AMPN_LACHE
ID AMPN_LACHE Reviewed; 844 AA.
AC Q10730;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Lactobacillus helveticus (Lactobacillus suntoryeus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CNRZ 32;
RX PubMed=7698673; DOI=10.1016/0378-1119(94)00924-h;
RA Christensen J.E., Lin D.-L., Palva A., Steele J.L.;
RT "Sequence analysis, distribution and expression of an aminopeptidase N-
RT encoding gene from Lactobacillus helveticus CNRZ32.";
RL Gene 155:89-93(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=53/7;
RX PubMed=7851738; DOI=10.1111/j.1574-6968.1994.tb07302.x;
RA Varmanen P., Vesanto E., Steele J.L., Palva A.;
RT "Characterization and expression of the pepN gene encoding a general
RT aminopeptidase from Lactobacillus helveticus.";
RL FEMS Microbiol. Lett. 124:315-320(1994).
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; U08224; AAA81951.1; -; Genomic_DNA.
DR EMBL; Z30323; CAA82978.1; -; Genomic_DNA.
DR PIR; JC4054; JC4054.
DR PIR; S47274; S47274.
DR AlphaFoldDB; Q10730; -.
DR SMR; Q10730; -.
DR STRING; 326425.lhe_0331; -.
DR MEROPS; M01.002; -.
DR eggNOG; COG0308; Bacteria.
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; Zinc.
FT CHAIN 1..844
FT /note="Aminopeptidase N"
FT /id="PRO_0000095072"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253..257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 376
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT VARIANT 39
FT /note="F -> I (in strain: 53/7)"
FT VARIANT 44
FT /note="L -> F (in strain: 53/7)"
FT VARIANT 342
FT /note="S -> A (in strain: 53/7)"
FT VARIANT 455
FT /note="K -> R (in strain: 53/7)"
FT VARIANT 496
FT /note="S -> N (in strain: 53/7)"
FT VARIANT 527
FT /note="H -> L (in strain: 53/7)"
SQ SEQUENCE 844 AA; 95838 MW; 1EA5DE6AC69410F4 CRC64;
MAVKRFYKTF HPEHYDLRIN VNRKNKTING TSTITGDVFE NPVLINQKFM TIDSVKVDGK
NVDFDVIEKD EAIKIKTGVT GKAVIEIAYS APLTDTMMGI YPSYYELEGK KKQIIGTQFE
TTFARQAFPC VDEPEAKATF SLALKWDEQD GEVALANMPE VEVDKDGYHH FEETVRMSSY
LVAFAFGELQ SKTTHTKDGV LIGVYATKAH KPKELDFALD IAKRAIEFYE EFYQTKYPLP
QSLQLALPDF SAGAMENWGL VTYREAYLLL DPDNTSLEMK KLVATVITHE LAHQWFGDLV
TMKWWDNLWL NESFANMMEY LSVDGLEPDW HIWEMFQTSE ASSALNRDAT DGVQPIQMEI
NDPADIDSVF DSAIVYAKGS RMLVMVRSLL GDDALRKGLK YYFDHHKFGN ATGDDLWDAL
STATDLDIGK IMHSWLKQPG YPVVNAFVAE DGHLKLTQKQ FFIGEGEDKG RQWQIPLNAN
FDAPKIMSDK EIDLGSYKVL REEAGHPLRL NVGNNSHFIV EYDKTLHDDI LSDVNELDPI
DKLQLLQDLR LLAEGKQISY ASIVPLLVKF ADSKSSLVIN ALYTTAAKLR QFVEPESNEE
KNLKKLYDLL SKDQVARLGW EVKPGESDED VQIRPYELSA SLYAENADSI KAAHQIFTEN
EDNLEALNAD IRPYVLINEV KNFGNAELVD KLIKEYQRTA DPSYKVDLRS AVTSTKDLAA
IKAIVGDFEN ADVVKPQDLC DWYRGLLANH YGQQAAWDWI REDWDWLDKT VGGDMEFAKF
ITVTAGVFHT PERLKEFKEF FEPKINVPLL SREIKMDVKV IESKVNLIEA EKDAVNDAVA
KAID
