(data stored in ACNUC7421 zone)

SWISSPROT: LPXA_ECO27

ID   LPXA_ECO27              Reviewed;         262 AA.
AC   B7UJ82;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
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=E2348C_0186;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS07734.1; -; Genomic_DNA.
DR   RefSeq; WP_000565966.1; NC_011601.1.
DR   SMR; B7UJ82; -.
DR   EnsemblBacteria; CAS07734; CAS07734; E2348C_0186.
DR   KEGG; ecg:E2348C_0186; -.
DR   KO; K00677; -.
DR   OMA; ECVTINR; -.
DR   BioCyc; ECOL574521:E2348C_RS00960-MONOMER; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000008205; 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; B7UJ82.
DR   SWISS-2DPAGE; B7UJ82.
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_1000134383.
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
//

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