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. 2015 Jun 3;14:74. doi: 10.1186/s12934-015-0263-z

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© Gratz et al. 2015

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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Structure of the a CK2α- and b CK2β-autotransporter fusion proteins. The restriction endonuclease recognition sites that were used for construction of the corresponding fusion genes are annotated and surrounding DNA- and amino acid sequences are given. The fusion protein domain sequence is as follows: the N-terminal signal peptide is needed for translocation through the bacterial inner membrane (sequence in italics) and is cut subsequently, the open reading frames of CK2α (a) or CK2β (b) are referred to as the passenger domain, which is supposed to be presented at the cell surface (given in bold letters). Linker and β-barrel domain facilitate translocation through and anchoring in the outer membrane.