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Q5HN46

- MAP1_STAEQ

UniProt

Q5HN46 - MAP1_STAEQ

Protein

Methionine aminopeptidase

Gene

map

Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
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 (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

    BioCyciRETL1328306-WGS:GSTH-3162-MONOMER.
    SEPI176279:GJJB-1490-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:SERP1426
    OrganismiStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
    Taxonomic identifieri176279 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000531: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 251251Methionine aminopeptidasePRO_0000148962Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi176279.SERP1426.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5HN46.
    SMRiQ5HN46. 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.

    Q5HN46-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIVKTDEELQ ALKEIGYICA KVRDTMKEAT KPGVTTRELD HIAKDLFEEH    50
    GAISAPIHDE NFPGQTCISV NEEVAHGIPG KRVIHEGDLV NIDVSALKNG 100
    YYADTGISFV VGKSDQPLKQ KVCDVATMAF ENAMKKVKPG TKLSNIGKAV 150
    HATARQNDLT VIKNLTGHGV GQSLHEAPNH VMNYFDPKDK TLLKEGQVIA 200
    VEPFISTHAT FVTEGKNEWA FETKDKSYVA QIEHTVIVTK DGPLLTTKID 250
    D 251
    Length:251
    Mass (Da):27,531
    Last modified:February 15, 2005 - v1
    Checksum:iA105F719EC8571E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000029 Genomic DNA. Translation: AAW54790.1.
    RefSeqiYP_188995.1. NC_002976.3.

    Genome annotation databases

    EnsemblBacteriaiAAW54790; AAW54790; SERP1426.
    GeneIDi3241924.
    KEGGiser:SERP1426.
    PATRICi19613781. VBIStaEpi130894_1394.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000029 Genomic DNA. Translation: AAW54790.1 .
    RefSeqi YP_188995.1. NC_002976.3.

    3D structure databases

    ProteinModelPortali Q5HN46.
    SMRi Q5HN46. Positions 1-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 176279.SERP1426.

    Protein family/group databases

    MEROPSi M24.036.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW54790 ; AAW54790 ; SERP1426 .
    GeneIDi 3241924.
    KEGGi ser:SERP1426.
    PATRICi 19613781. VBIStaEpi130894_1394.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci RETL1328306-WGS:GSTH-3162-MONOMER.
    SEPI176279:GJJB-1490-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: ATCC 35984 / RP62A.

    Entry informationi

    Entry nameiMAP1_STAEQ
    AccessioniPrimary (citable) accession number: Q5HN46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: February 15, 2005
    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, Reference 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