Flagellar hook-associated protein; Required for 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.

Flagellar hook-filament junction protein 1 (HAP1). no signal peptide no TMHs; High confidence in function and specificity.

Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.

ATP synthase (EC 3.6.3.14). Probable catalytic subunit of a protein translocase for flagellum-specific export or a proton translocase involved in local circuits at the flagellum. May be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. InterPro: ATP synthase alpha and beta subunit central region Pfam: ATP synthase alpha/beta family no signal peptide no TMHs; High confidence in function and specificity.

Probable flagellar protein; Protein flaG. Although these proteins are known to be important for flagellar their exact function is unknown TREMBL:Q82UA2: 56% identity, 79% similarity. InterPro:IPR005186; FlaG. Pfam:PF03646; FlaG L12: ribosomal protein L7/L12 Nonsecretory protein with low signal peptide probability (0.041): SignalP predicted Transmembrane helices 0; High confidence in function and specificity.

Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity.

Flagellar hook-associated protein 3 (HAP3) (Hook-filament junction protein). no signal peptide no TMHs; High confidence in function and specificity.

Flagellar basal-body rod protein flgG (Distal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.

Flagellar motor switch protein fliN (Flagellar motor switch protein mopA) (Fragment). FliN is one of three proteins (FliG FliN FliM) that form a switch complex that is proposed to be located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins in addition to contacting components of the motor that determine the dirction of flagellar rotation (by similarity). InterPro: Surface presentation of antigens (SPOA) protein, Flagellar motor switch FliN protein Pfam: Surface presentation of antigens (SPOA) protein no signal peptide no TMHs; High confid [...]