Cell division is the fundamental process during the bacterial cell cycle that ensures the successful production of two daughter cells with complete genomes for the next generation.  Division itself is attained after a set of specialized proteins localize to the middle position of the bacterial cell where they assemble into a large multiprotein complex called the divisome.  Assembly of the divisome can be divided in two steps. In the first step, the tubulin-like FtsZ protein polymerizes into a ring-shaped structure known as the Z ring. Subsequently, the Z ring serves as a scaffold for the recruitment and assembly of the remaining components of the divisome. Z-ring formation is a key regulatory step of division and seems to be modulated by a number of proteins that interact with FtsZ and affect its polymerization properties. One of these is FtsA, a widely conserved division protein that shows structural similarity with actin. Even though not necessary for Z-ring assembly, FtsA was reported necessary for division septum formation in previous works in E. coli.  In this work we sought to characterize the role of FtsA in B. subtilis. To do that, we initially studied a temperature-sensitive ftsA mutant, which was previously described but never characterized cytologically. When observed by fluorescence microscopy, this strain presented the division inhibition phenotype expected for a ftsA null mutant upon growth at restrictive temperature. To determine the stage of the division block caused by the ftsA(ts) mutation, a gfp-ftsZ fusion allele was inserted into the ftsA(ts) strain, allowing for the visualization of Z-rings. This demonstrated that division inhibition correlated with a reduction in Z-ring formation. To corroborate the results obtained with ftsA(ts), we constructed a conditional mutant of ftsA that only expresses ftsA upon xylose addition to the growth media.  Experiments of ftsA depletion using this mutant have confirmed that FtsA absence results in the reduction in the number of Z-rings in B. subtilis, thus suggesting that, differently from E.coli, FtsA is essential to Z-ring formation in B. subtilis. Finally, we have also found that the division inhibition was exacerbated if we combined the ftsA(ts) mutation with a mutation in zapA, another FtsZ-interacting protein recently discovered by our group. This indicates that there could be a redundant role for FtsA and ZapA in Z-ring formation and stabilization during division.