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. 2019 Jan 17;9:154. doi: 10.1038/s41598-018-36427-8

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© The Author(s) 2019

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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Modular organization of type-I CdiA proteins. (a) The cladogram was generated from a ClustalW alignment of the reported proteins. ESPR (extended signal peptide region), TPS (two-partner secretion domain), HET (Heterogeneity region), DUF637 (domain of unknown function 637), PT-VENN (pretoxin PT-VENN domain) and CT (C-terminal toxic region) are shown. Homologous protein regions are coloured similarly. Similar CT regions are outlined (b) Coiled-coil conformation of pit-A4 and bau-B4 CdiA proteins predicted by the MARCOIL program. (c) Swapping of HET modules. Chimeric pit-A5 and pit-A4 proteins are shown. (d) Chimeric pit-B5 CdiA proteins. In panels a, c and d the proteins are not drawn to scale.