGIWTAESIALDGNDA FT HVGSTLYQEKDSTDVVMNMVLGNGARLYVDHAHPEYSSPESMTPRDAVLWDQAGDEVMR FT RAAATAQRLGSGELLLYKNNTDNKSVSYGSHENYLMPRDVEFSSIASGLTPFFASRQIF FT CGAGRVGQGMLNERASFQISQRADFFEAEVGLETTVNRPIINTRDEPHANWDKYRRLHV FT IIGDANLGQISTLLRVGTTNLVLSLIEAGMAPRLELEEPVVALQQISHDPTLKTKVRLR FT GGVQLSAIEIQRHYLQAAENYCADRGIDDPDTTEILNRWAEILDMLERDPMEAADQVDW FT IAKYKLITSFTARHQLSLADPRVAMMDLQWADLRTDKGLYYRMAERGAIQGLFSQEQIN FT QAVANPPEDTRAYLRGMTLQRYAPFVVAANWDALSFAVPGARKISRFHMPEPLRGTRNQ FT IGELFEAQLEIAEFIDELARRR" FT CDS 1868425..1868610 FT /transl_table=11 FT /locus_tag="AARI_16380" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VW49" FT /db_xref="InterPro:IPR008515" FT /db_xref="UniProtKB/TrEMBL:E1VW49" FT /protein_id="CBT75852.1" FT /translation="MTQESFSARRNTQNQQTEAEQVQVNTTGQSAGVDDLLDEIDSVLE FT SNAEEFVRGFVQKGGQ" FT CDS 1868689..1870065 FT /transl_table=11 FT /locus_tag="AARI_16390" FT /product="putative proteasome component" FT /function="3.10 Protein degradation" FT /note="identified by match to protein family PF03136: FT DUF245, putative proteasome component. Proteasomes are FT large protein complexes, which main function is to degrade FT unneeded or damaged proteins" FT /db_xref="GOA:E1VW50" FT /db_xref="InterPro:IPR004347" FT /db_xref="InterPro:IPR022279" FT /db_xref="UniProtKB/TrEMBL:E1VW50" FT /protein_id="CBT75853.1" FT /translation="MDRRIFGLETEFGLNYVPSDGRRLTPEDAARHLFKPVVSWGRSSN FT VFLENGSRLYLDVGSHPEYATAECDQLEQLIAHDRAGEVYMLDLVDQAEDQLAEEGHEG FT RIYMFKNNVDSAGNSYGCHENYLIPRKIEFKRLADMLIPFLVTRQILCGAGHLVSDDQG FT QVNYAFSQRADHMWEGVSSATTRSRPIINTRDEPHADAEYHRRLHVIVGDSTMSETTQL FT LKIGATDLVLRLIESGEIYHDLRLENPIRSIRQISHDFTGQSVVRLMGGDEPTALQIQW FT ILFESVKEFIARHGAHHDQVDTVLELWERTLNAVETQDFSLIDKDIDWAIKHKLLMGYA FT QKNSLELSAPRLAQLNLTYHDIDPQRGLFHLLKRRGLATSVVSDAQILDAVNNPPATTR FT AAVRSKFIRAARANGRRYSADWVHMKYEDGPGGIVLCKDPFATVNAQVDELIELMGQQL FT " FT CDS 1870184..1871119 FT /transl_table=11 FT /locus_tag="AARI_16400" FT /product="putative peptidylprolyl isomerase precursor" FT /function="3.9 Protein folding" FT /EC_number="5.2.1.8" FT /note="identified by match to protein family PF00254: FKBP- FT type peptidyl-prolyl cis-trans isomerase. Peptidylprolyl FT isomerase is an enzyme that accelerates protein folding by FT catalyzing the cis-trans isomerization of proline imidic FT peptide bonds in oligopeptides. Signal peptide predicted by FT SignalP 3.0 HMM (probability: 1) with cleavage site FT probability 0.529 between position 27 and 28" FT /db_xref="GOA:E1VW51" FT /db_xref="InterPro:IPR001179" FT /db_xref="InterPro:IPR023566" FT /db_xref="UniProtKB/TrEMBL:E1VW51" FT /protein_id="CBT75854.1" FT /translation="MRKVLAVCATASILALASCGSGSSSLSDIDVKPAADNKTAPEVTF FT DAPLLTEKAEAVTVVEGEGADIKEGDTIQIQSGLYKTIDGLLTNENFTAEPAPMKVDAT FT LKEQMPELYETLLKSQIGDWIAYAAIEGVQQADGSVSEPAEGSRAERLIVINIADSKSP FT SKALGKEEVQKLKDEGKLPTVKTGKGEPKITIPKDTEAPAGLAVDILEEGDGPAVGATS FT KVTAHYHGVRWEDGKKFDGNFGSKEGYEADMAGGVIEGWLQGFQGLKEGSKVLLTIPTD FT LAYGETAEAQGRPAGPLVFYVELDKVSESK" FT CDS 1871136..1871531 FT /transl_table=11 FT /locus_tag="AARI_16410" FT /product="peptidylprolyl isomerase" FT /function="3.9 Protein folding" FT /EC_number="5.2.1.8" FT /note="identified by match to protein family PF00254: FKBP- FT type peptidyl-prolyl cis-trans isomerase. Peptidylprolyl FT isomerase is an enzyme that accelerates protein folding by FT catalyzing the cis-trans isomerization of proline imidic FT peptide bonds in oligopeptides" FT /db_xref="GOA:E1VW52" FT /db_xref="InterPro:IPR001179" FT /db_xref="InterPro:IPR023566" FT /db_xref="UniProtKB/TrEMBL:E1VW52" FT /protein_id="CBT75855.1" FT /translation="MSFGERNYDRTKPEIDFPGTDAPEELVITDLVEGTGAEVTPGTTV FT EAHYVGVAWSTGEEFDSSWGRGQTLDFPVGVGMVIQGWDQGLLGMKVGGRRRLDIPSHL FT AYGERGAPGAIAPNEALIFVVDLMGTK" FT CDS 1871625..1873628 FT /transl_table=11 FT /locus_tag="AARI_16420" FT /product="putative transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /db_xref="UniProtKB/TrEMBL:E1VW53" FT /protein_id="CBT75856.1" FT /translation="MSTKQTSGPSKAERLTSLIYALATTSRKFNAERIGSYLAPEGSKE FT TREKALDRLKDDIRNDFGLQLNKEVIDGVTYYSIDTTDWFLPPVEFSPAEAGLVALAAS FT LWKDTKLQSLGLNAAARVTGHEGDTSPVASLAGSLVPRLSLDEPNFRECALAVFNHNTL FT KFDYRSSNGAPSQRIVDVWGIGQRYGNWYFTGYDHTRQDTRVFRLSRVQGKFVNYRHGS FT GASDPSYRARPEDFDMTKVLQDFDLQNPGLVATVKLLGEEAIPLRAQAVNGRSDQDELQ FT IGYADPHSFAQQLAGYGPAVKVLAPGELVNQVRQILGDARTAQLEQGTKDSYADTKFRP FT HRATGRGTTTTQVMRNIDMIQYVHAHGIVEVEELAQRYSMTVAKVREELAMIMMCGVPY FT GQHDELINVNDGDVESDTVTISNAALLAEPQKLAPLEAVAILGGLNALASIPEFEHQQV FT LNAALAKVNSAVARFDGWNGALGFALSKARENDIPQQLIQAIRAQEVVRIDYYSARSRT FT HQERDVEPIRLIEDGAVQYLRAWCRKRESLLTFRVDRMLCVENAGEQFALAVRHEDQQD FT VQIRYESSADDLEVMVHVDAEFLPVIEAFHPLSWSAGKVGAGYLANVRFSDHQVAAPLV FT ARHSGKLTVVSPDATREHVVNWLDEAIRLYED" FT CDS 1873632..1873991 FT /transl_table=11 FT /locus_tag="AARI_16430" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="signal peptide predicted by SignalP 3.0 HMM FT (probability: 0.673) with cleavage site probability 0.443 FT between position 23 and 24" FT /db_xref="UniProtKB/TrEMBL:E1VW54" FT /protein_id="CBT75857.1" FT /translation="MLPWWFWVLLWTVLVLATVLVAALAGFRLFKRGMAVVEGLGDAAD FT HISAGLSQEGTVVQYAPNPRRYPHGTDATHADPEEIKTLRDQGKAERIEARRVRRVTRR FT AERGQAQNMRDLRLF" FT CDS 1874024..1874239 FT /transl_table=11 FT /gene="tatA" FT /locus_tag="AARI_16440" FT /product="twin-arginine translocation protein TatA/E" FT /function="1.6 Protein secretion" FT /note="identified by match to protein family TIGR01411: FT twin-arginine translocation protein TatA/E. The twin- FT arginine translocation system is a Sec-independent exporter FT for folded proteins, often with a redox cofactor already FT bound, across the bacterial inner membrane" FT /db_xref="GOA:E1VW55" FT /db_xref="InterPro:IPR003369" FT /db_xref="InterPro:IPR006312" FT /db_xref="UniProtKB/TrEMBL:E1VW55" FT /protein_id="CBT75858.1" FT /translation="MMGLQGWHIVIIIVLALLLFGAPKLPGLARSMGQSLRIFKSEVRQ FT MKDDDPKSETVDGTVNEQNPNEKNNS" FT CDS 1874249..1875118 FT /transl_table=11 FT /gene="tatC" FT /locus_tag="AARI_16450" FT /product="twin-arginine translocation protein TatC" FT /function="1.6 Protein secretion" FT /note="identified by match to protein family PF00902: Sec- FT independent protein translocase protein (TatC). The twin- FT arginine translocation system is a Sec-independent exporter FT for folded proteins, often with a redox cofactor already FT bound, across the bacterial inner membrane" FT /db_xref="GOA:E1VW56" FT /db_xref="InterPro:IPR002033" FT /db_xref="InterPro:IPR019822" FT /db_xref="UniProtKB/TrEMBL:E1VW56" FT /protein_id="CBT75859.1" FT /translation="MATNKDKTPRSKKKRVKDAEGRMALKEHLIEARNRLFKSLIALTL FT GTIAGFFVYDWLLALLIAPVKAAGGSVVFTAVMSPFDIMIKVALFVGLIVSSPVWLYQL FT WAFIVPGLKKNERRMSYSFVAAAVPLFLGGVAMAYFVLPFALEFFISLSPENSDNLLNI FT SEYLPFIIRLLLAFGLAMLVPVLMVGLNLVGILPAKLILKHWRITVFLIALVAAMAAPG FT GDAITMFALAGPLFLTFAAATLICHFNDKKRAKKLAAQEAENERLAAGGVATDIDAPST FT IDEPKSQL" FT CDS 1875147..1877930 FT /transl_table=11 FT /locus_tag="AARI_16460" FT /product="putative ATP-dependent RNA helicase" FT /function="3 Information pathways" FT /EC_number="3.6.1.-" FT /note="putative DEAD box helicase. The DEAD box helicases FT are involved in various aspects of RNA metabolism, FT including nuclear transcription, pre mRNA splicing, FT ribosome biogenesis, nucleocytoplasmic transport, FT translation, RNA decay and organellar gene expression" FT /db_xref="GOA:E1VW57" FT /db_xref="InterPro:IPR001650" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR011545" FT /db_xref="InterPro:IPR012961" FT /db_xref="InterPro:IPR014001" FT /db_xref="UniProtKB/TrEMBL:E1VW57" FT /protein_id="CBT75860.1" FT /translation="MTSPAERYANSKARQVENGTALPDFRASLSFDLDPFQAEACQKVA FT EGHSVLVAAPTGAGKTVVGEYAIYQALRENRKAFYTTPIKALSNQKYSELVNRYGAQKV FT GLLTGDTSINSEAQIVVMTTEVLRNMLYADSQTLDGLGYVIMDEVHYLADKFRGAVWEE FT VIIHLPSNVQIISLSATVSNAEEFGGWLDTVRGQTDIIVSEHRPVPLFQHVMVGPNVVD FT LFAEDVAFDKVAEDDSKASVNPELRKLVRTHNSGGRVQRGRGRGGRGPQRSAGMGHRIN FT RPSVIGKLDRAGLLPAIFFIFSRKGCDMAVQQCAMADLRLTTNEEAAEIAQALDEVAFR FT IPSEDLDVLEFWSWRDGLVRGFASHHAGLLPIFKEIVEDLFARNLIKVVFATETLALGV FT NMPARSVVLEKLVKFNGESHVQISSGEYTQLTGRAGRRGIDVEGHSIVVWNPDLEPEAL FT AGLASKRTYPLNSSFRPTYNMSTNLLAQFGREQTRQILESSFAQYQADRSVVGMARQVR FT SKEESLAGYAKSMECHLGDFTEYLKLQRNLAQVEKNAAKDRRNQRRSAAEQSLQSVIRG FT DVVDLPGGRRFGRAVIVELDKAMYNPRHTVLTEEAQLRRISTEDLNGPVQIVSRIKVPK FT GFTGRAPKERRDLASSLRNAIYESRPPRQDAQSFDFEGTDSFEREINELRLELKDHPCH FT ACSEKDQHMRWADRYWKLKKDTEKARRAIRGRTNTIATQFDKVCKVLEQFEYLMPANDG FT EDFELTGSGRRLRRIYGDRDLLTSQILETGKLTALNAEELCAVVASLVYQARRDGDRAD FT PKMPTSKIDEIWNSTIKIWGELSDAEEALNLDPTAPPESGLIWPMYKWARGSSLNSALR FT GTDLAPGDFVRWAKQVIDTLDQFAKNTDLPPLLVRNAYKAVDQIKRGVVAYSNVLD" FT CDS 1877987..1879594 FT /transl_table=11 FT /locus_tag="AARI_16470" FT /product="putative amidohydrolase family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF07969: FT amidohydrolase family" FT /db_xref="GOA:E1VW58" FT /db_xref="InterPro:IPR011059" FT /db_xref="InterPro:IPR013108" FT /db_xref="UniProtKB/TrEMBL:E1VW58" FT /protein_id="CBT75861.1" FT /translation="MAKTLYRNGSIYSAADPFATAMVVDGDTIAWLGGEDAAERHAGTV FT DEVVDLNGGLVAPAFVESHTHLAALGRTLSGADLGAASSASSLLSLIAEHAQNSTNMVL FT AQGWDNSDWANQELPAETDLTSAVGGRGYYLARRDVHSALVNQELLDLLDLGHLSSGTI FT AGADHDAVREALTKTQKAEQEYQRLALEHYASRGFASVVEMAAPHLEGREALDQLLSID FT SSKLPQVYAYWGELVADADHAQELTASFPAGKLLGLGGDLRVDGSLGSHTAYLREDYSD FT KPGQRGTLYLNREEIAAHLVACSSRGIQASFHVIGDGALDEVLAGFDLASEQIGIAKLQ FT MCRHRLEHVEMVDEATRARLLQYAIMVSMQPVFDQAWGGSNGMYIQRLGEERAASMNNL FT SAMLSAGVPMVLGSDAPVTEVDGWQVVRAGMNMNNTDARISARAAFLAQTRSTYRAMGE FT MNPYAGQLVIGAPATFAVWTASELAVQTPDVRISSWSTDARAGTPMLPVVDQEIPQCLR FT TVRAGVTLFNALEPSESA" FT CDS 1880009..1880737 FT /transl_table=11 FT /locus_tag="AARI_16480" FT /product="putative family 2 glycosyl transferase" FT /function="1 Cell envelope and cellular processes" FT /note="match to PF00535: glycosyl transferase family 2. FT This domain is found in a diverse family of glycosyl FT transferases that transfer the sugar from UDP-glucose, UDP- FT N-acetyl-galactosamine, GDP-mannose or CDP-abequose, to a FT range of substrates including cellulose, dolichol phosphate FT and teichoic acids" FT /db_xref="GOA:E1VW59" FT /db_xref="InterPro:IPR001173" FT /db_xref="UniProtKB/TrEMBL:E1VW59" FT /protein_id="CBT75862.1" FT /translation="MRVITIIPTYNELESLPLTVGRLRTAVPDSDVLIVDDNSPDGTGE FT LADKMAAEDSNINVLHRTGKDGLGAAYIAGFEWALARDYDVLVEMDADGSHMPEQLPRL FT LEASAAGADLVIGSRWVKGGEVVNWPLLRKIISRGGSFYSRTMLGLPLRDITAGYRAFK FT RETLEAIDFDAVESRGYGFQVDMTFRVAMLRKKIVEVPVTFVERELGASKMSGNIVFEA FT MWNVTRWGLGARWKKLTSKK" FT CDS complement(1880951..1881298) FT /transl_table=11 FT /locus_tag="AARI_16490" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="UniProtKB/TrEMBL:E1VW60" FT /protein_id="CBT75863.1" FT /translation="MSDRSLRGMRLGAQSMESEAGVEPAARQRVEYRTEEGETVFVVFA FT AEAEIPAIWHTKTGKEAKLVHGEAKAEEPGNEKPVRTHWDMLLERRSEEELEKTLADRL FT QQLRTARGDAV" FT CDS complement(1881483..1882421) FT /transl_table=11 FT /locus_tag="AARI_16500" FT /product="band 7 family protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="identified by match to protein family PF01145. The FT band 7 protein is an integral membrane protein which is FT thought to regulate cation conductance. A variety of FT proteins belong to this family" FT /db_xref="GOA:E1VW62" FT /db_xref="InterPro:IPR001107" FT /db_xref="InterPro:IPR001972" FT /db_xref="InterPro:IPR018080" FT /db_xref="UniProtKB/TrEMBL:E1VW62" FT /protein_id="CBT75864.1" FT /translation="MKSDGFGLTIVLVVLAIFVIVVLLRSVRIVPQARAGIVERLGKYN FT RTLNPGLTILIPFVDRLLPLLDLREQVVSFPPQPVITEDNLVVSIDTVIYFQITEPRAA FT TYEIANYIQAVEQLTTTTLRNVVGGLNLEEALTSRDQINGQLRGVLDEATGKWGIRVSR FT VELKAIDPPISIQDSMEKQMRADRDRRAAILTAEGVKQSSILTAEGARQSSILKAEGDA FT QASILRADGEAQAIQKVFDAIHAGKPDQELLAYQYLQTLPKLAEGTSNTLWVIPSELTE FT ALKGIGGALGGSGASSKPAAPEAPSAPENGL" FT CDS complement(1882479..1882955) FT /transl_table=11 FT /locus_tag="AARI_16510" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="3 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR002810" FT /db_xref="InterPro:IPR012340" FT /db_xref="UniProtKB/TrEMBL:E1VW61" FT /protein_id="CBT75865.1" FT /translation="MTTAEWIISNAWVIWLALFLLLAIIEMLSLDLYFIMLGVGALGGV FT AVALLNGPMWLQVLVFCLISLLMIFLVRPIAVKHLRKSPEGFRTNIERLIGADALILEP FT TSRMSGSAKIRGEIWTARADANVPSMNPGTYAVVSRIDGATAYLTAKSPDPADG" FT CDS complement(1883060..1883911) FT /transl_table=11 FT /gene="rrmA" FT /locus_tag="AARI_16520" FT /product="putative rRNA (guanine-N(1)-)-methyltransferase" FT /function="3.6 RNA modification" FT /EC_number="2.1.1.51" FT /note="rRNA methyltransferase catalyzes the following FT reaction: S-adenosyl-L-methionine + rRNA => S-adenosyl-L- FT homocysteine + rRNA containing N(1)-methylguanine. It is FT required for translation and cell growth" FT /db_xref="GOA:E1VW63" FT /db_xref="InterPro:IPR013216" FT /db_xref="InterPro:IPR016718" FT /db_xref="UniProtKB/TrEMBL:E1VW63" FT /protein_id="CBT75866.1" FT /translation="MSSGTTTITCPVCEQTLSLDETPRRSLNCESGHRFDAAKQGYFNF FT LTGKGTNFLEDTSAMVQARDAFQSKGHYEPLVLALSKLINDHHEASTLDVLDAGAGTGY FT YLEKILEHSPAPSHDALALDISRYAMRKAAKVPATLAVVWDVWRKLPTADQSRDVVLNC FT FAPHNPAEFRRVLRPNGLCLVVTGEPDHLNEVIEPLGMLSVAEGKQAALAEKFGAEGLR FT HVESQKLSYQMDLQSEDLFNLAFMGPAGHHLSPETLEQQALALGPQQVTASFGVHAFVP FT QA" FT CDS complement(1883911..1884552) FT /transl_table=11 FT /gene="def" FT /locus_tag="AARI_16530" FT /product="peptide deformylase" FT /function="3.7 Protein synthesis" FT /EC_number="3.5.1.88" FT /note="involved in polypeptide synthesis by removal of the FT formyl-group from methionine in growing polypeptides" FT /db_xref="GOA:E1VW64" FT /db_xref="InterPro:IPR000181" FT /db_xref="InterPro:IPR023635" FT /db_xref="UniProtKB/TrEMBL:E1VW64" FT /protein_id="CBT75867.1" FT /translation="MNTEYTAQDIETIVRDVLSSADENLVLPIVQLGHPVLRQQAVAYE FT NQLPTDLLEELLEAMRQTMYDAPGVGLAAPQVGIPLQIAVLEDLYPIPEEAATMREREP FT LEYFEIFNPEYVSASEREAVFYEGCLSFDGFQGVVTRPADISATYKDRDGQEITRSFSG FT WQARIVQHEADHLSGTVYIDKAETRSLIDETELWRHEGMDVATAQKVLNF" FT CDS complement(1884549..1885601) FT /transl_table=11 FT /locus_tag="AARI_16540" FT /product="putative ATPase" FT /function="4.6 Miscellaneous" FT /note="identified by match to protein family PF03969: FT AFG1_ATPase, AFG1-like ATPase" FT /db_xref="GOA:E1VW65" FT /db_xref="InterPro:IPR003593" FT /db_xref="InterPro:IPR005654" FT /db_xref="UniProtKB/TrEMBL:E1VW65" FT /protein_id="CBT75868.1" FT /translation="MTTPLLRIPDRNKYAQKITKVLEQQHIQVDPVQRELIEILDRCLG FT KSKSAAHPGIYIYGPPGRGKTLIMNTLVSLMPPATTARYHFHEFFQRLNSPANRIPGQR FT LGAIFAQGLERELAGLELLVFDEFHCTEPGDAMFMAKLVRHCAEHRIQLITTSNYGPEK FT LLDDDTFHHLVQPTIDRIKNDFVIFALDHQVDYRQLDADPQQVLEGYRLGSLNLFETPA FT AQPEHDTMIQIGYDEIGPVHLNAETIWITFDQICRTRRNTADYLELAGRYSCWHVTGIP FT ASTNMPMDEERRLANLIDIFYDKNVEVHLYAADNLGNLGHMLHDTEKARLTSRLAQLQL FT NEYERTSASS" FT CDS 1885924..1886271 FT /transl_table=11 FT /locus_tag="AARI_16550" FT /product="putative ArsR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to PF01022. ArsR-family FT transcriptional regulators include several proteins that FT appear to dissociate from DNA in the presence of metal FT ions" FT /db_xref="GOA:E1VW66" FT /db_xref="InterPro:IPR001845" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VW66" FT /protein_id="CBT75869.1" FT /translation="MTSEFIAHVAEDEIVSSDLLDMSVTVLKTLSDPARLQMLWALSTE FT DLSLSDLAQLVGVSSTVASQLLSRLRTAGVLQTRKSGRHVIYSMHDERSREFIRQTLDF FT ARHRLELQDKA" FT CDS 1886467..1886937 FT /transl_table=11 FT /locus_tag="AARI_16560" FT /product="hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="match to protein family PF03969: activator of Hsp90 FT ATPase homolog 1-like protein" FT /db_xref="GOA:E1VW67" FT /db_xref="InterPro:IPR013538" FT /db_xref="InterPro:IPR023393" FT /db_xref="UniProtKB/TrEMBL:E1VW67" FT /protein_id="CBT75870.1" FT /translation="MPLLRKSFDVPSGTVCLQWTLDASSGLIWRALTGIEPLQRWLGTL FT LSGTFSIGSNVEIEHAQDYVCTSRIISCKPGQSLEMTWKFPDEDPSQVSFTIESTAGSQ FT ILTVRHIGLTKEVGEYLTGWQTHLLYLEDFLNGTPRPMSDFWGEYERVKNAP" FT CDS 1887275..1887736 FT /transl_table=11 FT /locus_tag="AARI_16570" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR023845" FT /db_xref="UniProtKB/TrEMBL:E1VW68" FT /protein_id="CBT75871.1" FT /translation="MTPSSLYRTVARAEAVTWTMLIIALILKYGVKIGDWPVSIAGFIH FT GFVFLTYATMAVLIGMNQRWRKGLIVGAAATAVVPFLTIPFDKWLERNGKLEGPWRTAA FT TDHPDDRKWTDATMRWLVARPLLTTVLLFIVIVAIFATMLVVGPPGGEH" FT CDS complement(1887870..1888844) FT /transl_table=11 FT /locus_tag="AARI_16580" FT /product="putative sodium-dependent transporter" FT /function="1.2 Transport/binding proteins and lipoproteins" FT /note="identified by match to protein family PF01758. Bile FT acid:Na+ symporter (BASS) family (TC 2.A.28.y.z): these FT symporters exhibit broad specificity, taking up a variety FT of non bile organic compounds as well as taurocholate and FT other bile salts" FT /db_xref="GOA:E1VW69" FT /db_xref="InterPro:IPR002657" FT /db_xref="UniProtKB/TrEMBL:E1VW69" FT /protein_id="CBT75872.1" FT /translation="MNSWPGYARMQSHQILLYLLAIAAGVLTGLALPAAAPALQSAINP FT FLALLLYATFLSMPLTKLAGALGDIRFMGALMLANFVAVPLVVFALTRFIAHDKALLFG FT VLLVLLAPCVDYVIVFTGLAGGDSHKLLAATPLLLVSQVLLLPVFMYLFAGPATTGLIE FT PEPFVRSLLGLIVLPLAAAAITQMITRKYSEFAVVGDWADYLMVPLMMGTLFSVVGSQI FT HGVAAQISSLFQAIMIFALFILLMVFIAWAIGRIFKLGIQSLRAVAFSGVTRNSLVVLP FT LALALPVELAFASTVVVTQTLVELLGMLLMVRFIPALIRQKSN" FT CDS 1888989..1889363 FT /transl_table=11 FT /locus_tag="AARI_16590" FT /product="conserved hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="InterPro:IPR021414" FT /db_xref="UniProtKB/TrEMBL:E1VW70" FT /protein_id="CBT75873.1" FT /translation="MKESIQKWPLWAAIDLVLIILFALLGRREHEHALSIVGILMTALP FT FLIAYVIMTLLSKPNKTINKLFPVGLLVWIGTVALGLALRIALGSTAAVPFIIVAFLVL FT GAFLMGRRLVTSLVARKLNK" FT CDS complement(1889352..1889894) FT /transl_table=11 FT /locus_tag="AARI_16600" FT /product="hypothetical membrane protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /note="4 transmembrane helices predicted by TMHMM2.0" FT /db_xref="UniProtKB/TrEMBL:E1VW71" FT /protein_id="CBT75874.1" FT /translation="MVWIAWGSLSLATVIACVGAYLGYAMGKRARAREWLTVAAGFFAL FT LAAVLAAASQTAVEQSPLAPVYAIALSSIFAISFGGPFTELVFRLAAKNDVELAKEESD FT PSPLRGGLWIGLLERTAIVASLWAGWPEGIAIVLAVKGLGRFSELKNHRAAEQFILGTF FT SSGLVAAGSYGLGLLLI" FT CDS complement(1889895..1890491) FT /transl_table=11 FT /locus_tag="AARI_16610" FT /product="conserved hypothetical protein" FT /function="5.2 Protein of unknown function similar to FT proteins from other organisms" FT /db_xref="GOA:E1VW72" FT /db_xref="InterPro:IPR007630" FT /db_xref="InterPro:IPR010982" FT /db_xref="UniProtKB/TrEMBL:E1VW72" FT /protein_id="CBT75875.1" FT /translation="MIVLTIDQRRSRSTEDKVEALVKQANATVSVVRPFQRTAGDEVQA FT VLDDANEAIRLAVMMAASGDWSVGLGFGQVETPLPEETRAGRGPAFEFARVAVERAKNT FT NAHLAVHGPSHEATRLEAELQLTACIVSKRRATAWEAGTLADEGMTQQEIAKELGITQQ FT AVSSRLSAALWFEANRMMDEAAKSLNRQLNMLKEQ" FT CDS 1890654..1890938 FT /transl_table=11 FT /locus_tag="AARI_16620" FT /product="putative AsnC/Lrp-family transcriptional FT regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF01037: FT AsnC_trans_reg, AsnC family" FT /db_xref="GOA:E1VW73" FT /db_xref="InterPro:IPR011008" FT /db_xref="InterPro:IPR019887" FT /db_xref="UniProtKB/TrEMBL:E1VW73" FT /protein_id="CBT75876.1" FT /translation="MMVTAFVMIQTATDSIPECAQQISAISGISEVYSVAGDWDLIAIA FT RVNKHEDLAEVIANKLSKIQGIRGTQTHIAFRAYSEHDLEAAFSLGLGD" FT CDS complement(1891026..1892045) FT /transl_table=11 FT /gene="trpD" FT /locus_tag="AARI_16630" FT /product="anthranilate phosphoribosyltransferase" FT /function="2.2 Metabolism of amino acids and related FT molecules" FT /EC_number="2.4.2.18" FT /note="involved in tryptophane biosynthesis" FT /db_xref="GOA:E1VW74" FT /db_xref="InterPro:IPR000312" FT /db_xref="InterPro:IPR005940" FT /db_xref="InterPro:IPR017459" FT /db_xref="InterPro:IPR020072" FT /db_xref="UniProtKB/TrEMBL:E1VW74" FT /protein_id="CBT75877.1" FT /translation="MATLITGGDLSREQAAWAMNEIMSGEASDVQIAGFLVALRSKGET FT VAELTGLVDSMVANARPLSIDAQTLDIVGTGGDRQNTVNISTMSTLVCAGAGVNIVKHG FT NRASSSSSGSADVLEALGVRLEVPIERLVEVYNKVGIAFCFANVFHPSMRHVAGARRQL FT RVPTAFNFMGPLTNPALPSASAIGCSDATMAPIMAGVLASRNVRGLVFRGDDGLDELTT FT TAPNRVWEVRDGKVSEFTFDAQDVGIARATLDDLRGGDALHNAGVVREIVDGATGPVRD FT AVLLNAAAGMVAYANDADGSFEDRMRLAIEKAAQSIDSGAAKATLDSWASTTQAIVGE" FT CDS 1892381..1893019 FT /transl_table=11 FT /gene="ctaE" FT /locus_tag="AARI_16640" FT /product="cytochrome aa3 subunit 3" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="1.9.3.1" FT /note="in Corynebacterium glutamicum, a cytochrome aa3 FT terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 FT complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA FT (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC FT (cytochrome c1). Cytochrome aa3 is composed of subunits I FT (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits FT form the cytochrome bc1-aa3 supercomplex" FT /db_xref="GOA:E1VW75" FT /db_xref="InterPro:IPR000298" FT /db_xref="InterPro:IPR013833" FT /db_xref="InterPro:IPR024791" FT /db_xref="UniProtKB/TrEMBL:E1VW75" FT /protein_id="CBT75878.1" FT /translation="MTTATHAPNTTAPHAPNRPNMVSVGTMVWLSSELMFFAALFAMYF FT SLRAAAPELWANETAKLNVPFALVNTIILVSSSFSCQLGVFRAEEFKPRRTGGIFNFKE FT WGMIEWFILTFFLGAIFVSVQAYEYAVLVSEGVAFNSNSYASAFYITTGFHGIHVAGGL FT IAFLLIIGRAMLAKKFGHFEATGSIVVSYYWHFVDVVWIALFAIIYFLK" FT CDS 1893096..1893890 FT /transl_table=11 FT /gene="qcrC" FT /locus_tag="AARI_16650" FT /product="cytochrome bc1 complex cytochrome c1 subunit" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="1.10.2.2" FT /note="in Corynebacterium glutamicum, a cytochrome aa3 FT terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 FT complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA FT (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC FT (cytochrome c1). Cytochrome aa3 is composed of subunits I FT (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits FT form the cytochrome bc1-aa3 supercomplex" FT /db_xref="GOA:E1VW76" FT /db_xref="InterPro:IPR003088" FT /db_xref="InterPro:IPR009056" FT /db_xref="InterPro:IPR009152" FT /db_xref="UniProtKB/TrEMBL:E1VW76" FT /protein_id="CBT75879.1" FT /translation="MKALSKKRRHPLAAVALLLFGLLITGSLYTAAGNISEAKAAETTT FT ASQADVEEGQKLFVANCATCHGMNAEGSDSGPSLIGVGAASVDFQVGTGRMPMQMQGPQ FT AQVKPVQFDDEQISQLAAYVASLGAGPAIPDEEYLDTTQGDAAHGGTIFRVNCAMCHNA FT AAAGGALTRGKFAPTLSGVSEKHIYEAMATGPQNMPVFNDSNITPEEKRDVITFLKTIE FT ANGSAGGAALGSLGPVAEGLFTWTAGLGIIIAFTIWLTSRPS" FT CDS 1893961..1895010 FT /transl_table=11 FT /gene="qcrA" FT /locus_tag="AARI_16660" FT /product="cytochrome bc1 complex iron sulfur subunit" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="1.10.2.2" FT /note="in Corynebacterium glutamicum, a cytochrome aa3 FT terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 FT complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA FT (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC FT (cytochrome c1). Cytochrome aa3 is composed of subunits I FT (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits FT form the cytochrome bc1-aa3 supercomplex" FT /db_xref="GOA:E1VW77" FT /db_xref="InterPro:IPR017941" FT /db_xref="UniProtKB/TrEMBL:E1VW77" FT /protein_id="CBT75880.1" FT /translation="MGDHSHGSPENSGTVAKADDVAQDRFPDPGLPPHRPRLADRDPRA FT AKRHERQVALLFTISIIGTLFFFVAYFVLGHLGEMTFAELRVQNAALGLGTAFAMLGIG FT VGIVHWAKTLMPDHELMEMRHEIRSEEDRQDAVEIIDTVLEESGIKRRPLIRNTLIGAI FT ALAPIPAIFMFRDLDRTGNTAHQMIDSLRHTMWDKGIRLTRDPSGTPIKASDVQIGSAF FT HVIPEGLNETEHPLNEKAKAVVLLMRMDPAEMQISEGRETWNVDGIVAYSKICTHVGCP FT IALYEQHTHHLLCPCHQSTFDLTQECKVIFGPAGHALPQLPITVDSEGYLVAQSDFHEP FT VGPSYWERG" FT CDS 1895013..1896683 FT /transl_table=11 FT /gene="qcrB" FT /locus_tag="AARI_16670" FT /product="cytochrome bc1 complex cytochrome b subunit" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="1.10.2.2" FT /note="in Corynebacterium glutamicum, a cytochrome aa3 FT terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 FT complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA FT (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC FT (cytochrome c1). Cytochrome aa3 is composed of subunits I FT (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits FT form the cytochrome bc1-aa3 supercomplex" FT /db_xref="GOA:E1VW78" FT /db_xref="InterPro:IPR005797" FT /db_xref="InterPro:IPR016174" FT /db_xref="InterPro:IPR016175" FT /db_xref="UniProtKB/TrEMBL:E1VW78" FT /protein_id="CBT75881.1" FT /translation="MTTTNEYQASTATGRIANFVDSRVGASGMVKEFGRKIFPDHWSFM FT FGEVAMYTFVLLLLSGTFLTFFFDPSMAHVIYNGSYVPMKGIGMSTAMASTMDISFDVR FT GGLFMRQVHHWSALLFVASLSVHMLRVFFTGAFRRPRELNWVVGGVLLIMGLAAGFTGY FT SLPDDLLSGNGLRIIDGVMKALPIVGTYLSMFFFGGEFPGDAVIPRLYSLHIMIVPAVI FT ILLIVVHLFMVVTHKHTQYPGPGRTNDNVVGFPVGPVYAAKAGGFFFIVFGIVAFIAGV FT FQINPVWNYGPYDPSPVSAGTQPDWYIGFVDGALRLMPGYLGNFSFEWIIPFPWGDNTL FT VMSVLLPALVPAGALFAVMFAWPWIERWITKDNREHHLLDRPRNAPFRTAVGAAGVVFY FT CVMWAAASSDLIATHFHVSLNDVTYWLRTLFFLGPIFAFWLTRRICLSLQRKDREIVLH FT GREAGIIQMSPEGGFSEKHEEVDVYKRYLLTNYVDRQYIPAQPDAAGHVSGSEKRRAAI FT SKFFFEDRVAPVTPSELEAAHAAHGHHEVEGDKQDAVQK" FT CDS complement(1897400..1898182) FT /transl_table=11 FT /locus_tag="AARI_16680" FT /product="GntR-family transcriptional regulator" FT /function="3.5.2 Transcription regulation" FT /note="identified by match to protein family PF00392. This FT family of regulatory proteins consists of the N-terminal FT HTH region of GntR-like bacterial transcription factors. At FT the C-terminus there is usually an effector- FT binding/oligomerisation domain. The GntR-like proteins can FT be divided into six sub-families: MocR, YtrR, FadR, AraR, FT HutC and PlmA. Many of these proteins have been shown FT experimentally to be autoregulatory, enabling the FT prediction of operator sites and the discovery of cis/trans FT relationships" FT /db_xref="GOA:E1VW79" FT /db_xref="InterPro:IPR000524" FT /db_xref="InterPro:IPR011663" FT /db_xref="InterPro:IPR011991" FT /db_xref="UniProtKB/TrEMBL:E1VW79" FT /protein_id="CBT75882.1" FT /translation="MRHAPQPDVQAHLDPTSKQSKYRQIREILKTHAREACKPGYKLPP FT ERVLAEHFSVARKTIRQAIDALVDEQVLKRVVGIGTFVVPEKLDLRVRLHSYSEDMMRR FT GMVPDAHVLEFAEIKAGASLASQLMLDEGTPVVQFKRLLLADGTPMSLDENYMPADLVP FT GFVDGEPPSKLYQALHERYGILLEWGEDQVESTAASKKQAVLLGVEPGFPLLQITRYAY FT IGDRLADYSVSLYRSDRYKLFVPLQRVGTRTPRYTDTF" FT CDS complement(1898296..1898697) FT /transl_table=11 FT /gene="ctaF" FT /locus_tag="AARI_16690" FT /product="cytochrome aa3 subunit 4" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="1.9.3.1" FT /note="in Corynebacterium glutamicum, a cytochrome aa3 FT terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 FT complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA FT (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC FT (cytochrome c1). Cytochrome aa3 is composed of subunits I FT (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits FT form the cytochrome bc1-aa3 supercomplex" FT /db_xref="GOA:E1VW80" FT /db_xref="InterPro:IPR021050" FT /db_xref="UniProtKB/TrEMBL:E1VW80" FT /protein_id="CBT75883.1" FT /translation="MKVESWIFLGGVFFFTPVAIVYGYMTNWNEWVGFLALLMLVGLCL FT MVGGYLLFTAKRVGNRPEDRVDGEIHENAGDIGMFSPWSWWPLVLASAAAIGFLGLAVG FT WWVFFIGAGLAVVGVTGWVYEYSRGDHAH" FT CDS complement(1898700..1900418) FT /transl_table=11 FT /gene="ctaD" FT /locus_tag="AARI_16700" FT /product="cytochrome aa3 subunit 1" FT /function="1.4 Membrane bioenergetics (electron transport FT chain and ATP synthase)" FT /EC_number="1.9.3.1" FT /note="in Corynebacterium glutamicum, a cytochrome aa3 FT terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 FT complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA FT (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC FT (cytochrome c1). Cytochrome aa3 is composed of subunits I FT (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits FT form the cytochrome bc1-aa3 supercomplex" FT /db_xref="GOA:E1VW81" FT /db_xref="InterPro:IPR000883" FT /db_xref="InterPro:IPR014241" FT /db_xref="InterPro:IPR023615" FT /db_xref="InterPro:IPR023616" FT /db_xref="UniProtKB/TrEMBL:E1VW81" FT /protein_id="CBT75884.1" FT /translation="MTTFEYATDDAKSIAPAVVPKSKGRLFVDYITSTDHKKIGYMYLI FT SSFILFCVGGVMALLIRAELFEPGMQILQTKEQYNQLFTMHGTVMLLMFATPLFAGFAN FT VMMPLQIGSPDVAFPRLNALAFWFFSLGSIIALAGYLTPQGAASFGWFAYAPLSNTTFS FT PGIGGDLWVFGLALSGFGTILGAVNFITTIICLRAPGMTMWRMSIFSWNTLITSLLILM FT AFPPLAAALFALGADRRFGAHIFDPDNGGAVLWQHLFWFFGHPEVYIIALPFFGIVSEI FT FPVFARKPIFGYKGLVFATISIAALSVSVWAHHMYVTGSVMLPFFGFMTMLIAVPTGVK FT FFNWIGTLWRGSITFETPMLWSMGFMITFLFGGLTGIILSAPVMDFHVSDTYFVVAHFH FT YVVFGTVVFAMFAGFYFWWPKWTGKMLNERLGKIHFWLLFIGFHGTFLIQHWLGVMGMP FT RRYADYMPEDGFTTMNQVSTVFAFILGASMIPFFWNVWVT