v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | Bacterial flagella are responsible for motility and chemotaxis [ ]. They comprise a basal body, a hook and a filament, the latter accounting for 98% of the mass []. Flagellin is the subunit protein that polymerises to form the flagella [], the subunits being transported through the centre of the filament to the tip, where they then polymerise []. Both the N- and C-termini of the subunit protein, which are α-helical in structure [ ], are required to mediate polymerisation. Although no export or assembly, consensus sequences have been identified: Ala, Val, Leu, Ile, Gly, Ser, Thr, Asn, Gln and Asp tend to make up around 90% of the sequence, Cys and Trp being absent [].Flagellin plays a role in the activation of innate and adaptive immunity. It is an specific ligand for Toll-like receptor 5 (TLR5) in the host, which has lead to great interest to use it as adjuvant for vaccines [ , , ]. The protein is also recognised by the intracellular NAIP5/NLRC4 inflammasome receptor [ ]. This entry represents the C-terminal domain of Flagellin and similar bacterial proteins. This domain comes together with the N-terminal domain ( ) to form the D0 and D1 structural domains [ ]. These domains are responsible for the activation of TLR5, with the C-terminal D0 region playing a key role [, , ]. |
| Short Name | Flagellin_C |