Novel bacterial rhodopsins from Haloarcula vallismortis.

New bacterial rhodopsins of the cruxrhodopsin (cR) tribe were identified in a type strain Haloarcula vallismortis. The genes encoding a bacteriorhodopsin-like ion pump (named cR-3), a halorhodopsin-like ion pump (chR-3) and a sensor rhodopsin (csR-3) were cloned and sequenced. Together with the data for vsRII (Seidel et al., Proc. Natl. Acad. Sci. USA 92, 3036-3040 (1995); cpR-3 in our notation), the primary structures of a set of four rhodopsins are now all known only in this species. They are separated by almost the same distances in homology, suggesting that they have derived from a single ancestral rhodopsin. The degree of conservation in the amino acid sequence of each helix showed that helices C and G are relatively well conserved in all rhodopsins, whereas helices DEF are conserved especially in sensor rhodopsin-I, possibly because these helices are needed for interaction with the transducer protein (Htr).