ArticleJournal of bacteriology2010
Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 75 citations in OpenAlex.
- Article
- Staphylococcus aureus sensor histidine kinase VraS mutations linked to antibiotic resistance affect enzymatic catalysis, stability, and substrate interactions.Archives of biochemistry and biophysics · 2026Article
- Insights Into the Conformational Dynamics of the Cytoplasmic Domain of Metal-Sensing Sensor Histidine Kinase ZraS.Proteins · 2025Article
- The accessory protein CvnF8 modulates histidine kinase activity in an Actinobacterial G protein system inbioRxiv : the preprint server for biology · 2025Article
- NH125 Sensitizes Staphylococcus aureus to Cell Wall-Targeting Antibiotics through the Inhibition of the VraS Sensor Histidine Kinase.Microbiology spectrum · 2023Article
- Phosphorylation chemistry of the Bordetella PlrSR TCS and its contribution to bacterial persistence in the lower respiratory tract.Molecular microbiology · 2023Article
- Roles of RodZ and class A PBP1b in the assembly and regulation of the peripheral peptidoglycan elongasome in ovoid-shaped cells of Streptococcus pneumoniae D39.Molecular microbiology · 2022Article
- The W-Acidic Motif of Histidine Kinase WalK Is Required for Signaling and Transcriptional Regulation inFrontiers in microbiology · 2022Article
- MgaVirulence · 2021Article
- Dissecting the Role of VicK Phosphatase in Aggregation and Biofilm Formation ofJournal of dental research · 2021Article
- ChiS is a noncanonical DNA-binding hybrid sensor kinase that directly regulates the chitin utilization program inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation.Journal of bacteriology · 2020Article
- Metal-induced sensor mobilization turns on affinity to activate regulator for metal detoxification in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The SrrAB two-component system regulatesProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Regulation of pneumococcal epigenetic and colony phases by multiple two-component regulatory systems.PLoS pathogens · 2020Article
- The Staphylococcus aureus ArlRS two-component system regulates virulence factor expression through MgrA.Molecular microbiology · 2020Article
- Screening serine/threonine and tyrosine kinase inhibitors for histidine kinase inhibition.Bioorganic & medicinal chemistry · 2018Article
- Phosphatase activity of the control of virulence sensor kinase CovS is critical for the pathogenesis of group A streptococcus.PLoS pathogens · 2018Article
- Exploration of the Effects of γ-Phosphate-Modified ATP Analogues on Histidine Kinase Autophosphorylation.Biochemistry · 2018Article
- SpdC, a novel virulence factor, controls histidine kinase activity in Staphylococcus aureus.PLoS pathogens · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The WalRK two-component system plays important roles in maintaining cell wall homeostasis and responding to antibiotic stress in low-GC Gram-positive bacteria. In the major human pathogen, Streptococcus pneumoniae, phosphorylated WalR(Spn) (VicR) response regulator positively controls the transcription of genes encoding the essential PcsB division protein and surface virulence factors. WalR(Spn) is phosphorylated by the WalK(Spn) (VicK) histidine kinase. Little is known about the signals sensed by WalK histidine kinases. To gain information about WalK(Spn) signal transduction, we performed a kinetic characterization of the WalRK(Spn) autophosphorylation, phosphoryltransferase, and phosphatase reactions. We were unable to purify soluble full-length WalK(Spn). Consequently, these analyses were performed using two truncated versions of WalK(Spn) lacking its single transmembrane domain. The longer version (Delta35 amino acids) contained most of the HAMP domain and the PAS, DHp, and CA domains, whereas the shorter version (Delta195 amino acids) contained only the DHp and CA domains. The autophosphorylation kinetic parameters of Delta35 and Delta195 WalK(Spn) were similar [K(m)(ATP) approximately 37 microM; k(cat) approximately 0.10 min(-1)] and typical of those of other histidine kinases. The catalytic efficiency of the two versions of WalK(Spn) approximately P were also similar in the phosphoryltransfer reaction to full-length WalR(Spn). In contrast, absence of the HAMP-PAS domains significantly diminished the phosphatase activity of WalK(Spn) for WalR(Spn) approximately P. Deletion and point mutations confirmed that optimal WalK(Spn) phosphatase activity depended on the PAS domain as well as residues in the DHp domain. In addition, these WalK(Spn) DHp domain and DeltaPAS mutations led to attenuation of virulence in a murine pneumonia model.
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