SpoIVA is designated stage IV sporulation protein A. It acts in the mother cell compartment and plays a role in spore coat morphogenesis. A comparative genome analysis of all sequenced genomes of Firmicutes shows that the proteins are strictly conserved among the sub-set of endospore-forming species. This protein assembles into static polymers driven by ATP hydrolyzis and is anchored to the outer forespore membrane through its C-terminal domain. This entry represents the ATPase domain located at the N-terminal of SpoIVA. It contains a conserved 'sensor' threonine residue that is involved in coordinating a Mg+2 ion.
Jiyao W et al.(2023). "The conserved domain database in 2023.",