| General Information |
| MoonProt ID | 698 |
| First appeared in release | 4.0 |
| Name(s) | Trigger factor |
| UniProt ID | P0A850 |
| GO terms | "GO:0009408 response to heat
GO:0043335 protein unfolding
GO:0043335 protein unfolding
GO:0051083 'de novo' cotranslational protein folding
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0042802 identical protein binding
GO:0043022 ribosome binding
GO:0044183 protein folding chaperone
GO:0044183 protein folding chaperone
GO:0044183 protein folding chaperone
GO:0006457 protein folding
GO:0015031 protein transport
GO:0043335 protein unfolding
GO:0051083 'de novo' cotranslational protein folding
GO:0051301 cell division
GO:1990169 stress response to copper ion
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane" |
| Organisms for which functions have been demonstrated | Escherichia coli (strain K12) |
| Sequence length | 432.0 |
| FASTA sequence | >sp|P0A850|TIG_ECOLI Trigger factor OS=Escherichia coli (strain K12) OX=83333 GN=tig PE=1 SV=1 MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNIVAQRYGA SVRQDVLGDLMSRNFIDAIIKEKINPAGAPTYVPGEYKLGEDFTYSVEFEVYPEVELQGL EAIEVEKPIVEVTDADVDGMLDTLRKQQATWKEKDGAVEAEDRVTIDFTGSVDGEEFEGG KASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKV EERELPELTAEFIKRFGVEDGSVEGLRAEVRKNMERELKSAIRNRVKSQAIEGLVKANDI DVPAALIDSEIDVLRRQAAQRFGGNEKQALELPRELFEEQAKRRVVVGLLLGEVIRTNEL KADEERVKGLIEEMASAYEDPKEVIEFYSKNKELMDNMRNVALEEQAVEAVLAKAKVTEK ETTFNELMNQQA |
| Structure Information |
| PDB ID | 1L1P 1OMS 1P9Y 1W26 1W2B 2MLX 2MLY 2MLZ 2VRH 4URD 5OWI 5OWJ 5ZR0 6D6S 7D6Z 7D80 |
| Quaternary structure | homodimer |
| SCOP | "80292181W26 A
80415971W26 A
80252731OMS C:1-117
80376521OMS C:1-117
80292151W26 A:248-432
80292181W26 A:132-247
80415941W26 A:248-432
80415971W26 A:132-247" |
| CATH | "1l1pA00
1omsA00
1omsB00
1omsC00
1p9yA00
1p9yB00
1w26A01
1w26A02
1w26A03
1w26B01
1w26B02
1w26B03
1w2bJ00
1w2bK01
1w2bK02
1w2bL00
1w2bM00
1w2bN00
1w2bO01
1w2bO02
1w2bO03
1w2bP00
2mlxA01
2mlxA02
2mlxA03
2mlyA01
2mlyA02
2mlyA03
2mlzA01
2mlzA02
2mlzA03" |
| TM Helix Prediction | 0 |
| DisProt Annotation | |
| Predicted Disorder Regions | |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | enzyme, peptidyl-prolyl isomerase |
| References for function | Kramer G, Patzelt H, Rauch T, Kurz TA, Vorderwülbecke S, Bukau B, Deuerling E. Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. J Biol Chem. 2004 Apr 2;279(14):14165-70. doi: 10.1074/jbc.M313635200. Epub 2004 Jan 16. PMID: 14729669. |
| E.C. number | EC:5.2.1.8 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | chaperone |
| References for function | Kramer G, Patzelt H, Rauch T, Kurz TA, Vorderwülbecke S, Bukau B, Deuerling E. Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. J Biol Chem. 2004 Apr 2;279(14):14165-70. doi: 10.1074/jbc.M313635200. Epub 2004 Jan 16. PMID: 14729669. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | Cytosol |
| Comments | |