A chemotaxis gene encoding a protein with receptorlike properties has been identified in Salmonella typhimurium and termed tip for taxis-involved protein. Based on the stringency of DNA hybridization, the tip gene has about 75% homology with a region of the tar gene encoding the cytoplasmic domain of the aspartate receptor. Introduction of the tip gene into a smooth-swimming Escherichia coli receptor mutant (tar tsr tap) restored both chemotaxis ability on soft-agar-tryptone plates and a wild-type swimming phenotype. We have shown, by overexpressing the CheY protein, that shifting of the mutant swimming bias in the absence of receptors is insufficient to restore chemotaxis ability. This suggests that in addition to resetting the swimming bias, the tip gene product functions as a receptor. By functional criteria, we found that Tip is not a duplicate aspartate (Tar) or serine (Tsr) receptor gene. Based on behavioral properties, the S. typhimurium Tip receptor provides functional features similar to those of the E. coli Tap receptor.Bacteria detect and respond to a variety of chemicals in their surroundings (4,16,27). The receptor genes for several of these chemoeffectors have been identified and cloned from Escherichia coli and Salmonella typhimurium strains. The membrane-bound primary receptors for aspartate and serine are encoded by the tar and tsr genes, respectively (25,26,33). The trg gene encodes a receptor which recognizes the ligand-occupied forms of the ribose-and galactosebinding proteins' (12). An additional gene with receptorlike properties, tap (taxis-associated protein) has been identified tandem to the E. coli aspartate receptor gene (3,25,34). The specificity of the tap receptor is not known, but it is not a duplicate aspartate or serine receptor gene (25).Recently, the sequences for the tar, tsr, tap, and trg receptor genes were determined (1, 2, 18, 24). The receptor sequences show a striking degree of structural homology (1, 18). Although the different receptors from both E. coli and S. typhimurium are homologous, this identity is more pronounced in certain regions of the sequence. In the carboxyterminal domains there is greater than 75% identity between the aspartate and serine receptors, yet in the amino-terminal halves the sequences diverge to less than 25% identity. This divergence probably reflects differences in substrate specificity. Therefore, for DNA hybridization a probe covering the carboxy-terminal region would be most likely to detect receptorlike sequences. Such an approach has been used to identify several potential receptor genes in the Salmonella chromosome (D. Clegg and D. E. Koshland, Jr., unpublished observations).In the initial cloning of chemotaxis genes from S. typhimurium, DeFranco and Koshland (9) isolated an EcoRI restriction fragment which complemented the chemotactic migration of a triple-receptor mutant (RP4372) on soft-agar plates containing tryptone (A. DeFranco, Ph.D. thesis, University of California, Berkeley, 1979). This mutant lacks the aspartate'(Tar), serine ...