Glutamyl endopeptidase preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. It is required for proteolytic maturation of thiol protease sspB and inactivation of sspC, an inhibitor of sspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. It may also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. It may be involved in the stability of secreted lipases.