(data stored in ACNUC7421 zone)

SWISSPROT: Q3Z4H0_SHISS

ID   Q3Z4H0_SHISS            Unreviewed;       160 AA.
AC   Q3Z4H0;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 83.
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:AAZ87342.1};
GN   Synonyms=pagP {ECO:0000256|HAMAP-Rule:MF_00837};
GN   OrderedLocusNames=SSON_0576 {ECO:0000313|EMBL:AAZ87342.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87342.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87342.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87342.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87342.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87342; AAZ87342; SSON_0576.
DR   KEGG; ssn:SSON_0576; -.
DR   HOGENOM; HOG000117945; -.
DR   KO; K12973; -.
DR   OMA; AQTWNEP; -.
DR   Proteomes; UP000002529; 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; Q3Z4H0.
DR   SWISS-2DPAGE; Q3Z4H0.
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:UP000002529};
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}.
FT   ACT_SITE     32     32       {ECO:0000256|HAMAP-Rule:MF_00837}.
FT   ACT_SITE     75     75       {ECO:0000256|HAMAP-Rule:MF_00837}.
FT   ACT_SITE     76     76       {ECO:0000256|HAMAP-Rule:MF_00837}.
FT   SITE         41     41       Role in lipopolysaccharide recognition.
FT                                {ECO:0000256|HAMAP-Rule:MF_00837}.
FT   SITE        146    146       Role in the phospholipid gating.
FT                                {ECO:0000256|HAMAP-Rule:MF_00837}.
SQ   SEQUENCE   160 AA;  18805 MW;  CFE5CCA2564EA6D3 CRC64;
     MESLPTTFRE NIAQTWQQPE HYDLYIPAIT WHARFAYDKE KTDRYNERPW GGGFGQSRWD
     EKGNWHGLYA MAFKDSWNKW EPIAGYGWES TWRPLADENF HLGLGFTAGV TARDNWNYIP
     LPVLLPLASV GYGPVTFQMT YIPGTYNNGN VYFAWMRFQF
//

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