Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Expression of bGSDM and the neighboring protease gene (Ga0334635_1659) is toxic in E.coli (PubMed:35025633). Cleavage of this precursor by its dedicated protease 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 (Probable). The pyroptosis-like-inducing activity is carried by the released N-terminal domain (Gasdermin bGSDM, N-terminus) (By similarity). Monomer in solution. 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. Full-length, unmodified protein expressed in E.coli. Full-length, palmitoylated protein expressed in E.coli. Full-length, modified protein expressed in E.coli. Belongs to the bacterial gasdermin family.