ID   AMPN_LACLM              Reviewed;         846 AA.
AC   A2RI32; P37897;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
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; Synonyms=lap; OrderedLocusNames=llmg_0319;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-25.
RX   PubMed=1352755; DOI=10.1016/0014-5793(92)80827-4;
RA   Tan P.S.T., van Alen-Boerrigter I.J., Poolman B., Siezen R.J., de Vos W.M.,
RA   Konings W.N.;
RT   "Characterization of the Lactococcus lactis pepN gene encoding an
RT   aminopeptidase homologous to mammalian aminopeptidase N.";
RL   FEBS Lett. 306:9-16(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167, AND CHARACTERIZATION.
RX   PubMed=1685079; DOI=10.1128/aem.57.9.2555-2561.1991;
RA   van Alen-Boerrigter I.J., Baankreis R., de Vos W.M.;
RT   "Characterization and overexpression of the Lactococcus lactis pepN gene
RT   and localization of its product, aminopeptidase N.";
RL   Appl. Environ. Microbiol. 57:2555-2561(1991).
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; M87840; AAA25205.1; -; Genomic_DNA.
DR   EMBL; S39955; AAB22460.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL96925.1; -; Genomic_DNA.
DR   EMBL; M65867; AAA25162.1; -; Genomic_DNA.
DR   PIR; S23157; S23157.
DR   RefSeq; WP_011834382.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; A2RI32; -.
DR   SMR; A2RI32; -.
DR   STRING; 416870.llmg_0319; -.
DR   MEROPS; M01.002; -.
DR   KEGG; llm:llmg_0319; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_003705_0_1_9; -.
DR   OrthoDB; 100605at2; -.
DR   PhylomeDB; A2RI32; -.
DR   Proteomes; UP000000364; 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; 1.25.50.20; -; 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; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1352755"
FT   CHAIN           2..846
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000285237"
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;  95369 MW;  3288DB1A43DBDEF8 CRC64;
     MAVKRLIETF VPENYKIFLD IDRKTKKIKG QVAITGEAKD TVVSFHTKGL HFNKVRAFSV
     DTNFIENEED EEIVVKIGET GRVTVSFEYE AELTDNMMGI YPSYYEVNGE KKMLIGTQFE
     SHFARQAFPS IDEPEAKATF DLSVKFDEEE GDIIVSNMPE LLNINGIHVF ERTVKMSSYL
     LAFVFGELQY KKGKTKSGVE VGAFATKAHS QAALDFPLDI AIRSIEFYED YYQTPYPLPH
     SWHIALPDFS AGAMENWGCI TYREVCMLVD PENATIQSKQ YVATVIAHEL AHQWFGDLVT
     MQWWDDLWLN ESFANNMEYV CMDALEPSWN VWESFSISEA NMALNRDATD GVQSVHVEVT
     HPDEIGTLFD PAIVYAKGSR LMVMLRKWLG DEDFAAGLAL YFKRHQYGNT VGDNLWDALA
     EVSGKDVAAF MHSWVNQPGY PVVTAEVVDD TLILSQKQFF VGEGVDKGRL WNVPLNTNWT
     GLPDLLSSEK VEIPGFAALK TKNNGKALFL NDANMAHYII DYKGALLTDL LSEVESLENV
     TKFQILQDRK LLAKAGVISY ADVVNILPSF TNEESYLVNT GLSQLISELE LFVDEDSETE
     KAFQSLVGKL FAKNYARLGW DKVAGESAGD ESLRGIVLSK TLYSENADAK TKASQIFAAH
     KENLASIPAD IRPIVLNNEI KTTNSAELVK TYRETYIKTS LQEFKRELEG AVALIKDEKV
     IAELLESFKN ADIVKPQDIA FSWFYLLRND FSQDAAWAWE KANWAFLEEK LGGDMSYDKF
     VIYPGNTFKT ADKLAEYKAF FEPKLENQGL KRSIEMAIKQ ITARVALIDS QKAAVDKAIT
     DIAEKL
//