COLA_VIBPA
ID COLA_VIBPA Reviewed; 816 AA.
AC Q56696;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Microbial collagenase;
DE EC=3.4.24.3;
DE AltName: Full=prtVp;
DE Flags: Precursor;
GN Name=prt; OrderedLocusNames=VPA0459;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-601, AND CHARACTERIZATION.
RC STRAIN=93;
RX PubMed=7582017; DOI=10.1099/13500872-141-10-2569;
RA Lee C., Su S., Liaw R.;
RT "Molecular analysis of an extracellular protease gene from Vibrio
RT parahaemolyticus.";
RL Microbiology 141:2569-2576(1995).
CC -!- FUNCTION: Possesses gelatinolytic activity. Can cause weak haemolysis
CC on blood agar.
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 -!- SIMILARITY: Belongs to the peptidase M9A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA86734.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BA000032; BAC61802.1; -; Genomic_DNA.
DR EMBL; Z46782; CAA86734.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; NP_799969.1; NC_004605.1.
DR RefSeq; WP_005479219.1; NC_004605.1.
DR AlphaFoldDB; Q56696; -.
DR SMR; Q56696; -.
DR STRING; 223926.28808625; -.
DR MEROPS; M09.004; -.
DR EnsemblBacteria; BAC61802; BAC61802; BAC61802.
DR GeneID; 1191147; -.
DR KEGG; vpa:VPA0459; -.
DR PATRIC; fig|223926.6.peg.3400; -.
DR eggNOG; COG4934; Bacteria.
DR HOGENOM; CLU_011878_0_0_6; -.
DR OMA; PLGSEHD; -.
DR BRENDA; 3.4.24.3; 15981.
DR Proteomes; UP000002493; 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 1: Evidence at protein level;
KW Collagen degradation; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..816
FT /note="Microbial collagenase"
FT /id="PRO_0000028679"
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 175
FT /note="M -> I (in Ref. 2; CAA86734)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..312
FT /note="KQ -> NE (in Ref. 2; CAA86734)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="T -> S (in Ref. 2; CAA86734)"
FT /evidence="ECO:0000305"
FT CONFLICT 542..543
FT /note="QQ -> HE (in Ref. 2; CAA86734)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="E -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 816 AA; 91444 MW; 25AB529725C6F6CB CRC64;
MSHIRFFPRH RLALACMLAS VSSFSFAQNQ CAVADLQQSR DLAAAVSGAE YDCYHAWFSA
PSATLNDIYS EASLSRIQVA LDQEIARYRG EAEQARVLEN LGEFVRAAYY VRYNAGTGTP
EFSEALSQRF AQSTNLFLNN PHALDQGREQ VGAMKSLTLM VDNVKQLPLT MDSMMAALMH
FNRDTAKDTQ WVDGLNNLFR SMAGHAANDA FYRYMANNTH HIDTLARFAS DNAWALDTDA
NFIVFNALRE TGRLLASPDQ ETKRKALAVM QQVMQRYPLG SEHDKLWLAA VEMMSYYAPE
GLNGLNLEQA KQDLAARVMP NRFECQGPAI IRSEDLTDAQ AAKACEVLAA KEADFHQVAN
TGNQPVADDL NDRVEVAVFA SNDSYVDYSS FLFGNTTDNG GQYLEGTPSR ADNTARFVAY
RYANGEDLSI LNLEHEYTHY LDARFNQYGS FSDNLAHGHI VWWLEGFAEY MHYKQGYKAA
IDLIPSGKLS LSTVFDTTYS HDSNRIYRWG YLAVRFMLEN HPQDVESLLA LSRSGQFAQW
AQQVTVLGQQ YDAEFERWLD TLEVVVEPEQ PGTDPEEPSE PTDPEVQVTE LAANQSLQLS
GEAYSEKLFY VDVPANTVRF NVSIEGAGDA DLYMSYNKVA HYYDFEMSQY ADGSNEEIQF
APEQNGYVKA GRYYISLTGR DSYDSVNLVA ALEVEAQTPP TQVQDDLAPV VLESGEAKVL
TVHQQRYAAV YVPEGVKEVR VWMSSQSNAN DPYGAGNVDL YASRKHWPTA EQHEYASNYA
GSNEYLAIPV TEAGYVHFSL QAPQQGDDVE MLVYFF
