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PGPB_ECO57
ID   PGPB_ECO57              Reviewed;         254 AA.
AC   P0A925; P18201;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Z2529, ECs1851;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG56535.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35274.1; -; Genomic_DNA.
DR   PIR; C85759; C85759.
DR   PIR; C90860; C90860.
DR   RefSeq; NP_309878.1; NC_002695.1.
DR   RefSeq; WP_001256538.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A925; -.
DR   SMR; P0A925; -.
DR   STRING; 155864.EDL933_2412; -.
DR   EnsemblBacteria; AAG56535; AAG56535; Z2529.
DR   EnsemblBacteria; BAB35274; BAB35274; ECs_1851.
DR   GeneID; 66674897; -.
DR   GeneID; 912812; -.
DR   KEGG; ece:Z2529; -.
DR   KEGG; ecs:ECs_1851; -.
DR   PATRIC; fig|386585.9.peg.1950; -.
DR   eggNOG; COG0671; Bacteria.
DR   HOGENOM; CLU_083863_0_0_6; -.
DR   OMA; AWFLWCL; -.
DR   UniPathway; UPA00084; UER00504.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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_0000058361"
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
 
 
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