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. 2023 Sep 23;14:5947. doi: 10.1038/s41467-023-41719-3

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© The Author(s) 2023

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 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/.

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Fig. 1 — a Schematics showing the amino acid sequence characteristics of classical bacterial qs propeptides and LCPs. Ss—secretion signal sequence; cs—protease cleavage sites; cs with dashed lines—indicate the presence of additional cleavage sites in a subset of propeptides. b The unrooted phylogenetic tree comprises 953 RopB homologs and was inferred from a trimmed alignment of 204 sites. Blues dots indicate branches supported by >90% bootstraps. Branch lengths are proportional to the expected number of substitutions per site, as indicated by the scale bar at the top left. Each highlighted clan corresponds to receptors for which the most likely translated adjacent usORF encodes a remarkable class of qs peptides. The two Rgg clans (red and yellow) are enriched in receptor-SHP propeptide pairs, while the RopB clan (green) is enriched in receptor-LCP pairs. c The distribution of RopB-LCP, Rgg I-SHPs, and Rgg II - SHPs systems in different bacterial taxa.