The bacterial Tat system has a remarkable ability to transport folded proteins even enzyme complexes across the cytoplasmic membrane. It is structurally and mechanistically similar to the Delta pH-driven thylakoidal protein import pathway. A functional Tat system or Delta pH-dependent pathway requires three integral membrane proteins: TatA/Tha4, TatB/Hcf106 and TatC/cpTatC. The TatC protein is essential for the function of both pathways. It might be involved in twin-arginine signal peptide recognition, protein translocation and proton translocation. Sequence analysis predicts that TatC contains six transmembrane helices (TMHs), and experimental data confirmed that N- and C-termini of TatC or cpTatC are exposed to the cytoplasmic or stromal face of the membrane. The cytoplasmic N-terminus and the first cytoplasmic loop region of the Escherichia coli TatC protein are essential for protein export. At least two TatC molecules co-exist within each Tat translocon [[cite:PUB00011123]].
","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Twin-arginine_translocation_pathway","extract":"The twin-arginine translocation pathway is a protein export, or secretion pathway found in plants, bacteria, and archaea. In contrast to the Sec pathway which transports proteins in an unfolded manner, the Tat pathway serves to actively translocate folded proteins across a lipid membrane bilayer. In plants, the Tat translocase is located in the thylakoid membrane of the chloroplast, where it acts to export proteins into the thylakoid lumen. In bacteria, the Tat translocase is found in the cytoplasmic membrane and serves to export proteins to the cell envelope, or to the extracellular space. The existence of a Tat translocase in plant mitochondria is also proposed.
","thumbnail":null}],"literature":{"PUB00011123":{"PMID":12163163,"ISBN":null,"volume":"525","issue":"1-3","year":2002,"title":"Topology determination and functional analysis of the Escherichia coli TatC protein.","URL":null,"raw_pages":"65-70","medline_journal":"FEBS Lett","ISO_journal":"FEBS Lett.","authors":["Gouffi K","Santini CL","Wu LF."],"DOI_URL":"http://dx.doi.org/10.1016/S0014-5793(02)03069-7"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":28,"interactions":0,"matches":19252,"pathways":0,"proteins":18890,"proteomes":16293,"sets":0,"structural_models":{"alphafold":12534},"structures":11,"taxa":23768},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":502,"alignment:full":9634},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}