flagellar biosynthesis anti-sigma factor FlgM [Treponema pallidum]
Protein Classification
flagellar biosynthesis anti-sigma factor FlgM( domain architecture ID 10515847)
flagellar biosynthesis anti-sigma factor FlgM binds and inhibits the activity of the transcription factor sigma 28
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| FlgM | pfam04316 | Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor ... |
31-75 | 8.45e-03 | ||
Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor sigma 28. Inhibition of sigma 28 prevents the expression of genes from flagellar transcriptional class 3, which include genes for the filament and chemotaxis. Correctly assembled basal body-hook structures export FlgM, relieving inhibition of sigma 28 and allowing expression of class 3 genes. NMR studies show that free FlgM is mostly unfolded, which may facilitate its export. The C terminal half of FlgM adopts a tertiary structure when it binds to sigma 28. All mutations in FlgM that prevent sigma 28 inhibition affect the C-terminal domain and is the region thought to constitute the binding domain. A minimal binding domain has been identified between Glu 64 and Arg 88 in Salmonella typhimurium. The N-terminal portion remains unstructured and may be necessary for recognition by the export machinery. : Pssm-ID: 461260 Cd Length: 54 Bit Score: 31.69 E-value: 8.45e-03
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| Name | Accession | Description | Interval | E-value | ||
| FlgM | pfam04316 | Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor ... |
31-75 | 8.45e-03 | ||
Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor sigma 28. Inhibition of sigma 28 prevents the expression of genes from flagellar transcriptional class 3, which include genes for the filament and chemotaxis. Correctly assembled basal body-hook structures export FlgM, relieving inhibition of sigma 28 and allowing expression of class 3 genes. NMR studies show that free FlgM is mostly unfolded, which may facilitate its export. The C terminal half of FlgM adopts a tertiary structure when it binds to sigma 28. All mutations in FlgM that prevent sigma 28 inhibition affect the C-terminal domain and is the region thought to constitute the binding domain. A minimal binding domain has been identified between Glu 64 and Arg 88 in Salmonella typhimurium. The N-terminal portion remains unstructured and may be necessary for recognition by the export machinery. Pssm-ID: 461260 Cd Length: 54 Bit Score: 31.69 E-value: 8.45e-03
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| Name | Accession | Description | Interval | E-value | ||
| FlgM | pfam04316 | Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor ... |
31-75 | 8.45e-03 | ||
Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor sigma 28. Inhibition of sigma 28 prevents the expression of genes from flagellar transcriptional class 3, which include genes for the filament and chemotaxis. Correctly assembled basal body-hook structures export FlgM, relieving inhibition of sigma 28 and allowing expression of class 3 genes. NMR studies show that free FlgM is mostly unfolded, which may facilitate its export. The C terminal half of FlgM adopts a tertiary structure when it binds to sigma 28. All mutations in FlgM that prevent sigma 28 inhibition affect the C-terminal domain and is the region thought to constitute the binding domain. A minimal binding domain has been identified between Glu 64 and Arg 88 in Salmonella typhimurium. The N-terminal portion remains unstructured and may be necessary for recognition by the export machinery. Pssm-ID: 461260 Cd Length: 54 Bit Score: 31.69 E-value: 8.45e-03
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