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. Author manuscript; available in PMC: 2010 Jun 1.
Published in final edited form as: J Struct Biol. 2009 Mar 24;166(3):303–315. doi: 10.1016/j.jsb.2009.03.009

Figure 1. Family sequence alignment of the first cytoplasmic domain of EpsF and selected T2SS homologues.

Figure 1

Identical residues are in red, similar residues according to the Risler matrix are in yellow. The predicted transmembrane helix (Met 171 – Val 192) is indicated with a green bar. The extent of the construct is marked with the black arrows above the sequences. The blue bar below the sequences indicates the solvent accessibility of each residue: dark blue is solvent exposed, white is buried. Residues involved in Ca2+-binding are marked with red triangles. Residues which are part of the dimer interface are marked with blue stars. Alpha-helical secondary structure symbols above the cyto1-EpsF sequence represent the observed structure in our experimental model.