Identification of TlpC, a novel 62 kDa MCP-like protein from Bacillus subtilis.
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.
Hanlon
D W
DW
Department of Biochemistry, University of Illinois, Urbana 61801-3618.
Rosario
M M
MM
Ordal
G W
GW
Venema
G
G
Van Sinderen
D
D
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification*; D001483:Base Sequence; D004926:Escherichia coli / Q000737:chemistry; D005798:Genes, Bacterial; D008565:Membrane Proteins / Q000737:chemistry; D000072236:Methyl-Accepting Chemotaxis Proteins; D008745:Methylation; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C089936:TlpC protein, Bacillus subtilis