(data stored in ACNUC1104 zone)

SWISSPROT: E6V5D2_VARPE

ID   E6V5D2_VARPE            Unreviewed;       195 AA.
AC   E6V5D2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 48.
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   OrderedLocusNames=Varpa_0517 {ECO:0000313|EMBL:ADU34738.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34738.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34738.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34738.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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; CP002417; ADU34738.1; -; Genomic_DNA.
DR   STRING; 595537.Varpa_0517; -.
DR   EnsemblBacteria; ADU34738; ADU34738; Varpa_0517.
DR   KEGG; vpe:Varpa_0517; -.
DR   eggNOG; COG1267; LUCA.
DR   HOGENOM; HOG000256113; -.
DR   KO; K01095; -.
DR   OMA; PKAPGTF; -.
DR   UniPathway; UPA00084; UER00504.
DR   Proteomes; UP000008917; 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; E6V5D2.
DR   SWISS-2DPAGE; E6V5D2.
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR006162};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR006162};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
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   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Transmembrane {ECO:0000256|PIRNR:PIRNR006162,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     58     91       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    112    136       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    167    192       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       36    192       PgpA. {ECO:0000259|Pfam:PF04608}.
SQ   SEQUENCE   195 AA;  21235 MW;  23886B2F6EC4E755 CRC64;
     MQAASPSSSS HATASGAMPQ PSIRRPTLRF LFGHPAHAIA LGFGSGLPRF APGTVGTLWA
     WVAFAVMQLW FTPATIGWII LASLPIGWWA CTVTARDMNI ADPGAIVWDE VVAFWIVLWL
     VTPAGLFAQA IAFGLFRFFD AAKPGPVAWA DGLFKQRDAV QTSQVRWWHA GFGIILDDLV
     AAFCTLLVIA LWRAW
//

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