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P0A078

- MAP1_STAAM

UniProt

P0A078 - MAP1_STAAM

Protein

Methionine aminopeptidase

Gene

map

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      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 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions.
    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 – 761Substrate
    Metal bindingi93 – 931Divalent metal cation 1
    Metal bindingi104 – 1041Divalent metal cation 1
    Metal bindingi104 – 1041Divalent metal cation 2; catalytic
    Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogen
    Binding sitei175 – 1751Substrate
    Metal bindingi202 – 2021Divalent metal cation 2; catalytic
    Metal bindingi233 – 2331Divalent metal cation 1
    Metal bindingi233 – 2331Divalent metal cation 2; catalytic

    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

    BioCyciSAUR158878:GJJ5-1943-MONOMER.

    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:SAV1888
    OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
    Taxonomic identifieri158878 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000002481: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252Methionine aminopeptidasePRO_0000148955Add
    BLAST

    2D gel databases

    World-2DPAGE0002:P0A078.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi158878.SAV1888.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 2924
    Helixi36 – 5015
    Helixi55 – 606
    Beta strandi63 – 708
    Beta strandi73 – 753
    Beta strandi89 – 9810
    Beta strandi101 – 11010
    Helixi118 – 13417
    Helixi144 – 15613
    Beta strandi167 – 1693
    Beta strandi171 – 18111
    Beta strandi197 – 2015
    Beta strandi204 – 2085
    Beta strandi216 – 2194
    Beta strandi229 – 2379

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QXWX-ray1.67A1-252[»]
    1QXYX-ray1.04A1-252[»]
    1QXZX-ray1.68A1-252[»]
    ProteinModelPortaliP0A078.
    SMRiP0A078. Positions 1-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A078.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030426.
    KOiK01265.
    OMAiFHEMIDI.
    OrthoDBiEOG6MWNDS.
    PhylomeDBiP0A078.

    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.

    P0A078-1 [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:March 1, 2005 - v1
    Checksum:i3E42E623286B537B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB58050.1.
    RefSeqiNP_372412.1. NC_002758.2.

    Genome annotation databases

    EnsemblBacteriaiBAB58050; BAB58050; SAV1888.
    GeneIDi1121901.
    KEGGisav:SAV1888.
    PATRICi19564622. VBIStaAur52173_1950.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB58050.1 .
    RefSeqi NP_372412.1. NC_002758.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QXW X-ray 1.67 A 1-252 [» ]
    1QXY X-ray 1.04 A 1-252 [» ]
    1QXZ X-ray 1.68 A 1-252 [» ]
    ProteinModelPortali P0A078.
    SMRi P0A078. Positions 1-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158878.SAV1888.

    Chemistry

    BindingDBi P0A078.

    2D gel databases

    World-2DPAGE 0002:P0A078.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB58050 ; BAB58050 ; SAV1888 .
    GeneIDi 1121901.
    KEGGi sav:SAV1888.
    PATRICi 19564622. VBIStaAur52173_1950.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030426.
    KOi K01265.
    OMAi FHEMIDI.
    OrthoDBi EOG6MWNDS.
    PhylomeDBi P0A078.

    Enzyme and pathway databases

    BioCyci SAUR158878:GJJ5-1943-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A078.

    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: Mu50 / ATCC 700699.
    2. "Crystal structures of Staphylococcus aureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate."
      Douangamath A., Dale G.E., D'Arcy A., Almstetter M., Eckl R., Frutos-Hoener A., Henkel B., Illgen K., Nerdinger S., Schulz H., Mac Sweeney A., Thormann M., Treml A., Pierau S., Wadman S., Oefner C.
      J. Med. Chem. 47:1325-1328(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) IN COMPLEXES WITH COBALT IONS AND INHIBITOR.

    Entry informationi

    Entry nameiMAP1_STAAM
    AccessioniPrimary (citable) accession number: P0A078
    Secondary accession number(s): Q9KWL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: March 1, 2005
    Last modified: October 1, 2014
    This is version 74 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

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3