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Q9Z6Q0

- MAP1_CHLPN

UniProt

Q9Z6Q0 - MAP1_CHLPN

Protein

Methionine aminopeptidase

Gene

map

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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

    BioCyciCPNE115711:GI7B-871-MONOMER.
    CPNE115713:GHEY-1053-MONOMER.
    CPNE138677:GH8N-1043-MONOMER.
    CPNE182082:GH4N-1082-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:CPn_1009, CP_0844, CpB1046
    OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
    Taxonomic identifieri83558 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    ProteomesiUP000000424: Chromosome, UP000000583: Chromosome, UP000000801: Chromosome, UP000000802: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 291291Methionine aminopeptidasePRO_0000148933Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi115713.CPn1009.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z6Q0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    KOiK01265.
    OMAiCQITARI.
    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.

    Q9Z6Q0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRNDPCWCG SGRKWKQCHY PQPPKMSPEA LKQHYASQYN ILLKTPEQKA    50
    KIYNACQITA RILDELCKAS QKGVTTNELD ELSQELHKKY DAIAAPFHYG 100
    SPPFPKTICT SLNEVICHGI PNDIPLKDGD IMNIDVSCIV DGYYGDCSRM 150
    VMIGEVPEIK KKICQAALEC LNDSIAILKP GIPLCEIGEA IEARADTYGF 200
    SVVDQFVGHG VGIEFHENPY VPHYRNRSMI PLAPGMIFTI EPMINVGKKE 250
    GVVDPKNQWE ARTCDNQPSA QWEHTIAITE TGYEILTLLN D 291
    Length:291
    Mass (Da):32,596
    Last modified:May 1, 1999 - v1
    Checksum:i094F6D6E17F23DE9
    GO

    Sequence cautioni

    The sequence AAF38634.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAP98976.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001363 Genomic DNA. Translation: AAD19146.1.
    AE002161 Genomic DNA. Translation: AAF38634.1. Different initiation.
    BA000008 Genomic DNA. Translation: BAA99216.1.
    AE009440 Genomic DNA. Translation: AAP98976.1. Different initiation.
    PIRiA81531.
    E72008.
    F86616.
    RefSeqiNP_225203.1. NC_000922.1.
    NP_301064.1. NC_002491.1.
    NP_445382.2. NC_002179.2.
    NP_877319.2. NC_005043.1.

    Genome annotation databases

    EnsemblBacteriaiAAD19146; AAD19146; CPn_1009.
    AAF38634; AAF38634; CP_0844.
    AAP98976; AAP98976; CpB1046.
    BAA99216; BAA99216; BAA99216.
    GeneIDi1467726.
    894643.
    919776.
    963127.
    KEGGicpa:CP0844.
    cpj:CPj1009.
    cpn:CPn1009.
    cpt:CpB1046.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001363 Genomic DNA. Translation: AAD19146.1 .
    AE002161 Genomic DNA. Translation: AAF38634.1 . Different initiation.
    BA000008 Genomic DNA. Translation: BAA99216.1 .
    AE009440 Genomic DNA. Translation: AAP98976.1 . Different initiation.
    PIRi A81531.
    E72008.
    F86616.
    RefSeqi NP_225203.1. NC_000922.1.
    NP_301064.1. NC_002491.1.
    NP_445382.2. NC_002179.2.
    NP_877319.2. NC_005043.1.

    3D structure databases

    ProteinModelPortali Q9Z6Q0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 115713.CPn1009.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD19146 ; AAD19146 ; CPn_1009 .
    AAF38634 ; AAF38634 ; CP_0844 .
    AAP98976 ; AAP98976 ; CpB1046 .
    BAA99216 ; BAA99216 ; BAA99216 .
    GeneIDi 1467726.
    894643.
    919776.
    963127.
    KEGGi cpa:CP0844.
    cpj:CPj1009.
    cpn:CPn1009.
    cpt:CpB1046.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CPNE115711:GI7B-871-MONOMER.
    CPNE115713:GHEY-1053-MONOMER.
    CPNE138677:GH8N-1043-MONOMER.
    CPNE182082:GH4N-1082-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: CWL029.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AR39.
    3. "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
      Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
      Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: J138.
    4. "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
      Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TW-183.

    Entry informationi

    Entry nameiMAP1_CHLPN
    AccessioniPrimary (citable) accession number: Q9Z6Q0
    Secondary accession number(s): Q9JQD4, Q9K1X1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 109 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

    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