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P0A926

- PGPB_SHIFL

UniProt

P0A926 - PGPB_SHIFL

Protein

Phosphatidylglycerophosphatase B

Gene

pgpB

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (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 By similarity.By similarity

    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.

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. phosphatidylglycerol biosynthetic process Source: UniProtKB-UniPathway
    2. 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

    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:SF1282, S1365
    OrganismiShigella flexneri
    Taxonomic identifieri623 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

    Subcellular locationi

    Cell inner membrane By similarity; Multi-pass membrane protein By similarity. Cell outer membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. cell outer membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 254254Phosphatidylglycerophosphatase BPRO_0000058364Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.By similarity

    Interactioni

    Protein-protein interaction databases

    STRINGi198214.SF1282.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A926.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicBy similarity
    Topological domaini30 – 4718PeriplasmicBy similarityAdd
    BLAST
    Topological domaini69 – 713CytoplasmicBy similarity
    Topological domaini93 – 15866PeriplasmicBy similarityAdd
    BLAST
    Topological domaini180 – 1845CytoplasmicBy similarity
    Topological domaini206 – 2105PeriplasmicBy similarity
    Topological domaini232 – 25423CytoplasmicBy similarityAdd
    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.

    P0A926-1 [UniParc]FASTAAdd to Basket

    « Hide

    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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN42894.1.
    AE014073 Genomic DNA. Translation: AAP16778.1.
    RefSeqiNP_707187.1. NC_004337.2.
    NP_836971.1. NC_004741.1.

    Genome annotation databases

    EnsemblBacteriaiAAN42894; AAN42894; SF1282.
    AAP16778; AAP16778; S1365.
    GeneIDi1024235.
    1077744.
    KEGGisfl:SF1282.
    sfx:S1365.
    PATRICi18703976. VBIShiFle31049_1492.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN42894.1 .
    AE014073 Genomic DNA. Translation: AAP16778.1 .
    RefSeqi NP_707187.1. NC_004337.2.
    NP_836971.1. NC_004741.1.

    3D structure databases

    ProteinModelPortali P0A926.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198214.SF1282.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN42894 ; AAN42894 ; SF1282 .
    AAP16778 ; AAP16778 ; S1365 .
    GeneIDi 1024235.
    1077744.
    KEGGi sfl:SF1282.
    sfx:S1365.
    PATRICi 18703976. VBIShiFle31049_1492.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00084 ; UER00504 .

    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. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
      Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
      , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
      Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 301 / Serotype 2a.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700930 / 2457T / Serotype 2a.

    Entry informationi

    Entry nameiPGPB_SHIFL
    AccessioniPrimary (citable) accession number: P0A926
    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 67 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3