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. 2023 Feb 2;30:9. doi: 10.1186/s12929-023-00902-w

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© The Author(s) 2023

Open AccessThis 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/. 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 in a credit line to the data.

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Fig. 2 — Multiple sequence alignment of the N-terminal region (1–360 aa) of representative TpsA proteins using CLUSTAL omega (https://www.ebi.ac.uk/Tools/msa/clustalo/). The numbering on the left corresponds to the amino acid number for each protein. N terminal amino acid residues of TpsA proteins (TpsA1 to 6) of P. aeruginosa were compared with, B. pertussis FHA protein (A) and H. influenzae HMW1 protein (B). Bold line indicates the position of motifs that have been identified in N-terminal TPS domains that are important for the secretion of TpsA proteins