Is responsible for site-2 cleavage of the RsiW anti-sigma factor (PubMed:15130127). This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (PubMed:16899079). Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane (PubMed:21810987). No cleavage of signal peptides. Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this enzyme), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein. Belongs to the peptidase M50B family.