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. 2020 Apr 30;10:7384. doi: 10.1038/s41598-020-64115-z

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© The Author(s) 2020

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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Schematic representation of the putative role of PorE in anchoring T9SS to the bacterial cell wall. PorE is a lipoprotein composed of four domains (1: tetratricopeptide repeat domain (TPR), 2: β–propeller domain (WD40), 3: carboxypeptidase regulatory domain-like fold (CRD), and 4: OmpA_C-like putative peptidoglycan-binding domain). Therefore, PorE is anchored to the inner leaflet of the OM through its N-terminal acylation, and could interact with the peptidoglycan network through the C-terminal OmpA_C-like domain. Interaction with (a) putative T9SS component(s) could be mediated by the TPR and WD40 domains that are structural scaffolds often involved in protein-protein interactions. The figure was prepared using MICROSOFT PowerPoint (version 16.16.20).