A DNA probe to the signaling domain of a halobacterial transducer for
phototaxis (HtrI) was used to clone and sequence four members of a new
family of transducer proteins (Htps) in Halobacterium salinarium pote
ntially involved in chemo- or phototactic signal transduction. The sig
naling domains in these proteins have 31-43% identity when compared wi
th each other or with their bacterial analogs, the methyl-accepting ch
emotaxis proteins. An additional region of homology found in three of
the Htps has 31-43% identity with HtrI. The Htps contain from 0 to 3 t
ransmembrane helices and Western blotting showed that HtpIII is solubl
e. The arrangement of the domains in these Htps suggests a modular arc
hitecture in their construction.