InterPro : IPR003852

Name  Signal transduction histidine kinase, osmosensitive K+ channel sensor, N-terminal Short Name  Sig_transdc_His_kinase_KdpD_N
Type  Domain Description  Signal transducing histidine kinases are the key elements in two-component signal transduction systems, which control complex processes such as the initiation of development in microorganisms [, ]. Examples of histidine kinases are EnvZ, which plays a central role in osmoregulation [], and CheA, which plays a central role in the chemotaxis system []. Histidine kinases usually have an N-terminal ligand-binding domain and a C-terminal kinase domain, but other domains may also be present. The kinase domain is responsible for the autophosphorylation of the histidine with ATP, the phosphotransfer from the kinase to an aspartate of the response regulator, and (with bifunctional enzymes) the phosphotransfer from aspartyl phosphate back to ADP or to water []. The kinase core has a unique fold, distinct from that of the Ser/Thr/Tyr kinase superfamily. HKs can be roughly divided into two classes: orthodox and hybrid kinases [, ]. Most orthodox HKs, typified by the Escherichia coliEnvZ protein, function as periplasmic membrane receptors and have a signal peptide and transmembrane segment(s) that separate the protein into a periplasmic N-terminal sensing domain and a highly conserved cytoplasmic C-terminal kinase core. Members of this family, however, have an integral membrane sensor domain. Not all orthodox kinases are membrane bound, e.g., the nitrogen regulatory kinase NtrB (GlnL) is a soluble cytoplasmic HK []. Hybrid kinases contain multiple phosphodonor and phosphoacceptor sites and use multi-step phospho-relay schemes instead of promoting a single phosphoryl transfer. In addition to the sensor domain and kinase core, they contain a CheY-like receiver domain and a His-containing phosphotransfer (HPt) domain.This entry represents the N-terminal domain found in KdpD sensor kinase proteins, which regulate the kdpFABC operon responsible for potassium transport []. The N-terminal domain forms part of the cytoplasmic region of the protein, which may be the sensor domain responsible for sensing turgor pressure [].
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10 Publications

First Author Title Year Journal Volume Pages
Stock AM Two-component signal transduction. 2000 Annu Rev Biochem 69 183-215
Bilwes AM Structure of CheA, a signal-transducing histidine kinase. 1999 Cell 96 131-41
Perego M Protein aspartate phosphatases control the output of two-component signal transduction systems. 1996 Trends Genet 12 97-101
Tomomori C Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. 1999 Nat Struct Biol 6 729-34
Vierstra RD Bacteriophytochromes: new tools for understanding phytochrome signal transduction. 2000 Semin Cell Dev Biol 11 511-21
Treuner-Lange A The kdp system of Clostridium acetobutylicum: cloning, sequencing, and transcriptional regulation in response to potassium concentration. 1997 J Bacteriol 179 4501-12
Walderhaug MO KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators. 1992 J Bacteriol 174 2152-9
West AH Histidine kinases and response regulator proteins in two-component signaling systems. 2001 Trends Biochem Sci 26 369-76
Alex LA Protein histidine kinases and signal transduction in prokaryotes and eukaryotes. 1994 Trends Genet 10 133-8
Parkinson JS Communication modules in bacterial signaling proteins. 1992 Annu Rev Genet 26 71-112



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)