Protein Domain : Trigger factor/SurA domain superfamily IPR027304

Type	Homologous_superfamily
Description	The C-terminal domain of trigger factor and the peptide-binding domain of porin chaperone SurA share a multi-helical structure consisting of an irregular array of long and short helices.In the Escherichia coli cytosol, a fraction of the newly synthesised proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central PPIase domain with homology to FKBP proteins, and a C-terminal substrate-binding domain [ , ]. 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 [, ].The porin chaperon SurA facilitates correct folding of outer membrane proteins in Gram-negative bacteria [ , ].
Short Name	Trigger_fact/SurA_dom_sf