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Q5HEN6

- MAP1_STAAC

UniProt

Q5HEN6 - MAP1_STAAC

Protein

Methionine aminopeptidase

Gene

map

Organism
Staphylococcus aureus (strain COL)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    • Comment

    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

    BioCyciSAUR93062:GCEP-1941-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:SACOL1946
    OrganismiStaphylococcus aureus (strain COL)
    Taxonomic identifieri93062 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000530: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252Methionine aminopeptidasePRO_0000148954Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi93062.SACOL1946.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5HEN6.
    SMRiQ5HEN6. 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.

    Q5HEN6-1 [UniParc]FASTAAdd to Basket

    « Hide

    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:February 15, 2005 - v1
    Checksum:i3E42E623286B537B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000046 Genomic DNA. Translation: AAW38387.1.
    RefSeqiYP_186771.1. NC_002951.2.

    Genome annotation databases

    EnsemblBacteriaiAAW38387; AAW38387; SACOL1946.
    GeneIDi3237517.
    KEGGisac:SACOL1946.
    PATRICi19530169. VBIStaAur112458_1901.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000046 Genomic DNA. Translation: AAW38387.1 .
    RefSeqi YP_186771.1. NC_002951.2.

    3D structure databases

    ProteinModelPortali Q5HEN6.
    SMRi Q5HEN6. Positions 1-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 93062.SACOL1946.

    Chemistry

    BindingDBi Q5HEN6.

    Protein family/group databases

    MEROPSi M24.036.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW38387 ; AAW38387 ; SACOL1946 .
    GeneIDi 3237517.
    KEGGi sac:SACOL1946.
    PATRICi 19530169. VBIStaAur112458_1901.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SAUR93062:GCEP-1941-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. "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
      Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.
      , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
      J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: COL.

    Entry informationi

    Entry nameiMAP1_STAAC
    AccessioniPrimary (citable) accession number: Q5HEN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 70 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