InterPro : IPR005467

Name  Signal transduction histidine kinase, core Short Name  Sig_transdc_His_kinase_core
Type  Domain Description  Most prokaryotic signal-transduction systems and a few eukaryotic pathways use phosphotransfer schemes involving two conserved components, a histidine protein kinase (HK) 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 domain. Phosphorylation induces a conformational change in RR that results in activation of an associated domain that effects the response.Both prokaryotic and eukaryotic HKs contain the same basic signaling components, namely a diverse sensing domain and a highly conserved kinase core that has a unique fold, distinct from that of the Ser/Thr/Tyr kinase superfamily. The overall activity of the kinase is modulated by input signals to the sensing domain. HKs undergo an ATP-dependent autophosphorylation at a conserved His residue in the kinase core. Autophosphorylation is a bimolecular reaction between homodimers, in which one HK monomer catalyzes the phosphorylation of the conserved His residue in the second monomer.The sensing domains are variable in sequence, reflective of the many different environmental signals to which HKs are responsive, whereas theabout 250-residue kinase core is more conserved. The kinase core is composed of a dimerization domain and an ATP/ADP-binding phosphotransfer or catalytic domain and can be identified by five conserved primary sequence motifs present in both eukaryotic and procaryotic HKs. These motifs have been termed the H, N, G1, F and G2 boxes. The conserved His substrate is the central feature in the H box, whereas the N, G1, F and G2 boxes define the nucleotide binding cleft. In most HKs, the H box is part of the dimerization domain. However, for some proteins, like CheA, the conserved His is located at the far N terminus of the protein in a separate HPt domain. The N, G1, F and G2 boxes are usually contiguous, but the spacing between these motifs is somewhat varied. The catalytic core forms an alpha-beta sandwich consisting of five antiparallel beta strands and three alpha helices [, , ].The entry represents the histidine kinase core.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



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3 Publications

First Author Title Year Journal Volume Pages
Stock AM Two-component signal transduction. 2000 Annu Rev Biochem 69 183-215
West AH Histidine kinases and response regulator proteins in two-component signaling systems. 2001 Trends Biochem Sci 26 369-76
Foussard M The molecular puzzle of two-component signaling cascades. 2001 Microbes Infect 3 417-24

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)