A5EKB0 · TIG_BRASB
- ProteinTrigger factor
- Genetig
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids452 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Molecular Function | protein folding chaperone | |
Molecular Function | ribosome binding | |
Biological Process | 'de novo' cotranslational protein folding | |
Biological Process | cell division | |
Biological Process | chaperone-mediated protein folding | |
Biological Process | protein transport | |
Biological Process | protein unfolding |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTrigger factor
- EC number
- Short namesTF
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium
Accessions
- Primary accessionA5EKB0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_1000022649 | 1-452 | Trigger factor | ||
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 171-256 | PPIase FKBP-type | |||
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.
Sequence similarities
Belongs to the FKBP-type PPIase family. Tig subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length452
- Mass (Da)50,179
- Last updated2007-06-12 v1
- MD5 Checksum07D889EF109EBDC0E61BCE4FD8A682D9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000494 EMBL· GenBank· DDBJ | ABQ36604.1 EMBL· GenBank· DDBJ | Genomic DNA |