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P56527

- APHA_PROMI

UniProt

P56527 - APHA_PROMI

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Protein
Class B acid phosphatase
Gene
aphA, napA
Organism
Proteus mirabilis
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Dephosphorylates several organic phosphate monoesters. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds By similarity.

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactori

Binds 1 magnesium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Nucleophile By similarity
Metal bindingi69 – 691Magnesium By similarity
Active sitei71 – 711Proton donor By similarity
Metal bindingi71 – 711Magnesium; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Class B acid phosphatase (EC:3.1.3.2)
    Short name:
    CBAP
    Gene namesi
    Name:aphA
    Synonyms:napA
    OrganismiProteus mirabilis
    Taxonomic identifieri584 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

    Subcellular locationi

    Periplasm By similarity

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: InterPro
    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323 By similarity
    Add
    BLAST
    Chaini24 – ›160›137Class B acid phosphatase
    PRO_0000024007Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer By similarity.

    Structurei

    3D structure databases

    ProteinModelPortaliP56527.
    SMRiP56527. Positions 31-160.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni137 – 1382Substrate binding By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR005519. Acid_phosphat_B.
    IPR023214. HAD-like_dom.
    IPR010025. HAD-SF_ppase_IIIB_AphA.
    [Graphical view]
    PfamiPF03767. Acid_phosphat_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01672. AphA. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

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

    P56527-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKVTLTLSA IALALSLNGA AMAKVHMPEV VSQGVTVTEL AHQQPIKWVS    50
    VAEIEKSLEG QAPMAVGFDI DDTFWFSSPG FYRVKLEYSP NDFSYLKNPE 100
    FWEKMNNEWD KFSMPKQVGI DLVQMHLKRG DTVYFITGRT QTKTETCVTK 150
    YVQEGLNIPA 160
    Length:160
    Mass (Da):18,081
    Last modified:July 15, 1998 - v1
    Checksum:i395541C45A456735
    GO

    Sequence cautioni

    The sequence M11587 differs from that shown. Reason: Frameshift at several positions.

    Non-terminal residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei160 – 1601

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11587 Genomic DNA. No translation available.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11587 Genomic DNA. No translation available.

    3D structure databases

    ProteinModelPortali P56527.
    SMRi P56527. Positions 31-160.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.1000. 1 hit.
    InterProi IPR005519. Acid_phosphat_B.
    IPR023214. HAD-like_dom.
    IPR010025. HAD-SF_ppase_IIIB_AphA.
    [Graphical view ]
    Pfami PF03767. Acid_phosphat_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01672. AphA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence analysis of the cat gene of Proteus mirabilis: comparison with the type I (Tn9) cat gene."
      Charles I.G., Keyte J.W., Shaw W.V.
      J. Bacteriol. 164:123-129(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and characterization of the NapA acid phosphatase/phosphotransferase of Morganella morganii: identification of a new family of bacterial acid-phosphatase-encoding genes."
      Thaller M.C., Lombardi G., Berlutti F., Schippa S., Rossolini G.M.
      Microbiology 141:147-154(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, CONCEPTUAL TRANSLATION.

    Entry informationi

    Entry nameiAPHA_PROMI
    AccessioniPrimary (citable) accession number: P56527
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: April 16, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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