Trigger_N

• PFAM accession number: PF05697
• Interpro abstract (IPR008881):

  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 at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains [ (PUBMED:12603737) ]. This group of sequences contain the ribosomal subunit association domain.

• GO process: protein folding (GO:0006457), protein transport (GO:0015031)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Trigger_N