Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Cleavage of this precursor by its dedicated, neighboring protease (G563DRAFT_02009) releases the active moiety (gasdermin bGSDM, N-terminus) which inserts into membranes, forming pores and triggering cell death (PubMed:35025633). Expression of bGSDM and its protease is highly toxic in E.coli (PubMed:35025633). Cells expressing the gene pair stop dividing and lose membrane integrity (PubMed:35025633). Both proteins are required to kill E.coli (PubMed:35025633). Pore-forming protein that causes membrane permeabilization via a pyroptosis-like activity (PubMed:35025633). Makes ring-like pores with walls about 50 Angstroms thick and an interior pore diameter of 200-300 Angstroms, when integrated in liposomes (PubMed:35025633). 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 (PubMed:35025633). The pyroptosis-like-inducing activity is carried by the released N-terminal domain (gasdermin bGSDM, N-terminus) (PubMed:35025633). Monomer in solution. Forms large, probably homooligomeric ring-shaped pores when inserted in membranes. Upon proteolysis the protein forms membrane-associated puncta. 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. The C-terminal region can assume multiple conformations. Cleavage by the adjacently encoded protease (G563DRAFT_02009) between Leu-247 and Gly-248 relieves autoinhibition, releasing the N-terminus which initiates loss of cell integrity. Palmitoylation helps stabilize the inactive state; may self-palmitoylate. Palmitoylation is not required for permeabilization of liposomes by the ring-like pores in vitro. Gasdermin bGSDM, N-terminus, palmitoylated. 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.