UniProt functional annotation for Q9KMU6



	UniProt functional annotation for Q9KMU6

UniProt code: Q9KMU6.

Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.

Function: Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen. {ECO:0000269|PubMed:18479458, ECO:0000269|PubMed:24492010, ECO:0000305|PubMed:9371455}.

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:24492010};

Activity regulation: Calcium plays an important structural role, providing stability to this protein in the cytoplasm. Outside the cell, the decrease of the calcium concentration triggers the autoproteolysis. PrtV activity is increased by 25 mM of Sr(2+) or Mg(2+) and to some extent by Ba(2+); however, Ba(2+) inhibits PrtV at higher concentrations. Completely inhibited by EDTA and 1,10-phenanthroline. {ECO:0000269|PubMed:18479458}.

Subcellular location: Secreted {ECO:0000269|PubMed:18479458}.

Ptm: PrtV is expressed as an inactive, multidomain, 102 kDa pre-pro- metalloprotease. To form a catalytically active protease, PrtV is first secreted, and then it undergoes N- and C-terminal cleavages during envelope translocation to yield a 81 kDa pro-metalloprotease. Outside the cell, the 81 kDa pro-metalloprotease undergoes an auto-cleavage. The two major products of autoproteolysis (37 kDa and 18 kDa) together form the so called 55 kDa active complex. {ECO:0000269|PubMed:18479458, ECO:0000269|PubMed:24492010}.

Similarity: Belongs to the peptidase M6 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.



Function:		Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen. {ECO:0000269\|PubMed:18479458, ECO:0000269\|PubMed:24492010, ECO:0000305\|PubMed:9371455}.


Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305\|PubMed:24492010};
Activity regulation:		Calcium plays an important structural role, providing stability to this protein in the cytoplasm. Outside the cell, the decrease of the calcium concentration triggers the autoproteolysis. PrtV activity is increased by 25 mM of Sr(2+) or Mg(2+) and to some extent by Ba(2+); however, Ba(2+) inhibits PrtV at higher concentrations. Completely inhibited by EDTA and 1,10-phenanthroline. {ECO:0000269\|PubMed:18479458}.
Subcellular location:		Secreted {ECO:0000269\|PubMed:18479458}.
Ptm:		PrtV is expressed as an inactive, multidomain, 102 kDa pre-pro- metalloprotease. To form a catalytically active protease, PrtV is first secreted, and then it undergoes N- and C-terminal cleavages during envelope translocation to yield a 81 kDa pro-metalloprotease. Outside the cell, the 81 kDa pro-metalloprotease undergoes an auto-cleavage. The two major products of autoproteolysis (37 kDa and 18 kDa) together form the so called 55 kDa active complex. {ECO:0000269\|PubMed:18479458, ECO:0000269\|PubMed:24492010}.
Similarity:		Belongs to the peptidase M6 family. {ECO:0000305}.