| IED ID | IndEnz0002001407 |
| Enzyme Type ID | protease001407 |
| Protein Name |
Trigger factor TF EC 5.2.1.8 PPIase |
| Gene Name | tig b0436 JW0426 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNIVAQRYGASVRQDVLGDLMSRNFIDAIIKEKINPAGAPTYVPGEYKLGEDFTYSVEFEVYPEVELQGLEAIEVEKPIVEVTDADVDGMLDTLRKQQATWKEKDGAVEAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELPELTAEFIKRFGVEDGSVEGLRAEVRKNMERELKSAIRNRVKSQAIEGLVKANDIDVPAALIDSEIDVLRRQAAQRFGGNEKQALELPRELFEEQAKRRVVVGLLLGEVIRTNELKADEERVKGLIEEMASAYEDPKEVIEFYSKNKELMDNMRNVALEEQAVEAVLAKAKVTEKETTFNELMNQQA |
| Enzyme Length | 432 |
| Uniprot Accession Number | P0A850 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:8633085}; |
| DNA Binding | |
| EC Number | 5.2.1.8 |
| Enzyme Function | FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates (PubMed:24812405). Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. {ECO:0000269|PubMed:12226666, ECO:0000269|PubMed:24812405, ECO:0000269|PubMed:8521806, ECO:0000269|PubMed:8633085}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (18); Chain (1); Domain (1); Helix (15); Modified residue (1); Mutagenesis (3); Region (2); Sequence conflict (2); Turn (4) |
| Keywords | 3D-structure;ADP-ribosylation;Cell cycle;Cell division;Chaperone;Cytoplasm;Direct protein sequencing;Isomerase;Reference proteome;Rotamase |
| Interact With | P0A910; P0A7M2; P02359; Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8633085}. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. {ECO:0000269|PubMed:8633085}. |
| Modified Residue | MOD_RES 45; /note=ADP-ribosylarginine; /evidence=ECO:0000269|PubMed:16112649 |
| Post Translational Modification | PTM: (Microbial infection) ADP-ribosylated by the phage T4 protein ModB. {ECO:0000269|PubMed:16112649}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (8); Electron microscopy (4); X-ray crystallography (4) |
| Cross Reference PDB | 1L1P; 1OMS; 1P9Y; 1W26; 1W2B; 2MLX; 2MLY; 2MLZ; 2VRH; 4URD; 5OWI; 5OWJ; 5ZR0; 6D6S; 7D6Z; 7D80; |
| Mapped Pubmed ID | 14656439; 15334087; 15690043; 16606699; 16858726; 18497744; 19737520; 19834901; 27320387; 29222465; 29714686; 30093407; 33761323; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,193 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16237 |
| Cross Reference Brenda |