(data stored in ACNUC10821 zone)

SWISSPROT: C8U2Y5_ECO10

ID   C8U2Y5_ECO10            Unreviewed;       186 AA.
AC   C8U2Y5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Lipid A palmitoyltransferase PagP {ECO:0000256|HAMAP-Rule:MF_00837, ECO:0000256|SAAS:SAAS00061485};
DE            EC=2.3.1.251 {ECO:0000256|HAMAP-Rule:MF_00837, ECO:0000256|SAAS:SAAS00527268};
DE   AltName: Full=Lipid A acylation protein {ECO:0000256|HAMAP-Rule:MF_00837};
GN   Name=crcA {ECO:0000313|EMBL:BAI29493.1};
GN   Synonyms=pagP {ECO:0000256|HAMAP-Rule:MF_00837};
GN   OrderedLocusNames=ECO103_0630 {ECO:0000313|EMBL:BAI29493.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29493.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29493.1, 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: Transfers a palmitate residue from the sn-1 position of
CC       a phospholipid to the N-linked hydroxymyristate on the proximal
CC       unit of lipid A or its precursors. {ECO:0000256|HAMAP-
CC       Rule:MF_00837, ECO:0000256|SAAS:SAAS00527260}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid
CC         A (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl
CC         lipid A; Xref=Rhea:RHEA:46864, ChEBI:CHEBI:57875,
CC         ChEBI:CHEBI:77369, ChEBI:CHEBI:87048, ChEBI:CHEBI:134257;
CC         EC=2.3.1.251; Evidence={ECO:0000256|HAMAP-Rule:MF_00837,
CC         ECO:0000256|SAAS:SAAS01122393};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid
CC         IIA = a 2-acyl-sn-glycero-3-phosphocholine + lipid IIB;
CC         Xref=Rhea:RHEA:46872, ChEBI:CHEBI:57875, ChEBI:CHEBI:77369,
CC         ChEBI:CHEBI:86226, ChEBI:CHEBI:87058; EC=2.3.1.251;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00837,
CC         ECO:0000256|SAAS:SAAS01122394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid
CC         IVA (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + lipid
CC         IVB; Xref=Rhea:RHEA:46868, ChEBI:CHEBI:57875, ChEBI:CHEBI:58603,
CC         ChEBI:CHEBI:77369, ChEBI:CHEBI:87049; EC=2.3.1.251;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00837,
CC         ECO:0000256|SAAS:SAAS01122392};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00837,
CC       ECO:0000256|SAAS:SAAS00061416}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00837, ECO:0000256|SAAS:SAAS00064691}.
CC   -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00837, ECO:0000256|SAAS:SAAS00559749}.
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DR   EMBL; AP010958; BAI29493.1; -; Genomic_DNA.
DR   RefSeq; WP_001103094.1; NC_013353.1.
DR   SMR; C8U2Y5; -.
DR   EnsemblBacteria; BAI29493; BAI29493; ECO103_0630.
DR   KEGG; eoh:ECO103_0630; -.
DR   HOGENOM; HOG000117945; -.
DR   KO; K12973; -.
DR   OMA; AQTWNEP; -.
DR   BioCyc; ECOL585395:ECO103_RS03285-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016416; F:O-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00837; PagP_transferase; 1.
DR   InterPro; IPR011250; OMP/PagP_b-brl.
DR   InterPro; IPR009746; Peptid-resist/lipidA_acyl_PagP.
DR   Pfam; PF07017; PagP; 1.
DR   ProDom; PD103779; PagP; 1.
DR   SUPFAM; SSF56925; SSF56925; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2Y5.
DR   SWISS-2DPAGE; C8U2Y5.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00837,
KW   ECO:0000256|SAAS:SAAS00064682};
KW   Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_00837,
KW   ECO:0000256|SAAS:SAAS00061470};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00837,
KW   ECO:0000256|SAAS:SAAS00448558};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00837};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00837,
KW   ECO:0000256|SAAS:SAAS00446759, ECO:0000313|EMBL:BAI29493.1}.
FT   ACT_SITE     58     58       {ECO:0000256|HAMAP-Rule:MF_00837}.
FT   ACT_SITE    101    101       {ECO:0000256|HAMAP-Rule:MF_00837}.
FT   ACT_SITE    102    102       {ECO:0000256|HAMAP-Rule:MF_00837}.
FT   SITE         67     67       Role in lipopolysaccharide recognition.
FT                                {ECO:0000256|HAMAP-Rule:MF_00837}.
FT   SITE        172    172       Role in the phospholipid gating.
FT                                {ECO:0000256|HAMAP-Rule:MF_00837}.
SQ   SEQUENCE   186 AA;  21770 MW;  4BC35B02286844A7 CRC64;
     MNVSKYVAIF SFVFIQLISV GKVFANADEW MTTFRENIAQ TWQQPEHYDL YIPAITWHAR
     FAYDKEKTDR YNERPWGGGF GLSRWDEKGN WHGLYAMAFK DSWNKWEPIA GYGWESTWRP
     LADENFHLGL GFTAGVTARD NWNYIPLPVL LPLASVGYGP VTFQMTYIPG TYNNGNVYFA
     WMRFQF
//

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