LPXA_ECOLI
ID LPXA_ECOLI Reviewed; 262 AA.
AC P0A722; P10440; P78243;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387};
GN Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387};
GN OrderedLocusNames=b0181, JW0176;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3277952; DOI=10.1128/jb.170.3.1268-1274.1988;
RA Coleman J., Raetz C.R.H.;
RT "First committed step of lipid A biosynthesis in Escherichia coli: sequence
RT of the lpxA gene.";
RL J. Bacteriol. 170:1268-1274(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 64-65 AND 125.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-262.
RX PubMed=2824445; DOI=10.1128/jb.169.12.5727-5734.1987;
RA Crowell D.N., Reznikoff W.S., Raetz C.R.H.;
RT "Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide
RT synthase.";
RL J. Bacteriol. 169:5727-5734(1987).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RX PubMed=7481807; DOI=10.1126/science.270.5238.997;
RA Raetz C.R.H., Roderick S.L.;
RT "A left-handed parallel beta helix in the structure of UDP-N-
RT acetylglucosamine acyltransferase.";
RL Science 270:997-1000(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP SUBUNIT.
RX PubMed=16835299; DOI=10.1073/pnas.0604465103;
RA Williams A.H., Immormino R.M., Gewirth D.T., Raetz C.R.;
RT "Structure of UDP-N-acetylglucosamine acyltransferase with a bound
RT antibacterial pentadecapeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10877-10882(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
RP UDP-N-ACETYL-GLUCOSAMINE, AND SUBUNIT.
RX PubMed=17434525; DOI=10.1016/j.jmb.2007.03.039;
RA Ulaganathan V., Buetow L., Hunter W.N.;
RT "Nucleotide substrate recognition by UDP-N-acetylglucosamine
RT acyltransferase (LpxA) in the first step of lipid A biosynthesis.";
RL J. Mol. Biol. 369:305-312(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH
RP UDP-3-O-(R-3-HYDROXYMYRISTOYL)-GLCNAC, AND SUBUNIT.
RX PubMed=17698807; DOI=10.1073/pnas.0705833104;
RA Williams A.H., Raetz C.R.;
RT "Structural basis for the acyl chain selectivity and mechanism of UDP-N-
RT acetylglucosamine acyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13543-13550(2007).
CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated
CC glycolipid that anchors the lipopolysaccharide to the outer membrane of
CC the cell.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine =
CC a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-
CC [ACP]; Xref=Rhea:RHEA:67812, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:57705, ChEBI:CHEBI:64479, ChEBI:CHEBI:78827,
CC ChEBI:CHEBI:173225; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00387};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 1/6. {ECO:0000255|HAMAP-
CC Rule:MF_00387}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387,
CC ECO:0000269|PubMed:16835299, ECO:0000269|PubMed:17434525,
CC ECO:0000269|PubMed:17698807}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}.
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DR EMBL; M19334; AAC36918.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08610.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73292.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77856.2; -; Genomic_DNA.
DR PIR; E64742; XUECDP.
DR RefSeq; NP_414723.1; NC_000913.3.
DR RefSeq; WP_000565966.1; NZ_STEB01000032.1.
DR PDB; 1LXA; X-ray; 2.60 A; A=1-262.
DR PDB; 2AQ9; X-ray; 1.80 A; A=1-262.
DR PDB; 2JF2; X-ray; 1.80 A; A=1-262.
DR PDB; 2JF3; X-ray; 3.00 A; A=1-262.
DR PDB; 2QIA; X-ray; 1.74 A; A=1-262.
DR PDB; 2QIV; X-ray; 1.85 A; X=1-262.
DR PDB; 4J09; X-ray; 1.90 A; A=1-262.
DR PDB; 6HY2; X-ray; 1.60 A; X=1-262.
DR PDB; 6P9P; X-ray; 2.00 A; A=1-262.
DR PDB; 6P9Q; X-ray; 1.70 A; A=1-262.
DR PDB; 6P9R; X-ray; 1.75 A; A=1-262.
DR PDB; 6P9S; X-ray; 1.70 A; A=1-262.
DR PDB; 6P9T; X-ray; 1.75 A; A=1-262.
DR PDBsum; 1LXA; -.
DR PDBsum; 2AQ9; -.
DR PDBsum; 2JF2; -.
DR PDBsum; 2JF3; -.
DR PDBsum; 2QIA; -.
DR PDBsum; 2QIV; -.
DR PDBsum; 4J09; -.
DR PDBsum; 6HY2; -.
DR PDBsum; 6P9P; -.
DR PDBsum; 6P9Q; -.
DR PDBsum; 6P9R; -.
DR PDBsum; 6P9S; -.
DR PDBsum; 6P9T; -.
DR AlphaFoldDB; P0A722; -.
DR SMR; P0A722; -.
DR BioGRID; 4261091; 390.
DR DIP; DIP-48043N; -.
DR IntAct; P0A722; 36.
DR STRING; 511145.b0181; -.
DR BindingDB; P0A722; -.
DR SwissLipids; SLP:000001883; -.
DR jPOST; P0A722; -.
DR PaxDb; P0A722; -.
DR PRIDE; P0A722; -.
DR EnsemblBacteria; AAC73292; AAC73292; b0181.
DR EnsemblBacteria; BAA77856; BAA77856; BAA77856.
DR GeneID; 67416257; -.
DR GeneID; 944849; -.
DR KEGG; ecj:JW0176; -.
DR KEGG; eco:b0181; -.
DR PATRIC; fig|1411691.4.peg.2098; -.
DR EchoBASE; EB0540; -.
DR eggNOG; COG1043; Bacteria.
DR HOGENOM; CLU_061249_0_0_6; -.
DR InParanoid; P0A722; -.
DR OMA; ECVTINR; -.
DR PhylomeDB; P0A722; -.
DR BioCyc; EcoCyc:UDPNACETYLGLUCOSAMACYLTRANS-MON; -.
DR BioCyc; MetaCyc:UDPNACETYLGLUCOSAMACYLTRANS-MON; -.
DR BRENDA; 2.3.1.129; 2026.
DR UniPathway; UPA00359; UER00477.
DR EvolutionaryTrace; P0A722; -.
DR PRO; PR:P0A722; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03351; LbH_UDP-GlcNAc_AT; 1.
DR Gene3D; 1.20.1180.10; -; 1.
DR HAMAP; MF_00387; LpxA; 1.
DR InterPro; IPR029098; Acetyltransf_C.
DR InterPro; IPR037157; Acetyltransf_C_sf.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR010137; Lipid_A_LpxA.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43480; PTHR43480; 1.
DR Pfam; PF13720; Acetyltransf_11; 1.
DR Pfam; PF00132; Hexapep; 2.
DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01852; lipid_A_lpxA; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..262
FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT O-acyltransferase"
FT /id="PRO_0000188046"
FT BINDING 73..76
FT /ligand="substrate"
FT BINDING 125
FT /ligand="substrate"
FT BINDING 144
FT /ligand="substrate"
FT BINDING 161
FT /ligand="substrate"
FT VARIANT 189
FT /note="G -> S (in strain: SM101; temperature-sensitive)"
FT CONFLICT 64..65
FT /note="QF -> SV (in Ref. 1; AAC36918)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="H -> D (in Ref. 1; AAC36918)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2JF3"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2JF3"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6HY2"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6HY2"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6HY2"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6HY2"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6HY2"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:6HY2"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:6HY2"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6HY2"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6HY2"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:6HY2"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6HY2"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:6HY2"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:6HY2"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:6HY2"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6HY2"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:6HY2"
SQ SEQUENCE 262 AA; 28080 MW; B42B076F0045B44C CRC64;
MIDKSAFVHP TAIVEEGASI GANAHIGPFC IVGPHVEIGE GTVLKSHVVV NGHTKIGRDN
EIYQFASIGE VNQDLKYAGE PTRVEIGDRN RIRESVTIHR GTVQGGGLTK VGSDNLLMIN
AHIAHDCTVG NRCILANNAT LAGHVSVDDF AIIGGMTAVH QFCIIGAHVM VGGCSGVAQD
VPPYVIAQGN HATPFGVNIE GLKRRGFSRE AITAIRNAYK LIYRSGKTLD EVKPEIAELA
ETYPEVKAFT DFFARSTRGL IR
