Free-swimming bacteria modulate their swimming patterns in response to environmental changes. They are propelled by helical flagellar filaments connected to the basal body by a flexible hook and driven by a flagellar rotary motor. The basal body consists of a central rod and four coaxial structures, the L ring in the outer membrane, the P ring in the peptidoglycan layer, the MS ring in the cytoplasmic membrane, and the bellshaped C ring in the cytoplasm. In enterobacterial species like Escherichia coli and Salmonella enterica serovar Typhimurium, temporal and structural assembly of the flagellar apparatus is strictly regulated by a hierarchy of transcriptional controls (1,2,22,23,27,59). The MS ring complex appears at the very beginning of flagellar assembly. Then the C ring and the export apparatus, composed of six transmembrane proteins and two cytoplasmic proteins, are assembled on the cytoplasmic side of the M ring. The active and selective export of flagellar proteins starts with five proteins comprising the rod, followed by the hook, which is composed of FlgE subunits (13,21,34). Upon completion of the basal structure and the hook, genes necessary for the flagellar filament and the energizing motility complexes are expressed. At this assembly point, the flagellar protein export apparatus switches specificity from rod/hook-type substrates to filament-type substrates. Whereas the length of the flagellar filament is not strictly regulated, the length of the hook is well defined by the hook length control protein, FliK (19). The accurately defined length of the flexible hook is essential for proper formation of bundles of the flagellar filaments and therefore for efficient propulsion of the cell (14). Once the hook reaches its mature length (55 nm), the flagellar export protein FlhB, together with FliK, mediates the switching of export specificity (32, 59). Defects in fliK or flhB prevent this switch, resulting in abnormally long hooks, called polyhooks (15).The behavioral scheme of the nitrogen-fixing plant symbiont Sinorhizobium meliloti, a member of the ␣-subgroup of the Proteobacteria (39), differs from the enterobacterial (␥-subgroup) behavioral scheme in the filament structure, the mode of flagellar rotation, signal processing, and gene regulation (52). The rigid "complex" flagellar filaments consist of four related flagellin subunits, and interflagellin bonds lock the filaments in right-handedness (6,11,50). Hence, S. meliloti cells are propelled by exclusively clockwise rotating flagella, and swimming cells respond to tactic stimuli by modulating their rotary speed (3,49). This mode of motility control has a molecular corollary in two novel periplasmic motility proteins, MotC and MotE, which are present in addition to the ubiquitous MotA/MotB energizing proton channel. MotC binds to the periplasmic portion of MotB and requires a specific chaperone, MotE, for proper folding and stability (7). Platzer et al. (42) described the presence of an additional motility protein, MotD. These authors determined tha...