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. 2015 Feb 27;15:4. doi: 10.1186/s12900-015-0031-7

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© Gorgel et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. 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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Sequence alignment and construct of Pil _Bac1 . A: Sequence alignment of the N-terminal part of Pil_Bac1 (Pil_Bac1NT) with the N-terminal parts of type pilins and pseudopilins. Type IV pilins: PilE from N. gonorrhoeae, PilA from P. aeruginosa; PilA from D. nodosus, PilA from G. sulfurreducens.; Pseudopilins: XcpT from P. aeruginosa; EpsG from V. cholerae; EtpG from E. coli; PulG from K. oxytoca. The protease cleavage site is marked with an arrow and the hydrophobic transmembrane helix is framed in red and the residues introducing kink2 in blue. The alignment was performed with the program MUSCLE installed in CLC Genomics Workbench 6.9.1 [53]. B: Construct of Pil_Bac1∆N. SP: leader sequence; TM HELIX: transmembrane α-helix; His₆: 6 residue long Histidine tag; EK: enterokinase cleavage site; TEV: TEV protease cleavage site. The aromatics and the cysteines are highlighted in red and blue in the sequence respectively.