Protein Domain : Trigger factor IPR005215

Type	Family
Description	The trigger factor is found in several prokaryotes, and is involved in protein export. Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. It acts as a chaperone by maintaining the newly synthesised protein in an open conformation. It consists of three domains, an N-terminal ribosome-binding domain (RBD), a central peptidyl-prolyl cis/trans isomerase (PPIase) domain and a C-terminal substrate-binding domain (SBD) which is stabilised by a linker between the RBD and PPIase domains [ , , ]. The association between its N-terminal domain with the ribosomal protein L23 located next to the peptide tunnel exit is essential for the interaction with nascent polypeptides and its in vivo function. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY) [].The trigger factor-like protein included in this entry can be found in plant chloroplasts, where it may be involved in protein export.
Short Name	Trig_fac