(data stored in ACNUC7421 zone)

SWISSPROT: Q3Z4Z1_SHISS

ID   Q3Z4Z1_SHISS            Unreviewed;       172 AA.
AC   Q3Z4Z1;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 85.
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:AAZ87171.1};
GN   OrderedLocusNames=SSON_0395 {ECO:0000313|EMBL:AAZ87171.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87171.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87171.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87171.1,
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: 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; CP000038; AAZ87171.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87171; AAZ87171; SSON_0395.
DR   KEGG; ssn:SSON_0395; -.
DR   HOGENOM; HOG000256112; -.
DR   KO; K01095; -.
DR   OMA; PKAPGTF; -.
DR   BioCyc; SSON300269:G1GL2-457-MONOMER; -.
DR   UniPathway; UPA00084; UER00504.
DR   Proteomes; UP000002529; 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; Q3Z4Z1.
DR   SWISS-2DPAGE; Q3Z4Z1.
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR006162};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR006162};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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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