RT Journal Article SR Electronic(1) A1 Hanlon, David W. A1 Rosario, Mia Mae L. A1 Ordal, George W. A1 Venema, Gerard A1 Van Sinderen, DouweYR 1994 T1 Identification of TlpC, a novel 62 kDa MCP-like protein from Bacillus subtilis JF Microbiology, VO 140 IS 8 SP 1847 OP 1854 DO https://doi.org/10.1099/13500872-140-8-1847 PB Microbiology Society, SN 1465-2080, AB We report the sequence and characterization of the Bacillus subtilis tlpC gene. tlpC encodes a 61.8 kDa polypeptide (TlpC) which exhibits 30% amino acid identity with the Escherichia coli methyl-accepting chemotaxis proteins (MCPs) and 38% identity with B. subtilis MCPs within the C-terminal domain. The putative methylation sites parallel those of the B. subtilis MCPs, rather than those of the E. coli receptors. TlpC is methylated both in vivo and in vitro although the level of methylation is poor. In addition, the E. coli anti-Trg antibody is shown to cross-react with this membrane protein. Inactivation of the tlpC gene confirms that TlpC is not one of the previously characterized MCPs from B. subtilis. 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 B. subtilis arose., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-140-8-1847