|PROSITE documentation PDOC50110
Response regulatory domain profile
Most prokaryotic signal-transduction systems and a few eukaryotic pathways use
phosphotransfer schemes involving two conserved components, a histidine
protein kinase (HK) (see <PDOC50109>) and a response regulator protein (RR).
The HK, which is regulated by environmental stimuli, autophosphorylates at a
histidine residue, creating a high-energy phosphoryl group that is
subsequently transferred to an aspartate residue in the RR. Most RRs consist
of two domains: a conserved N-terminal regulatory domain and a variable C-terminal effector domain. Phosphorylation of the regulatory domain induces a
conformational change that results in activation of an associated domain that
effects the response. The regulatory domains of RRs have three activities.
First they interact with phosphorylated HKs and catalyze transfer of a
phosphoryl group to one of their own Asp residues. Second, they catalyze
autodephosphorylation. And finally they regulate the activities of their
associated effector domains in a phosphorylation-dependent manner. The
regulatory domains, often called receiver domains, can also be found within
hybrid histidine kinases or as isolated proteins within phosphorelay pathways.
In these contexts, the receiver domains are not physically connected to
effector domains and play no direct role in regulating effector domain
The RR domain has a doubly wound five-stranded α/β fold consisting of
about 125 residues (see <PDB:2CHY>). This fold consists a central five-stranded parallel β sheet flanked on both faces by five amphipathic α
helices. Residues that are highly conserved in all RR domains are clustered in
two regions: an active-site cleft formed by loops that extend from the C-terminal ends of β strands 1, 3 and 5, and a pair of residues that form a
diagonal path extending across the molecule from the active site. The active
site is a conserved acidic pocket and contains the phosphorylatable aspartate
The profile we developed covers the entire RR domain.
January 2002 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|RESPONSE_REGULATORY, PS50110; Response regulatory domain profile (MATRIX)
|Sequences known to belong to this class detected by the profile:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1A04 1A0O 1A2O 1AB5 ... [ALL]
||West A.H., Stock A.M.
||Histidine kinases and response regulator proteins in two-component signaling systems.
||Trends Biochem. Sci. 26:369-376(2001).
||Foussard M., Cabantous S., Pedelacq J.-D., Guillet V., Tranier S., Mourey L., Birck C., Samama J.-P.
||The molecular puzzle of two-component signaling cascades.
||Microbes Infect. 3:417-424(2001).
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
View entry in original PROSITE document format
View entry in raw text format (no links)