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Q6GFG9

- MAP1_STAAR

UniProt

Q6GFG9 - MAP1_STAAR

Protein

Methionine aminopeptidase

Gene

map

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.UniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

    Cofactori

    Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei76 – 761SubstrateUniRule annotation
    Metal bindingi93 – 931Divalent metal cation 1UniRule annotation
    Metal bindingi104 – 1041Divalent metal cation 1UniRule annotation
    Metal bindingi104 – 1041Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei175 – 1751SubstrateUniRule annotation
    Metal bindingi202 – 2021Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
    Metal bindingi233 – 2331Divalent metal cation 2; catalyticUniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-HAMAP
    2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. protein initiator methionine removal Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciSAUR282458:GJA5-2012-MONOMER.

    Protein family/group databases

    MEROPSiM24.036.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAPUniRule annotation
    Short name:
    MetAPUniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:mapUniRule annotation
    Ordered Locus Names:SAR1978
    OrganismiStaphylococcus aureus (strain MRSA252)
    Taxonomic identifieri282458 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000596: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252Methionine aminopeptidasePRO_0000148957Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi282458.SAR1978.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6GFG9.
    SMRiQ6GFG9. Positions 1-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030426.
    KOiK01265.
    OMAiEGMCFTI.
    OrthoDBiEOG6MWNDS.

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6GFG9-1 [UniParc]FASTAAdd to Basket

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    MIVKTEEELQ ALKEIGYICA KVRNTMQAAT KPGITTKELD NIAKELFEEY    50
    GAISAPIHDE NFPGQTCISV NEEVAHGIPS KRVIREGDLV NIDVSALKNG 100
    YYADTGISFV VGESDDPMKQ KVCDVATMAF ENAIAKVKPG TKLSNIGKAV 150
    HNTARQNDLK VIKNLTGHGV GLSLHEAPAH VLNYFDPKDK TLLTEGMVLA 200
    IEPFISSNAS FVTEGKNEWA FETSDKSFVA QIEHTVIVTK DGPILTTKIE 250
    EE 252
    Length:252
    Mass (Da):27,502
    Last modified:July 19, 2004 - v1
    Checksum:i3E42E623286B537B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571856 Genomic DNA. Translation: CAG40965.1.
    RefSeqiYP_041353.1. NC_002952.2.

    Genome annotation databases

    EnsemblBacteriaiCAG40965; CAG40965; SAR1978.
    GeneIDi2861219.
    KEGGisar:SAR1978.
    PATRICi19547591. VBIStaAur71814_1985.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571856 Genomic DNA. Translation: CAG40965.1 .
    RefSeqi YP_041353.1. NC_002952.2.

    3D structure databases

    ProteinModelPortali Q6GFG9.
    SMRi Q6GFG9. Positions 1-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 282458.SAR1978.

    Chemistry

    BindingDBi Q6GFG9.

    Protein family/group databases

    MEROPSi M24.036.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG40965 ; CAG40965 ; SAR1978 .
    GeneIDi 2861219.
    KEGGi sar:SAR1978.
    PATRICi 19547591. VBIStaAur71814_1985.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030426.
    KOi K01265.
    OMAi EGMCFTI.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci SAUR282458:GJA5-2012-MONOMER.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01974. MetAP_1.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MRSA252.

    Entry informationi

    Entry nameiMAP1_STAAR
    AccessioniPrimary (citable) accession number: Q6GFG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 72 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3