ID   AMPN_LACDL              Reviewed;         843 AA.
AC   P37896;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Aminopeptidase N;
DE            EC=3.4.11.2;
DE   AltName: Full=Alanine aminopeptidase;
DE   AltName: Full=Lysyl aminopeptidase;
DE            Short=Lys-AP;
GN   Name=pepN;
OS   Lactobacillus delbrueckii subsp. lactis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=29397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 7290;
RX   PubMed=8223547; DOI=10.1111/j.1432-1033.1993.tb18224.x;
RA   Klein J.R., Klein U., Schad M., Plapp R.;
RT   "Cloning, DNA sequence analysis and partial characterization of pepN, a
RT   lysyl aminopeptidase from Lactobacillus delbruckii ssp. lactis DSM7290.";
RL   Eur. J. Biochem. 217:105-114(1993).
CC   -!- FUNCTION: Aminopeptidase with broad substrate specificity to several
CC       peptides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5-7.0.;
CC       Temperature dependence:
CC         Optimum temperature is 54-55 degrees Celsius.;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=It may be secreted through an
CC       unknown mechanism.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; Z21701; CAA79805.1; -; Genomic_DNA.
DR   PIR; S38364; S38364.
DR   AlphaFoldDB; P37896; -.
DR   SMR; P37896; -.
DR   MEROPS; M01.002; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..843
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095071"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            375
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   843 AA;  95348 MW;  08EF9F8CBD7AB1B0 CRC64;
     MAVKRFYETF HPDHYDLYID VDRAARSFSG TSTIHGEIQE ETVLVHQKYM TISKVTVDGK
     EVPFTFGDDF EGIKIEAGKT GEAVIAIDYS APLTDTMMGI YPSYYQVDGV KKELIGTQFE
     TTFAREAFPC VDEPEAKATF SLALKFDEHE GETVLANMPE DRVENGVHYF KETVRMSSYL
     VAFAFGEMRS LTTHTKSGVL IGVYSTQAHT EKELTFSLDI AKRAIEFYED FYQTPYPLPQ
     SLQLALPDFS AGAMENWGLV TYREAYLLLD PDNTTLEMKK LVATVVTHEL AHQWFGDLVT
     MEWWDNLWLN ESFANMMEYL SVDHLEPNWH IWEMFQTSEA AAALTRDATD GVQSVHVEVN
     DPAEIDALFD GAIVYAKGSR MLVMVRSLLG DEALRKGLKR YFDKHKFGNA AGDDLWDALS
     TATDLNIGEI MHTWLDQPGY PVVNAFVEDG HLKLTQKQFF IGEGKEVGRK WEIPLNANFK
     APKIMSDVEL DLGDYQALRA EAGHALRLNV GNNSHFIVKY DQTLMDDIMK EAKDLDPVSQ
     LQLLQDLRLL AEGKQASYAD VVPVLELFKN SESHIVNDAL YTTADKLRQF APAGSEADKN
     LRALYNDLSK DQVARLGWLP KAGESDEDIQ TRPYVLSASL YGRNADSEKQ AHEIYVEYAD
     KLAELSADIR PYVLINEVEN YGSSELTDKL IGLYQATSDP SFKMDLEAAI VKSKDEGELK
     KIVSWFKNAE IVKPQDLRGW FSGVLSNPAG EQLAWDWIRD EWAWLEKTVG GDMEFATFIT
     VISRVFKTKE RYDEYNAFFT DKESNMLLNR EIKMDRKVIA NRVDLIASEQ ADVNAAVAAA
     LQK
//