| Description | This entry represents the cadmium(II) and/or lead(II) responsive transcriptional activator of the proteobacterial metal efflux system [ , ]. This protein contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X(6-9)-Cys, as well as a conserved and critical cysteine at the N-terminal end of the dimerization helix [].Pseudomonas aeruginosa CadR and Ralstonia metallidurans PbrR that regulate expression of the cadmium and lead resistance operons, are comprised of distinct domains that harbour the regulatory (effector-binding) site and the active (DNA-binding) site [ ]. Their conserved N-terminal domains contain predicted winged helix-turn-helix motifs that mediate DNA binding, while the C-terminal domains have the three conserved cysteines which form a putative metal binding site. Some members in this group have a histidine-rich C-terminal extension. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements []. | Name | Cd(II)/Pb(II)-responsive transcriptional regulator |
| Short Name | CadR-PbrR | Type | Family |
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