A0A2P7MU45 · A0A2P7MU45_9CYAN
- ProteinTrigger factor
- Genetig
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids474 (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
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Prochlorococcaceae > Cyanobium
Accessions
- Primary accessionA0A2P7MU45
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
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MSSAAAPAASPLSIKASPRP | ||||||
Domain | 180-242 | PPIase FKBP-type | ||||
Sequence: GDVAVLSFSGIYVDSGEAISGGSSDAMEVELEEGRMIPGFVEGVIGMAIGASKTIDCQFPESY | ||||||
Coiled coil | 378-405 | |||||
Sequence: ALKALAAAEAIEVEAKELETKIKEISRG | ||||||
Region | 441-474 | Disordered | ||||
Sequence: TEKAATPADADPDAAGEEQAKAKAKAKAKPAKAQ |
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.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length474
- Mass (Da)51,059
- Last updated2018-05-23 v1
- Checksum7995D488847147B2
Keywords
- Technical term