Fig. 1

Characterization of Leptospiral ligase A by in silico analysis: The hydrophobic regions in the protein are indicated by as patches (a-I) and the hydrophobicity residues are plotted graphically (a-II) where − 3 represents the most hydrophilic residues, while 3 represents the most hydrophobic ones. Amino acids imparting solubility and aggregating formation ability to LigA are presented with their relative scores in the figure (a-III), where positive and negative values indicate aggregate and soluble tendencies of the residues. (a-iv) and (a-v) The position of most soluble and aggregate-forming residues respectively. There is no transmembrane stretch present in the protein as predicted by TMHMM (b-1) and OCTOPUS servers (b-II). The protein was found to be non-membrane bound which confirms its cytosolic location (b-III, b-IV).This is further supported by the absence of any signal sequences as predicted by SignalP 5.0 server (c-I). The possible magnesium-binding regions are highlighted in red (c-II). (d-I) and (d-II) The domains present in the protein. Migration of the protein in a 2D gel electrophoresis is presented (e) which supports the physical characters predicted by the Swiss-Prot module