(data stored in SCRATCH zone)

SWISSPROT: C8U1P9_ECO10

ID   C8U1P9_ECO10            Unreviewed;       262 AA.
AC   C8U1P9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00720086};
DE            Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE            EC=2.3.1.129 {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01080267};
GN   Name=lpxA {ECO:0000256|HAMAP-Rule:MF_00387,
GN   ECO:0000313|EMBL:BAI29057.1};
GN   OrderedLocusNames=ECO103_0179 {ECO:0000313|EMBL:BAI29057.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29057.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29057.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS00943771}.
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:0000256|HAMAP-
CC         Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};
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:0000256|HAMAP-
CC       Rule:MF_00387, ECO:0000256|SAAS:SAAS01080285}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS01080283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS00943784}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       LpxA subfamily. {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS01080288}.
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DR   EMBL; AP010958; BAI29057.1; -; Genomic_DNA.
DR   RefSeq; WP_000565966.1; NC_013353.1.
DR   SMR; C8U1P9; -.
DR   EnsemblBacteria; BAI29057; BAI29057; ECO103_0179.
DR   KEGG; eoh:ECO103_0179; -.
DR   HOGENOM; HOG000294326; -.
DR   KO; K00677; -.
DR   OMA; ECVTINR; -.
DR   BioCyc; ECOL585395:ECO103_RS00915-MONOMER; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000000959; 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; C8U1P9.
DR   SWISS-2DPAGE; C8U1P9.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080269};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS00943803};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080263};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080278};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080268};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS00720071};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080266, ECO:0000313|EMBL:BAI29057.1}.
FT   DOMAIN      180    261       Acetyltransf_11. {ECO:0000259|Pfam:
FT                                PF13720}.
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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