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. 2019 Jan 4;13(4):1056–1071. doi: 10.1038/s41396-018-0332-5

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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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Fig. 5 — Hypothetical model of multiprotein complex (planctosome) involved in peptide degradation. The complex is tethered to extracellular membrane through a lamin A/C globular tail domain (LTD). The “anchoring” protein (2,210 aa) consists of a N-terminus signal peptide (26 aa) followed by the LTD, multiple proprotein convertase P-domains (PCD) divided by thrombospondin type 3 repeats (TSP), and a cohesin domain (CD). The “adaptor” protein contains a N-terminus signal peptide (26 aa), a dockerin domain (DD), a hyaline repeat domain (HYRD) and a cohesin (CD). The “adapter” binds Zn²⁺-dependent endo- (M12B Reprolysin4-like) and exopeptidases (M14 carboxypeptidase subfamily A) through Ca²⁺-dependent cohesin-dockerin interactions