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. 2016 Mar 8;11(3):e0150234. doi: 10.1371/journal.pone.0150234

Fig 1. Domain organization of LuxR proteins that are classified into four sub-families based on domain architecture and mechanism of regulatory activation.

Fig 1

A. GacA is a LuxR-like protein in Pss B728a part of a global signal transduction system characterized as having an N-terminal receiver domain activated by phosphorylated and an C-terminal HTH DNA-binding domain that is characteristic of the first sub-family of LuxR-like proteins. B. AhlR is part of quorum sensing system in Pss B728a with AhlI. It has an N-terminal auto-inducer binding domain where hexanoyl-homoserine lactone binds to activate transcription of ahlI and has a C-terminal HTH DNA-binding domain. This domain organization is typical of the second sub-family of LuxRs associated with quorum sensing. C. Psyr_0993, which has not been characterized in Pss B728a, shares homology to malT in E. coli. These genes encode a subfamily of LuxR-like proteins have an N-terminal AAA ATPase domain that requires ATP for transcriptional activation and has a C-terminal HTH DNA binding domain. D. SyrG, which has been implicated in virulence and syringomycin production in Pss B728a lacks any defined N-terminal regulatory domain and has a C-terminal HTH DNA binding domain. This domain organization is typically seen in the fourth subfamily of LuxR-like proteins, which have not been fully defined functionally. LuxR-like proteins characterized in this family of LuxRs have been associated with secondary metabolism in Pss B728a.