Multiple protein sequence alignments of <i>B</i>. <i>pseudomallei</i> QseB and QseC relative to homologous proteins from other <i>Burkholderia</i> species and <i>E</i>. <i>coli</i> O157:H7.

QseB and QseC amino acid sequences from B. pseudomallei K96243 (UniProt accession numbers: Q63WT5, Q63WT4) was compared with those from B. mallei ATCC 23344 (UniProt accession numbers: A0A0H2WJH0, A0A0H2WIM0), B. thailandensis E264 (UniProt accession numbers: Q2T0S0, Q2T0R9), B. cepacia ATCC25416 (UniProt accession numbers: A0A806UVQ1, A0A806V178), B. cenocepacia ATCCJ2315 (UniProt accession numbers: B4EA15, B4EA14), B. multivorans ATCC17616 (UniProt accession numbers: A0A0H3KLT5, A0A0H3KH15), B. gladioli (UniProt accession numbers: A0A095FGQ9, A0A095FGJ4), B. dolosa AU0158 (UniProt accession numbers: A2W7S9, A2W7T0), B. glumae BGR1 (UniProt accession numbers: C5ACR6, C5ACR5) and E. coli O157:H7 (UniProt accession numbers: Q8XBS3, Q8X524). Residues in the periplasmic domain of E. coli O157:H7 QseC that are conserved across QseC homologues from diverse bacteria are highlighted in yellow. The symbols demonstrate the scale of conservation, whereby asterisk (*) indicates a fully conserved residue, colon (:) indicates conservation between groups of strongly similar properties and period (.) indicates conservation between groups of weakly similar properties. The functional domains were predicted using a Simple Modular Architecture Research Tool or SMART (http://smart.embl.de). The functional regions were highlighted in different colors (green, receiver domain; blue, transcriptional regulatory domain; grey, transmembrane region; orange, HAMP domain; pink, histidine kinase domain; brown, histidine kinase-like ATPase). (PDF)