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   20-JAN-2009, entry version 58.
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; Lactobacillales; Streptococcaceae; Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=AM2;
RX   MEDLINE=93175873; PubMed=8439160;
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   MEDLINE=98207691; 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
CC       as di- and tripeptides in which the half-cystine residue is
CC       involved in a disulfide loop, notably in oxytocin and vasopressin.
CC       Has also a bleomycin hydrolase activity.
CC   -!- CATALYTIC ACTIVITY: Inactivates bleomycin B2 (a cytotoxic
CC       glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-
CC       aminoalanine, but also shows general aminopeptidase activity. The
CC       specificity varies somewhat with source, but amino acid arylamides
CC       of Met, Leu and Ala are preferred.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
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DR   EMBL; M86245; AAA74514.1; -; Genomic_DNA.
DR   PIR; B48957; B48957.
DR   HSSP; Q13867; 1CB5.
DR   MEROPS; C01.086; -.
DR   BRENDA; 3.4.22.40; 289716.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR004134; Peptidase_C1B.
DR   PANTHER; PTHR10363; Peptidase_C1B; 1.
DR   Pfam; PF03051; Peptidase_C1_2; 1.
DR   PIRSF; PIRSF005700; PepC; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; FALSE_NEG.
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      1       Removed.
FT   CHAIN         2    436       Aminopeptidase C.
FT                                /FTId=PRO_0000050593.
FT   ACT_SITE     68     68       By similarity.
FT   ACT_SITE    356    356       By similarity.
FT   ACT_SITE    378    378       By similarity.
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
//