COLA_CLOPE
ID COLA_CLOPE Reviewed; 1104 AA.
AC P43153;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Collagenase ColA {ECO:0000303|PubMed:9922257};
DE EC=3.4.24.3;
DE AltName: Full=120 kDa collagenase;
DE AltName: Full=Microbial collagenase;
DE Flags: Precursor;
GN Name=colA; OrderedLocusNames=CPE0173;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 87-113, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 3628 / NCIMB 10662 / Type C;
RX PubMed=8282691; DOI=10.1128/jb.176.1.149-156.1994;
RA Matsushita O., Yoshihara K., Katayama S., Minami J., Okabe A.;
RT "Purification and characterization of Clostridium perfringens 120-
RT kilodalton collagenase and nucleotide sequence of the corresponding gene.";
RL J. Bacteriol. 176:149-156(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1073-1104.
RC STRAIN=ATCC 3628 / NCIMB 10662 / Type C;
RA Matsushita O.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DISCUSSION OF SEQUENCE, AND DOMAIN.
RX PubMed=9922257; DOI=10.1128/jb.181.3.923-933.1999;
RA Matsushita O., Jung C.-M., Katayama S., Minami J., Takahashi Y., Okabe A.;
RT "Gene duplication and multiplicity of collagenases in Clostridium
RT histolyticum.";
RL J. Bacteriol. 181:923-933(1999).
CC -!- FUNCTION: Clostridial collagenases are among the most efficient
CC degraders of eukaryotic collagen known; saprophytes use collagen as a
CC carbon source while pathogens additionally digest collagen to aid in
CC host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and
CC endopeptidase activities; the endopeptidase cuts within the triple
CC helix region of collagen while tripeptidylcarboxypeptidase successively
CC digests the exposed ends, thus clostridial collagenases can digest
CC large sections of collagen (By similarity).
CC {ECO:0000250|UniProtKB:Q899Y1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Digestion of native collagen in the triple helical region at
CC Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for
CC Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala
CC or Arg at P3'.; EC=3.4.24.3; Evidence={ECO:0000250|UniProtKB:Q899Y1};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q899Y1};
CC Note=Binds about 6 Ca(2+) per subunit (Probable). The metallopeptidase
CC and PKD domains bind 1 Ca(2+), while CDB binds 2 (Probable).
CC {ECO:0000250|UniProtKB:Q899Y1, ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q899Y1};
CC Note=Binds 1 zinc ion. {ECO:0000250|UniProtKB:Q899Y1};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8282691}.
CC -!- DOMAIN: The mature protein has 4 domains; a metalloprotease domain (S1,
CC approximately residues 87-761), S2 (762-860, equivalent to PKD), and 2
CC collagen-binding domains S3a (865-979) and S3b (992-1104)
CC (PubMed:9922257). The metalloprotease S1 domain is composed of 3
CC subdomains which together resemble a saddle; an activator domain
CC (residues 93-367), the catalytic peptidase subdomain (377-646) and a
CC helper subdomain (654-767) (By similarity).
CC {ECO:0000250|UniProtKB:Q899Y1, ECO:0000305|PubMed:9922257}.
CC -!- MISCELLANEOUS: Clostridial collagenases enable the bacteria to
CC infiltrate and colonize host tissue, and contribute to gas gangrene
CC (myonecrosis) pathogenesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M9B family. Collagenase subfamily.
CC {ECO:0000305}.
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DR EMBL; D13791; BAA02941.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB79879.1; -; Genomic_DNA.
DR EMBL; D50309; BAA08848.1; -; Genomic_DNA.
DR PIR; A36866; A36866.
DR RefSeq; WP_011009653.1; NC_003366.1.
DR AlphaFoldDB; P43153; -.
DR SMR; P43153; -.
DR STRING; 195102.gene:10489417; -.
DR BindingDB; P43153; -.
DR ChEMBL; CHEMBL2802; -.
DR MEROPS; M09.005; -.
DR PRIDE; P43153; -.
DR EnsemblBacteria; BAB79879; BAB79879; BAB79879.
DR KEGG; cpe:CPE0173; -.
DR HOGENOM; CLU_012279_0_0_9; -.
DR OMA; YEREGSY; -.
DR BRENDA; 3.4.24.3; 1503.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR041379; ColG_subdomain.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013661; Peptidase_M9_N_dom.
DR InterPro; IPR002169; Peptidase_M9A/M9B.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR Pfam; PF18496; ColG_sub; 1.
DR Pfam; PF01752; Peptidase_M9; 1.
DR Pfam; PF08453; Peptidase_M9_N; 1.
DR PRINTS; PR00931; MICOLLPTASE.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49299; SSF49299; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Virulence; Zinc; Zymogen.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT PROPEP 40..86
FT /evidence="ECO:0000305|PubMed:8282691"
FT /id="PRO_0000028674"
FT CHAIN 87..1104
FT /note="Collagenase ColA"
FT /id="PRO_0000028675"
FT DOMAIN 774..862
FT /note="PKD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT REGION 87..761
FT /note="S1 metalloprotease domain"
FT /evidence="ECO:0000305|PubMed:9922257"
FT REGION 93..367
FT /note="Activator domain"
FT /evidence="ECO:0000250|UniProtKB:Q899Y1"
FT REGION 377..646
FT /note="Catalytic subdomain"
FT /evidence="ECO:0000250|UniProtKB:Q899Y1"
FT REGION 654..767
FT /note="Helper subdomain"
FT /evidence="ECO:0000250|UniProtKB:Q899Y1"
FT REGION 762..860
FT /note="S2 domain"
FT /evidence="ECO:0000305|PubMed:9922257"
FT REGION 865..979
FT /note="S3a collagen-binding domain"
FT /evidence="ECO:0000305|PubMed:9922257"
FT REGION 992..1104
FT /note="S3b collagen-binding domain"
FT /evidence="ECO:0000305|PubMed:9922257"
FT ACT_SITE 503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 477
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q899Y1"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9X721,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9X721,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q899Y1"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q899Y1"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q899Y1"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 772
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 773
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 802
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 841
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 866
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 868
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 868
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 870
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 894
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 894
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 897
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 897
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 993
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 995
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 995
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 997
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 1016
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 1020
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 1020
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 1022
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 1023
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT BINDING 1023
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9X721"
FT CONFLICT 38
FT /note="L -> F (in Ref. 1; BAA02941)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="I -> M (in Ref. 1; BAA02941)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="G -> E (in Ref. 1; BAA02941)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="V -> E (in Ref. 1; BAA02941)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="T -> A (in Ref. 1; BAA02941)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="A -> E (in Ref. 1; BAA02941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1098
FT /note="I -> T (in Ref. 1; BAA02941 and 3; BAA08848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1104 AA; 125936 MW; F4B7377194ED021C CRC64;
MKKNLKRGEL TKLKLVERWS ATFTLAAFIL FNSSFKVLAA DKKVENSNNG QITREINADQ
ISKTELNNEV ATDNNRPLGP SIAPSRARNN KIYTFDELNR MNYSDLVELI KTISYENVPD
LFNFNDGSYT FFSNRDRVQA IIYGLEDSGR TYTADDDKGI PTLVEFLRAG YYLGFYNKQL
SYLNTPQLKN ECLPAMKAIQ YNSNFRLGTK AQDGVVEALG RLIGNASADP EVINNCIYVL
SDFKDNIDKY GSNYSKGNAV FNLMKGIDYY TNSVIYNTKG YDAKNTEFYN RIDPYMERLE
SLCTIGDKLN NDNAWLVNNA LYYTGRMGKF REDPSISQRA LERAMKEYPY LSYQYIEAAN
DLDLNFGGKN SSGNDIDFNK IKADAREKYL PKTYTFDDGK FVVKAGDKVT EEKIKRLYWA
SKEVKAQFMR VVQNDKALEE GNPDDILTVV IYNSPEEYKL NRIINGFSTD NGGIYIENIG
TFFTYERTPE ESIYTLEELF RHEFTHYLQG RYVVPGMWGQ GEFYQEGVLT WYEEGTAEFF
AGSTRTDGIK PRKSVTQGLA YDRNNRMSLY GVLHAKYGSW DFYNYGFALS NYMYNNNMGM
FNKMTNYIKN NDVSGYKDYI ASMSSDYGLN DKYQDYMDSL LNNIDNLDVP LVSDEYVNGH
EAKDINEITN DIKEVSNIKD LSSNVEKSQF FTTYDMRGTY VGGRSQGEEN DWKDMNSKLN
DILKELSKKS WNGYKTVTAY FVNHKVDGNG NYVYDVVFHG MNTDTNTDVH VNKEPKAVIK
SDSSVIVEEE INFDGTESKD EDGEIKAYEW DFGDGEKSNE AKATHKYNKT GEYEVKLTVT
DNNGGINTES KKIKVVEDKP VEVINESEPN NDFEKANQIA KSNMLVKGTL SEEDYSDKYY
FDVAKKGNVK ITLNNLNSVG ITWTLYKEGD LNNYVLYATG NDGTVLKGEK TLEPGRYYLS
VYTYDNQSGT YTVNVKGNLK NEVKETAKDA IKEVENNNDF DKAMKVDSNS KIVGTLSNDD
LKDIYSIDIQ NPSDLNIVVE NLDNIKMNWL LYSADDLSNY VDYANADGNK LSNTCKLNPG
KYYLCVYQFE NSGTGNYIVN LQNK
