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Q10730

- AMPN_LACHE

UniProt

Q10730 - AMPN_LACHE

Protein

Aminopeptidase N

Gene

pepN

Organism
Lactobacillus helveticus (Lactobacillus suntoryeus)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.By similarity

    Catalytic activityi

    Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei120 – 1201SubstrateBy similarity
    Metal bindingi289 – 2891Zinc; catalyticPROSITE-ProRule annotation
    Active sitei290 – 2901Proton acceptorPROSITE-ProRule annotation
    Metal bindingi293 – 2931Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi312 – 3121Zinc; catalyticPROSITE-ProRule annotation
    Sitei376 – 3761Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB-KW
    3. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM01.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase N (EC:3.4.11.2)
    Alternative name(s):
    Alanine aminopeptidase
    Lysyl aminopeptidase
    Short name:
    Lys-AP
    Gene namesi
    Name:pepN
    OrganismiLactobacillus helveticus (Lactobacillus suntoryeus)
    Taxonomic identifieri1587 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 844844Aminopeptidase NPRO_0000095072Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ10730.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni253 – 2575Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Family and domain databases

    InterProiIPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q10730-1 [UniParc]FASTAAdd to Basket

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    MAVKRFYKTF HPEHYDLRIN VNRKNKTING TSTITGDVFE NPVLINQKFM    50
    TIDSVKVDGK NVDFDVIEKD EAIKIKTGVT GKAVIEIAYS APLTDTMMGI 100
    YPSYYELEGK KKQIIGTQFE TTFARQAFPC VDEPEAKATF SLALKWDEQD 150
    GEVALANMPE VEVDKDGYHH FEETVRMSSY LVAFAFGELQ SKTTHTKDGV 200
    LIGVYATKAH KPKELDFALD IAKRAIEFYE EFYQTKYPLP QSLQLALPDF 250
    SAGAMENWGL VTYREAYLLL DPDNTSLEMK KLVATVITHE LAHQWFGDLV 300
    TMKWWDNLWL NESFANMMEY LSVDGLEPDW HIWEMFQTSE ASSALNRDAT 350
    DGVQPIQMEI NDPADIDSVF DSAIVYAKGS RMLVMVRSLL GDDALRKGLK 400
    YYFDHHKFGN ATGDDLWDAL STATDLDIGK IMHSWLKQPG YPVVNAFVAE 450
    DGHLKLTQKQ FFIGEGEDKG RQWQIPLNAN FDAPKIMSDK EIDLGSYKVL 500
    REEAGHPLRL NVGNNSHFIV EYDKTLHDDI LSDVNELDPI DKLQLLQDLR 550
    LLAEGKQISY ASIVPLLVKF ADSKSSLVIN ALYTTAAKLR QFVEPESNEE 600
    KNLKKLYDLL SKDQVARLGW EVKPGESDED VQIRPYELSA SLYAENADSI 650
    KAAHQIFTEN EDNLEALNAD IRPYVLINEV KNFGNAELVD KLIKEYQRTA 700
    DPSYKVDLRS AVTSTKDLAA IKAIVGDFEN ADVVKPQDLC DWYRGLLANH 750
    YGQQAAWDWI REDWDWLDKT VGGDMEFAKF ITVTAGVFHT PERLKEFKEF 800
    FEPKINVPLL SREIKMDVKV IESKVNLIEA EKDAVNDAVA KAID 844
    Length:844
    Mass (Da):95,838
    Last modified:October 1, 1996 - v1
    Checksum:i1EA5DE6AC69410F4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391F → I in strain: 53/7.
    Natural varianti44 – 441L → F in strain: 53/7.
    Natural varianti342 – 3421S → A in strain: 53/7.
    Natural varianti455 – 4551K → R in strain: 53/7.
    Natural varianti496 – 4961S → N in strain: 53/7.
    Natural varianti527 – 5271H → L in strain: 53/7.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08224 Genomic DNA. Translation: AAA81951.1.
    Z30323 Genomic DNA. Translation: CAA82978.1.
    PIRiJC4054.
    S47274.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08224 Genomic DNA. Translation: AAA81951.1 .
    Z30323 Genomic DNA. Translation: CAA82978.1 .
    PIRi JC4054.
    S47274.

    3D structure databases

    ProteinModelPortali Q10730.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M01.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis, distribution and expression of an aminopeptidase N-encoding gene from Lactobacillus helveticus CNRZ32."
      Christensen J.E., Lin D.-L., Palva A., Steele J.L.
      Gene 155:89-93(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CNRZ 32.
    2. "Characterization and expression of the pepN gene encoding a general aminopeptidase from Lactobacillus helveticus."
      Varmanen P., Vesanto E., Steele J.L., Palva A.
      FEMS Microbiol. Lett. 124:315-320(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 53/7.

    Entry informationi

    Entry nameiAMPN_LACHE
    AccessioniPrimary (citable) accession number: Q10730
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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