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. 2016 Oct 4;16:231. doi: 10.1186/s12866-016-0850-0

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© The Author(s). 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — Amino acid sequence alignment of cdPadR1 from Clostridium difficile R20291 (CDR20291_0991) and 630 (CD630_1154) with structural homologues listed by accession number as follows: 4ESB (bcPadR2) from Bacillus cereus ATCC 10987 [10], 4ESF (bcPadR1) from B. cereus ATCC 14579 [10], 3F8B (LmrR) from Lactococcus lactis MG1363 [11], and 1XMA (CtPadR) from Clostridium thermocellum (unpublished). cdPadR1 and CD630_1154 share 100 % amino acid sequence identity. Conserved residues are shaded black. Alpha helices are indicated by black bars and β-sheets are indicated with black arrows. The highly conserved W residue is demarcated with a black asterisk (*)