PF00158

Sigma-54 interaction domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameSigma54_activat
ClanP-loop_NTPase
Author Sonnhammer ELL;0000-0002-9015-5588
Sequence Ontology0000417

Description
Imported from 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
[1, 2]
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
[3]
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
[4]
. 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.

References
Imported from IPR002078

1.The sigma 54 bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of their functional domains. Morett E, Segovia L. J. Bacteriol. 175, 6067-74, (1993). View articlePMID: 8407777

2.Influence of a mutation in the putative nucleotide binding site of the nitrogen regulatory protein NTRC on its positive control function. Austin S, Kundrot C, Dixon R. Nucleic Acids Res. 19, 2281-7, (1991). View articlePMID: 2041769

3.Prokaryotic signal transduction mediated by sensor and regulator protein pairs. Albright LM, Huala E, Ausubel FM. Annu. Rev. Genet. 23, 311-36, (1989). View articlePMID: 2694934

4.The prokaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent. Austin S, Dixon R. EMBO J. 11, 2219-28, (1992). View articlePMID: 1534752

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