Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it provides nearly 100-fold protection against phages T5 and T6 and about 8-fold against phage T4. The operon without bGSDM no longer protects against phage (PubMed:35025633). Cleavage of this precursor by its dedicated protease(s) releases the active moiety (gasdermin bGSDM, N-terminus) which inserts into membranes, forming pores and triggering cell death (By similarity). Pore-forming protein that causes membrane permeabilization via a pyroptosis-like activity. Makes ring-like pores when released. The full-length protein before cleavage is inactive: intramolecular interactions between the N-terminal domain and the C-terminal region as well as the lipid modification, mediate autoinhibition. The pyroptosis-like-inducing activity is carried by the released N-terminal domain (Gasdermin bGSDM, N-terminus). Monomer. Forms large, probably homooligomeric ring-shaped pores when inserted in membranes. The N-terminus has marked structural similarity to the mammalian gasdermin N-terminal domain. The C-terminal region wraps around the twisted beta sheet core, probably stabilizing the inactive state. Palmitoylation helps stabilize the inactive state; may self palmitoylate. When deleted from its operon, no longer protects E.coli against bacteriophages T4, T5 or T6. Belongs to the bacterial gasdermin family.