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P68768

- AMPA_ECO57

UniProt

P68768 - AMPA_ECO57

Protein

Cytosol aminopeptidase

Gene

pepA

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place By similarity.By similarity

    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.
    Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Inhibited by zinc and EDTA.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi270 – 2701Manganese 2By similarity
    Metal bindingi275 – 2751Manganese 1By similarity
    Metal bindingi275 – 2751Manganese 2By similarity
    Active sitei282 – 2821Sequence Analysis
    Metal bindingi293 – 2931Manganese 2By similarity
    Metal bindingi352 – 3521Manganese 1By similarity
    Metal bindingi354 – 3541Manganese 1By similarity
    Metal bindingi354 – 3541Manganese 2By similarity
    Active sitei356 – 3561Sequence Analysis

    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

    BioCyciECOL386585:GJFA-5245-MONOMER.
    ECOO157:PEPA-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosol aminopeptidase (EC:3.4.11.1)
    Alternative name(s):
    Aminopeptidase A/I
    Leucine aminopeptidase (EC:3.4.11.10)
    Short name:
    LAP
    Leucyl aminopeptidase
    Gene namesi
    Name:pepA
    Synonyms:carP, xerB
    Ordered Locus Names:Z5872, ECs5237
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-HAMAP

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 503503Cytosol aminopeptidasePRO_0000165752Add
    BLAST

    Proteomic databases

    PRIDEiP68768.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Protein-protein interaction databases

    STRINGi155864.Z5872.

    Structurei

    3D structure databases

    ProteinModelPortaliP68768.
    SMRiP68768. Positions 1-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M17 family.Curated

    Phylogenomic databases

    eggNOGiCOG0260.
    HOGENOMiHOG000243132.
    KOiK01255.
    OMAiANEAKMS.
    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.

    P68768-1 [UniParc]FASTAAdd to Basket

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    MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG    50
    ELEGKPGQTL LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL 100
    NDTGSMEAVC FLTELHVKGR NNYWKVRQAV ETAKETLYSF DQLKTNKSEP 150
    RRPLRKMVFN VPTRRELTSG ERAIQHGLAI AAGIKAAKDL GNMPPNICNA 200
    AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG QGSQNESLMS 250
    VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV 300
    YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN 350
    TDAEGRLVLC DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN 400
    PLAHELIAAS EQSGDRAWRL PLGDEYQEQL ESNFADMANI GGRPGGAITA 450
    GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG ATGRPVALLA QFLLNRAGFN 500
    GEE 503
    Length:503
    Mass (Da):54,880
    Last modified:December 21, 2004 - v1
    Checksum:i643DED17EAC44DCD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG59459.1.
    BA000007 Genomic DNA. Translation: BAB38660.1.
    PIRiE91283.
    G86124.
    RefSeqiNP_290893.1. NC_002655.2.
    NP_313264.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG59459; AAG59459; Z5872.
    BAB38660; BAB38660; BAB38660.
    GeneIDi913804.
    959777.
    KEGGiece:Z5872.
    ecs:ECs5237.
    PATRICi18360111. VBIEscCol44059_5188.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG59459.1 .
    BA000007 Genomic DNA. Translation: BAB38660.1 .
    PIRi E91283.
    G86124.
    RefSeqi NP_290893.1. NC_002655.2.
    NP_313264.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P68768.
    SMRi P68768. Positions 1-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z5872.

    Proteomic databases

    PRIDEi P68768.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG59459 ; AAG59459 ; Z5872 .
    BAB38660 ; BAB38660 ; BAB38660 .
    GeneIDi 913804.
    959777.
    KEGGi ece:Z5872.
    ecs:ECs5237.
    PATRICi 18360111. VBIEscCol44059_5188.

    Phylogenomic databases

    eggNOGi COG0260.
    HOGENOMi HOG000243132.
    KOi K01255.
    OMAi ANEAKMS.
    OrthoDBi EOG6FV8B3.

    Enzyme and pathway databases

    BioCyci ECOL386585:GJFA-5245-MONOMER.
    ECOO157:PEPA-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiAMPA_ECO57
    AccessioniPrimary (citable) accession number: P68768
    Secondary accession number(s): P11648
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 62 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