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O83814

- MAP1_TREPA

UniProt

O83814 - MAP1_TREPA

Protein

Methionine aminopeptidase

Gene

map

Organism
Treponema pallidum (strain Nichols)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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 bindingi167 – 1671Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei174 – 1741SubstrateUniRule annotation
    Metal bindingi201 – 2011Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
    Metal bindingi232 – 2321Divalent 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

    BioCyciTPAL243276:GC1H-890-MONOMER.

    Protein family/group databases

    MEROPSiM24.001.

    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:TP_0842
    OrganismiTreponema pallidum (strain Nichols)
    Taxonomic identifieri243276 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
    ProteomesiUP000000811: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 255255Methionine aminopeptidasePRO_0000148966Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    IntActiO83814. 7 interactions.
    STRINGi243276.TP0842.

    Structurei

    3D structure databases

    ProteinModelPortaliO83814.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiATTYEAM.
    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.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O83814-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIRIKTPEQI DGIRASCKAL ARLFDVLIPL VKPGVQTQEL DAFCQRFIRS    50
    VGGVPAWFSE GFPAAACISI NEEVIHGLPS ARVIQDGDLV SLDVGINLNG 100
    YISDACRTVP VGGVAHERLE LLRVTTECLR AGIKACRAGA RVRAVSRAVY 150
    AVAARHRFGV VYEYCGHGVG LAVHEEPNIP NVPGLEGPNP RFLPGMVVAI 200
    EPMLTLGTDE VRTSADGWTV VTADGSCACH VEHTVAVFAD HTEVLTEPTE 250
    VERTG 255
    Length:255
    Mass (Da):27,316
    Last modified:November 1, 1998 - v1
    Checksum:i4EDE582C67F3526A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000520 Genomic DNA. Translation: AAC65810.1.
    PIRiB71273.
    RefSeqiNP_219278.1. NC_000919.1.
    YP_008091667.1. NC_021490.2.

    Genome annotation databases

    EnsemblBacteriaiAAC65810; AAC65810; TP_0842.
    GeneIDi15852132.
    2611002.
    KEGGitpa:TP0842.
    tpw:TPANIC_0842.
    PATRICi20531791. VBITrePal57110_0893.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000520 Genomic DNA. Translation: AAC65810.1 .
    PIRi B71273.
    RefSeqi NP_219278.1. NC_000919.1.
    YP_008091667.1. NC_021490.2.

    3D structure databases

    ProteinModelPortali O83814.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O83814. 7 interactions.
    STRINGi 243276.TP0842.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC65810 ; AAC65810 ; TP_0842 .
    GeneIDi 15852132.
    2611002.
    KEGGi tpa:TP0842.
    tpw:TPANIC_0842.
    PATRICi 20531791. VBITrePal57110_0893.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OMAi ATTYEAM.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci TPAL243276:GC1H-890-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.
    PROSITEi PS00680. MAP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiMAP1_TREPA
    AccessioniPrimary (citable) accession number: O83814
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 99 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