ArticleScientific reports2020
Transport and kinase activities of CbrA of Pseudomonas putida KT2440.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 13 citations in OpenAlex.
- Structure and conformational dynamics of the Pseudomonas CbrA transceptor.Protein science : a publication of the Protein Society · 2026Article
- Structure and conformational dynamics of thebioRxiv : the preprint server for biology · 2026Article
- Upcycling of polyamides through chemical hydrolysis and engineered Pseudomonas putida.Nature microbiology · 2025Article
- Combinatorial control ofmSystems · 2024Article
- The S-component fold: a link between bacterial transporters and receptors.Communications biology · 2024Article
- Contribution of Uncharacterized Target Genes of MxtR/ErdR to Carbon Source Utilization by Pseudomonas putida KT2440.Microbiology spectrum · 2023Article
- Review
- RpuS/R Is a Novel Two-Component Signal Transduction System That Regulates the Expression of the Pyruvate Symporter MctP inFrontiers in microbiology · 2022Article
- The Regulatory Functions of σInternational journal of molecular sciences · 2021Review
- Involvement of the MxtR/ErdR (CrbS/CrbR) Two-Component System in Acetate Metabolism inMicroorganisms · 2021Article
- Role of a local transcription factor in governing cellular carbon/nitrogen homeostasis in Pseudomonas fluorescens.Nucleic acids research · 2021Article
- Prokaryotic Solute/Sodium Symporters: Versatile Functions and Mechanisms of a Transporter Family.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CbrA/CbrB system is a two-component signal transduction system known to participate in the regulation of the cellular carbon/nitrogen balance and to play a central role in carbon catabolite repression in Pseudomonas species. CbrA is composed of a domain with similarity to proteins of the solute/sodium symporter family (SLC5) and domains typically found in bacterial sensor kinases. Here, the functional properties of the sensor kinase CbrA and its domains are analyzed at the molecular level using the system of the soil bacterium P. putida KT2440 as a model. It is demonstrated that CbrA can bind and transport L-histidine. Transport is specific for L-histidine and probably driven by an electrochemical proton gradient. The kinase domain is not required for L-histidine uptake by the SLC5 domain of CbrA, and has no significant impact on transport kinetics. Furthermore, it is shown that the histidine kinase can autophosphorylate and transfer the phosphoryl group to the response regulator CbrB. The SLC5 domain is not essential for these activities but appears to modulate the autokinase activity. A phosphatase activity of CbrA is not detected. None of the activities is significantly affected by L-histidine. The results demonstrate that CbrA functions as a L-histidine transporter and sensor kinase.
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