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. 2022 Aug 25;23(Suppl 6):558. doi: 10.1186/s12864-022-08796-y

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© The Author(s) 2022

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — Structural analysis of HisR and TrpR regulators. A Alignment of TrpR repressor from E. coli and HisR protein from Eubacterium eligens. An asterisk marks identical residues. Pink boxes mark the position of alpha-helices in both structures. Helix-turn-helix (HTH) motif of DNA binding region is marked. Residues involved in contacts between TrpR and DNA operator within the HTH motif are shown in green (according to [28]). Tryptophan binding residues in TrpR are shown in purple (according to the 1ZT9 structure). B Pairwise structure alignment of E. coli TrpR (1ZT9) and E.eligens HisR (3G1C) obtained by the RCSB PDB web tool. C Sequence logo of the HTH motif in HisR proteins. Logo was built based on alignment of all analyzed HisR proteins from 492 genomes of Firmicutes and other lineages. Positively and negatively charged amino acids are shown in blue and red, respectively