(data stored in SCRATCH zone)

SWISSPROT: C8U2A2_ECO10

ID   C8U2A2_ECO10            Unreviewed;       172 AA.
AC   C8U2A2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
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:BAI29260.1};
GN   OrderedLocusNames=ECO103_0392 {ECO:0000313|EMBL:BAI29260.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29260.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29260.1, 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: 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; AP010958; BAI29260.1; -; Genomic_DNA.
DR   RefSeq; WP_000154044.1; NC_013353.1.
DR   EnsemblBacteria; BAI29260; BAI29260; ECO103_0392.
DR   KEGG; eoh:ECO103_0392; -.
DR   HOGENOM; HOG000256112; -.
DR   KO; K01095; -.
DR   OMA; PKAPGTF; -.
DR   BioCyc; ECOL585395:ECO103_RS02055-MONOMER; -.
DR   UniPathway; UPA00084; UER00504.
DR   Proteomes; UP000000959; 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; C8U2A2.
DR   SWISS-2DPAGE; C8U2A2.
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR006162};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR006162};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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;  19418 MW;  9DA1C817CA36C8B9 CRC64;
     MTILPRHKDV AKSRLKMSNP WHLLAVGFGS GLSPIVPGTM GSLAAIPFWY LMTFLPWQLY
     SLVVMLGICI GVYLCHQTAK DMGVHDHGSI VWDEFIGMWI TLMALPTNDW QWVAAGFVIF
     RILDMWKPWP IRWFDRNVHG GMGIMIDDIV AGVISAGILY FIGHHWPLGI LS
//

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