P47480 (TIG_MYCGE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Trigger factor Short name=TF EC=5.2.1.8 Alternative name(s): PPIase | ||||
| Gene names |
| ||||
| Organism | Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 243273 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma › ![]() |
Protein attributes
| Sequence length | 444 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. HAMAP-Rule MF_00303 |
| Catalytic activity | Peptidylproline (omega=180) = peptidylproline (omega=0). HAMAP-Rule MF_00303 |
| 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. HAMAP-Rule MF_00303 |
| 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. HAMAP-Rule MF_00303 |
| Sequence similarities | Belongs to the FKBP-type PPIase family. Tig subfamily. Contains 1 PPIase FKBP-type domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division |
| Cellular component | Cytoplasm |
| Molecular function | Chaperone Isomerase Rotamase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell divisionInferred from electronic annotation. Source: UniProtKB-KW protein foldingInferred from electronic annotation. Source: HAMAP protein peptidyl-prolyl isomerizationInferred from electronic annotation. Source: GOC protein transportInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||
Molecule processing | ||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 444 | 444 | Trigger factor HAMAP-Rule MF_00303 | PRO_0000179382 | ||||||||||||||||||
Regions | ||||||||||||||||||||||
| Domain | 170 – 255 | 86 | PPIase FKBP-type | |||||||||||||||||||
Secondary structure | ||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||
| Beta strand | 169 – 181 | 13 | ||||||||||||||||||||
| Beta strand | 192 – 198 | 7 | ||||||||||||||||||||
| Helix | 207 – 212 | 6 | ||||||||||||||||||||
| Beta strand | 216 – 222 | 7 | ||||||||||||||||||||
| Beta strand | 230 – 233 | 4 | ||||||||||||||||||||
| Helix | 234 – 236 | 3 | ||||||||||||||||||||
| Beta strand | 241 – 246 | 6 | ||||||||||||||||||||
Sequences
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References
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L43967 Genomic DNA. Translation: AAC71459.1. U01772 Genomic DNA. Translation: AAD10591.1. | ||||||||||||
| PIR | C64226. | ||||||||||||
| RefSeq | NP_072904.1. NC_000908.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P47480. | ||||||||||||
| SMR | P47480. Positions 166-250. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 243273.MG_238. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC71459; AAC71459; MG_238. | ||||||||||||
| GeneID | 875304. | ||||||||||||
| KEGG | mge:MG_238. | ||||||||||||
| PATRIC | 20009958. VBIMycGen98045_0275. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0544. | ||||||||||||
| KO | K03545. | ||||||||||||
| OMA | LVHEELM. | ||||||||||||
| ProtClustDB | CLSK335216. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | MGEN243273:GH2R-285-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 1.10.3120.10. 1 hit. 3.30.70.1050. 1 hit. | ||||||||||||
| HAMAP | MF_00303. Trigger_factor_Tig. | ||||||||||||
| InterPro | IPR001179. PPIase_FKBP_dom. IPR005215. Trig_fac. IPR008880. Trigger_fac_C. IPR008881. Trigger_fac_ribosome-bd_bac. IPR027304. Trigger_fact/SurA_dom. [Graphical view] | ||||||||||||
| Pfam | PF00254. FKBP_C. 1 hit. PF05698. Trigger_C. 1 hit. PF05697. Trigger_N. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF003095. Trigger_factor. 1 hit. | ||||||||||||
| SUPFAM | SSF109998. Trigger_fac_C_bac. 1 hit. SSF102735. Trigger_fac_ribosome-bd_bac. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00115. tig. 1 hit. | ||||||||||||
| PROSITE | PS50059. FKBP_PPIASE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P47480. | ||||||||||||
Entry information
| Entry name | TIG_MYCGE | ||||||||
| Accession | Primary (citable) accession number: P47480 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Mycoplasma genitalium Mycoplasma genitalium (strain G-37): entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
