Gene Symbol: tatAD
Description: Sec-independent protein translocase protein TatAd
Species: Bacillus subtilis subsp. subtilis str. 168

Top Publications

  1. Jongbloed J, Grieger U, Antelmann H, Hecker M, Nijland R, Bron S, et al. Two minimal Tat translocases in Bacillus. Mol Microbiol. 2004;54:1319-25 pubmed
    ..Importantly, these minimal TatAC translocases of B. subtilis are representative for the Tat machinery of the vast majority of Gram-positive bacteria, Streptomycetes being the only known exception with TatABC translocases...
  2. Pop O, Westermann M, Volkmer Engert R, Schulz D, Lemke C, Schreiber S, et al. Sequence-specific binding of prePhoD to soluble TatAd indicates protein-mediated targeting of the Tat export in Bacillus subtilis. J Biol Chem. 2003;278:38428-36 pubmed
    ..for twin-arginine signal peptide containing phosphodiesterase PhoD of Bacillus subtilis consists of one TatA/TatC (TatAd/TatCd) pair of proteins...
  3. Hu Y, Zhao E, Li H, Xia B, Jin C. Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis. J Am Chem Soc. 2010;132:15942-4 pubmed publisher
    ..Moreover, the structure of TatA(d) revealed the structural importance of several conserved residues at the hinge region, thus shedding new light on further elucidation of the protein transport mechanism of the Tat system...
  4. Schreiber S, Stengel R, Westermann M, Volkmer Engert R, Pop O, M ller J. Affinity of TatCd for TatAd elucidates its receptor function in the Bacillus subtilis twin arginine translocation (Tat) translocase system. J Biol Chem. 2006;281:19977-84 pubmed publisher
    ..In addition, the presence of the substrate prePhoD was the prerequisite for appropriate localization in the cytosolic membrane of B. subtilis as demonstrated by freeze-fracture experiments...
  5. M ller S, De Angelis A, Walther T, Grage S, Lange C, Opella S, et al. Structural characterization of the pore forming protein TatAd of the twin-arginine translocase in membranes by solid-state 15N-NMR. Biochim Biophys Acta. 2007;1768:3071-9 pubmed publisher
    ..in the translocation mechanism, the structure and alignment in the membrane of the well-folded segments 2-45 of TatAd from Bacillus subtilis was studied here...
  6. Walther T, Grage S, Roth N, Ulrich A. Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy. J Am Chem Soc. 2010;132:15945-56 pubmed publisher
    ..This finding implies that the amphiphilic region of TatA is not just a flexible attachment to the transmembrane anchor but might be able to form intra- or even intermolecular salt-bridges, which could play a key role in pore assembly...
  7. Jongbloed J, Martin U, Antelmann H, Hecker M, Tjalsma H, Venema G, et al. TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway. J Biol Chem. 2000;275:41350-7 pubmed
    ..subtilis. ..
  8. Ridder A, de Jong E, Jongbloed J, Kuipers O. Subcellular localization of TatAd of Bacillus subtilis depends on the presence of TatCd or TatCy. J Bacteriol. 2009;191:4410-8 pubmed publisher
    ..Importantly, the localization of TatAd-GFP was similar when the protein was expressed from its own promoter under phosphate starvation conditions, ..
  9. Barnett J, Lawrence J, Mendel S, Robinson C. Expression of the bifunctional Bacillus subtilis TatAd protein in Escherichia coli reveals distinct TatA/B-family and TatB-specific domains. Arch Microbiol. 2011;193:583-94 pubmed publisher
    ..We have used a mutagenesis approach to delineate TatA/B-type domains in the bifunctional TatAd protein from Bacillus subtilis...

More Information


  1. Westermann M, Pop O, Gerlach R, Appel T, Schl rmann W, Schreiber S, et al. The TatAd component of the Bacillus subtilis twin-arginine protein transport system forms homo-multimeric complexes in its cytosolic and membrane embedded localisation. Biochim Biophys Acta. 2006;1758:443-51 pubmed publisher
    ..Here, the molecular organisation of soluble and membrane embedded Bacillus subtilis TatAd was analysed using negative contrast and freeze-fractured electron microscopy...