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. 2019 Sep 25;9:13816. doi: 10.1038/s41598-019-49975-4

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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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Protein alignment of S. thermophilus SMQ-301 MetAP with 4 other MetAP for which the structure is available. The WebLogo was only kept when the residue was conserved in all sequences. The secondary structures are represented over each sequence and diamonds indicate active sites and substrate binding sites. Red boxes highlight the mutations that provide phage resistance listed in Table 4. When linked, they occurred in the same MetAP mutant of S. thermophilus SMQ-301. Uniprot accession number of the protein sequences: E. coli K12 (P0AE18), Rickettsia prowazekii Madrid E (Q9ZCD3), S. pneumonia TIGR4 (B2IQ22) and M. tuberculosis H37Rv (P9WK19).