(data stored in ACNUC9543 zone)

SWISSPROT: LPXA_YERPA

ID   LPXA_YERPA              Reviewed;         262 AA.
AC   Q1CAM2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 84.
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=YPA_0532;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of lipid A, a
CC       phosphorylated glycolipid that anchors the lipopolysaccharide to
CC       the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-
CC         glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00387};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-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.
CC       LpxA subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}.
DR   EMBL; CP000308; ABG12500.1; -; Genomic_DNA.
DR   RefSeq; WP_002212143.1; NZ_CP009906.1.
DR   SMR; Q1CAM2; -.
DR   EnsemblBacteria; ABG12500; ABG12500; YPA_0532.
DR   KEGG; ypa:YPA_0532; -.
DR   HOGENOM; HOG000294326; -.
DR   KO; K00677; -.
DR   OMA; ECVTINR; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000001971; 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; 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   3: Inferred from homology;
DR   PRODOM; Q1CAM2.
DR   SWISS-2DPAGE; Q1CAM2.
KW   Acyltransferase; Complete proteome; Cytoplasm; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Repeat; Transferase.
FT   CHAIN         1    262       Acyl-[acyl-carrier-protein]--UDP-N-
FT                                acetylglucosamine O-acyltransferase.
FT                                /FTId=PRO_0000302614.
SQ   SEQUENCE   262 AA;  28117 MW;  C749FF7F53216DF8 CRC64;
     MIDKTAFIHP SSIVEEGAII GAGVYIGPFC IVGSQVEIGA GTELKSHVVV NGITKIGCDN
     QIYQFASIGE ANQDLKYAGE PTRVEVGDRN RIRESVTIHR GTTQGGGVTK VGCDNLLMVN
     THVAHDCVIG NRCILANNAA LGGHVEIDDY AIIGGMTAIH QFCVIGAHVM VGGCSGITQD
     VPPFVIAQGN HATPFGINIE GLKRRGFDKE SLHAIRSAYK LLYRSGRTLD EVKPEIAELA
     EQYPVVKAFN DFFARSTRGI IR
//

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