Coordinates cortex and coat assembly during sporulation (PubMed:22463703, PubMed:8231808). Associates with the spore coat protein SpoIVA and with the outer forespore membrane, thereby serving as a membrane anchor that tethers SpoIVA and the entire spore coat to the forespore surface (PubMed:17427285). May also serve as a competitive inhibitor of FtsH activity during sporulation (PubMed:9287010). Interacts with SpoIVA (PubMed:17427285). May interact with the ATP-dependent protease FtsH (PubMed:9287010). SpoVM is an atypical amphipathic alpha-helix deeply embedded in the membrane (PubMed:25825747). Proper localization depends on SpoIVA (PubMed:17427285). Expressed during sporulation and is regulated by the mother cell-specific transcription factors sigma E and SpoIIID (PubMed:8231808). There is a lag-phase of approximately 2 hours between the onset of transcription and translation (PubMed:18820968). The 5' untranslated region negatively influences its own translation (PubMed:18820968). Residues in the N-terminal region are required for proper localization. Nanomolar concentrations inhibit biofilm formation in situ, in S.aureus and in P.aeruginosa, suggesting it might be useful controlling bacterial infections. Preferentially localizes to slightly convex membranes (PubMed:25825747, PubMed:29102609). This preferential adsorption is accurately modeled as a two-step 'dash-and-recruit' mechanism: first, an initial binding event occurs with a faster on rate, then cooperative recruitment of additional SpoVM molecules follows (PubMed:29102609).