van dijl et al 1992 have been identified in b subtilis it is suggested that signal peptide dependent protein secretion in b subtilis utilizes a sec pathway that is similar to that of e coli so far secb which is considered to be the major chaperone in e coli seems to be the only chaperone which has a direct binding affinity for seca and so contributes to the accurate targeting of the preprotein secb complex to the membrane bound translocase the secb protein is needed for only a subset of the envelope proteins so secb independent proteins will enter the sec pathway with the aid of helper proteins like groel groes dnak dnaj or other proteins like srp in eukaryotic organism srp mainly is responsible for the translocation across the er membrane recently more evidence has become available of the existence of an srp mediated secretion route in bacteria because the eukaryotic pathway has probably evolved from the bacteria it is thinkable that said proteins are also dependent on this pathway when said proteins are expressed in bacteria like bacillus thus optimisation of this particularly pathway in bacillus will be more profitable for heterologous eukaryotic proteins secretion than the optimisation of the well known sec pathway this invention relates to the cloning of the bacillus ftsy gene and its effect after over expression alone or in combination with other members of the bacterial srp upon heterologous proteins for the cloning of b subtillis ftsy degenerate primers were synthesized making use of the existing homology boxes between the sr u03b1 homologues of different organism fig2 a after an.