Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring

A key step in bacterial cell division is the polymerization of FtsZ at midcell into a ring-like structure. This so-called Z ring forms a scaffold for the other cell division proteins. FtsA anchors the Z ring to the cell membrane; however, many bacterial species do not have FtsA. Here, we show that the conserved protein SepF, which forms large protein rings, also functions as a membrane anchor for the Z ring. We determined the molecular structure of the FtsZ-binding and ring-forming domain of SepF and show that the membrane-binding domain is located at the very beginning of the protein. These results explain why FtsA and SepF can fulfill similar functions in bacterial cell division.