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winged helix-turn-helix transcriptional regulator
MarR family transcriptional regulator
The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds [1]. The structure of MarR is known [2] and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif. [1]. 9068629. The Salmonella typhimurium mar locus: molecular and genetic. analyses and assessment of its role in virulence.. Sulavik MC, Dazer M, Miller PF;. J Bacteriol 1997;179:1857-1866.. [2]. 11473263. The crystal structure of MarR, a regulator of multiple. antibiotic resistance, at 2.3 A resolution.. Alekshun MN, Levy SB, Mealy TR, Seaton BA, Head JF;. Nat Struct Biol 2001;8:710-714. (from Pfam)
CodY helix-turn-helix domain
This family consists of the C-terminal helix-turn-helix domain found in several bacterial GTP-sensing transcriptional pleiotropic repressor CodY proteins. CodY has been found to repress the dipeptide transport operon (dpp) of Bacillus subtilis in nutrient-rich conditions [1]. The CodY protein also has a repressor effect on many genes in Lactococcus lactis during growth in milk [2]. [1]. 7783641. A gene required for nutritional repression of the Bacillus. subtilis dipeptide permease operon.. Slack FJ, Serror P, Joyce E, Sonenshein AL;. Mol Microbiol 1995;15:689-702.. [2]. 11401725. Pleiotropic transcriptional repressor CodY senses the. intracellular pool of branched-chain amino acids in Lactococcus. lactis.. Guedon E, Serror P, Ehrlich SD, Renault P, Delorme C;. Mol Microbiol 2001;40:1227-1239. (from Pfam)
HTH domain-containing protein
This family includes helix-turn-helix domains in a wide variety of proteins. (from Pfam)
CodY GAF-like domain
This domain is a GAF-like domain found at the N-terminus of several bacterial GTP-sensing transcriptional pleiotropic repressor CodY proteins. This domain is involved in GTP binding and also branched chain amino acids (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). CodY has been found to repress the dipeptide transport operon (dpp) of Bacillus subtilis in nutrient-rich conditions [1]. The CodY protein also has a repressor effect on many genes in Lactococcus lactis during growth in milk [2]. [1]. 7783641. A gene required for nutritional repression of the Bacillus. subtilis dipeptide permease operon.. Slack FJ, Serror P, Joyce E, Sonenshein AL;. Mol Microbiol 1995;15:689-702.. [2]. 11401725. Pleiotropic transcriptional repressor CodY senses the. intracellular pool of branched-chain amino acids in Lactococcus. lactis.. Guedon E, Serror P, Ehrlich SD, Renault P, Delorme C;. Mol Microbiol 2001;40:1227-1239. (from Pfam)
codY_Gpos family protein
GTP-sensing pleiotropic transcriptional regulator CodY
This model represents the full length of CodY, a pleiotropic repressor in Bacillus subtilis and other Firmicutes (low-GC Gram-positive bacteria) that responds to intracellular levels of GTP and branched chain amino acids. The C-terminal helix-turn-helix DNA-binding region is modeled by PF08222 in Pfam.
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