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Q9PL68

- MAP1_CHLMU

UniProt

Q9PL68 - MAP1_CHLMU

Protein

Methionine aminopeptidase

Gene

map

Organism
Chlamydia muridarum (strain MoPn / Nigg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (27 Apr 2001)
      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 sitei118 – 1181SubstrateUniRule annotation
    Metal bindingi135 – 1351Divalent metal cation 1UniRule annotation
    Metal bindingi146 – 1461Divalent metal cation 1UniRule annotation
    Metal bindingi146 – 1461Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi209 – 2091Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei216 – 2161SubstrateUniRule annotation
    Metal bindingi241 – 2411Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi273 – 2731Divalent metal cation 1UniRule annotation
    Metal bindingi273 – 2731Divalent 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

    BioCyciCMUR243161:GHYU-253-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:TC_0240
    OrganismiChlamydia muridarum (strain MoPn / Nigg)
    Taxonomic identifieri243161 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    ProteomesiUP000000800: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 291291Methionine aminopeptidasePRO_0000148932Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243161.TC0240.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9PL68.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    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.
    IPR004027. SEC_C_motif.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    PF02810. SEC-C. 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.

    Q9PL68-1 [UniParc]FASTAAdd to Basket

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    MKRNDPCWCG SQKKWKHCHY PTKPERPSDN LRQLYASRYD IIIKTPDQIE    50
    KIRKACQVTA RILDALCKAA KEGVTTNELD QLSCNLHKQY NAIPAPLNYG 100
    QPPFPKTICT SLNEVICHGI PNDTPLQNGD IMNIDVSCIV DGFYGDCSRM 150
    VMIGEVPEIK KKVCEASLEA LNAAIAILEP NLPLYEIGEV IENCAARYGF 200
    SVVDQFVGHG VGVRFHENPY VAHHRNSCKI PLAPGMTFTI EPMINVGKKE 250
    GFIDPTNHWE ARTCDHQPSA QWEHTVLITD SGYEILTLLD N 291
    Length:291
    Mass (Da):32,646
    Last modified:April 27, 2001 - v2
    Checksum:iBAA33E190FC6160E
    GO

    Sequence cautioni

    The sequence AAF39111.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF39111.1. Different initiation.
    PIRiG81724.
    RefSeqiNP_296619.3. NC_002620.2.

    Genome annotation databases

    EnsemblBacteriaiAAF39111; AAF39111; TC_0240.
    GeneIDi1246409.
    KEGGicmu:TC_0240.
    PATRICi20371872. VBIChlMur19118_0263.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF39111.1 . Different initiation.
    PIRi G81724.
    RefSeqi NP_296619.3. NC_002620.2.

    3D structure databases

    ProteinModelPortali Q9PL68.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243161.TC0240.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF39111 ; AAF39111 ; TC_0240 .
    GeneIDi 1246409.
    KEGGi cmu:TC_0240.
    PATRICi 20371872. VBIChlMur19118_0263.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OrthoDBi EOG6MWNDS.

    Enzyme and pathway databases

    BioCyci CMUR243161:GHYU-253-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.
    IPR004027. SEC_C_motif.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    PF02810. SEC-C. 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: MoPn / Nigg.

    Entry informationi

    Entry nameiMAP1_CHLMU
    AccessioniPrimary (citable) accession number: Q9PL68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 94 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