Fig. 4

Predicted structure of CheR1 and CheR2 from H. titanicae KHS3. Amino acid sequences of both cheRs were modeled using Phyre2 server. a Comparison between the template and models. Structure of the template CheR from S. typhimurium (PDB accession code 1af7, left panel) and the models for CheR1 Ht (middle panel) and CheR2 Ht (right panel). Residues R98 and Y235 from CheR St or the equivalent positions in the models are shown as red spheres (see full alignment in Additional file 2: Figure S1). The β-subdomain that contains the loop responsible for interaction with chemoreceptor pentapeptides is colored fuchsia and the critical residue for this interaction (R197 in CheR St) is colored cyan. b Portion of the amino acid sequence alignment from CheR St (P07801), CheR Ec (P07364), CheR1 Pa (PA3348), CheR2 Pa (PA0175) and CheR3 Pa (PA0412), CheR1 Ht (RO22_21465) and CheR2 Ht (RO22_21165). Residues that constitute the β-loop responsible for interaction with chemoreceptor pentapeptides are highlighted fuchsia. Residue R197 from CheR St and its equivalents are highlighted cyan. For a complete alignment see Additional file 2: Figure S1