gelE
Function
Metalloprotease capable of the hydrolysis of insoluble hydrophobic substrates. Hydrolyzes azocoll and gelatin and, at a lower rate, soluble and insoluble collagens. Does not cleave short synthetic peptides. Preferentially hydrolyzes the 24-Phe-|-Phe-25 bond in the insulin B-chain, followed by the 5-His-|-Leu-6 bond. Inactivates endothelin-1, primarily by cleavage of the 5-Ser-|-Leu-6 and 16-His-|-Leu-17 bonds. Hydrolyzes the alpha chain of C3 to generate a C3b-like protein. Inhibits complement-mediated hemolysis and opsinization of bacteria. Hydrolyzes the insect antimicrobial peptide cecropin. Decreases the length of E.faecalis chains via the activation of autolysin. Degrades polymerized fibrin.
Sequence Similarities
Belongs to the peptidase M4 family.
Cellular localization
- Secreted
Alternative names
EF_1818, gelE, Gelatinase, Coccolysin