Dissociation between the critical role of ClpB of Francisella tularensis for the heat shock response and the DnaK interaction and its important role for efficient type VI secretion and bacterial virulence
Fig 5
Sequence alignment and structural comparison of the N-terminals of V. cholerae ClpV and VipB with F. tularensis ClpB and IglB.
(A). ClpV and ClpB sequences were retrieved from NCBI (https://www.ncbi.nlm.nih.gov/) and sequence alignments were performed using MAFFT (https://mafft.cbrc.jp/alignment/server/), and the corresponding image was generated using the web server ESPript 3 (http://espript.ibcp.fr). The first 174 amino acids (156 for Francisella ClpB) of the N-terminal domain of the ClpV-ClpB alignment is shown. Secondary structures as predicted for V. cholerae ClpV are displayed above the alignment. (B). The VipB and IglB sequences were retrieved from NCBI (https://www.ncbi.nlm.nih.gov/), and essentially the same procedure for alignment was performed as aforementioned. The first 110 amino acids, including the N-terminal domain (1–95 aa), of the VipB-IglB alignment is shown. Secondary structure elements as predicted for V. cholerae VipB are displayed above the alignment. The VipB α-helix known to interact with the ClpV N-terminal is boxed and highlighted in yellow. Conserved consensus sequence residues that contribute to the interaction with the ClpV-N-terminal are boxed and colored in yellow in helix 1. Identical amino acids are highlighted with red color. (C). Ribbon view of the F. tularensis IglB (IglB in pink; PDB: 3j9o) superimposed on the V. cholerae VipB (VipB in blue; PDB: 5mxn).