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. 2020 Dec 1;11:573679. doi: 10.3389/fmicb.2020.573679

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Copyright © 2020 Luqman, Zabel, Rahmdel, Merz, Gruenheit, Harter, Nieselt and Götz.

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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SadA in TA-producing staphylococci is highly conserved. (A) We aligned multiple sequences of the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I) domain (accession cd06450) of SadA from species within the genus Staphylococcus and visualized using Jalview 2.11 (Letunic and Bork., 2019). The proposed PLP-binding domain (green) of SadA and the catalytic site Lysine (red) are highly conserved. (B) The 475 aa SadA sequence from S. pseudintermedius ED99 (WP_014612792) was used as a reference to identify homologs within the Staphylococcus genus using BLASTP. All best hits were used to construct the phylogenetic tree, using the Randomized Axelerated maximum-likelihood (RaxML) method (version8.2.9) (Sievers et al., 2011). Node support is indicated by bootstrap values from 100 resamplings of the alignment.