Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation.
Chemotactic receptors at the bacterial cell surface communicate with flagellar basal structures to elicit appropriate motor behavior in response to extracellular stimuli. Genetic and physiological studies indicate that the product of the cheY gene interacts directly with components of the flagellar motor to control swimming behavior. We have purified and characterized the Salmonella typhimurium CheY protein and have determined the nucleotide sequence of the cheY gene. Amino acid sequence comparisons showed CheY to be homologous over its entire length (129 residues) to the N-terminal regulatory domain of another protein involved in chemotaxis, the CheB methyl esterase. The entire CheY protein and the regulatory domain of CheB also homologous to the N-terminal portions of the Escherichia coli OmpR and Dye proteins and the Bacillus subtilis Spo0A protein. These homologies suggest an evolutionary and functional relationship between the chemotaxis system and systems that are thought to regulate gene expression in response to changing environmental conditions.
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000502:physiology*; D001483:Base Sequence; D005075:Biological Evolution; D002633:Chemotaxis; D005798:Genes, Bacterial; D008745:Methylation; D008970:Molecular Weight; D018272:Porins; D012486:Salmonella typhimurium / Q000502:physiology*; D013171:Spores, Bacterial; D014157:Transcription Factors / Q000502:physiology
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D018272:Porins; D014157:Transcription Factors