ID   AMPN_STRLI              Reviewed;         857 AA.
AC   Q11010;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, 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   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 415-439.
RC   STRAIN=66 / 1326;
RX   PubMed=7909302; DOI=10.1016/0378-1119(94)90137-6;
RA   Butler M.J., Aphale J.S., Binnie C., Dizonno M.A., Krygsman P.,
RA   Soltes G.A., Walczyk E., Malek L.T.;
RT   "The aminopeptidase N-encoding pepN gene of Streptomyces lividans 66.";
RL   Gene 141:115-119(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=66 / 1326;
RX   PubMed=7765336; DOI=10.1007/bf01569658;
RA   Butler M.J., Aphale J.S., Dizonno M.A., Krygsman P., Walczyk E.,
RA   Malek L.T.;
RT   "Intracellular aminopeptidases in Streptomyces lividans 66.";
RL   J. Ind. Microbiol. 13:24-29(1994).
CC   -!- FUNCTION: Aminopeptidase with broad substrate specificity to several
CC       peptides. Shows strong preference for leucine but cleaves also next to
CC       Arg and lysine in peptide-bond-containing substrates.
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.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; L23172; AAA26696.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11010; -.
DR   SMR; Q11010; -.
DR   MEROPS; M01.009; -.
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   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; IPR012778; Pept_M1_aminopeptidase.
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   TIGRFAMs; TIGR02412; pepN_strep_liv; 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   CHAIN           1..857
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095076"
FT   ACT_SITE        299
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         264..268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
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         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            386
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   857 AA;  94424 MW;  40B749F78D201A7D CRC64;
     MPGTNLTREE ARQRATLLTV DSYEIDLDLT GAQEGGTYRS VTTVRFDVAE GGGESFIDLV
     APTVHEVTLN GDALDTAEVF QDSRIALPGL LPGRNILRVV ADCAYTNTGE GLHRFVDPVD
     DQAYLYTQFE VPDARRVFAS FEQPDLKATF QFTVKAPEGW TVISNSPTPE PKDNVWEFEP
     TPRISSYVTA LIVGPYHSVH SVYEKDGQSV PLGIYCRPSL AEHLDADAIF EVTRQGFDWF
     QEKFDYAYPF KKYDQLFVPE FNAGAMENAG AVTIRDQYVF RSKVTDAAYE VRAATILHEL
     AHMWFGDLVT MEWWNDLWLN ESFATYAEAA CQAAAPGSKW PHSWTTFANQ MKTWAYRQDQ
     LPSTHPIMAD ISDLDDVLVN FDGITYAKGA SVLKQLVAYV GEEAFFKGVQ AYFKRHAFGN
     TRLSDLLGAL EETSGRDLKT WSKAWLETAG INVLRPEIET DADGVITSFA IRQEAPALPA
     GAKGEPTLRP HRIAIGAYDL DGAGKLVRGD RVELDVDGEL TAVPQLVGKA RPAVLLLNDD
     DLSYAKVRLD EQSLAVVTEH LGDFTESLPR ALCWASAWDM TRDAELATRD YLALVLSGIG
     KESDIGVVQS LHRQVKLAID QYAAPTAREA LLTRWTEATL AHLRAAEAGS DHQLAWARAF
     AATARTPEQL DLLDALLDGT QTIEGLAVDT ELRWAFVQRL AAVGRFGGSE IAAEYERDKT
     AAGERHAATA RAARPTEAAK AEAWESVVES DKLPNAVQEA VIAGFVQTDQ RELLAAYTER
     YFEALKDVWA SRSHEMAQQI AVGLYPAVQV SQDTLDRTDA WLASAEPNAA LRRLVSESRS
     GIERALRAQA ADAAAAE