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O52787

- PTP_ACIJO

UniProt

O52787 - PTP_ACIJO

Protein

Low molecular weight protein-tyrosine-phosphatase ptp

Gene

ptp

Organism
Acinetobacter johnsonii
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    • Comment

    Functioni

    Dephosphorylates ptk. May be involved in the production and the transport of exopolysaccharides.

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Enzyme regulationi

    Inhibited by ammonium molybdate, sodium orthovanadate, N-ethylmaleimide and iodoacetic acid.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei10 – 101NucleophileBy similarity
    Active sitei15 – 151By similarity
    Active sitei115 – 1151Proton donorBy similarity

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Exopolysaccharide synthesis

    Enzyme and pathway databases

    UniPathwayiUPA00631.

    Protein family/group databases

    PptaseDBiP3D040495.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Low molecular weight protein-tyrosine-phosphatase ptp (EC:3.1.3.48)
    Gene namesi
    Name:ptp
    OrganismiAcinetobacter johnsonii
    Taxonomic identifieri40214 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101C → S: Loss of activity. 1 Publication
    Mutagenesisi16 – 161R → K: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 142142Low molecular weight protein-tyrosine-phosphatase ptpPRO_0000046566Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO52787.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR023485. Ptyr_pPase_SF.
    IPR000106. Tyr_phospatase/Ars_reductase.
    IPR017867. Tyr_phospatase_low_mol_wt.
    [Graphical view]
    PANTHERiPTHR11717. PTHR11717. 1 hit.
    PfamiPF01451. LMWPc. 1 hit.
    [Graphical view]
    PRINTSiPR00719. LMWPTPASE.
    SMARTiSM00226. LMWPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52788. SSF52788. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O52787-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQFKNILVVC IGNICRSPMA EYLLKQNYPQ LTIHSAGISG MIGYSADEKA    50
    QLCMERIGID MSPHIAKKLN AELLKQADLI LVMSQNQQKH IEQTWPFAKG 100
    KTFRLGHWQG KNIPDPYQHD QAFFDETSLL IQTCVADWTK HI 142
    Length:142
    Mass (Da):16,215
    Last modified:June 1, 1998 - v1
    Checksum:i62B53F3BDDBA5986
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15162 Genomic DNA. Translation: CAA75430.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15162 Genomic DNA. Translation: CAA75430.1 .

    3D structure databases

    ProteinModelPortali O52787.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    PptaseDBi P3D040495.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00631 .

    Family and domain databases

    InterProi IPR023485. Ptyr_pPase_SF.
    IPR000106. Tyr_phospatase/Ars_reductase.
    IPR017867. Tyr_phospatase_low_mol_wt.
    [Graphical view ]
    PANTHERi PTHR11717. PTHR11717. 1 hit.
    Pfami PF01451. LMWPc. 1 hit.
    [Graphical view ]
    PRINTSi PR00719. LMWPTPASE.
    SMARTi SM00226. LMWPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52788. SSF52788. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a bacterial gene encoding an autophosphorylating protein tyrosine kinase."
      Grangeasse C., Doublet P., Vaganay E., Vincent C., Deleage G., Duclos B., Cozzone A.J.
      Gene 204:259-265(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Functional characterization of the low-molecular-mass phosphotyrosine-protein phosphatase of Acinetobacter johnsonii."
      Grangeasse C., Doublet P., Vincent C., Vaganay E., Riberty M., Duclos B., Cozzone A.J.
      J. Mol. Biol. 278:339-347(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-10 AND ARG-16.

    Entry informationi

    Entry nameiPTP_ACIJO
    AccessioniPrimary (citable) accession number: O52787
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3