Protein Family Models

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)

Date:

2024-10-16

This HMM represents (Twin-Arginine Translocation B) of a Sec-independent system for transporting folded proteins, often with a bound redox cofactor, across the bacterial inner membrane. TatC is the multiple membrane spanning component. TatB, like the related TatA/E proteins, appears to span the membrane one time. The tat system recognizes proteins with an elongated signal sequence containing a conserved R-R in a motif approximated by RRxFLK N-terminal to the transmembrane helix. TIGRFAMs model TIGR01409 describes this twin-Arg signal sequence. A similar system, termed Delta-pH-dependent transport, operates on chloroplast-encoded proteins.

Gene:

tatB

Date:

2024-06-04

Sec-independent protein translocase subunit TatB, together with TatC, forms the binding site that directly interacts with Tat signal peptides within the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes

Date:

2018-07-02