Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family

Abstract

AbstractThe trigger factor of Escherichia coli is known as a chaperone protein which forms soluble complexes with the precursor to outer membrane protein A and assists in the maintenance of translocation competence. Sequence analysis shows that trigger factor contains a domain belonging to the FK506-binding protein (FKBP) family and possessing all the amino acids necessary for FK506 binding and peptidyl-prolyl cis-trans isomerase (Ppiase) activity. Consequently, this protein could be directly involved in the unfolding/folding processes occurring during translocation across the E. coli plasma membrane and, more generally, in facilitating protein folding. The central position of the FKBP domain within the trigger factor sequence as well as several original features of the loops surrounding the FK506-binding pocket are not found in any other FKBPs, making it undetectable by the Fkbp-Ppiase signature patterns