We report the sequence and characterization of the gene. encodes a 61.8 kDa polypeptide (TlpC) which exhibits 30% amino acid identity with the methyl-accepting chemotaxis proteins (MCPs) and 38% identity with MCPs within the C-terminal domain. The putative methylation sites parallel those of the MCPs, rather than those of the receptors. TlpC is methylated both and although the level of methylation is poor. In addition, the anti-Trg antibody is shown to cross-react with this membrane protein. Inactivation of the gene confirms that TlpC is not one of the previously characterized MCPs from Capillary assays were performed using a variety of chemoeffectors, which included all 20 amino acids, several sugars, and several compounds previously classified as repellents. However, no chemotactic defect was observed for any of the chemoeffectors tested. We suggest that TlpC is similar to an evolutionary intermediate from which the major chemotactic transducers from arose.


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