LPXA_HELPY
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 03-AUG-2022, entry version 130.
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}; OrderedLocusNames=HP_1375;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; 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.C694_07095; -.
DR DrugBank; DB08558; 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL.
DR DrugBank; DB01694; D-tartaric acid.
DR PaxDb; O25927; -.
DR EnsemblBacteria; AAD08418; AAD08418; HP_1375.
DR KEGG; hpy:HP_1375; -.
DR PATRIC; fig|85962.47.peg.1472; -.
DR eggNOG; COG1043; Bacteria.
DR OMA; ECVTINR; -.
DR PhylomeDB; O25927; -.
DR BioCyc; MetaCyc:HP_RS06790-MON; -.
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; 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; 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; 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
