PGPB_HAEIN
ID PGPB_HAEIN Reviewed; 241 AA.
AC P44570;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phosphatidylglycerophosphatase B;
DE EC=3.1.3.27;
DE AltName: Full=Diacylglycerol pyrophosphate phosphatase;
DE Short=DGPP phosphatase;
DE EC=3.1.3.81;
DE AltName: Full=Phosphatidate phosphatase;
DE EC=3.1.3.4;
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase;
DE EC=3.6.1.27;
DE AltName: Full=Undecaprenyl-diphosphatase;
GN Name=pgpB; OrderedLocusNames=HI_0211;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the dephosphorylation of diacylglycerol diphosphate
CC (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA
CC to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate
CC phosphatase activity, required for the biosynthesis of the lipid
CC carrier undecaprenyl phosphate. Can also use lysophosphatidic acid
CC (LPA) and phosphatidylglycerophosphate as substrates. The pattern of
CC activities varies according to subcellular location, PGP phosphatase
CC activity is higher in the cytoplasmic membrane, whereas PA and LPA
CC phosphatase activities are higher in the outer membrane. Activity is
CC independent of a divalent cation ion and insensitive to inhibition by
CC N-ethylmaleimide (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) +
CC H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate;
CC Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.1.3.81;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27;
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell outer membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; L42023; AAC21879.1; -; Genomic_DNA.
DR PIR; I64054; I64054.
DR RefSeq; NP_438379.1; NC_000907.1.
DR RefSeq; WP_005694086.1; NC_000907.1.
DR AlphaFoldDB; P44570; -.
DR SMR; P44570; -.
DR STRING; 71421.HI_0211; -.
DR EnsemblBacteria; AAC21879; AAC21879; HI_0211.
DR KEGG; hin:HI_0211; -.
DR PATRIC; fig|71421.8.peg.215; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_083863_0_0_6; -.
DR OMA; AWFLWCL; -.
DR PhylomeDB; P44570; -.
DR BioCyc; HINF71421:G1GJ1-221-MON; -.
DR UniPathway; UPA00084; UER00504.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050380; F:undecaprenyl-diphosphatase 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 InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell outer membrane; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Phospholipid degradation;
KW Phospholipid metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..241
FT /note="Phosphatidylglycerophosphatase B"
FT /id="PRO_0000058363"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 22..52
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 53..62
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 63..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 68..91
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 92..158
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 159..173
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 174..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 205..210
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 211..235
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 236..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT REGION 94..102
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000305"
FT REGION 157..160
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000305"
FT REGION 202..213
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000305"
FT ACT_SITE 160
FT /note="Proton donor; for a subset of substrates"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT ACT_SITE 209
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT SITE 213
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
SQ SEQUENCE 241 AA; 27491 MW; 86896C8B066D2A41 CRC64;
MFKRLSLYTL LLCLVPFFIW GISYQWHGNS QLTQADYWLY LLTETGSVPY ALITCVLFTL
LFAFLFKNPK QWILGVIVMG ISVIATQAAK TGAKALFEEP RPFTVYLAEQ THSTPENFYK
NDRTLRAEIA KNFYSMDAIT PAWLVHHYEN ETGYSFPSGH TIFAATWLML AVGFTQLLGN
RSFKAKLLVV GIAVWGLLML ISRVRLGMHY PIDLLVATLL AWLINSIIFA FLKKKAIFVM
K
