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. 2018 Aug 17;9:1897. doi: 10.3389/fmicb.2018.01897

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Copyright © 2018 Winter, Born and Pfeifer.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Sequence alignment of GvpA, GvpJ, and GvpM and predicted structural models of these proteins. (A) Sequence alignment of A, J, and M including the α-helices and β-strands proposed. These structures are highlighted in gray. (B) 3D-structural model of GvpA (Strunk et al., 2011) and homology models of GvpJ and GvpM calculated by I-Tasser server (Zhang, 2008; Roy et al., 2010; Yang et al., 2015) based on the in silico model of GvpA. In the case of GvpM, the helices α1 through α3, as well as the fragments M(25N), M(25–59), and M(25C) are indicated and color-coded. N and C designate the N- or C-terminus of these proteins.