<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>194(5)</volume><submitter>Dogra G</submitter><pubmed_abstract>Retrophosphorylation of the histidine kinase CheA in the chemosensory transduction chain is a widespread mechanism for efficient dephosphorylation of the activated response regulator. First discovered in Sinorhizobium meliloti, the main response regulator CheY2-P shuttles its phosphoryl group back to CheA, while a second response regulator, CheY1, serves as a sink for surplus phosphoryl groups from CheA-P. We have identified a new component in this phospho-relay system, a small 97-amino-acid protein named CheS. CheS has no counterpart in enteric bacteria but revealed distinct similarities to proteins of unknown function in other members of the α subgroup of proteobacteria. Deletion of cheS causes a phenotype similar to that of a cheY1 deletion strain. Fluorescence microscopy revealed that </pubmed_abstract><journal>Journal of bacteriology</journal><pagination>1075-87</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3294773</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Sinorhizobium meliloti CheA complexed with CheS exhibits enhanced binding to CheY1, resulting in accelerated CheY1 dephosphorylation.</pubmed_title><pmcid>PMC3294773</pmcid><pubmed_authors>Dogra G</pubmed_authors><pubmed_authors>Purschke FG</pubmed_authors><pubmed_authors>Ray WK</pubmed_authors><pubmed_authors>Scharf BE</pubmed_authors><pubmed_authors>Kriehuber T</pubmed_authors><pubmed_authors>Niemeyer M</pubmed_authors><pubmed_authors>Gilbert C</pubmed_authors><pubmed_authors>Wagner V</pubmed_authors><pubmed_authors>Hughes JG</pubmed_authors><pubmed_authors>Helm RF</pubmed_authors><pubmed_authors>Haslbeck M</pubmed_authors><pubmed_authors>Van Tassell ML</pubmed_authors></additional><is_claimable>false</is_claimable><name>Sinorhizobium meliloti CheA complexed with CheS exhibits enhanced binding to CheY1, resulting in accelerated CheY1 dephosphorylation.</name><description>Retrophosphorylation of the histidine kinase CheA in the chemosensory transduction chain is a widespread mechanism for efficient dephosphorylation of the activated response regulator. First discovered in Sinorhizobium meliloti, the main response regulator CheY2-P shuttles its phosphoryl group back to CheA, while a second response regulator, CheY1, serves as a sink for surplus phosphoryl groups from CheA-P. We have identified a new component in this phospho-relay system, a small 97-amino-acid protein named CheS. CheS has no counterpart in enteric bacteria but revealed distinct similarities to proteins of unknown function in other members of the α subgroup of proteobacteria. Deletion of cheS causes a phenotype similar to that of a cheY1 deletion strain. Fluorescence microscopy revealed that </description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Mar</publication><modification>2026-05-01T17:21:18.492Z</modification><creation>2026-04-07T17:05:08.081Z</creation></dates><accession>S-EPMC3294773</accession><cross_references><pubmed>22194454</pubmed><doi>10.1128/jb.06505-11</doi><doi>10.1128/JB.06505-11</doi></cross_references></HashMap>