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Protein substrates are characterized by usually amino-terminal signal peptides harboring a conserved twin-arginine sequence motif. Phylogenetic analyses suggest that a Tat system was already present in the last universal common ancestor. Today, Tat systems are found in bacteria, archaea, and bacteria-derived organelles. Minimally, Tat systems are composed of one TatC-family component and one TatA\/B-family component, with multiple copies of these components forming the functional translocon, while more complex Tat systems exist that require additional homologs of TatA\/B or TatC. Due to its ability to translocate folded proteins with bound cofactors, the Tat system is essential for a wide range of important physiological pathways, such as many anaerobic respirations or photosynthesis. With a focus on evolutionary aspects, and by including recent structural and mechanistic insights, we herein review our current knowledge on this mechanistically unique translocation pathway.<\/jats:p>","DOI":"10.1093\/femsre\/fuag052","type":"journal-article","created":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T11:13:23Z","timestamp":1789989203000},"source":"Crossref","is-referenced-by-count":0,"title":["Tat-dependent protein translocation and its evolution"],"prefix":"10.1093","volume":"50","author":[{"given":"Thomas","family":"Br\u00fcser","sequence":"first","affiliation":[{"name":"Institute of Microbiology, Leibniz University Hannover , 30419 Hannover ,","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carsten","family":"Sanders","sequence":"additional","affiliation":[{"name":"Millersville University Department of Biology, , Millersville, PA 17551 ,","place":["USA"]},{"name":"Biology and Chemistry Programs, School of Science and Mathematics, HACC Central Pennsylvania\u2019s Community College , Harrisburg, PA 17110 ,","place":["USA"]},{"name":"Saint Joseph\u2019s University \u2013 Lancaster Campus Department of Chemistry and Biochemistry, , Lancaster, PA 17601 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,9,22]]},"reference":[{"key":"2026101610161720900_bib1","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"2026101610161720900_bib2","doi-asserted-by":"publisher","first-page":"E3650","DOI":"10.1073\/pnas.1306738110","article-title":"Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system","volume":"110","author":"Alcock","year":"2013","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026101610161720900_bib3","doi-asserted-by":"publisher","first-page":"e30127","DOI":"10.7554\/eLife.30127","article-title":"In vivo experiments do not support the charge zipper model for Tat translocase assembly","volume":"6","author":"Alcock","year":"2017","journal-title":"eLife"},{"key":"2026101610161720900_bib4","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/s0092-8674(03)00032-1","article-title":"Energetics of protein transport across biological membranes. 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