ID   PEPE_LACHE              Reviewed;         438 AA.
AC   P94870;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Aminopeptidase E;
DE            EC=3.4.22.-;
GN   Name=pepE; Synonyms=pepG;
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=9098049; DOI=10.1128/jb.179.8.2529-2533.1997;
RA   Fenster K.M., Parkin K.L., Steele J.L.;
RT   "Characterization of a thiol-dependent endopeptidase from Lactobacillus
RT   helveticus CNRZ32.";
RL   J. Bacteriol. 179:2529-2533(1997).
CC   -!- FUNCTION: Can hydrolyze internal peptide bonds in Met-enkephalin and
CC       bradykinin; however, hydrolysis of alpha-, beta-, and kappa-caseins is
CC       not detected.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.5.;
CC       Temperature dependence:
CC         Optimum temperature is 32-37 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR   EMBL; U77050; AAB52540.1; -; Genomic_DNA.
DR   RefSeq; WP_003625562.1; NZ_WCFT01000007.1.
DR   AlphaFoldDB; P94870; -.
DR   SMR; P94870; -.
DR   STRING; 326425.lhe_1868; -.
DR   MEROPS; C01.088; -.
DR   GeneID; 66451459; -.
DR   eggNOG; COG3579; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00585; Peptidase_C1B; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR004134; Peptidase_C1B.
DR   PANTHER; PTHR10363; PTHR10363; 1.
DR   Pfam; PF03051; Peptidase_C1_2; 1.
DR   PIRSF; PIRSF005700; PepC; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..438
FT                   /note="Aminopeptidase E"
FT                   /id="PRO_0000050598"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   438 AA;  50022 MW;  6811F1B653010B5C CRC64;
     MAHELTVQEL EKFSADFNKN PKNKVVARAA QRSGVLEASY NDRVQSELTR VFSTELDTDN
     VTNQKHSGRC WLFATLNVLR HEFGKKYKAK DFTFSQAYNF FWDKIERANM FYNRILDSAD
     MPLDSRQVKT DLDFAGTDGG QFQMAAALVE KYGVVPSYAM PETFNTNDTT GFATALGDKL
     KKDALVLRKL KQEGKDDEIK KTREKFLSEV YQMTAIAVGE PPKKFDLEYR DDDKKYHLEK
     DLTPLEFLHK YLGGVDFDDY VVLTNAPDHE YDKLYGLPAE DNVSGSIRIK LLNVPMEYLT
     AASIAQLKDG EAVWFGNDVL RQMDRKTGYL DTNLYKLDDL FGVDLKMSKA DRLKTGVGEV
     SHAMTLVGVD EDNGEVRQWK VENSWGDKSG AKGYYVMNNE WFNDYVYEVV VHKKYLTDKQ
     KELAEGPITD LPAWDSLA