| Type: | Conserved_site | Name: | Sigma-54 interaction domain, conserved site |
| Description: | Some bacterial regulatory proteins activate the expression of genes from promoters recognised by core RNA polymerase associated with the alternativesigma-54 factor. These have a conserved domain of about 230 residues involved in the ATP-dependent [, ] interaction with sigma-54. About half of the proteins in which this domain is found (algB, dcdT, flbD, hoxA, hupR1, hydG, ntrC, pgtA and pilR) belong to signal transduction two-component systems [] and possess a domain that can be phosphorylated by a sensor-kinase protein in their N-terminal section. Almost all of these proteins possess a helix-turn-helix DNA-binding domain in their C-terminal section.The domain involved in interaction with the sigma-54 factor has an ATPase activity. This may be required to promote a conformational change necessary for the interaction []. The domain contains an atypical ATP-binding motif A (P-loop) as well as a form of motif B. This entry represents a conserved site found in the C-terminal section of the sigma-54 interaction domain. | Short Name: | Sigma_54_int_dom_CS |
