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Significance The flagellum is a highly sophisticated organelle rotated by a motor that confers swarming motility to bacterial cells. Such motility is essential for the full pathogenicity of several virulence bacteria. Several proteins are required for the assembly and operation of the flagellum. Here we report the structural characterization of FliT, a key flagellar chaperone, in the unliganded state and in complex with two substrate flagellar proteins. FliT adopts an autoinhibited structure in order to avoid futile interactions with the export gate in the absence of a substrate. Substrate binding to FliT activates complex targeting to the export gate followed by either the export of the substrate or its assembly to the export apparatus.

Recognition and targeting mechanisms by chaperones in flagellum assembly and operation