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. 2022 Jun 24;13:3627. doi: 10.1038/s41467-022-31144-3

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© The Author(s) 2022

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Sequence alignment of AimR^Kat and AimR^SPβ. Identical residues are in red colour. Structural elements are shown above and below of AimR^Kat and AimR^SPβ sequences, respectively, and labelled by helices for the former or domains for the latter. b Sequence alignment of AimP^Kat, AimR^SPβ and AimP^Phi. Mature AimPs are highlighted in red with differential positions between AimP^Kat and AimR^SPβ mature peptides underlined. c Sequences of DNA operators upstream of the putative aimX genes for AimR^Kat (aimX-box^Kat), AimR^SPβ (aimX-box^SPβ) and AimR^Phi (aimX-box^Phi), with the 6 bp inverted repeats highlighted in red. The two different positions between aimX-box^Kat and aimX-box^SPβ operator spacers are highlighted underlined. d EMSA analysis shown that both AimR^Kat and AimR^SPβ are able to recognise reciprocally their aimX operators but not the operator for phage phi3T. The AimR^Kat binding to its operator is specifically disrupted by AimP^Kat. EMSA assays have been repeated independently three times with similar results. Source data are provided as a Source Data file. e ITC measurement of AimR^Kat-AimP^Kat binding affinity. Thermogram is adjusted to two-binding site model and the two K_D (K_D1 and K_D2) values, one per monomer in the AimR dimer, are shown.