Skip to main content
. Author manuscript; available in PMC: 2008 Nov 24.
Published in final edited form as: Mol Microbiol. 2007 Oct 9;66(4):930–947. doi: 10.1111/j.1365-2958.2007.05966.x

Fig. 4.

Fig. 4

Map of the TraI N-terminal region.

A. A SignalP 3.0 algorithm analysis of the Ng TraI amino acid sequence predicted the presence of a signal sequence (0.923 probability) with a cleavage site between Tyr21 and Leu22 (0.5 probability). The hydrophobic (h) region is interrupted by polar residues (P), which results in the secondary structure prediction of an amphipathic α helix (c, coil; h, helix; e, sheet).

B. Helical wheel of amino acids 5 to 12. Black font, white background represents amino acids in the polar side of the helix. White font, black background represents amino acids in the hydrophobic side. *Charged residues were introduced into the hydrophobic side of the predicted amphipathic α helix at positions 6 and 12 (L6K/L12K).