Q6MTF5 · TIG_MYCMS
- ProteinTrigger factor
- Genetig
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids428 (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
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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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 > Mycoplasmatota > Mollicutes > Mycoplasmataceae > Mycoplasma
Accessions
- Primary accessionQ6MTF5
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_0000179385 | 1-428 | Trigger factor | |||
Sequence: MIFAQEKFVDQGQGKWTVTIQDDQWTEFLKKAKNRLKTNLVVPGFRKGKAPESETAKYLTPIKIYNEAFKIVVKPAFDFALSQENKIQNDNSPTPVIVKVSDKEIVIDFIFDLVLELKVGEYKNITTVKKPVVEVNQEDVDNVIDMYRSRFAMQKEKQADDQIQKGDIVTFDFKGYVDDQAFEGGEAKDFVLEIGSNQFVPGFEDSMIGLKVGENQEINVKFPEEYIPSLAGKDAKFVLNIKNIKEKILPAKDDELVKDLNLPDITTYEQLEQKVKEDVLEQKTKISKSEFVENIIDEIIKTSEFQIPKTIIERQIKDVKKEFEDQLAQQKITLDKYKEITKITQEEIDEELKSDAIHRIKSFLVASEIKNKENIVASEEAINAKFEEFANLYGIEADKIKSLIDNQAIKHQVESELLETFIFENNGN |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 166-250 | PPIase FKBP-type | ||||
Sequence: GDIVTFDFKGYVDDQAFEGGEAKDFVLEIGSNQFVPGFEDSMIGLKVGENQEINVKFPEEYIPSLAGKDAKFVLNIKNIKEKILP |
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
- Length428
- Mass (Da)49,183
- Last updated2004-07-05 v1
- Checksum522953D63BAF7982
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX293980 EMBL· GenBank· DDBJ | CAE77081.1 EMBL· GenBank· DDBJ | Genomic DNA |