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. 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 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. Belongs to the peptidase M6 family.