ID   AMPN_ACEPA              Reviewed;         355 AA.
AC   Q10736;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Aminopeptidase N;
DE            EC=3.4.11.2;
DE   AltName: Full=Alpha-aminoacylpeptide hydrolase;
DE   Flags: Fragment;
GN   Name=pepN;
OS   Acetobacter pasteurianus (Acetobacter turbidans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9325 / NCTC 6249 / NRRL B-570;
RA   Weber M.;
RT   "Cloning and DNA sequence analysis of the 5' end of aminopeptidase N (pepN)
RT   from Acetobacter turbidans ATCC9325.";
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Aminopeptidase N is involved in the degradation of
CC       intracellular peptides generated by protein breakdown during normal
CC       growth as well as in response to nutrient starvation. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; X94692; CAA64355.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q10736; -.
DR   SMR; Q10736; -.
DR   MEROPS; M01.010; -.
DR   PRIDE; Q10736; -.
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; 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; 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; Zinc.
FT   CHAIN           1..>355
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095067"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         290..294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   NON_TER         355
SQ   SEQUENCE   355 AA;  38820 MW;  8F214BDB2B368232 CRC64;
     MRRLLTLTTL LAGVPLAAPV CAEQVFSFQR AAGQLPKTVV PVSYGINIST DIDNLKLTGQ
     ETIQVDVRTP TEDVTLNQAG LHLAGAVLDN GVKATITQDD AAETATLHFP AKVSKGAHTL
     VITYSGPILK TPNGIYVDDY TAPSGETKRM LVTQFEVADA RRMFPGWDEP AFKATFQLNV
     TLPKEAVAVS NMPVTQSTPE GTSQKRVSFA TTPRMSTYLL ALVAGDMKSV QGQADGTPLA
     VYAPSGLEEQ GEYALHASEK ILPYYNNYFG VKYPLPQMDM VAIPGNYQAG AMENWGLLTY
     IDNVLLFDPP NSTPRTRELI YEVVAHEMAH QWSGDLVTMG WWDNIWLNEG FASWM