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twin-arginine translocase TatA/TatE family subunit
Members of this protein family are involved in a sec independent translocation mechanism. This pathway has been called the DeltapH pathway in chloroplasts [2]. Members of this family in E.coli are involved in export of redox proteins with a "twin arginine" leader motif [1]. [1]. 9546395. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Weiner JH, Bilous PT, Shaw GM, Lubitz SP, Frost L, Thomas GH, Cole JA, Turner RJ;. Cell 1998;93:93-101. [2]. 9367960. Sec-independent protein translocation by the maize Hcf106 protein. Settles AM, Yonetani A, Baron A, Bush DR, Cline K, Martienssen R;. Science 1997;278:1467-1470. (from Pfam)
Sec-independent protein translocase subunit TatA
Sec-independent protein translocase subunit TatA may form the protein-conducting channel of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes
This HMM distinguishes TatA/E from the related TatB, but does not distinguish TatA from TatE. The Tat (twin-arginine translocation) system is a Sec-independent exporter for folded proteins, often with a redox cofactor already bound, across the bacterial inner membrane. Functionally equivalent systems are found in the chloroplast and some in archaeal species. The signal peptide recognized by the Tat system is modeled by TIGR01409.
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