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P37896

- AMPN_LACDL

UniProt

P37896 - AMPN_LACDL

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Protein
Aminopeptidase N
Gene
pepN
Organism
Lactobacillus delbrueckii subsp. lactis
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Aminopeptidase with broad substrate specificity to several peptides.

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.

pH dependencei

Optimum pH is 6.5-7.0.

Temperature dependencei

Optimum temperature is 54-55 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201Substrate By similarity
Metal bindingi288 – 2881Zinc; catalytic By similarity
Active sitei289 – 2891Proton acceptor By similarity
Metal bindingi292 – 2921Zinc; catalytic By similarity
Metal bindingi311 – 3111Zinc; catalytic By similarity
Sitei375 – 3751Transition state stabilizer By similarity

GO - Molecular functioni

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

GO - Biological processi

    Complete GO annotation...

    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 delbrueckii subsp. lactis
    Taxonomic identifieri29397 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

    Subcellular locationi

    Cytoplasm
    Note: It may be secreted through an unknown mechanism.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed By similarity
    Chaini2 – 843842Aminopeptidase N
    PRO_0000095071Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer By similarity.

    Structurei

    3D structure databases

    ProteinModelPortaliP37896.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni252 – 2565Substrate binding By similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P37896-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVKRFYETF HPDHYDLYID VDRAARSFSG TSTIHGEIQE ETVLVHQKYM    50
    TISKVTVDGK EVPFTFGDDF EGIKIEAGKT GEAVIAIDYS APLTDTMMGI 100
    YPSYYQVDGV KKELIGTQFE TTFAREAFPC VDEPEAKATF SLALKFDEHE 150
    GETVLANMPE DRVENGVHYF KETVRMSSYL VAFAFGEMRS LTTHTKSGVL 200
    IGVYSTQAHT EKELTFSLDI AKRAIEFYED FYQTPYPLPQ SLQLALPDFS 250
    AGAMENWGLV TYREAYLLLD PDNTTLEMKK LVATVVTHEL AHQWFGDLVT 300
    MEWWDNLWLN ESFANMMEYL SVDHLEPNWH IWEMFQTSEA AAALTRDATD 350
    GVQSVHVEVN DPAEIDALFD GAIVYAKGSR MLVMVRSLLG DEALRKGLKR 400
    YFDKHKFGNA AGDDLWDALS TATDLNIGEI MHTWLDQPGY PVVNAFVEDG 450
    HLKLTQKQFF IGEGKEVGRK WEIPLNANFK APKIMSDVEL DLGDYQALRA 500
    EAGHALRLNV GNNSHFIVKY DQTLMDDIMK EAKDLDPVSQ LQLLQDLRLL 550
    AEGKQASYAD VVPVLELFKN SESHIVNDAL YTTADKLRQF APAGSEADKN 600
    LRALYNDLSK DQVARLGWLP KAGESDEDIQ TRPYVLSASL YGRNADSEKQ 650
    AHEIYVEYAD KLAELSADIR PYVLINEVEN YGSSELTDKL IGLYQATSDP 700
    SFKMDLEAAI VKSKDEGELK KIVSWFKNAE IVKPQDLRGW FSGVLSNPAG 750
    EQLAWDWIRD EWAWLEKTVG GDMEFATFIT VISRVFKTKE RYDEYNAFFT 800
    DKESNMLLNR EIKMDRKVIA NRVDLIASEQ ADVNAAVAAA LQK 843
    Length:843
    Mass (Da):95,348
    Last modified:January 23, 2007 - v3
    Checksum:i08EF9F8CBD7AB1B0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21701 Genomic DNA. Translation: CAA79805.1.
    PIRiS38364.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21701 Genomic DNA. Translation: CAA79805.1 .
    PIRi S38364.

    3D structure databases

    ProteinModelPortali P37896.
    ModBasei 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. "Cloning, DNA sequence analysis and partial characterization of pepN, a lysyl aminopeptidase from Lactobacillus delbruckii ssp. lactis DSM7290."
      Klein J.R., Klein U., Schad M., Plapp R.
      Eur. J. Biochem. 217:105-114(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 7290.

    Entry informationi

    Entry nameiAMPN_LACDL
    AccessioniPrimary (citable) accession number: P37896
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: May 14, 2014
    This is version 79 of the entry and version 3 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

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