Sigma54_activat

Sigma54_activat
PFAM accession number:PF00158
Interpro abstract (IPR002078):

Some bacterial regulatory proteins activate the expression of genes from promoters recognised by core RNA polymerase associated with the alternative sigma-54 factor. These have a conserved domain of about 230 residues involved in the ATP-dependent [ (PUBMED:8407777) (PUBMED:2041769) ] 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 [ (PUBMED:2694934) ] 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 which interacts with the sigma-54 factor has an ATPase activity. This may be required to promote a conformational change necessary for the interaction [ (PUBMED:1534752) ]. The domain contains an atypical ATP-binding motif A (P-loop) as well as a form of motif B. The two ATP-binding motifs are located in the N-terminal section of the domain.

GO process:regulation of transcription, DNA-templated (GO:0006355)
GO function:transcription factor binding (GO:0008134), ATP binding (GO:0005524)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Sigma54_activat