InterPro : IPR008358

Name  Signal transduction histidine kinase/phosphatase, lantibiotic regulatory protein MprB Short Name  Sig_transdc_His_kin/Pase_MprB
Type  Family 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 [, ].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.Pathogenic bacteria produce a number of virulence factors to facilitate host infection, and to combat competing species. Antibiotics are secreted by some pathogenic prokaryotes to lyse cells, some of which have been adapted by humans for use against virulent microbes. Amongst these are the lantibiotics, produced exclusively by Gram-positive bacteria. Lantibiotics are small, heavily post-translationally modified peptides that inhibit rival cell growth and are strongly cationic. Lantibiotic genes reside on the bacterial chromosome, where they cluster with genes that adapt and secrete them to the extracellular space. Many of these so-called 'pathogenicity islands' have been characterised, including the epidermin (epi) cluster in Staphylococcus epidermis, and the nisin (nis) cluster in Lactococcus lactis[]. The gene encoding the lantibiotic is flanked by 3 regulatory genes: 2 that are usually involved in a 2-component regulatory system, and another that cleaves the signal peptide from the precursor to produce the mature lantibiotic.The archetypal example of lantibiotic synthesis is witnessed in the Lactococcus lactisnis operon. In this cluster, the 2-component regulatory system is controlled by the nisK/nisR genes. NisK is believed to function as a membrane-associated protein kinase that phosphorylates NisR in response to external stimuli []. It shows some similarity to other bacterial kinases, and contains a single histidine kinase domain.
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

3 Contains

Id Name Short Name Type
IPR003594 Histidine kinase-like ATPase, C-terminal domain HATPase_C Domain
IPR003661 Signal transduction histidine kinase EnvZ-like, dimerisation/phosphoacceptor domain EnvZ-like_dim/P Domain
IPR003660 HAMP linker domain HAMP_linker_domain Domain

0 Found In

0 Parent Features

15 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
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
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
Engelke G Regulation of nisin biosynthesis and immunity in Lactococcus lactis 6F3. 1994 Appl Environ Microbiol 60 814-25
van der Meer JR Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis. 1993 J Bacteriol 175 2578-88



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)