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. 2017 Jun 2;8:941. doi: 10.3389/fmicb.2017.00941

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Copyright © 2017 Xu, He, Zhang, Guo and Kong.

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) or licensor 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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Multiple sequence alignment of FaeLam, FaeLac, FaeLfa, FaeLfe, and Lj0536, with the classical serine esterase catalytic motif GXSXG in the box. Lj0536 is an FAE derived from L. johnsonii N6.2. Asterisk indicates that amino acid residues are conserved in all proteins. The proteins of FaeLam, FaeLac, FaeLfa and FaeLfe showed sequence identity in the range of 45–85%, and sequence identity with Lj0536 from 44 to 71%. Alignment was done using Clustal W with the algorithm of Myers and Miller, and the percentage of similarity was calculated using BioEdit software.