ID   CLOS_HATHI              Reviewed;         526 AA.
AC   P09870; P09869;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 90.
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   Hathewaya histolytica (Clostridium histolyticum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX   NCBI_TaxID=1498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   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 is
RT   encoded by a single gene.";
RL   Mol. Gen. Genet. 240:140-145(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 51-181.
RX   PubMed=6391922; 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   PubMed=6337850; 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 thiol
RT   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:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, including Arg-|-Pro bond,
CC         but not Lys-|-Xaa.; EC=3.4.22.8;
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain held together
CC       by strong non-covalent forces rather than by intramolecular disulfide
CC       bridges.
CC   -!- SIMILARITY: Belongs to the peptidase C11 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="https://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   AlphaFoldDB; P09870; -.
DR   SMR; P09870; -.
DR   ChEMBL; CHEMBL5572; -.
DR   MEROPS; C11.001; -.
DR   PRIDE; P09870; -.
DR   KEGG; ag:CAA45212; -.
DR   BRENDA; 3.4.22.8; 1481.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR014173; Pept_C11_CLOspp.
DR   InterPro; IPR005077; Peptidase_C11.
DR   PANTHER; PTHR37835; PTHR37835; 1.
DR   Pfam; PF03415; Peptidase_C11; 1.
DR   TIGRFAMs; TIGR02806; clostrip; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..50
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028511"
FT   CHAIN           51..181
FT                   /note="Clostripain light chain"
FT                   /id="PRO_0000028512"
FT   PROPEP          182..190
FT                   /note="Linker"
FT                   /id="PRO_0000028513"
FT   CHAIN           191..526
FT                   /note="Clostripain heavy chain"
FT                   /id="PRO_0000028514"
FT   ACT_SITE        231
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        127
FT                   /note="R -> NQL (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176..179
FT                   /note="HGGG -> GDGH (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="S -> H (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213
FT                   /note="I -> L (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="H -> T (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="L -> M (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
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