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P0A924

- PGPB_ECOLI

UniProt

P0A924 - PGPB_ECOLI

Protein

Phosphatidylglycerophosphatase B

Gene

pgpB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Catalyzes 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.4 Publications

    Catalytic activityi

    Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.
    1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate.
    A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
    Ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate.

    Enzyme regulationi

    Inhibited by Mn2+ ions.

    Kineticsi

    1. KM=530 µM for undecaprenyl pyrophosphate2 Publications
    2. KM=96 µM for farnesyl pyrophosphate2 Publications
    3. KM=80 µM for diacylglycerol pyrophosphate2 Publications
    4. KM=1700 µM for phosphatidate2 Publications

    Vmax=2167 nmol/min/mg enzyme with diacylglycerol pyrophosphate as substrate2 Publications

    Vmax=313 nmol/min/mg enzyme with phosphatidate as substrate2 Publications

    pH dependencei

    Optimum pH is 6.5 for DGPP phosphatase activity and 6.5-7.5 for undecaprenyl pyrophosphate phosphatase activity.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. diacylglycerol diphosphate phosphatase activity Source: UniProtKB-EC
    2. phosphatidate phosphatase activity Source: UniProtKB-EC
    3. phosphatidylglycerophosphatase activity Source: EcoCyc
    4. undecaprenyl-diphosphatase activity Source: EcoCyc

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. glycerophospholipid biosynthetic process Source: EcoCyc
    3. peptidoglycan biosynthetic process Source: EcoCyc
    4. phosphatidylglycerol biosynthetic process Source: UniProtKB-UniPathway
    5. phospholipid catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:PGPPHOSPHAB-MONOMER.
    ECOL316407:JW1270-MONOMER.
    MetaCyc:PGPPHOSPHAB-MONOMER.
    UniPathwayiUPA00084; UER00504.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylglycerophosphatase B (EC:3.1.3.27)
    Alternative name(s):
    Diacylglycerol pyrophosphate phosphatase (EC:3.1.3.81)
    Short name:
    DGPP phosphatase
    Phosphatidate phosphatase (EC:3.1.3.4)
    Undecaprenyl pyrophosphate phosphatase (EC:3.6.1.27)
    Undecaprenyl-diphosphatase
    Gene namesi
    Name:pgpB
    Ordered Locus Names:b1278, JW1270
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10705. pgpB.

    Subcellular locationi

    Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell outer membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. cell outer membrane Source: EcoCyc
    2. integral component of plasma membrane Source: EcoCyc
    3. plasma membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cell outer membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 254253Phosphatidylglycerophosphatase BPRO_0000058362Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A924.

    Interactioni

    Protein-protein interaction databases

    IntActiP0A924. 1 interaction.
    STRINGi511145.b1278.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A924.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 87CytoplasmicSequence Analysis
    Topological domaini30 – 4718PeriplasmicSequence AnalysisAdd
    BLAST
    Topological domaini69 – 713CytoplasmicSequence Analysis
    Topological domaini93 – 15866PeriplasmicSequence AnalysisAdd
    BLAST
    Topological domaini180 – 1845CytoplasmicSequence Analysis
    Topological domaini206 – 2105PeriplasmicSequence Analysis
    Topological domaini232 – 25423CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei48 – 6821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei72 – 9221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei159 – 17921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei185 – 20521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei211 – 23121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 1059Phosphatase sequence motif I
    Regioni160 – 1634Phosphatase sequence motif II
    Regioni200 – 21112Phosphatase sequence motif IIIAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0671.
    HOGENOMiHOG000286191.
    KOiK01096.
    OMAiGMHYPID.
    OrthoDBiEOG60CWKV.

    Family and domain databases

    Gene3Di1.20.144.10. 2 hits.
    InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view]
    PfamiPF01569. PAP2. 1 hit.
    [Graphical view]
    SMARTiSM00014. acidPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48317. SSF48317. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A924-1 [UniParc]FASTAAdd to Basket

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    MRSIARRTAV GAALLLVMPV AVWISGWRWQ PGEQSWLLKA AFWVTETVTQ    50
    PWGVITHLIL FGWFLWCLRF RIKAAFVLFA ILAAAILVGQ GVKSWIKDKV 100
    QEPRPFVIWL EKTHHIPVDE FYTLKRAERG NLVKEQLAEE KNIPQYLRSH 150
    WQKETGFAFP SGHTMFAASW ALLAVGLLWP RRRTLTIAIL LVWATGVMGS 200
    RLLLGMHWPR DLVVATLISW ALVAVATWLA QRICGPLTPP AEENREIAQR 250
    EQES 254
    Length:254
    Mass (Da):29,021
    Last modified:July 19, 2005 - v1
    Checksum:i9F4E6E88C34D458C
    GO

    Mass spectrometryi

    Molecular mass is 30151 Da from positions 2 - 254. Determined by MALDI. Reported mass includes mass of a C-terminal His6 tag.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23628 Unassigned DNA. Translation: AAB36618.1.
    U00096 Genomic DNA. Translation: AAC74360.1.
    AP009048 Genomic DNA. Translation: BAA14832.1.
    PIRiA30193. PAECGB.
    RefSeqiNP_415794.1. NC_000913.3.
    YP_489546.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74360; AAC74360; b1278.
    BAA14832; BAA14832; BAA14832.
    GeneIDi12933201.
    945863.
    KEGGiecj:Y75_p1253.
    eco:b1278.
    PATRICi32117818. VBIEscCol129921_1329.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23628 Unassigned DNA. Translation: AAB36618.1 .
    U00096 Genomic DNA. Translation: AAC74360.1 .
    AP009048 Genomic DNA. Translation: BAA14832.1 .
    PIRi A30193. PAECGB.
    RefSeqi NP_415794.1. NC_000913.3.
    YP_489546.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0A924.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A924. 1 interaction.
    STRINGi 511145.b1278.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74360 ; AAC74360 ; b1278 .
    BAA14832 ; BAA14832 ; BAA14832 .
    GeneIDi 12933201.
    945863.
    KEGGi ecj:Y75_p1253.
    eco:b1278.
    PATRICi 32117818. VBIEscCol129921_1329.

    Organism-specific databases

    EchoBASEi EB0699.
    EcoGenei EG10705. pgpB.

    Phylogenomic databases

    eggNOGi COG0671.
    HOGENOMi HOG000286191.
    KOi K01096.
    OMAi GMHYPID.
    OrthoDBi EOG60CWKV.

    Enzyme and pathway databases

    UniPathwayi UPA00084 ; UER00504 .
    BioCyci EcoCyc:PGPPHOSPHAB-MONOMER.
    ECOL316407:JW1270-MONOMER.
    MetaCyc:PGPPHOSPHAB-MONOMER.

    Miscellaneous databases

    PROi P0A924.

    Gene expression databases

    Genevestigatori P0A924.

    Family and domain databases

    Gene3Di 1.20.144.10. 2 hits.
    InterProi IPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view ]
    Pfami PF01569. PAP2. 1 hit.
    [Graphical view ]
    SMARTi SM00014. acidPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48317. SSF48317. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Membrane-bound phosphatases in Escherichia coli: sequence of the pgpB gene and dual subcellular localization of the pgpB product."
      Icho T.
      J. Bacteriol. 170:5117-5124(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-28, DUAL SUBCELLULAR LOCATION.
      Strain: K12 / CS520.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity."
      Dillon D.A., Wu W.I., Riedel B., Wissing J.B., Dowhan W., Carman G.M.
      J. Biol. Chem. 271:30548-30553(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: K12.
    6. "Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli."
      El Ghachi M., Derbise A., Bouhss A., Mengin-Lecreulx D.
      J. Biol. Chem. 280:18689-18695(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Global topology analysis of the Escherichia coli inner membrane proteome."
      Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
      Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
      Strain: K12 / MG1655 / ATCC 47076.
    8. "Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase."
      Touze T., Blanot D., Mengin-Lecreulx D.
      J. Biol. Chem. 283:16573-16583(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
    9. "Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli."
      Lu Y.H., Guan Z., Zhao J., Raetz C.R.
      J. Biol. Chem. 286:5506-5518(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

    Entry informationi

    Entry nameiPGPB_ECOLI
    AccessioniPrimary (citable) accession number: P0A924
    Secondary accession number(s): P18201
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3