ArticleJournal of bacteriology2009
The StkP/PhpP signaling couple in Streptococcus pneumoniae: cellular organization and physiological characterization.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Competence Regulation inCurrent medicinal chemistry · 2025Review
- Evolution and classification of Ser/Thr phosphatase PP2C family in bacteria: Sequence conservation, structures, domain distribution.PloS one · 2025Article
- Inhibitors targeting the autophosphorylation of serine/threonine kinase ofFrontiers in microbiology · 2022Article
- Comparative Phenotypic, Proteomic, and Phosphoproteomic Analysis Reveals Different Roles of Serine/Threonine Phosphatase and Kinase in the Growth, Cell Division, and Pathogenicity ofMicroorganisms · 2021Article
- Protein Tyrosine and Serine/Threonine Phosphorylation in Oral Bacterial Dysbiosis and Bacteria-Host Interaction.Frontiers in cellular and infection microbiology · 2021Review
- The Cell Wall ofMicrobiology spectrum · 2019Review
- Proteomic Investigation Uncovers Potential Targets and Target Sites of Pneumococcal Serine-Threonine Kinase StkP and Phosphatase PhpP.Frontiers in microbiology · 2019Article
- Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments.International journal of molecular sciences · 2018Review
- Crosstalk between the serine/threonine kinase StkP and the response regulator ComE controls the stress response and intracellular survival of Streptococcus pneumoniae.PLoS pathogens · 2018Article
- Phosphorylation-dependent activation of the cell wall synthase PBP2a inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Do Shoot the Messenger: PASTA Kinases as Virulence Determinants and Antibiotic Targets.Trends in microbiology · 2018Review
- A serine/threonine phosphatase 1 ofJournal of veterinary science · 2017Article
- Suppression and synthetic-lethal genetic relationships of ΔgpsB mutations indicate that GpsB mediates protein phosphorylation and penicillin-binding protein interactions in Streptococcus pneumoniae D39.Molecular microbiology · 2017Article
- Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.The Journal of biological chemistry · 2016Article
- Characterization of pneumococcal Ser/Thr protein phosphatase phpP mutant and identification of a novel PhpP substrate, putative RNA binding protein Jag.BMC microbiology · 2016Article
- Distribution of PASTA domains in penicillin-binding proteins and serine/threonine kinases of Actinobacteria.The Journal of antibiotics · 2016Review
- Article
- Contribution of eukaryotic-type serine/threonine kinase to stress response and virulence of Streptococcus suis.PloS one · 2014Article
- Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Strain-specific regulatory role of eukaryote-like serine/threonine phosphatase in pneumococcal adherence.Infection and immunity · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Streptococcus pneumoniae, stkP and phpP, encoding the eukaryotic-type serine-threonine kinase and PP2C phosphatase, respectively, form an operon. PhpP has the features of a so-called "soluble" protein, whereas StkP protein is membrane associated. Here we provide the first genetic and physiological evidence that PhpP and StkP, with antagonist enzymatic activities, constitute a signaling couple. The StkP-PhpP couple signals competence upstream of the competence-specific histidine kinase ComD, receptor for the oligopeptide pheromone "competence stimulating peptide." We show that PhpP activity is essential in a stkP(+) genetic background, suggesting tight control of StkP activity by PhpP. Proteins PhpP and StkP colocalized to the cell membrane subcellular fraction and likely belong to the same complex, as revealed by coimmunoprecipitation in cellular extracts. Specific coimmunoprecipitation of the N-kinase domain of StkP and PhpP recombinant proteins by PhpP-specific antibodies demonstrates direct interaction between these proteins. Consistently, flow cytometry analysis allowed the determination of the cytoplasmic localization of PhpP and of the N-terminal kinase domain of StkP, in contrast to the periplasmic localization of the StkP C-terminal PASTA (penicillin-binding protein and serine-threonine kinase associated) domain. A signaling route involving interplay between serine, threonine, and histidine phosphorylation is thus described for the first time in this human pathogen.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.