The binding targets of MalT consist of 10-nucleotide-long direct repeat sequences that possess conserved motifs; each monomer binds to one of these conserved sequences [13]. The gene malT is located upstream of the operon malPQ and in the opposite direction [6, 14, 22]. This transcriptional activator [23] belongs to the LuxR family of activators. MalT subunits consist of four domains: the C-terminal DNA-binding domain, the N-terminal ATP-binding domain, and two domains (DT2 and DT3) involved in effector recognition (maltotriose) [2, 24, 25, 26, 27]. Based on an alanine-scanning mutagenesis approach, it was shown that the inducer maltotriose binds inside the cavity of the tetratricopeptide-like sensor domain of MalT, a bacterial STAND transcription factor [19]. Maltotriose plays a dual role in signal transduction by MalT; it triggers nucleotide-binding oligomerization domain (NOD) opening and renders the MalT multimeric platform competent for downstream signaling [20]. MalT activity is negatively regulated by Aes and MalY through direct protein-protein interactions and competition with maltotriose for MalT binding [27, 28, 29, 30]. These characteristics point toward identical modes of action for MalY and Aes. However, the identification of an amino acid substitution in MalT that suppresses Aes inhibition without interfering with MalY inhibition suggests that the binding sites of the two inhibitory proteins are not the same [27, 29]. In addition, MalK inhibits maltotriose binding by MalT; interestingly, however, MalK interacts directly with MalT in the absence of maltotriose but not in the presence of maltotriose [2, 31]. A potential RNA G-quadruplex structure, formed by guanine-rich sequences located in the coding sequence region of the gene, was identified for malT. This structure could regulate the expression of the gene, as observed for hemL gene expression [32].