Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR008881 is a Trigger factor, ribosome-binding, bacterial.
<p>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<i>in vitro</i>. 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 [[cite:PUB00011507]]. This group of sequences contain the ribosomal subunit association domain.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Biological process | Protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. | ||
| Biological process | Protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: trigger factor-like [Cicer arietinum] gi|502127355|ref|XP_004499671.1| | 6 | ||
| – | PREDICTED: trigger factor-like [Glycine max] gi|356552817|ref|XP_003544759.1| | 11 | ||
| – | Trigger factor; TAIR: AT5G55220.1 trigger factor type chaperone family protein; Swiss-Prot: sp|Q8S9L5|TIG_ARATH Trigger factor-like protein TIG, Chloroplastic; TrEMBL-Plants: tr|I1JJE0|I1JJE0_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0024000 | 23 | ||
| – | Trigger factor-like protein, putative; TAIR: AT2G30695.1 bacterial trigger factor; Swiss-Prot: sp|Q5N1P5|TIG_SYNP6 Trigger factor; TrEMBL-Plants: tr|I3S2E8|I3S2E8_LOTJA Uncharacterized protein; Found in the gene: LotjaGi3g1v0501900 | 14 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| SignalP-TM | SignalP_GRAM_NEGATIVE | 1 | 25.00 |