Amyloid proteins have been known to be responsible for many neurodegenerative diseases of mammals including humans. Histopathologically, amyloid fibres are known to be formed due to mis-folds, mutations and other induction events concerned with these proteins in the patients. Once formed, these amyloid proteins have been well reported to undergo nucleation and form fibrous projections that result in cell-death. In living system (microorganisms and higher organisms alike), similar functional amyloid proteins are known to be produced with similar nucleation process. In this report the homologous proteins were created for functional amyloids from Escherichia coli, Bacillus thuringiensis, Bacillus atropheus, Streptococcus pyogenes and Dinoroseobacter shibae. Using the Z-dock server, analysed their interaction with each other. This report will help in understanding the self-folding and nucleation process of the functional amyloids in bacteria and further correlate the functional amyloids of bacteria with pathological amyloids in mammals.