ID   PEPC_STRTR              Reviewed;         445 AA.
AC   Q56115;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Aminopeptidase C;
DE            EC=3.4.22.40;
DE   AltName: Full=Bleomycin hydrolase;
GN   Name=pepC;
OS   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNRZ 302;
RX   PubMed=7925365; DOI=10.1111/j.1432-1033.1994.00497.x;
RA   Chapot-Chartier M.P., Rul F., Nardi M., Gripon J.-C.;
RT   "Gene cloning and characterization of PepC, a cysteine aminopeptidase from
RT   Streptococcus thermophilus, with sequence similarity to the eucaryotic
RT   bleomycin hydrolase.";
RL   Eur. J. Biochem. 224:497-506(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by
CC         hydrolysis of a carboxyamide bond of beta-aminoalanine, but also
CC         shows general aminopeptidase activity. The specificity varies
CC         somewhat with source, but amino acid arylamides of Met, Leu and Ala
CC         are preferred.; EC=3.4.22.40;
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
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; Z30315; CAA82960.1; -; Genomic_DNA.
DR   PIR; S48143; S48143.
DR   RefSeq; WP_014607929.1; NZ_QFFS01000007.1.
DR   AlphaFoldDB; Q56115; -.
DR   SMR; Q56115; -.
DR   STRING; 322159.STER_0276; -.
DR   MEROPS; C01.086; -.
DR   eggNOG; COG3579; Bacteria.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..445
FT                   /note="Aminopeptidase C"
FT                   /id="PRO_0000050596"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  50415 MW;  AD83B0891E3A65C5 CRC64;
     MTSLSTDFTE KLFADYEANA KYGAIENAVT HNGLLKSIET RQSEVENDFV FSIDLTKDEV
     SNQKASGRCW MFAALNTFRH KLISDFKLES FELSQAHTFF WDKYEKSNWF LEQIIATADQ
     EIGSRKVKFL LDTPQQDGGQ WDMVVSLFEK YGVVPKSVYP ESVASSNSRE LNQYLNKLLR
     QDAQILRDLI ASGADQAAVQ AKKEEFLQEI FNYLAMTLGL PPRQFDFAYR DKDDNYRSEK
     GITPRAFFEK YVGLKLSDYV SVINAPTADK PYGKSYTVEM LGNVVGAPSV RYINLPMDRF
     KELAIAQMKA GESVWFGSDV GQVSDRQKGI LATNVYDFTA SMDINWTQDK AGRLDYSESL
     MTHAMVLTGV DLDADGKPIK WKIENSWGDK VGQKGYFVAS DAWMDEYTYQ IVVRKDFLTA
     EELAAYEADP QVLAPWDPMG SLASK