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A1A7L2

- A1A7L2_ECOK1

UniProt

A1A7L2 - A1A7L2_ECOK1

Protein

Methionine aminopeptidase

Gene

map

Organism
Escherichia coli O1:K1 / APEC
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Removes the N-terminal methionine from nascent proteins.UniRule annotation
    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.UniRule annotation
    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 sitei79 – 791SubstrateUniRule annotation
    Metal bindingi97 – 971Divalent metal cation 1UniRule annotation
    Metal bindingi108 – 1081Divalent metal cation 1UniRule annotation
    Metal bindingi108 – 1081Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Metal bindingi204 – 2041Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi235 – 2351Divalent metal cation 1UniRule annotation
    Metal bindingi235 – 2351Divalent 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

    AminopeptidaseUniRule annotationImported, Hydrolase, Protease

    Keywords - Ligandi

    Metal-bindingUniRule annotation

    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 annotationImported
    ORF Names:APECO1_1819Imported
    OrganismiEscherichia coli O1:K1 / APECImported
    Taxonomic identifieri405955 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000008216: Chromosome

    PTM / Processingi

    Proteomic databases

    PRIDEiA1A7L2.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi405955.APECO1_1819.

    Structurei

    3D structure databases

    ProteinModelPortaliA1A7L2.
    SMRiA1A7L2. Positions 2-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    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.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A1A7L2-1 [UniParc]FASTAAdd to Basket

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    MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV    50
    NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV 100
    IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG 150
    AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT 200
    FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL 250
    RKDDTIPAII SHDE 264
    Length:264
    Mass (Da):29,331
    Last modified:January 23, 2007 - v1
    Checksum:iF2D0B57715A67851
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000468 Genomic DNA. Translation: ABI99651.1.
    RefSeqiYP_851366.1. NC_008563.1.

    Genome annotation databases

    EnsemblBacteriaiABI99651; ABI99651; APECO1_1819.
    GeneIDi4493689.
    KEGGiecv:APECO1_1819.
    PATRICi18211731. VBIEscCol127180_0179.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000468 Genomic DNA. Translation: ABI99651.1 .
    RefSeqi YP_851366.1. NC_008563.1.

    3D structure databases

    ProteinModelPortali A1A7L2.
    SMRi A1A7L2. Positions 2-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405955.APECO1_1819.

    Chemistry

    BindingDBi A1A7L2.

    Proteomic databases

    PRIDEi A1A7L2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABI99651 ; ABI99651 ; APECO1_1819 .
    GeneIDi 4493689.
    KEGGi ecv:APECO1_1819.
    PATRICi 18211731. VBIEscCol127180_0179.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    KOi K01265.
    OMAi EGMCFTI.
    OrthoDBi EOG6MWNDS.

    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. "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
      Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
      J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: APEC O1Imported.

    Entry informationi

    Entry nameiA1A7L2_ECOK1
    AccessioniPrimary (citable) accession number: A1A7L2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: January 23, 2007
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3