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P0A1X6

- MAP1_SALTY

UniProt

P0A1X6 - MAP1_SALTY

Protein

Methionine aminopeptidase

Gene

map

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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.1 PublicationUniRule 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

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-214-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
    Synonyms:pepM
    Ordered Locus Names:STM0215
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 264263Methionine aminopeptidasePRO_0000148952Add
    BLAST

    Proteomic databases

    PaxDbiP0A1X6.
    PRIDEiP0A1X6.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi99287.STM0215.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A1X6.
    SMRiP0A1X6. 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.
    PhylomeDBiP0A1X6.

    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.

    P0A1X6-1 [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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1383GIK → ALR AA sequence (PubMed:2651123)Curated
    Sequence conflicti145 – 1451R → N AA sequence (PubMed:2651123)Curated
    Sequence conflicti148 – 1481T → E AA sequence (PubMed:2651123)Curated
    Sequence conflicti159 – 1591G → A AA sequence (PubMed:2651123)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55778 Genomic DNA. Translation: CAA39298.1.
    AE006468 Genomic DNA. Translation: AAL19179.1.
    PIRiS12027.
    RefSeqiNP_459220.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL19179; AAL19179; STM0215.
    GeneIDi1251733.
    KEGGistm:STM0215.
    PATRICi32378717. VBISalEnt20916_0228.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55778 Genomic DNA. Translation: CAA39298.1 .
    AE006468 Genomic DNA. Translation: AAL19179.1 .
    PIRi S12027.
    RefSeqi NP_459220.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali P0A1X6.
    SMRi P0A1X6. Positions 2-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM0215.

    Proteomic databases

    PaxDbi P0A1X6.
    PRIDEi P0A1X6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL19179 ; AAL19179 ; STM0215 .
    GeneIDi 1251733.
    KEGGi stm:STM0215.
    PATRICi 32378717. VBISalEnt20916_0228.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    KOi K01265.
    OMAi EGMCFTI.
    OrthoDBi EOG6MWNDS.
    PhylomeDBi P0A1X6.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-214-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. "Cloning and nucleotide sequence of the Salmonella typhimurium pepM gene."
      Movva N.R., Semon D., Meyer C., Kawashima E., Wingfield P., Miller J.L., Miller C.G.
      Mol. Gen. Genet. 223:345-348(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: LT2.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "Purification and characterization of a methionine-specific aminopeptidase from Salmonella typhimurium."
      Wingfield P., Graber P., Turcatti G., Movva N.R., Pelletier M., Craig S., Rose K., Miller C.G.
      Eur. J. Biochem. 180:23-32(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-264, FUNCTION.

    Entry informationi

    Entry nameiMAP1_SALTY
    AccessioniPrimary (citable) accession number: P0A1X6
    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 75 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, Direct protein sequencing, 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