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Bacillus subtilis  is a commensal member of the human oral and gut microbiomes, which can become infectious to immunocompromised patients. It possesses a conjugative transposon, ICE Bs1 , which includes &gt; 20 genes and can be passed by horizontal gene transfer to other bacteria, including pathogenic  Bacillus anthracis  and  Listeria monocytogenes . ICE Bs1  is regulated by the ImmR/ImmA tandem, which are a transcriptional repressor that constitutively blocks transcription and a metallopeptidase that acts as anti-repressor and inactivates ImmR by proteolytic cleavage. We here report the production and purification of 127-residue ImmR from ICE Bs1  and the crystal structure of its DNA-binding domain. It features a five-helix bundle centred on a helix-turn-helix motif potentially binding the major grove of double-stranded target DNA. ImmR shows structural and mechanistic similarity with the  B. subtilis  SinR repressor, which is engaged in sporulation inhibition.

Crystal structure report of the ImmR transcriptional regulator DNA-binding domain of the Bacillus subtilis ICEBs1 transposon