PGPB_SHIFL
ID PGPB_SHIFL Reviewed; 254 AA.
AC P0A926; P18201;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=SF1282, S1365;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AE005674; AAN42894.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16778.1; -; Genomic_DNA.
DR RefSeq; NP_707187.1; NC_004337.2.
DR RefSeq; WP_001256538.1; NZ_WPGW01000009.1.
DR AlphaFoldDB; P0A926; -.
DR SMR; P0A926; -.
DR STRING; 198214.SF1282; -.
DR EnsemblBacteria; AAN42894; AAN42894; SF1282.
DR EnsemblBacteria; AAP16778; AAP16778; S1365.
DR GeneID; 1024235; -.
DR GeneID; 66674897; -.
DR KEGG; sfl:SF1282; -.
DR KEGG; sfx:S1365; -.
DR PATRIC; fig|198214.7.peg.1503; -.
DR HOGENOM; CLU_083863_0_0_6; -.
DR OMA; AWFLWCL; -.
DR OrthoDB; 1928533at2; -.
DR UniPathway; UPA00084; UER00504.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; IEA:UniProtKB-SubCell.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT CHAIN 2..254
FT /note="Phosphatidylglycerophosphatase B"
FT /id="PRO_0000058364"
FT TRANSMEM 2..24
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 25..54
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 55..66
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 67..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 95..161
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 162..176
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 177..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 203..208
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TRANSMEM 209..232
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT TOPO_DOM 233..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT REGION 97..105
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000305"
FT REGION 160..163
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000305"
FT REGION 200..211
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000305"
FT ACT_SITE 163
FT /note="Proton donor; for a subset of substrates"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT SITE 211
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
SQ SEQUENCE 254 AA; 29021 MW; 9F4E6E88C34D458C CRC64;
MRSIARRTAV GAALLLVMPV AVWISGWRWQ PGEQSWLLKA AFWVTETVTQ PWGVITHLIL
FGWFLWCLRF RIKAAFVLFA ILAAAILVGQ GVKSWIKDKV QEPRPFVIWL EKTHHIPVDE
FYTLKRAERG NLVKEQLAEE KNIPQYLRSH WQKETGFAFP SGHTMFAASW ALLAVGLLWP
RRRTLTIAIL LVWATGVMGS RLLLGMHWPR DLVVATLISW ALVAVATWLA QRICGPLTPP
AEENREIAQR EQES
