ID   COLA_VIBAL              Reviewed;         814 AA.
AC   P43154;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Microbial collagenase;
DE            EC=3.4.24.3;
DE   Flags: Precursor;
OS   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Chemovar. Iophagus;
RX   PubMed=1311172; DOI=10.1042/bj2810703;
RA   Takeuchi H., Shibano Y., Morihara K., Fukushima J., Inami S., Keil B.,
RA   Gilles A.-M., Kawamoto S., Okuda K.;
RT   "Structural gene and complete amino acid sequence of Vibrio alginolyticus
RT   collagenase.";
RL   Biochem. J. 281:703-708(1992).
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.
CC   -!- PTM: Proteolytic cleavage might yield three different active forms.
CC   -!- SIMILARITY: Belongs to the peptidase M9A family. {ECO:0000305}.
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DR   EMBL; X62635; CAA44501.1; -; Genomic_DNA.
DR   PIR; S19658; S19658.
DR   AlphaFoldDB; P43154; -.
DR   SMR; P43154; -.
DR   STRING; 663.BAU10_05955; -.
DR   MEROPS; M09.001; -.
DR   PRIDE; P43154; -.
DR   eggNOG; COG3291; Bacteria.
DR   BRENDA; 3.4.24.3; 6624.
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   Gene3D; 2.60.40.10; -; 1.
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; 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   Collagen degradation; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..75
FT                   /id="PRO_0000028676"
FT   CHAIN           76..814
FT                   /note="Microbial collagenase"
FT                   /id="PRO_0000028677"
FT   DOMAIN          609..697
FT                   /note="PKD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT   ACT_SITE        478
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         477
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         481
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   814 AA;  89963 MW;  E0E19C0884D2185E CRC64;
     MELKILSVAI ATTLTSTGVF ALSEPVSQVT EQHAHSAHTH GVEFNRVEYQ PTATLPIQPS
     KATRVQSLES LDESSTACDL EALVTESSNQ LISEILSQGA TCVNQLFSAE SRIQESVFSS
     DHMYNIAKHT TTLAKGYTGG GSDELETLFL YLRAGYYAEF YNDNISFIEW VTPAVKESVD
     AFVNTASFYE NSDRHGKVLS EVIITMDSAG LQHAYLPQVT QWLTRWNDQY AQHWYMRNAV
     NGVFTILFGG QWNEQFVQII GNQTDLAKAL GDFALRASSI GAEDEFMAAN AGRELGRLTK
     YTGNASSVVK SQLSRIFEQY EMYGRGDAVW LAAADTASYY ADCSEFGICN FETELKGLVL
     SQTYTCSPTI RILSQNMTQE QHAAACSKMG YEEGYFHQSL ETGEQPVKDD HNTQLQVNIF
     DSSTDYGKYA GPIFDISTDN GGMYLEGDPS QPGNIPNFIA YEASYANADH FVWNLEHEYV
     HYLDGRFDLY GGFSHPTEKI VWWSEGIAEY VAQENDNQAA LETILDGSTY TLSEIFETTY
     DGFDVDRIYR WGYLAVRFMF ENHKDDVNQM LVETRQGNWI NYKATITQWA NLYQSEFEQW
     QQTLVSNGAP NAVITANSKG KVGESITFSS ENSTDPNGKI VSVLWDFGDG STSTQTKPTH
     QYGSEGEYSV SLSVTDSEGL TATATHTVVI SALGGNDTLP QDCAVQSKVS GGRLTAGEPV
     CLANQQTIWL SVPAVNESSN LAITTGNGTG NLKLEYSNSG WPDDTNLHGW SDNIGNGECI
     TLSNQSNYWG YVKVSGDFEN AAIVVDFDAQ KCRQ