Figure 1
PP4397 exhibits limited sequence identity with YcgR but maintains key residues involved in c-di-GMP binding. (A) Schematic illustration of the domains and % identity of YcgR and PP4397/FlgZ as detailed in the text. (B) The amino acid sequence of PP4397 is shown with nine highly conserved residues of PilZ domains (highlighted in bold and underlined) that encompass the RXXXR and (D/N)XSXXG motifs of c-di-GMP binding-proficient type I PilZ domains34. Residues, which when substituted by alanine, essentially abolish c-di-GMP binding by PP4397/FlgZ25 are highlighted in grey. A complete alignment of PP4397 and YcgR as in15,25 using ESPript35 is shown in Fig. S1, while the extensive homology with FlgZ proteins of representative Pseudomonads is shown in Fig. S2.
