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flagellar export chaperone FliS This family contains flagellar export chaperone FliS, a protein critical for flagellar assembly and bacterial colonization. FliS prevents premature polymerization of flagellins, the major protein of the filament, by regulating interactions between structural components of the bacterial flagellum in the cytosol. It binds specifically to FliC (flagellin) which is sequentially secreted in large numbers through the central channel of the flagellum and polymerized to form the tail filament. FliS protects FliC from degradation and aggregation by binding to the FliC C-terminal helical domain, which contributes to stabilization of flagellin subunit interactions during polymerization. FliS has been shown to interact specifically with FlgM, whose role is to inhibit FliA, a flagellum-specific RNA polymerase responsible for flagellin transcription; FliA competes with FliS for FlgM binding. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",