Structural highlights
5gna is a 2 chain structure with sequence from Salty. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Gene: | fliT, STM1962 (SALTY), fliD, flaV, flbC, STM1960 (SALTY) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[FLIT_SALTY] Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.[1] [2] [3] [4] [FLID_SALTY] 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.
References
- ↑ Fraser GM, Bennett JC, Hughes C. Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly. Mol Microbiol. 1999 May;32(3):569-80. PMID:10320579
- ↑ Kutsukake K, Ikebe T, Yamamoto S. Two novel regulatory genes, fliT and fliZ, in the flagellar regulon of Salmonella. Genes Genet Syst. 1999 Dec;74(6):287-92. PMID:10791024
- ↑ Bennett JC, Thomas J, Fraser GM, Hughes C. Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT. Mol Microbiol. 2001 Feb;39(3):781-91. PMID:11169117
- ↑ Yamamoto S, Kutsukake K. FliT acts as an anti-FlhD2C2 factor in the transcriptional control of the flagellar regulon in Salmonella enterica serovar typhimurium. J Bacteriol. 2006 Sep;188(18):6703-8. PMID:16952964 doi:https://dx.doi.org/10.1128/JB.00799-06
