ID   CLOS_CLOHI              Reviewed;         526 AA.
AC   P09870; P09869;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   05-MAY-2009, entry version 56.
DE   RecName: Full=Clostripain;
DE            EC=3.4.22.8;
DE   AltName: Full=Clostridiopeptidase B;
DE   Contains:
DE     RecName: Full=Clostripain light chain;
DE   Contains:
DE     RecName: Full=Clostripain heavy chain;
DE   Flags: Precursor;
GN   Name=cloSI;
OS   Clostridium histolyticum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93341452; PubMed=8341259; DOI=10.1007/BF00276893;
RA   Dargatz H., Diefenthal T., Witte V., Reipen G., von Wettstein D.;
RT   "The heterodimeric protease clostripain from Clostridium histolyticum
RT   is encoded by a single gene.";
RL   Mol. Gen. Genet. 240:140-145(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 51-181.
RX   MEDLINE=85076641; PubMed=6391922;
RX   DOI=10.1111/j.1432-1033.1984.tb08579.x;
RA   Gilles A.M., Lecroisey A., Keil B.;
RT   "Primary structure of alpha-clostripain light chain.";
RL   Eur. J. Biochem. 145:469-476(1984).
RN   [3]
RP   PRELIMINARY PROTEIN SEQUENCE OF 51-73 AND 191-232.
RX   MEDLINE=83131688; PubMed=6337850;
RX   DOI=10.1111/j.1432-1033.1983.tb07174.x;
RA   Gilles A.M., de Wolf A., Keil B.;
RT   "Amino-acid sequences of the active-site sulfhydryl peptide and other
RT   thiol peptides from the cysteine proteinase alpha-clostripain.";
RL   Eur. J. Biochem. 130:473-479(1983).
CC   -!- FUNCTION: Cysteine endopeptidase with strict specificity.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, including
CC       Arg-|-Pro bond, but not Lys-|-Xaa.
CC   -!- SUBUNIT: Heterodimer of a light chain and an heavy chain held
CC       together by strong noncovalent forces rather than by
CC       intramolecular disulfide bridges.
CC   -!- SIMILARITY: Belongs to the peptidase C11 family.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="http://www.worthington-biochem.com/CP/";
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DR   EMBL; X63673; CAA45212.1; -; Genomic_DNA.
DR   PIR; A29174; A29174.
DR   PIR; A29175; A29175.
DR   PIR; B29175; B29175.
DR   PIR; S35190; S35190.
DR   MEROPS; C11.001; -.
DR   BRENDA; 3.4.22.8; 39549.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR014173; Pept_C11_CLOspp.
DR   InterPro; IPR005077; Peptidase_C11.
DR   Pfam; PF03415; Peptidase_C11; 1.
DR   TIGRFAMs; TIGR02806; clostrip; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL        1     27       Potential.
FT   PROPEP       28     50       Potential.
FT                                /FTId=PRO_0000028511.
FT   CHAIN        51    181       Clostripain light chain.
FT                                /FTId=PRO_0000028512.
FT   PROPEP      182    190       Linker.
FT                                /FTId=PRO_0000028513.
FT   CHAIN       191    526       Clostripain heavy chain.
FT                                /FTId=PRO_0000028514.
FT   ACT_SITE    231    231
FT   CONFLICT    127    127       R -> NQL (in Ref. 2; AA sequence).
FT   CONFLICT    176    179       HGGG -> GDGH (in Ref. 2; AA sequence).
FT   CONFLICT    197    197       S -> H (in Ref. 3; AA sequence).
FT   CONFLICT    213    213       I -> L (in Ref. 3; AA sequence).
FT   CONFLICT    216    216       H -> T (in Ref. 3; AA sequence).
FT   CONFLICT    232    232       L -> M (in Ref. 3; AA sequence).
SQ   SEQUENCE   526 AA;  59733 MW;  E151372FF6C95BE7 CRC64;
     MLRRKVSTLL MTALITTSFL NSKPVYANPV TKSKDNNLKE VQQVTSKSNK NKNQKVTIMY
     YCDADNNLEG SLLNDIEEMK TGYKDSPNLN LIALVDRSPR YSSDEKVLGE DFSDTRLYKI
     EHNKANRLDG KNEFPEISTT SKYEANMGDP EVLKKFIDYC KSNYEADKYV LIMANHGGGA
     REKSNPRLNR AICWDDSNLD KNGEADCLYM GEISDHLTEK QSVDLLAFDA CLMGTAEVAY
     QYRPGNGGFS ADTLVASSPV VWGPGFKYDK IFDRIKAGGG TNNEDDLTLG GKEQNFDPAT
     ITNEQLGALF VEEQRDSTHA NGRYDQHLSF YDLKKAESVK RAIDNLAVNL SNENKKSEIE
     KLRGSGIHTD LMHYFDEYSE GEWVEYPYFD VYDLCEKINK SENFSSKTKD LASNAMNKLN
     EMIVYSFGDP SNNFKEGKNG LSIFLPNGDK KYSTYYTSTK IPHWTMQSWY NSIDTVKYGL
     NPYGKLSWCK DGQDPEINKV GNWFELLDSW FDKTNDVTGG VNHYQW
//