InterPro : IPR016032

Name  Signal transduction response regulator, C-terminal effector Short Name  Sig_transdc_resp-reg_C-effctor
Type  Domain Description  Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions []. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk []. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more []. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) []. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK.A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [, ].This entry represents a structural domain usually found at the C-terminal of bipartite response regulators. These proteins are known to bind to DNA and RNA polymerases, and their N-terminal receiver domain belongs to the CheY family. The C-terminal effector domain consists of a 3-helical bundle in an up-an-down arrangement with a right-handed twist. This domain occurs in:PhoB-like proteins, which includes PhoB [], OmpR [], and DrrB []; these proteins contain a 4-stranded meander beta-sheet in the N-terminal extension.GerE-like proteins from the LuxR/UhpA family of proteins, which includes GerE [], TraR (quorum-sensing) [], NarL (nitrate/nitrite response regulator) [], and RcsB transcriptional regulator []; these proteins contain an additional fourth helix in the C-terminal extension.Spo0A proteins [], which are elaborated with additional helices.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR000792 Transcription regulator LuxR, C-terminal Tscrpt_reg_LuxR_C Domain
IPR014879 Sporulation initiation factor Spo0A, C-terminal Spo0A_C Domain

1 Contains

Id Name Short Name Type
IPR001867 Signal transduction response regulator, C-terminal Sig_transdc_resp-reg_C Domain

1 Found In

Id Name Short Name Type
IPR019941 Transcription regulator LuxR, chaperone HchA-associated Tscrpt_reg_LuxR_HchA-assoc Family

1 Parent Features

Id Name Short Name Type
IPR011991 Winged helix-turn-helix DNA-binding domain WHTH_DNA-bd_dom Domain

14 Publications

First Author Title Year Journal Volume Pages
Wolanin PM Histidine protein kinases: key signal transducers outside the animal kingdom. 2002 Genome Biol 3 REVIEWS3013
Stock AM Two-component signal transduction. 2000 Annu Rev Biochem 69 183-215
Skerker JM Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. 2005 PLoS Biol 3 e334
Laub MT Specificity in two-component signal transduction pathways. 2007 Annu Rev Genet 41 121-45
Varughese KI Molecular recognition of bacterial phosphorelay proteins. 2002 Curr Opin Microbiol 5 142-8
Hoch JA Keeping signals straight in phosphorelay signal transduction. 2001 J Bacteriol 183 4941-9
Ducros VM Crystal structure of GerE, the ultimate transcriptional regulator of spore formation in Bacillus subtilis. 2001 J Mol Biol 306 759-71
Pristovsek P Structural analysis of the DNA-binding domain of the Erwinia amylovora RcsB protein and its interaction with the RcsAB box. 2003 J Biol Chem 278 17752-9
Blanco AG Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. 2002 Structure 10 701-13
Vannini A The crystal structure of the quorum sensing protein TraR bound to its autoinducer and target DNA. 2002 EMBO J 21 4393-401
Lewis RJ The trans-activation domain of the sporulation response regulator Spo0A revealed by X-ray crystallography. 2000 Mol Microbiol 38 198-212
Kondo H Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site. 1997 Nat Struct Biol 4 28-31
Robinson VL Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily. 2003 J Bacteriol 185 4186-94
Baikalov I NarL dimerization? Suggestive evidence from a new crystal form. 1998 Biochemistry 37 3665-76

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)