Fig. 3 | Nature Communications

Fig. 3

From: Discovery of a proteolytic flagellin family in diverse bacterial phyla that assembles enzymatically active flagella

Fig. 3

Sequence analysis and structural modeling of the proteolytic flagellin family. a Multiple alignment of 86 proteolytic flagellin sequences from 74 species, with key functional motifs depicted as sequence logos b including a putative Ca++ ion-binding site (left), the zinc-binding HExxH motif [includes the zinc-binding His233 and His237 and general base Glu234 for hydrolysis] (middle) and a motif containing the third zinc-binding residue, Glu262 (right). Sequence numbering is according to the FliA(H) sequence, UniProt entry Q8RR94. In addition, the hydrophobic basement-forming residue (Ala265) located below the active site zinc is also conserved. c Structural model of proteolytic flagella [FliA(H)-hypervariable region] from C. haemolyticum based on the peptidase domain of collagenase H from C. histolyticum (PDB 4ar1). d The zinc-binding HExxH motif and Ca++ ion-binding site with important residues labeled. e Peptide-docking model of FliA(H)-hypervariable region complexed with the nonapeptide (AVTYY↓LVIA) showing the scissile bond (↓). The peptide sequence is based on the consensus specificity motif derived from the PICS assay results

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