title: Twin-arginine-specific protein export in Escherichia coli.
abstract: In many prokaryotic organisms, secretory proteins harboring a twin-arginine consensus motif are exported in a fully folded conformation via the twin-arginine translocation (Tat) pathway. In Escherichia coli, Tat involves the three structurally and functionally different membrane proteins TatA, TatB, and TatC. Whereas TatC proteins function in the specific recognition of substrate, TatA might be the major pore-forming subunit.
authors.affiliation: Institute of Biochemistry and Molecular Biology, University of Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany. matthias.mueller@biochemie.uni-freiburg.de
authors.forename: Matthias
authors.initials: M
authors.lastname: Müller
mesh_terms: D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000378:metabolism*; D021381:Protein Transport; D015398:Signal Transduction; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; C499697:TatA protein, E coli; C473116:TatB protein, E coli; C461379:TatC protein, E coli; C408585:twin-arginine translocase complex, E coli