(data stored in SCRATCH zone)

SWISSPROT: B7UJP1_ECO27

ID   B7UJP1_ECO27            Unreviewed;       172 AA.
AC   B7UJP1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Phosphatidylglycerophosphatase A {ECO:0000256|PIRNR:PIRNR006162};
DE            EC=3.1.3.27 {ECO:0000256|PIRNR:PIRNR006162};
DE   AltName: Full=Phosphatidylglycerolphosphate phosphatase A {ECO:0000256|PIRNR:PIRNR006162};
GN   Name=pgpA {ECO:0000313|EMBL:CAS07901.1};
GN   OrderedLocusNames=E2348C_0353 {ECO:0000313|EMBL:CAS07901.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07901.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07901.1, 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: Lipid phosphatase which dephosphorylates
CC       phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
CC       {ECO:0000256|PIRNR:PIRNR006162}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-
CC         phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-
CC         glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716;
CC         EC=3.1.3.27; Evidence={ECO:0000256|PIRNR:PIRNR006162};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006162};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol
CC       biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step
CC       2/2. {ECO:0000256|PIRNR:PIRNR006162}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|PIRNR:PIRNR006162}; Multi-pass membrane protein
CC       {ECO:0000256|PIRNR:PIRNR006162}.
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DR   EMBL; FM180568; CAS07901.1; -; Genomic_DNA.
DR   RefSeq; WP_000154049.1; NC_011601.1.
DR   EnsemblBacteria; CAS07901; CAS07901; E2348C_0353.
DR   KEGG; ecg:E2348C_0353; -.
DR   HOGENOM; HOG000256112; -.
DR   KO; K01095; -.
DR   OMA; PKAPGTF; -.
DR   BioCyc; ECOL574521:E2348C_RS01855-MONOMER; -.
DR   UniPathway; UPA00084; UER00504.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd06971; PgpA; 1.
DR   InterPro; IPR026037; PgpA.
DR   InterPro; IPR036681; PgpA-like_sf.
DR   InterPro; IPR007686; YutG/PgpA.
DR   PANTHER; PTHR36305; PTHR36305; 1.
DR   Pfam; PF04608; PgpA; 1.
DR   PIRSF; PIRSF006162; PgpA; 1.
DR   SUPFAM; SSF101307; SSF101307; 1.
PE   4: Predicted;
DR   PRODOM; B7UJP1.
DR   SWISS-2DPAGE; B7UJP1.
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR006162};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR006162};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006162};
KW   Lipid degradation {ECO:0000256|PIRNR:PIRNR006162};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR006162};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR006162};
KW   Membrane {ECO:0000256|PIRNR:PIRNR006162, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006162};
KW   Phospholipid degradation {ECO:0000256|PIRNR:PIRNR006162};
KW   Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR006162};
KW   Transmembrane {ECO:0000256|PIRNR:PIRNR006162,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     21     51       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     57     75       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    138    162       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       22    162       PgpA. {ECO:0000259|Pfam:PF04608}.
SQ   SEQUENCE   172 AA;  19448 MW;  9DA1DD02CA23DDB9 CRC64;
     MTILPRHKDV AKSRLKMSNP WHLLAVGFGS GLSPIVPGTM GSLAAIPFWY LMTFLPWQLY
     SLVVMLGICI GVYLCHQTAK DMGVHDHGSI VWDEFIGMWI TLMALPTNDW QWVTAGFVIF
     RILDMWKPWP IRWFDRNVHG GMGIMIDDIV AGVISAGILY FIGHHWPLGI LS
//

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