| Accession | TIGR00115 |
| Name | tig |
| Function | trigger factor |
| Gene Symbol | tig |
| Trusted Cutoff | 180.20 |
| Domain Trusted Cutoff | 180.20 |
| Noise Cutoff | 154.50 |
| Domain Noise Cutoff | 154.50 |
| Isology Type | equivalog |
| EC Number | 5.2.1.8 |
| HMM Length | 410 |
| Mainrole Category | Protein fate |
| Subrole Category | Protein folding and stabilization |
| Gene Ontology Term | GO:0003755: peptidyl-prolyl cis-trans isomerase activity molecular_function |
| | GO:0005854: nascent polypeptide-associated complex cellular_component |
| | GO:0051082: unfolded protein binding molecular_function |
| | GO:0051083: 'de novo' cotranslational protein folding biological_process |
| Author | Anolik RT, Richardson DL, Haft DH |
| Entry Date | Apr 20 1999 2:10PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. |
| References | RN [1]
RM PMID:15837180
RT A cradle for new proteins: trigger factor at the ribosome.
RA Maier T, Ferbitz L, Deuerling E, Ban N
RL Curr Opin Struct Biol. 2005 Apr;15(2):204-12.
RN [2]
RM PMID:15175291
RT Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.
RA Kramer G, Rutkowska A, Wegrzyn RD, Patzelt H, Kurz TA, Merz F, Rauch T, Vorderwulbecke S, Deuerling E, Bukau B
RL J Bacteriol. 2004 Jun;186(12):3777-84.
DR PROSITE; PS00453; FKBP_PPIASE_1
DR PROSITE; PS00454; FKBP_PPIASE_2
DR PROSITE; PS50059; FKBP_PPIASE_3
DR PROSITE; PDOC00426
SE TIGR
DR HAMAP; MF_00303; 489 of 514 |
| Genome Property | GenProp0799: bacterial core gene set, exactly 1 per genome (HMM) |
