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. 2022 Aug 12;12:13726. doi: 10.1038/s41598-022-18059-1

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Protein structure of wild-type and mutant PA4673. Protein structures were derived from the amino acid sequences of wild-type and mutant PA4673 using Phyre2. The red box indicates the structural change caused by the SNP. Functional domain identification in both PA4673 isoforms indicates that they likely function as GTP-binding proteins. As the SNP causes an amino acid change in the exterior portion of the predicted protein structure, it may lead to alteration of a binding site or protein function.