Chaperonins and chaperones including GroL (1.63 fold), GroS (3.49 fold), several heat shock proteins, etc. were also found to be relatively abundant in SK460 biofilm. Enhanced levels of chaperones ensure the proper protein folding which enables E. faecalis to thrive within the biofilm. Clp proteases involved in the degradation of misfolded proteins also showed elevated expression in biofilm stages. Several studies have proved the role of chaperone DnaK in curli-dependent biofilm formation and are considered as a potential target for anti-biofilm compounds [23–25].