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. 2019 Feb 27;9:2927. doi: 10.1038/s41598-019-39654-9

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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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The 3D models, acetylation sites and representative spectra of LpqH (A,B) and AcpM (C,D). The glycosylation sites in LpqH are clustered in the N-terminus between residues 27–48 of the 159 amino acid protein (A). The four sites, T40, T41, S43 and S48 were located in this binding domain of LpqH. In AcpM, three sites in the helix, S41, S43 and T51, were found in the carrier protein (CP) domain profile (C). (he = hexose).