ID   LPXA_HELPY              Reviewed;         270 AA.
AC   O25927;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 138.
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=HP_1375;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH R-3-HYDROXY-ACYL
RP   CARRIER PROTEIN, AND SUBUNIT.
RX   PubMed=14579368; DOI=10.1002/prot.10436;
RA   Lee B.I., Suh S.W.;
RT   "Crystal structure of UDP-N-acetylglucosamine acyltransferase from
RT   Helicobacter pylori.";
RL   Proteins 53:772-774(2003).
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. {ECO:0000255|HAMAP-Rule:MF_00387}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00387}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}.
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DR   EMBL; AE000511; AAD08418.1; -; Genomic_DNA.
DR   PIR; G64691; G64691.
DR   RefSeq; NP_208166.1; NC_000915.1.
DR   RefSeq; WP_000034151.1; NC_018939.1.
DR   PDB; 1J2Z; X-ray; 2.10 A; A=1-270.
DR   PDBsum; 1J2Z; -.
DR   AlphaFoldDB; O25927; -.
DR   SMR; O25927; -.
DR   STRING; 85962.HP_1375; -.
DR   DrugBank; DB08558; 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL.
DR   DrugBank; DB01694; D-tartaric acid.
DR   PaxDb; 85962-C694_07095; -.
DR   EnsemblBacteria; AAD08418; AAD08418; HP_1375.
DR   KEGG; hpy:HP_1375; -.
DR   PATRIC; fig|85962.47.peg.1472; -.
DR   eggNOG; COG1043; Bacteria.
DR   InParanoid; O25927; -.
DR   OrthoDB; 9807278at2; -.
DR   PhylomeDB; O25927; -.
DR   BioCyc; MetaCyc:HP_RS06790-MONOMER; -.
DR   UniPathway; UPA00359; UER00477.
DR   EvolutionaryTrace; O25927; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-UniRule.
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; 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; 1.
DR   PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
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..270
FT                   /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT                   O-acyltransferase"
FT                   /id="PRO_0000188052"
FT   BINDING         69..72
FT                   /ligand="substrate"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   STRAND          103..107
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   HELIX           195..201
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   HELIX           204..217
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   HELIX           224..234
FT                   /evidence="ECO:0007829|PDB:1J2Z"
FT   HELIX           239..250
FT                   /evidence="ECO:0007829|PDB:1J2Z"
SQ   SEQUENCE   270 AA;  29855 MW;  3668DF2ED248BA4E CRC64;
     MSKIAKTAII SPKAEINKGV EIGEFCVIGD GVKLDEGVKL HNNVTLQGHT FVGKNTEIFP
     FAVLGTQPQD LKYKGEYSEL IIGEDNLIRE FCMINPGTEG GIKKTLIGDK NLLMAYVHVA
     HDCVIGSHCI LANGVTLAGH IEIGDYVNIG GLTAIHQFVR IAKGCMIAGK SALGKDVPPY
     CTVEGNRAFI RGLNRHRMRQ LLESKDIDFI YALYKRLFRP IPSLRESAKL ELEEHANNPF
     VKEICSFILE SSRGVAYKSS EYSSEEKQEE
//