LMPD Database

LMP007594

UniProt Annotations

Entry Information
Gene Namephosphatidylglycerophosphatase B
Protein EntryPGPB_ECOLI
UniProt IDP0A924
SpeciesE. coli
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=530 uM for undecaprenyl pyrophosphate {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; KM=96 uM for farnesyl pyrophosphate {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; KM=80 uM for diacylglycerol pyrophosphate {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; KM=1700 uM for phosphatidate {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; Vmax=2167 nmol/min/mg enzyme with diacylglycerol pyrophosphate as substrate {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; Vmax=313 nmol/min/mg enzyme with phosphatidate as substrate {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; pH dependence: Optimum pH is 6.5 for DGPP phosphatase activity and 6.5-7.5 for undecaprenyl pyrophosphate phosphatase activity. {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025};
Catalytic Activity1,2-diacyl-sn-glycerol 3-diphosphate + H(2)O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate.
Catalytic ActivityA 1,2-diacylglycerol 3-phosphate + H(2)O = a 1,2-diacyl-sn-glycerol + phosphate.
Catalytic ActivityDitrans,octacis-undecaprenyl diphosphate + H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate.
Catalytic ActivityPhosphatidylglycerophosphate + H(2)O = phosphatidylglycerol + phosphate.
Enzyme RegulationInhibited by Mn(2+) ions.
FunctionCatalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. The pattern of activities varies according to subcellular location, PGP phosphatase activity is higher in the cytoplasmic membrane, whereas PA and LPA phosphatase activities are higher in the outer membrane. Activity is independent of a divalent cation ion and insensitive to inhibition by N- ethylmaleimide. {ECO:0000269|PubMed:15778224, ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:21148555, ECO:0000269|PubMed:8940025}.
Mass SpectrometryMass=30151; Method=MALDI; Range=2-254; Note=Reported mass includes mass of a C-terminal His6 tag.; Evidence={ECO:0000269|PubMed:18411271};
PathwayPhospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
PtmThe N-terminus is blocked.
SimilarityBelongs to the PA-phosphatase related phosphoesterase family. {ECO:0000305}.
Subcellular LocationCell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. Cell outer membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.