Flagellar assembly protein FliS; Essential for filament assembly. May act as a facilitator of flagellin (hag) secretion. Antagonizes translational repressor CsrA indirectly. Belongs to the FliS family.

Flagellar hook-associated capping protein 2 (HAP2); Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity); Belongs to the FliD family.

Flagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.

Flagellar component of cell-proximal portion of basal-body rod; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type s: structure; Belongs to the flagella basal body rod proteins family.

Putative flagellar hook-basal body protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type ps: putative structure; Belongs to the flagella basal body rod proteins family.

Putative flagellar basal-body rod protein; Not required for motility.

Flagellar hook assembly protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type pf: putative factor; Belongs to the FlgD family.

Flagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family.

Flagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliM family.