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The role of rotational molecular motors of the ATP synthase class is integralto the metabolism of cells. Yet the function of FliI6-FliJ complex - homologousto the F1 ATPase motor - within the flagellar export apparatus remains unclear.We use a simple two-state model adapted from studies of linear molecular motorsto identify key features of this motor. The two states are the 'locked' groundstate where the FliJ coiled coil filament experiences fluctuations in anasymmetric torsional potential, and a 'free' excited state in which FliJundergoes rotational diffusion. Michaelis-Menten kinetics was used to treattransitions between these two states, and obtain the average angular velocityof the FliJ filament within the FliI6 stator: ~9.0 rps. The motor was thenstudied under external counter torque conditions in order to ascertain itsmaximal power output: Pmax ~42 kBT/s, and the stall torque: ~3 kBT/rad. Twomodes of action within the flagellar export apparatus are proposed, in whichthe motor performs useful work either by continuously 'grinding' through theresistive environment, or by exerting equal and opposite stall force on it. Inboth cases, the resistance is provided by flagellin subunits entering theflagellar export channel prior to their unfolding. We therefore propose thatthe function of the FliI6-FliJ complex is to lower the energy barrier andtherefore assist in unfolding of the flagellar proteins before feeding theminto the transport channel.

FliI6-FliJ molecular motor assists with unfolding in the type III secretion export apparatus