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. 2021 Dec 15;19:266. doi: 10.1186/s12915-021-01171-5

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© The Author(s) 2021

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. 7 — Structural features unique to SecY which enable signal binding and substrate translocation. SecY is G. thermodenitrificans SecY/proOmpA (6itc). a Signal-binding and ribosome-binding sites on SecY H2/3, viewed laterally. b The substrate translocation channel, viewed from its extracytoplasmic side. Only H1-5 and h4h5 of SecY are shown. SecY is colour-coded by consensus element as in Fig. 4 (left), or rendered transparent and superimposed by the corresponding elements of archaeal YidC (M. jannaschii MJ0480, 5c8j), aligned to the SecY C-half (right)