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winged helix DNA-binding protein
Rrf2 family transcriptional regulator
Several proteins in this family form iron-sulfur clusters enabling iron dependent DNA transcription regulation [1]. The iron binding is mediated by three conserved cysteine residues. Members of this family can also bind O-acetyl-L-serine, [Fe-S] and nitric oxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 23644595. Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity. Rajagopalan S, Teter SJ, Zwart PH, Brennan RG, Phillips KJ, Kiley PJ;. Nat Struct Mol Biol. 2013;20:740-747. (from Pfam)
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)
RrF2 family transcriptional regulator
RrF2 family transcriptional regulator similar to Desulfovibrio vulgaris regulatory protein Rrf2, iron-sulfur cluster assembly regulator IscR, and nitric oxide-responsive regulator NsrR
This HMM represents a superfamily of probable transcriptional regulators. One member, RRF2 of Desulfovibrio vulgaris is an apparent regulatory protein experimentally (MEDLINE:97293189). The N-terminal region appears related to the DNA-binding biotin repressor region of the BirA bifunctional according to results after three rounds of PSI-BLAST with a fairly high stringency.
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