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. 2021 Jul 6;11:13909. doi: 10.1038/s41598-021-93158-z

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© The Author(s) 2021

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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Proposed model for the EcsAB mediated H1-resistance in S.haemolyticus. (A) RseP is a inner-membrane protease working together the ABC-transporter EcsAB to cleave the hormone prepeptide (Prephero) and export the mature hormone peptide (Phero) to the external milieu. RseP is acting also as the receptor for the bacteriocin H1 which forms pores and causes lethal cellular leakage across the membrane. (B) When rseP is mutated resulting in a non-functional receptor (RseP with glow), cells become resistant to H1. (C) When the ecs system is mutated, the malfunctional ABC transporter can no longer export the hormone peptide. This jammed situation of hormone prepeptide/peptide within the membrane results in a feedback (FB) loop somehow causing RseP inactivity. An inactive RseP (RseP with glow) loses its function as a bacteriocin receptor, and cells therefore become resistant to H1.