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   24-JAN-2024, entry version 149.
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; Pseudomonadota; 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   ChEMBL; CHEMBL4879550; -.
DR   SwissLipids; SLP:000001883; -.
DR   jPOST; P0A722; -.
DR   PaxDb; 511145-b0181; -.
DR   EnsemblBacteria; AAC73292; AAC73292; b0181.
DR   GeneID; 75202006; -.
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   OrthoDB; 9807278at2; -.
DR   PhylomeDB; P0A722; -.
DR   BioCyc; EcoCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER; -.
DR   BioCyc; MetaCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER; -.
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; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 1.20.1180.10; Udp N-acetylglucosamine O-acyltransferase, C-terminal domain; 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   NCBIfam; TIGR01852; lipid_A_lpxA; 1.
DR   PANTHER; PTHR43480; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR43480:SF1; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF13720; Acetyltransf_11; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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
//