COLA_VIBCH
ID COLA_VIBCH Reviewed; 818 AA.
AC Q9KRJ0; Q9X4F8;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Microbial collagenase;
DE EC=3.4.24.3;
DE AltName: Full=Exoprotease Vcc;
DE Flags: Precursor;
GN Name=vcc; OrderedLocusNames=VC_1650;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RA McKenzie R.;
RT "Novel exoprotease gene vcc in Vibrio cholerae.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Possesses gelatinolytic activity.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M9A family. {ECO:0000305}.
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DR EMBL; AF109145; AAD20592.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF94801.1; -; Genomic_DNA.
DR PIR; F82173; F82173.
DR RefSeq; NP_231287.1; NC_002505.1.
DR RefSeq; WP_000009926.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KRJ0; -.
DR SMR; Q9KRJ0; -.
DR STRING; 243277.VC_1650; -.
DR MEROPS; M09.004; -.
DR EnsemblBacteria; AAF94801; AAF94801; VC_1650.
DR KEGG; vch:VC_1650; -.
DR PATRIC; fig|243277.26.peg.1577; -.
DR eggNOG; COG4934; Bacteria.
DR HOGENOM; CLU_011878_0_0_6; -.
DR OMA; PLGSEHD; -.
DR BioCyc; VCHO:VC1650-MON; -.
DR BRENDA; 3.4.24.3; 15862.
DR Proteomes; UP000000584; Chromosome 1.
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:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR013661; Peptidase_M9_N_dom.
DR InterPro; IPR002169; Peptidase_M9A/M9B.
DR Pfam; PF01752; Peptidase_M9; 1.
DR Pfam; PF08453; Peptidase_M9_N; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00931; MICOLLPTASE.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Collagen degradation; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..818
FT /note="Microbial collagenase"
FT /id="PRO_0000028678"
FT REGION 562..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CONFLICT 574..585
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="P -> L (in Ref. 1; AAD20592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 818 AA; 92997 MW; D71F97018C4FE30D CRC64;
MSFQQRIQHH PIAWACVIAG LSYSSYSQAA CEIQDLQPAR DLPAQIAVAT QACYNSWFYA
PTATLDNLYS EASLAHLQTV LDAEIARYTG EAQQARRLEN YGEFIRAAYY VRYNAGREPY
SQALSQRFAQ SIDRFLRHPH AFDQGREQVG AMKSLSLMVD NVKQLPLTMD AMILALHRFN
RETAQDTQWV DGLNNLFRAM SGHVGNSEFY RYLAANTQHI DTLYRFALDN EWALETDAEF
LVYNALRETG RLLISPDAIT KQKARHVMRQ VIARYPLGSK HDKLWLAAVE MLHYYAPEVL
QQLGIDLDAA KRDLAARILP NRFECQGPAI IRSQDLSDAQ AAQACDVLDK KEQDFHQVAN
TGLAPVADDY NTRVEVVVFA NNSSYVNYSS FLFGNTTDNG GQYLEGNPAD QNNQARFVAY
RYANDADLSI LNLEHEYTHY LDARFNQYGS FSDNLAHGHI VWWLEGFAEY MHYKQGYQAA
VKLISQGKLS LSDVFATTYS NDTNRIYRWG YLAVRFMLEK HPQDVESLLA LSRTGQFDQW
AQSVKLLGER YNTEFSAWLD TLQRDNPDNP DNPDNPDNPD NPDNPEQPNP EPNAVTQLAA
NSSLTLTGKA YSEHLFYVDV PEYSREFHVQ ISGEGDADLY MSYQQVAHYY DYQVTEFTYG
SNEQITFKPE QNGYIKPGRY YLSVTGRADY SAVILNTHLV TEQPNEQPTI KDDLAPVLLE
AGNSQSLTVH RQRYVAIYVP KGVSEVQVWL TASEQNRGNV DLFAAKAYWP TREQFEHAST
GAGSHEYLRI PVTQEGYVHF SLNAQQLGDT VEMVAYFD
