ID   AMPN_LACLL              Reviewed;         849 AA.
AC   Q48656;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 103.
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   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=YRC001;
RA   Tsukasaki F., Motoshima H., Minagawa E., Kaminogawa S.;
RT   "Cloning of lysyl-aminopeptidase gene from Lactococcus lactis.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Aminopeptidase with broad substrate specificity to several
CC       peptides. It has more affinity for oligopeptides than for dipeptides.
CC       It plays an essential role in the metabolism, it may be involved in
CC       nitrogen supply or protein turnover.
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   -!- SUBUNIT: Monomer.
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; D38040; BAA07234.1; -; Genomic_DNA.
DR   PIR; JU0191; JU0191.
DR   AlphaFoldDB; Q48656; -.
DR   SMR; Q48656; -.
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; 2.60.40.1910; -; 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; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..849
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095074"
FT   ACT_SITE        295
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         259..263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            382
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   849 AA;  96565 MW;  E809F5437DFBD50F CRC64;
     MTASVARFIE SFIPENYNLF LDINRSEKTF TGNVAITGEA IDNHISLHQK DLTINSVLLD
     NESLNFQMDD ANEAFHIELP ETGVLTIFIE FSGRITDNMT GIYPSYYTYN GEKKEIISTQ
     FEISHFAREA FPCVDEPEAK ATFDLSLKFD AEEGDTALSN MPEINSHLRE ETGVWTFETT
     PRMSTYLLAF GFGALHGKTA KTKNGTEVGV FATVAQAENS FDFALDIAVR VIEFYEDYFQ
     VKYPIPLSYH LALPDFSAGA MENWGLVTYR EVYLLVDENS SAASRQQVAL VVAHELAHQW
     FGNLVTMKWW DDLWLNESFA NMMEYVSVNA IEPSWNIFEG FPNKLGVPNA LQRDATDGVQ
     SVHMEVSHPD EINTLFDSAI VYAKGSRLMH MLRRWLGDEA FAKGLKAYFE KHQYNNTVGR
     DLWNALSEAS GKDVSSFMDT WLEQPGYPVV SAEVVDDTLI LSQKQFFIGE HEDKGRLWEI
     PLNTNWNGLP DTLSGERIEI PNYSQLATEN NGVLRLNTAN TAHYITDYQG QLLDNILEDF
     ANLDTVSKLQ ILQERRLLAE SGRISYASLV GLLDLVEKEE SFFLISQAKS QILAGLKRFI
     DEDTEAEVHY KALVRRQFQN DFERLGFDAK EGESDEDEMV RQTALSYLIE ADYQPTVLAA
     ANVFQAHKEN IESIPASIRG LVLINQMKQE NSLSLVEEYI NAYVATNDSN FRRQLTQALS
     YLKNQEGLDY VLGQLKDKNV VKPQDLYLWY MNFLSKSFAQ ETVWDWAKEN WEWIKAALGG
     DMSFDSFVNI PAGIFKNQER LDQYIAFFEP QTSDKALERN ILMGIKTIAA RVDLIEKEKA
     AVESALKDY
//