Recombinant Escherichia coli Sec-independent protein translocase protein TatB (tatB), partial

1. It has been concluded that Tat signal peptides play roles in substrate targeting and in triggering assembly of the active TatABC translocase. PMID: 28223511
2. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, the authors find that TatA also associates with TatC at the polar cluster site. PMID: 27914200
3. In vitro cross-linking of residues located in the periplasmically-oriented part of the TatBC receptor to TorA[KQ]-30aa-MalE reporter variants harboring a more hydrophobic h-region in their signal peptides confirmed that unlike in TorA[KQ]-30aa-MalE with an unaltered h-region, the mutated reporters moved deep into the TatBC-binding cavity. PMID: 28515319
4. Twin-arginine translocation (Tat) system TatA exhibits a uniform distribution throughout the inner membrane and that altering the expression of TatBC shows a uncharacterised distribution of TatA in the inner membrane. PMID: 28280110
5. we confirm the evidence of interactions between TatC fragments and DmsD chaperone. Using a peptide overlapping array, it was shown that the different NarJ subfamily REMPs interact with different regions of the TatB cytoplasmic domains PMID: 26826271
6. Distributed TatA thus may serve to accompany membrane-interacting Tat substrates to the few TatBC spots in the cells. PMID: 25774531
7. The data thus suggest that mature protein domains are translocated through a TatA and TaTB environment. PMID: 25003386
8. A physical interaction between TatC helix 5 and the TatB transmembrane helix was confirmed by the formation of a site-specific disulphide bond between TatC M205C and TatB L9C variants. PMID: 22742417
9. The transmembrane helix of TatA makes contacts with TatC and precursors recognized by the TatBC complex PMID: 22041896
10. data are consistent with TatB forming an oligomeric binding site that transiently accommodates folded Tat precursors PMID: 20926683
11. findigs show the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein; truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised PMID: 21237157
12. Data show that homo- and hetero-oligomeric complexes of the TatA, TatB and TatC integral membrane proteins were consistent with the current model of translocase assembly. PMID: 20169075
13. the TatABC complex of the twin-arginine translocase in Escherichia coli has specific roles in assembly and stability PMID: 15571732
14. the data indicate the presence of an additional form of Tat complex containing TatA and TatB, but not TatC PMID: 15663945
15. Since TatC is invariably complexed with TatB in wild-type complexes, the combined data demonstrate that TatABC complexes are uniformly distributed throughout the E. coli plasma membrane. PMID: 15728576
16. Data show that the integrity of the TatA TM span is vital for Tat activity, whereas that of TatB can accommodate large-scale distortions and only substitutions of P48 and F94 in TatC blocks activity. PMID: 15853811
17. analysis of substrate specificity of the TatB and TatC translocases with the consensus motif of a Tat signal peptide PMID: 17229735
18. tatABC and tatAC expression has a role in the formation of interacting cytoplasmic TatA tubes in Escherichia coli PMID: 18644791

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KEGG: ecj:JW5580

STRING: 316385.ECDH10B_4028