ID   PEPC_LACLC              Reviewed;         436 AA.
AC   Q04723;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Aminopeptidase C;
DE            EC=3.4.22.40;
DE   AltName: Full=Bleomycin hydrolase;
GN   Name=pepC;
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], AND PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=AM2;
RX   PubMed=8439160; DOI=10.1128/aem.59.1.330-333.1993;
RA   Chapot-Chartier M.P., Nardi M., Chopin M.-C., Chopin A., Gripon J.-C.;
RT   "Cloning and sequencing of pepC, a cysteine aminopeptidase gene from
RT   Lactococcus lactis subsp. cremoris AM2.";
RL   Appl. Environ. Microbiol. 59:330-333(1993).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=9546047; DOI=10.1016/s0167-4838(97)00185-4;
RA   Mistou M.Y., Gripon J.-C.;
RT   "Catalytic properties of the cysteine aminopeptidase PepC, a bacterial
RT   bleomycin hydrolase.";
RL   Biochim. Biophys. Acta 1383:63-70(1998).
CC   -!- FUNCTION: Hydrolyzes naphthylamide-substituted amino acids as well as
CC       di- and tripeptides in which the half-cystine residue is involved in a
CC       disulfide loop, notably in oxytocin and vasopressin. Has also a
CC       bleomycin hydrolase activity.
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.
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; M86245; AAA74514.1; -; Genomic_DNA.
DR   PIR; B48957; B48957.
DR   RefSeq; WP_011676889.1; NZ_WJUW01000029.1.
DR   AlphaFoldDB; Q04723; -.
DR   SMR; Q04723; -.
DR   MEROPS; C01.086; -.
DR   PRIDE; Q04723; -.
DR   GeneID; 61110208; -.
DR   OMA; WDMIVNL; -.
DR   SABIO-RK; Q04723; -.
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   1: Evidence at protein level;
KW   Aminopeptidase; Direct protein sequencing; Hydrolase; Protease;
KW   Thiol protease.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8439160"
FT   CHAIN           2..436
FT                   /note="Aminopeptidase C"
FT                   /id="PRO_0000050593"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        378
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   436 AA;  49827 MW;  1464F6A6E873FCA1 CRC64;
     MTVTSDFTQK LYENFAENTK LRAVENAVTK NGLLSSLEVR GSHAANLPEF SLDLTKDPVT
     NQKQSGRCWM FAALNTFRHK FINEFKTEDF EFSQAYTFFW DKYEKSNWFM EQIIGDVAMD
     DRRLKFLLQT PQQDGGQWDM MVAIFDKYGI VPKAVYPESQ ASSSSRELNQ YLNKLLRQDA
     EILRYTIEQD GDVQAVKEEL LQEVFNFLAV TLGLPPQNFE FAFRNKDNEY KKFVGTPKEF
     YNEYVGIDLN NYVSVINAPT ADKPYNKSYT VEFLGNVVGG KEVKHLNVEM DRFKKLAIAQ
     MQAGETVWFG CDVGQESNRS AGLLTMDSYD FKSSLDIEFT QSKAGRLDYG ESLMTHAMVL
     AGVDLDADGN STKWKVENSW GKDAGQKGYF VASDEWMDEY TYQIVVRKDL LSEEELAAYE
     AKPQVLLPWD PMGALA