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| HAMAP annotation rule: MF_00303 |
| Accession |
MF_00303 |
| Dates |
1-JUN-2001 (Created) 21-NOV-2011 (Last updated, Version 23) |
| Protein name |
| RecName: |
Full=Trigger factor; Short=TF; EC=5.2.1.8; |
| AltName: |
Full=PPIase; |
|
FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).
case <OC:Escherichia> or <OC:Shigella>
SUBUNIT: Homodimer and monomer. In vivo most of the ribosomes are in complex with monomeric TF. Uncomplexed TF, however, is in a monomer-dimer equilibrium with approximately two thirds of TF existing in a dimeric state (By similarity).
end case
SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm (By similarity).
DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own (By similarity).
SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity.
GO:0006457; Biological process: protein folding.
GO:0015031; Biological process: protein transport.
| Size range: |
404-557 amino acids |
| Related UniRules: |
None |
| Template: |
P0A850 (TIG_ECOLI) |
| Scope: |
Bacteria |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
None |
| Plasmid encoded: |
None |
| Comments: |
Possible wrong start in AQUAE |
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