ID B2TJU5_CLOBB Unreviewed; 1235 AA.
AC B2TJU5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
DE AltName: Full=Microbial collagenase {ECO:0000256|ARBA:ARBA00034362};
GN Name=colG {ECO:0000313|EMBL:ACD21898.1};
GN OrderedLocusNames=CLL_A1484 {ECO:0000313|EMBL:ACD21898.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD21898.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000424};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M9B family. Collagenase subfamily.
CC {ECO:0000256|ARBA:ARBA00034318}.
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DR EMBL; CP001056; ACD21898.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TJU5; -.
DR MEROPS; M09.005; -.
DR KEGG; cbk:CLL_A1484; -.
DR HOGENOM; CLU_012279_0_0_9; -.
DR Proteomes; UP000001195; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 1.10.390.20; -; 1.
DR Gene3D; 2.60.120.380; -; 3.
DR Gene3D; 3.30.980.50; -; 1.
DR Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR041379; ColG_subdomain.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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 PANTHER; PTHR13062:SF9; A2M DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13062; COLLAGENASE; 1.
DR Pfam; PF18496; ColG_sub; 1.
DR Pfam; PF01752; Peptidase_M9; 1.
DR Pfam; PF08453; Peptidase_M9_N; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF04151; PPC; 3.
DR PRINTS; PR00931; MICOLLPTASE.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF89260; Collagen-binding domain; 3.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACD21898.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1235
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002780524"
FT DOMAIN 751..819
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 955..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..990
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 481
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 1235 AA; 140439 MW; 795ADF97905B924D CRC64;
MKKRLFTVLC TLALSFSLST ECFASISSST ENLNKIYSSK SYSVDEVNTE QNNGNLKEDV
AHASYEETNE TFPFKKLNKL SNEEIIELSS KISWKDIPDL FKYNEDTYEF YSNESRVQAM
IDGLYQKACS FTSTDDNGID TLVELLRSGF YLGFYNDSLN YLKDRTFTDR CIPALIAMEN
NPNFKLGEAG QDKVVLAFGK LIGNASCNPE VVNKSVSILN QYYDEVNQYP TDKLKADAVL
KVMSEVTYDI NQYCYDNNIG DGKNTPWTGK IDNFITAVSK FASISEITDD NGWLINNGIY
YTAKLAKYHS NPSTPHKVLD NCLKTLPSTS EQYITTLDLL KSDFDSKDSN GNNIDIDNII
EDKKNTFLPK TYTFDDGKMI IKAGDKVSES KIQRLYWASK EVKSQFHRII GSDEPLETGA
ADDVLTMVIY NNPKEYKLNR TLYGYSVDNG GIYIENIGTF FTYERTPKDS IFSLEELFRH
EFTHYLQGRY LVPGLFNQGD FYQGNNARLT WFEEGSAEFF AGSTRTTVLP RKSMVSAIGQ
NEEERLSANS LFHSSYSDGW NFYNYGYTFT DYMYNSNRNL FKDLVDSMKS NDVQGYDSII
ESSSNDANLN KKYQKHMDKL VDNYNNYTIP LVSDDYMKKC GNKNLEVIKK DIENAMGLNN
SEIVKESSDY FNTYTLKGTY KLDSNNGEFN NWSLMNERVN NTLETLNKLP WNGYKTVTGY
FINPRINSSN EVEYDVVFHG LLYHNDNFNE EPVITLMAPE QGNTGEKIKF TSECSTDDSN
LSYLWDFGDG NTTTEKNPIH IYKTSDNYTV KLTVTDSNGF ELEKYSEISI HKVLTGNPVC
EKEDNNRFEN ANEINLNDLV SGDLQADDSQ DTFSFEVTKP DDITITLENN SQDKNSFNWL
LFDAENTNDY FAFPETKMNQ LSKTVSIDKP GKYYLVVYQN SKEKTDYKFV VDGSFVETPE
VDPDEDTDET PTETPDTDED NNKDEDSNYD NINVDEEEYN DDFECANNIF KNQIMSGNLD
SSDKCDTFSF NALSAGTINV TLENSNSDSS TVNWLAYSSE DTDNYIGYAS ENDGNKFSGK
FKVNKPGKYY IVAYEVNGAD SKYKLKVDGD IENTSESKPE DKEEIKEEIN DDSFDSATKI
KANSTITDTL NGEDNKDICY FNVNNNSDLN IELNSLTNLG VAWQLFSEED LDNYIAYGSQ
SGDSIVGTAN VQPGKYYLLI YKYTQADGSY TFTIK
//
