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InterPro: IPR018357 Hexapeptide transferase, conserved site
Protein matches
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UniProtKB Matches: 7230 proteins |
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Accession
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IPR018357 Hexapep_transf_CS |
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Type
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Conserved_site |
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Signatures
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InterPro Relationships
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Found in
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IPR001451 Bacterial transferase hexapeptide repeat
IPR005664 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase
IPR005881 Serine O-acetyltransferase
IPR005882 Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
IPR007691 UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase
IPR010137 Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
IPR011004 Trimeric LpxA-like
IPR017694 Phosphonate metabolim protein, transferase hexapeptide repeat family
IPR019873 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase
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GO Term annotation
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Function
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GO:0016740 transferase activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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A variety of bacterial transferases contain a repeat structure composed of tandem repeats of a [LIV]-G-X(4) hexapeptide, which, in the tertiary structure of LpxA (UDP N-acetylglucosamine acyltransferase) [1], has been shown to form a left-handed parallel beta helix. A number of different transferase protein families contain this repeat, such as galactoside acetyltransferase-like proteins [2], the gamma-class of carbonic anhydrases [3], and tetrahydrodipicolinate-N-succinlytransferases (DapD), the latter containing an extra N-terminal 3-helical domain [4].
The signature pattern of this entry represents a fourfold repeat of the a [LIV]-G-x(4) hexapeptide.
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Structural links
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Database links
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Publications
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1.
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Raetz CR, Roderick SL.
A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase.
Science 270 997-1000 1995
[PubMed: 7481807]
http://www.sciencemag.org/cgi/content/abstract/270/5238/997
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2.
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Wang XG, Olsen LR, Roderick SL.
Structure of the lac operon galactoside acetyltransferase.
Structure 10 581-8 2002
[PubMed: 11937062]
http://dx.doi.org/10.1016/S0969-2126(02)00741-4
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3.
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Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC.
A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila.
Biochemistry 39 9222-31 2000
[PubMed: 10924115]
http://dx.doi.org/10.1021/bi000204s
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4.
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Beaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL.
Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.
Protein Sci. 11 974-9 2002
[PubMed: 11910040]
http://dx.doi.org/10.1110/ps.4310102
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Additional Reading
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Ulaganathan V, Buetow L, Hunter WN.
Nucleotide substrate recognition by UDP-N-acetylglucosamine acyltransferase (LpxA) in the first step of lipid A biosynthesis.
J. Mol. Biol. 369 2007 305-12
[PubMed: 17434525]
http://dx.doi.org/10.1016/j.jmb.2007.03.039
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Vaara M.
Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme.
FEMS Microbiol. Lett. 76 1992 249-54
[PubMed: 1427014]
http://dx.doi.org/10.1016/0378-1097(92)90344-N
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Olsen LR, Vetting MW, Roderick SL.
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Protein Sci. 16 2007 1230-5
[PubMed: 17473010]
http://dx.doi.org/10.1110/ps.072779707
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Nguyen L, Kozlov G, Gehring K.
Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding.
FEBS Lett. 582 2008 623-6
[PubMed: 18242192]
http://dx.doi.org/10.1016/j.febslet.2008.01.032
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Mochalkin I, Lightle S, Narasimhan L, Bornemeier D, Melnick M, Vanderroest S, McDowell L.
Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site.
Protein Sci. 17 2008 577-82
[PubMed: 18218712]
http://dx.doi.org/10.1110/ps.073271408
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Parent R, Roy PH.
The chloramphenicol acetyltransferase gene of Tn2424: a new breed of cat.
J. Bacteriol. 174 1992 2891-7
[PubMed: 1314803]
http://jb.asm.org/cgi/content/abstract/174/9/2891
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Mochalkin I, Lightle S, Zhu Y, Ohren JF, Spessard C, Chirgadze NY, Banotai C, Melnick M, McDowell L.
Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).
Protein Sci. 16 2007 2657-66
[PubMed: 18029420]
http://dx.doi.org/10.1110/ps.073135107
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Downie JA.
The nodL gene from Rhizobium leguminosarum is homologous to the acetyl transferases encoded by lacA and cysE.
Mol. Microbiol. 3 1989 1649-51
[PubMed: 2615659]
http://dx.doi.org/10.1111/j.1365-2958.1989.tb00150.x
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Vuorio R, Harkonen T, Tolvanen M, Vaara M.
The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of lipid A biosynthesis is conserved in various bacteria.
FEBS Lett. 337 1994 289-92
[PubMed: 8293817]
http://dx.doi.org/10.1016/0014-5793(94)80211-4
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InterPro 23.1
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