EC Number |
Natural Substrates |
---|
3.4.23.49 | alpha2-antiplasmin + H2O |
inactivation |
3.4.23.49 | cationic antimicrobial peptides from epithelial cells or macrophages + H2O |
- |
3.4.23.49 | cationic antimicrobial peptides from epithelial cells or macrophages + H2O |
OmpT, proteolytic degradation |
3.4.23.49 | ColE2-Im2 protein complex + H2O |
a small amount of the endonuclease colicin E2 associated with the cognate immunity protein Im2, is susceptible to proteolytic cleavage by omptin. The presence of outer membrane protein BtuB is required for ColE-Im2 cleavage by omptin. The amount of colicin cleaved is greatly enhanced when ColE2 is dissociated from Im2. Omptin cleaves the C-terminal DNase domain of the toxin. Strains that over-produce OmpT are less susceptible to infection by ColE2 than by ColE2-Im2 |
3.4.23.49 | colicin E1 + H2O |
function in degradation of colicin at the cell surface to protect sensitive cells from infection by colicins suggested |
3.4.23.49 | factor B + H2O |
- |
3.4.23.49 | factor H + H2O |
- |
3.4.23.49 | factor H + H2O |
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis |
3.4.23.49 | gelatine + H2O |
degradation |
3.4.23.49 | human antiprotease alpha2-antiplasmin + H2O |
involved in infection and pathogenesis |