Part:BBa_K4781002
Tat A - Tat pathway protein
The twin arginine translocase (Tat) is a protein transport pathway that exists in archaea, bacteria, and plant chloroplasts. In bacteria, it exports proteins across the plasma membrane and is important for many processes, including energy metabolism, formation of the cell envelope, biofilm formation, heavy metal resistance, nitrogen-fixing symbiosis, bacterial pathogenesis and others [1], [2]. What makes this protein transport system unusual compared to other transport systems (such as the general secretory, or Sec pathway) is its ability to transport fully folded proteins across membranes. This remarkable feat has no requirement for ATP as an energy source and relies solely on the proton motive force (PMF).
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
| biology | The twin-arginine translocation (Tat) system accomplishes the remarkable feat of translocating large, even dimeric, proteins across tightly sealed energy-transducing membranes. All of the available evidence indicates that it is unique in terms of both structure and mechanism. In Escherichia coli and other Gram-negative bacteria, TatA, TatB, and TatC are all essential for efficient translocation, and current models suggest that separate TatABC and TatA complexes coalesce at the point of translocation. |
| chassis | E.coli |
| uniprot | P69428 |