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PAGP_SHIF2
ID   PAGP_SHIF2              Reviewed;         186 AA.
AC   D2AA19;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Lipid A palmitoyltransferase PagP {ECO:0000255|HAMAP-Rule:MF_00837};
DE            EC=2.3.1.251 {ECO:0000255|HAMAP-Rule:MF_00837};
DE   AltName: Full=Lipid A acylation protein {ECO:0000255|HAMAP-Rule:MF_00837};
DE   Flags: Precursor;
GN   Name=pagP {ECO:0000255|HAMAP-Rule:MF_00837}; OrderedLocusNames=SFxv_0725;
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017;
RX   PubMed=19955273; DOI=10.1128/jcm.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(2010).
CC   -!- FUNCTION: Transfers a palmitate residue from the sn-1 position of a
CC       phospholipid to the N-linked hydroxymyristate on the proximal unit of
CC       lipid A or its precursors. {ECO:0000255|HAMAP-Rule:MF_00837}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid A
CC         (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid
CC         A; Xref=Rhea:RHEA:46864, ChEBI:CHEBI:57875, ChEBI:CHEBI:77369,
CC         ChEBI:CHEBI:87048, ChEBI:CHEBI:134257; EC=2.3.1.251;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00837};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA
CC         = 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:0000255|HAMAP-Rule:MF_00837};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA
CC         (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + lipid IVB;
CC         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:0000255|HAMAP-Rule:MF_00837};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00837}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00837}.
CC   -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00837}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADA73024.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001383; ADA73024.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005049488.1; NC_017328.1.
DR   AlphaFoldDB; D2AA19; -.
DR   BMRB; D2AA19; -.
DR   SMR; D2AA19; -.
DR   EnsemblBacteria; ADA73024; ADA73024; SFxv_0725.
DR   KEGG; sfe:SFxv_0725; -.
DR   PATRIC; fig|591020.3.peg.768; -.
DR   HOGENOM; CLU_104099_0_0_6; -.
DR   Proteomes; UP000001884; 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   SUPFAM; SSF56925; SSF56925; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell outer membrane; Membrane; Signal; Transferase.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   CHAIN           26..186
FT                   /note="Lipid A palmitoyltransferase PagP"
FT                   /id="PRO_0000414477"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   SITE            67
FT                   /note="Role in lipopolysaccharide recognition"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   SITE            172
FT                   /note="Role in the phospholipid gating"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ   SEQUENCE   186 AA;  21740 MW;  3BB35C055A4F6487 CRC64;
     MNVSKYVAIF SFVFIQLISV GKVFANADER MTTFRENIAQ TWQQPEHYDL YIPAITWHAR
     FAYDKEKTDR YNERPWGGGF GLSRWDEKGN WHGLYAMAFK DSWNKWEPIA GYGWESTWRP
     LADENFHLGL GFTAGVTARD NWNYIPLPVL LPLASVGYGP VTFQMTYIPG TYNNGNVYFA
     WMRFQF
 
 
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