A0A225CNF0 · A0A225CNF0_9MICO
- ProteinTrigger factor
- Genetig
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids483 (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 > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Clavibacter
Accessions
- Primary accessionA0A225CNF0
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 domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 165-211 | PPIase FKBP-type | ||||
Sequence: GDFVQIDLTATIAGNAVDTASGISYELGSGDLIDGIDEALESLTAGE | ||||||
Region | 432-483 | Disordered | ||||
Sequence: TEEPADADAEAVVADAPAEEASAPAAEEAPVEKPKKKAAPKKKAAEKAADSE |
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
- Length483
- Mass (Da)52,581
- Last updated2017-10-25 v1
- ChecksumBAA741CE73971776