{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Breland EJ"],"funding":["HHS | NIH | National Institute of Allergy and Infectious Diseases","National Science Foundation"],"pagination":["e00060-17"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5573081"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["199(18)"],"pubmed_abstract":["Two-component systems are prototypically comprised of a histidine kinase (sensor) and a response regulator (responder). The sensor kinases autophosphorylate at a conserved histidine residue, acting as a phosphodonor for subsequent phosphotransfer to and activation of a cognate response regulator. In rare cases, the histidine residue is also essential for response regulator dephosphorylation via a reverse-phosphotransfer reaction. In this work, we present an example of a kinase that relies on reverse phosphotransfer to catalyze the dephosphorylation of its cognate partner. The QseC sensor kinase is conserved across several Gram-negative pathogens; its interaction with its cognate partner QseB is critical for maintaining pathogenic potential. Here, we demonstrate that QseC-mediated dephospho"],"journal":["Journal of bacteriology"],"pubmed_title":["The Histidine Residue of QseC Is Required for Canonical Signaling between QseB and PmrB in Uropathogenic Escherichia coli."],"pmcid":["PMC5573081"],"funding_grant_id":["R01 AI107052-01","1445197","R01 AI107052-02"],"pubmed_authors":["Bermudez T","Zhang EW","Martinez CR","Breland EJ","Hadjifrangiskou M"],"additional_accession":[]},"is_claimable":false,"name":"The Histidine Residue of QseC Is Required for Canonical Signaling between QseB and PmrB in Uropathogenic Escherichia coli.","description":"Two-component systems are prototypically comprised of a histidine kinase (sensor) and a response regulator (responder). The sensor kinases autophosphorylate at a conserved histidine residue, acting as a phosphodonor for subsequent phosphotransfer to and activation of a cognate response regulator. In rare cases, the histidine residue is also essential for response regulator dephosphorylation via a reverse-phosphotransfer reaction. In this work, we present an example of a kinase that relies on reverse phosphotransfer to catalyze the dephosphorylation of its cognate partner. The QseC sensor kinase is conserved across several Gram-negative pathogens; its interaction with its cognate partner QseB is critical for maintaining pathogenic potential. Here, we demonstrate that QseC-mediated dephospho","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Sep","modification":"2025-04-05T14:29:50.51Z","creation":"2019-03-26T23:03:14Z"},"accession":"S-EPMC5573081","cross_references":{"pubmed":["28396353"],"doi":["10.1128/jb.00060-17","10.1128/JB.00060-17"]}}