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. 2009 Nov 6;192(2):410–417. doi: 10.1128/JB.00553-09

FIG. 1.

FIG. 1.

Multiple sequence alignment of M. alcaliphilum 20Z EctR1 and representative MarR family members: SlyA, a regulator of virulence factors from Enterococcus faecalis (NCBI accession no. 1LJ9_A) (41); OhrR, a repressor of an organic hydroperoxide resistance determinant from Bacillus subtilis (13); MarR, a regulator of multiple antibiotic resistance from E. coli (P27245) (1); MexR, a multidrug efflux system transcriptional repressor from Pseudomonas aeruginosa (AAO40258) (22); and HucR, a repressor of the uricase genes from Deinococcus radiodurans (2FBK_A) (47). The alignment was generated using Clustal X, and the amino acid numbering was based on the HucR sequence. Number signs (#) above the sequence indicate residues identified from the MarR crystal structure as forming the hydrophobic core of the monomeric DNA binding domain (1). The HTH DNA-binding motif and flanking “wing 1” region identified from the MarR crystal structure are indicated below the alignment. Shaded and open bars represent alpha-helices and beta-sheets, respectively.