Common Evolutionary Origin for the Rotor Domain of Rotary Atpases and Flagellar Protein Export Apparatus

The V₁- and F₁- rotary ATPases contain a rotor that rotates against a catalytic A₃B₃ or α₃β₃ stator. The rotor F₁-γ or V₁-DF is composed of both anti-parallel coiled coil and globular-loop parts. The bacterial flagellar type III export apparatus contains a V₁/F₁-like ATPase ring structure composed of FliI₆ homo-hexamer and FliJ which adopts an anti-parallel coiled coil structure without the globular-loop part. Here we report that FliJ of Salmonella enterica serovar Typhimurium shows a rotor like function in Thermus thermophilus A₃B₃ based on both biochemical and structural analysis. Single molecular analysis indicates that an anti-parallel coiled-coil structure protein (FliJ structure protein) functions as a rotor in A₃B₃. A rotary ATPase possessing an F₁-γ-like protein generated by fusion of the D and F subunits of V₁ rotates, suggesting F₁-γ could be the result of a fusion of the genes encoding two separate rotor subunits. Together with sequence comparison among the globular part proteins, the data strongly suggest that the rotor domains of the rotary ATPases and the flagellar export apparatus share a common evolutionary origin.