AMPN_LACLC
ID AMPN_LACLC Reviewed; 846 AA.
AC P0C2T8; P37897;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
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;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wg2;
RX PubMed=1563625; DOI=10.1016/0378-1119(92)90676-g;
RA Stroman P.;
RT "Sequence of a gene (lap) encoding a 95.3-kDa aminopeptidase from
RT Lactococcus lactis ssp. cremoris Wg2.";
RL Gene 113:107-112(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-34.
RC STRAIN=Wg2;
RX PubMed=16348128; DOI=10.1128/aem.56.2.526-532.1990;
RA Tan P.S.T., Konings W.N.;
RT "Purification and characterization of an aminopeptidase from Lactococcus
RT lactis subsp. cremoris Wg2.";
RL Appl. Environ. Microbiol. 56:526-532(1990).
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; X61230; CAA43547.1; -; Genomic_DNA.
DR PIR; JN0324; JN0324.
DR AlphaFoldDB; P0C2T8; -.
DR SMR; P0C2T8; -.
DR MEROPS; M01.002; -.
DR SABIO-RK; P0C2T8; -.
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 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:16348128"
FT CHAIN 2..846
FT /note="Aminopeptidase N"
FT /id="PRO_0000095075"
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; 95309 MW; 8606417173834D40 CRC64;
MAVKRLIETF VPENYKIFLD IDRKTKKIKG QVAITGEAKD TVVAFHAKGL HFNKVRAFSV
DTNFIENEED EEIVVKIGET GRVTVSFEYE AELTDNMMGI YPSYYEVNGE KKMLIGTQFE
SHFARQAFPS IDEPEAKATF DLSVKFDEEE GDIIVSNMPE LLNINGIHVF ERTVKMSSYL
LAFVFGELQY KKGKTKSGVE VGAFATKAHS QAALDFPLDI AIRSIEFYED YYQTPYPLPH
SWHIALPDFS SGAMENWGCI 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 TKASQIFATH
KENLASIPAD IRPIVLNNEI KTTNSAELVK TYRETYIKTS LQEFKRELEG AVALIKDEKV
IAELLESFKN ADIVKPQDIA FSWFYLLRND FSQDAAWAWE KANWASLEEK LGGDMSYDKF
VIYPGNTFKT ADKLAEYKAF FEPKLENQGL KRSIEMAIKQ ITARVALIDS QKAAVDKAIT
DIAEKL
