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P0A1X7

- MAP1_SALTI

UniProt

P0A1X7 - MAP1_SALTI

Protein

Methionine aminopeptidase

Gene

map

Organism
Salmonella typhi
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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 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

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    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
    Synonyms:pepM
    Ordered Locus Names:STY0238, t0216
    OrganismiSalmonella typhi
    Taxonomic identifieri90370 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000000541: Chromosome, UP000002670: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 264263Methionine aminopeptidasePRO_0000148951Add
    BLAST

    Proteomic databases

    PRIDEiP0A1X7.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi220341.STY0238.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A1X7.
    SMRiP0A1X7. 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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A1X7-1 [UniParc]FASTAAdd to Basket

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    MAISIKTSED IEKMRVAGRL AAEVLEMIEP YIKPGVTTGE LDRICNDYIV    50
    NEQHAISACL GYHGYPKSVC ISINEVVCHG IPDDAKHLKD GDIVNIDVTV 100
    IKDEFHGDTS KMFIVGKPTI LGERLCRVTQ ESLYLGIKMV KPGIRLRTIG 150
    AAIQKYAEGE GFSVVREYCG HGIGRGFHEE PQVLHYDADD GGVVLQPGMT 200
    FTIEPMLNAG DYRIRTMKDG WTVKTKDRSL SAQYEHTIVV TENGCEILTL 250
    RKDDTIPAII THDE 264
    Length:264
    Mass (Da):29,292
    Last modified:January 23, 2007 - v2
    Checksum:i8563A54BBE98A860
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL513382 Genomic DNA. Translation: CAD01369.1.
    AE014613 Genomic DNA. Translation: AAO67946.1.
    RefSeqiNP_454822.1. NC_003198.1.
    NP_804097.1. NC_004631.1.

    Genome annotation databases

    EnsemblBacteriaiAAO67946; AAO67946; t0216.
    CAD01369; CAD01369; CAD01369.
    GeneIDi1246727.
    KEGGisty:STY0238.
    PATRICi18538293. VBISalEnt120419_0238.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL513382 Genomic DNA. Translation: CAD01369.1 .
    AE014613 Genomic DNA. Translation: AAO67946.1 .
    RefSeqi NP_454822.1. NC_003198.1.
    NP_804097.1. NC_004631.1.

    3D structure databases

    ProteinModelPortali P0A1X7.
    SMRi P0A1X7. Positions 2-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 220341.STY0238.

    Proteomic databases

    PRIDEi P0A1X7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO67946 ; AAO67946 ; t0216 .
    CAD01369 ; CAD01369 ; CAD01369 .
    GeneIDi 1246727.
    KEGGi sty:STY0238.
    PATRICi 18538293. VBISalEnt120419_0238.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CT18.
    2. "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
      Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
      J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700931 / Ty2.

    Entry informationi

    Entry nameiMAP1_SALTI
    AccessioniPrimary (citable) accession number: P0A1X7
    Secondary accession number(s): P10882
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 71 of the entry and version 2 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