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CadC C-terminal domain 1
CadC is an integral membrane protein of 512 amino acids comprising an N-terminal cytoplasmic DNA-binding domain, a transmembrane helix, and a C-terminal periplasmic domain. CadC belongs to the ToxR-like regulators that encompass biochemically non-modified one-component systems with similar gross topology, including several low pH-induced transcription regulators. Structural analysis of the C-terminal periplasmic domain indicates that it resembles the sensory domain of a (pH-activated) ToxR-like regulator. Furthermore, it is composed of two subdomains with a cavity at their interface that is suited to accommodate cadaverine, the feedback inhibitor of the Cad system. This is the N-terminal subdomain of the C-terminal periplasmic domain. It is composed of five-stranded beta-sheets [1]. [1]. 21308846. Crystal structure of the sensory domain of Escherichia coli CadC, a member of the ToxR-like protein family. Eichinger A, Haneburger I, Koller C, Jung K, Skerra A;. Protein Sci. 2011;20:656-669. (from Pfam)
winged helix-turn-helix domain-containing protein
lysine decarboxylation/transport transcriptional activator CadC
CadC, a transcriptional activator of the cadAB operon, is membrane-associated, with a single transmembrane span. In response to acid stress and the presence of sufficient lysine, it undergoes a cleavage and then activates expression of the lysine decarboxylase CadA and the lysine-cadaverine antiporter CadB.
transcriptional regulator
DNA-binding transcriptional regulator containing a winged helix-turn-helix domain
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