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C1A138

- AMPA_RHOE4

UniProt

C1A138 - AMPA_RHOE4

Protein

Probable cytosol aminopeptidase

Gene

pepA

Organism
Rhodococcus erythropolis (strain PR4 / NBRC 100887)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (26 May 2009)
      Previous versions | rss
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    • Comment

    Functioni

    Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.UniRule annotation

    Catalytic activityi

    Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.UniRule annotation
    Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.UniRule annotation

    Cofactori

    Binds 2 manganese ions per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi269 – 2691Manganese 2UniRule annotation
    Metal bindingi274 – 2741Manganese 1UniRule annotation
    Metal bindingi274 – 2741Manganese 2UniRule annotation
    Active sitei281 – 2811UniRule annotation
    Metal bindingi292 – 2921Manganese 2UniRule annotation
    Metal bindingi351 – 3511Manganese 1UniRule annotation
    Metal bindingi353 – 3531Manganese 1UniRule annotation
    Metal bindingi353 – 3531Manganese 2UniRule annotation
    Active sitei355 – 3551UniRule annotation

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-HAMAP
    2. manganese ion binding Source: UniProtKB-HAMAP
    3. metalloexopeptidase activity Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciRERY234621:GHDE-3657-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable cytosol aminopeptidaseUniRule annotation (EC:3.4.11.1UniRule annotation)
    Alternative name(s):
    Leucine aminopeptidaseUniRule annotation (EC:3.4.11.10UniRule annotation)
    Short name:
    LAPUniRule annotation
    Leucyl aminopeptidaseUniRule annotation
    Gene namesi
    Name:pepAUniRule annotation
    Ordered Locus Names:RER_36150
    OrganismiRhodococcus erythropolis (strain PR4 / NBRC 100887)
    Taxonomic identifieri234621 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus
    ProteomesiUP000002204: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 505505Probable cytosol aminopeptidasePRO_1000203838Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi234621.RER_36150.

    Structurei

    3D structure databases

    ProteinModelPortaliC1A138.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M17 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0260.
    HOGENOMiHOG000243129.
    KOiK01255.
    OMAiGMENMTS.
    OrthoDBiEOG6FV8B3.

    Family and domain databases

    HAMAPiMF_00181. Cytosol_peptidase_M17.
    InterProiIPR011356. Leucine_aapep/pepB.
    IPR000819. Peptidase_M17_C.
    IPR023042. Peptidase_M17_leu_NH2_pept.
    IPR008283. Peptidase_M17_N.
    [Graphical view]
    PfamiPF00883. Peptidase_M17. 1 hit.
    PF02789. Peptidase_M17_N. 1 hit.
    [Graphical view]
    PRINTSiPR00481. LAMNOPPTDASE.
    PROSITEiPS00631. CYTOSOL_AP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C1A138-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTRTARSLG PDLVLAGTVA KRAEILVVGL TSGPDGPEIA LSEGIVAEDV    50
    LAEILDSLIA VGATGKPEQL TRVPAPSALS VTSVLAVGLG SADKLDSEQI 100
    RKSAGAAARS LSGIDTVATT LSILDLGAAA EGFALGAYSF TEFKSSMTAP 150
    GPDSQPLARV ELLVPSPRTK ETKATLARSA AIAEAVATAR EFVNTPPSHL 200
    YPAEFAARAK ALGVEAGLTV QVLDEKALEK GGYGGIIGVG KGSSRQPRLV 250
    RLEYASKKRG ARKVALVGKG ITFDTGGISI KPAAGMENMT SDMGGAAAVI 300
    STVVLAAKLG LPVNVVAYVP MAENMPSATA QRPGDVLTQY GGITIEVVNT 350
    DAEGRLILAD AMVRAGEDNP DYMIDTATLT GAQMVALGNR TPGVMGTDEF 400
    RDRVASISQS VGENGWAMPL PEELRGDLDS KVADMANVTP HRWGGMLVAA 450
    HYLKEFVPEG VQWAHIDVAG PAYNTSGPWG YTGKGGTGVP VRTMISVLED 500
    IAVNG 505
    Length:505
    Mass (Da):52,012
    Last modified:May 26, 2009 - v1
    Checksum:i437D2EFC0C97E40A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008957 Genomic DNA. Translation: BAH34323.1.
    RefSeqiYP_002767062.1. NC_012490.1.

    Genome annotation databases

    EnsemblBacteriaiBAH34323; BAH34323; RER_36150.
    GeneIDi7715119.
    KEGGirer:RER_36150.
    PATRICi23193706. VBIRhoEry66701_4131.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008957 Genomic DNA. Translation: BAH34323.1 .
    RefSeqi YP_002767062.1. NC_012490.1.

    3D structure databases

    ProteinModelPortali C1A138.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 234621.RER_36150.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAH34323 ; BAH34323 ; RER_36150 .
    GeneIDi 7715119.
    KEGGi rer:RER_36150.
    PATRICi 23193706. VBIRhoEry66701_4131.

    Phylogenomic databases

    eggNOGi COG0260.
    HOGENOMi HOG000243129.
    KOi K01255.
    OMAi GMENMTS.
    OrthoDBi EOG6FV8B3.

    Enzyme and pathway databases

    BioCyci RERY234621:GHDE-3657-MONOMER.

    Family and domain databases

    HAMAPi MF_00181. Cytosol_peptidase_M17.
    InterProi IPR011356. Leucine_aapep/pepB.
    IPR000819. Peptidase_M17_C.
    IPR023042. Peptidase_M17_leu_NH2_pept.
    IPR008283. Peptidase_M17_N.
    [Graphical view ]
    Pfami PF00883. Peptidase_M17. 1 hit.
    PF02789. Peptidase_M17_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00481. LAMNOPPTDASE.
    PROSITEi PS00631. CYTOSOL_AP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
      Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PR4 / NBRC 100887.

    Entry informationi

    Entry nameiAMPA_RHOE4
    AccessioniPrimary (citable) accession number: C1A138
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 38 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, 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