ID   COLA_VIBVU              Reviewed;         807 AA.
AC   Q8D4Y9;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Microbial collagenase;
DE            EC=3.4.24.3;
DE   Flags: Precursor;
GN   OrderedLocusNames=VV2_1146;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possesses gelatinolytic activity. {ECO:0000250}.
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; AE016796; AAO08047.1; -; Genomic_DNA.
DR   RefSeq; WP_011082042.1; NC_004460.2.
DR   AlphaFoldDB; Q8D4Y9; -.
DR   SMR; Q8D4Y9; -.
DR   MEROPS; M09.004; -.
DR   EnsemblBacteria; AAO08047; AAO08047; VV2_1146.
DR   KEGG; vvu:VV2_1146; -.
DR   HOGENOM; CLU_011878_0_0_6; -.
DR   OMA; PLGSEHD; -.
DR   Proteomes; UP000002275; Chromosome 2.
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   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..807
FT                   /note="Microbial collagenase"
FT                   /id="PRO_0000028680"
FT   REGION          562..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   807 AA;  90009 MW;  B597201DE4C6A466 CRC64;
     MSHLLPFPRR RLALACLLAS ISGASFGQTQ CDVAQLQQSP DLATAISSAD YACYSGWFSA
     SSDTLNNIYS EASLSRVQVA LHQAVQTYQG EAEQARAIEN LGEYVRAAYY VRYNAGNVAA
     FSDLLGQQFA HTINAFLANP HALDQGREQV GAMKSLTLMV DNIKQLPLTM DAMMLALQQF
     NPETAKNTQW VDGLNNLFRS MAGHIANDAF YRYLASNTQH IDMLEKFAND NAWALDTDAD
     FLVFNALRET GRLIASPDKA TKQKAVQVMQ RVMARYPLGS EHDKLWLAAV EMLSYFAPEA
     LNGLDLPQAK RDLAARVLPN RHECQGPAII RSQDLTPEQA AKACDVLAAK EADFHQVANT
     GMQPVADDHN QRVEVAVFAN NDSYVDYSAF LFGNTTDNGG QYLEGNPADE HNTARFVAYR
     YANGEELSIL NLEHEYTHYL DARFNQYGSF SDNLAHGYVV WWLEGFAEYM HYKQGYQAAI
     ELIAQGKMSL SQVFATSYSH DTNRIYRWGY LAVRFMLENH PQEVEGLLAL SRSGQFEQWA
     QQVQTLGQQY DGEFARWLDG LEVTPENPDT DPDTPTEPSD GVTQLQANQS ITLSGKAYSE
     KLFYVDVPAN TTHFSVAIEG DGDADLYMSY NQVAHYYDFE VSKFVDGSNE EIQFAADASG
     YVKPGRYYLS VTGRGRYQAV NLTATIDTAA PTPPTQEQDD LAPVMLQSGQ AQHLTVHQQR
     YAAVYVPEGV SEVRIWLSDL TSSDSQGNVN LYASREHWPT PEQHQFASRY AGSNQYLAIP
     VEQAGYLHFS LNAPQQGDDV EMVVYFH