(data stored in SCRATCH zone)

SWISSPROT: B7UKR4_ECO27

ID   B7UKR4_ECO27            Unreviewed;       186 AA.
AC   B7UKR4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
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=pagP {ECO:0000256|HAMAP-Rule:MF_00837,
GN   ECO:0000313|EMBL:CAS08071.1};
GN   OrderedLocusNames=E2348C_0523 {ECO:0000313|EMBL:CAS08071.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08071.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08071.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
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: 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; FM180568; CAS08071.1; -; Genomic_DNA.
DR   RefSeq; WP_001339337.1; NC_011601.1.
DR   EnsemblBacteria; CAS08071; CAS08071; E2348C_0523.
DR   KEGG; ecg:E2348C_0523; -.
DR   HOGENOM; HOG000117945; -.
DR   KO; K12973; -.
DR   OMA; AQTWNEP; -.
DR   BioCyc; ECOL574521:E2348C_RS02750-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UKR4.
DR   SWISS-2DPAGE; B7UKR4.
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:UP000008205};
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:CAS08071.1}.
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;  21624 MW;  17630222F5BE015C CRC64;
     MSTGKYIYAL LFVFTQLVGI EDASADTPQW LSTFKENVAE TWQQPQHYDL YIPAITWHAR
     FAYDKEKTDR YNERPWGGGF GQSRWDEKGN WHGLYAMAFK DSWNKWEPIA GYGWESTWRP
     LADENFHLGL GFTAGVTARD NWNYIPLPVL LPLASVGYGP ATFQMTYIPG TYNNGNVYFA
     WMRFQF
//

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