ID   AMPN_LACLA              Reviewed;         846 AA.
AC   Q9CIQ1;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
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; OrderedLocusNames=LL0305; ORFNames=L102360;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=It may be secreted
CC       through an unknown mechanism. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; AE005176; AAK04403.1; -; Genomic_DNA.
DR   PIR; A86663; A86663.
DR   RefSeq; NP_266461.1; NC_002662.1.
DR   RefSeq; WP_003131692.1; NC_002662.1.
DR   AlphaFoldDB; Q9CIQ1; -.
DR   SMR; Q9CIQ1; -.
DR   STRING; 272623.L102360; -.
DR   MEROPS; M01.002; -.
DR   PaxDb; Q9CIQ1; -.
DR   EnsemblBacteria; AAK04403; AAK04403; L102360.
DR   KEGG; lla:L102360; -.
DR   PATRIC; fig|272623.7.peg.335; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_003705_0_1_9; -.
DR   OMA; MMEYVAI; -.
DR   Proteomes; UP000002196; Chromosome.
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; 1.10.390.10; -; 1.
DR   Gene3D; 2.60.40.1730; -; 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   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; SSF63737; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Zinc.
FT   CHAIN           1..846
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095073"
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   846 AA;  95336 MW;  25AB6453A6A2681D CRC64;
     MAVKRLIETF VPENYKIFLD IDRKTKKIKG QVAITGEAKD SVIAFHAKGL HFSKVRAFSV
     DTNFIENEED EEIVVKIGET GRVTVSFEYE AELTDNMMGI YPSYYEVNGE KKMLIGTQFE
     SHFARQAFPS IDEPEAKATF DLSVKFDEEE GDIIVSNMPE LLNINGIHVF ERTVKMSSYL
     LAFVFGELQF KKGKTKSGVE VGAFATKDHS EAALDFPLDI AIRSIEFYED YYKTPYPLPH
     SWHIALPDFS AGAMENWGCI TYREVCMLVD PENATIQSKQ YVATVIAHEL AHQWFGDLVT
     MQWWDDLWLN ESFANNMEYV CMDALEPSWN VWESFSISEA NMALNRDATD GVQSVHVEVT
     HPDEIGTLFD PAIVYAKGSR LMVMLRKWLG DEDFAAGLAL YFKRHQYGNT VGDNLWDALA
     EVSGKDVAAF MHSWVNQPGY PVVTAEVIDD TLVLSQKQFF VGEGADKGRL WNVPLNTNWS
     GLPDLLSSEK VEIPGFAALK AKNDGKALFL NDANMAHYII DYKGQLLTDL LSEVETLENV
     TKFQILQDRK LLAKAGVISY ADVVNILPAF TNEESYLVNT GLSQLISELE LFVDEDSETE
     KAFQSLVGKL FAKNYARLGW DKVAGESAGD ESLRGIVLSK TLYAENADAK AKASQIFAAH
     KENLAGIPAD IRPIVLNNEI KTTNSAELVK TYRETYVKTS LQEFKRELEG AVALIKDEKV
     IAELLESFKN ADIVKPQDIA FSWFYLLRND FSQDAAWAWE KANWAFLEEK LGGDMSYDKF
     VIYPGNTFKT ADKLAEYKAF FEPKLENQGL KRSIEMAIKQ ITARVALIDS QKADVDKSIK
     EISEKL