UniProtKB - P0A850 (TIG_ECOLI)
Trigger factor
tig
Functioni
Catalytic activityi
- EC:5.2.1.81 Publication
GO - Molecular functioni
- identical protein binding Source: IntAct
- peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc
- protein folding chaperone Source: EcoCyc
- ribosome binding Source: EcoCyc
GO - Biological processi
- 'de novo' cotranslational protein folding Source: EcoCyc
- cell cycle Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- chaperone-mediated protein folding Source: EcoCyc
- protein transport Source: UniProtKB-UniRule
- protein unfolding Source: EcoCyc
- response to heat Source: EcoCyc
Keywordsi
Molecular function | Chaperone, Isomerase, Rotamase |
Biological process | Cell cycle, Cell division |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11003-MONOMER MetaCyc:EG11003-MONOMER |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:tig Ordered Locus Names:b0436, JW0426 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Note: About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.1 Publication
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 44 – 46 | FRK → AAA: Decreases association with ribosomes. 1 Publication | 3 | |
Mutagenesisi | 140 | M → E: Significantly decreases antiaggregation activity. 1 Publication | 1 | |
Mutagenesisi | 374 – 387 | MASAY…EVIEF → AASAAEDPKEAIEA: Significantly decreased affinity for substrate PhoA, significantly decreases antiaggregation activity. 1 PublicationAdd BLAST | 14 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000179347 | 1 – 432 | Trigger factorAdd BLAST | 432 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 45 | ADP-ribosylarginine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
ADP-ribosylationProteomic databases
jPOSTi | P0A850 |
PaxDbi | P0A850 |
PRIDEi | P0A850 |
2D gel databases
SWISS-2DPAGEi | P0A850 |
Interactioni
Subunit structurei
Homodimer and monomer. In vivo most of the ribosomes are in complex with monomeric TF (PubMed:12452438); binding as a dimer has also been suggested (PubMed:12581648). Uncomplexed TF is in a monomer-dimer equilibrium with approximately two thirds of TF existing in a dimeric state; binding to substrate PhoA induces monomerization, 3 TF monomers bind somewhat independently to a single substrate molecule (PubMed:12452438, PubMed:24812405). TF and SRP can simultaneously bind to ribosomes; TF binding is abolished when SRP is bound to FtsY in the presence of a non-hydrolyzable GTP analog (PubMed:15148364). Contacts ribosomal proteins L23 and L29 (PubMed:12226666).
5 PublicationsBinary interactionsi
Hide detailsP0A850
With | #Exp. | IntAct |
---|---|---|
ompA [P0A910] | 3 | EBI-544862,EBI-371347 |
rpmB [P0A7M2] | 4 | EBI-544862,EBI-543024 |
rpsG [P02359] | 4 | EBI-544862,EBI-543074 |
itself | 2 | EBI-544862,EBI-544862 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4259841, 557 interactors |
DIPi | DIP-36226N |
IntActi | P0A850, 130 interactors |
STRINGi | 511145.b0436 |
Structurei
Secondary structure
3D structure databases
SMRi | P0A850 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A850 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 161 – 246 | PPIase FKBP-typeAdd BLAST | 86 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 112 | Ribosome-binding1 PublicationAdd BLAST | 112 | |
Regioni | 148 – 251 | Dispensable for chaperone activity, although its removal significantly decreases antiaggregation activity2 PublicationsAdd BLAST | 104 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0544, Bacteria |
HOGENOMi | CLU_033058_2_0_6 |
InParanoidi | P0A850 |
PhylomeDBi | P0A850 |
Family and domain databases
Gene3Di | 1.10.3120.10, 1 hit 3.30.70.1050, 1 hit |
HAMAPi | MF_00303, Trigger_factor_Tig, 1 hit |
InterProi | View protein in InterPro IPR001179, PPIase_FKBP_dom IPR005215, Trig_fac IPR008880, Trigger_fac_C IPR037041, Trigger_fac_C_sf IPR008881, Trigger_fac_ribosome-bd_bac IPR036611, Trigger_fac_ribosome-bd_sf IPR027304, Trigger_fact/SurA_dom_sf |
PANTHERi | PTHR30560, PTHR30560, 1 hit |
Pfami | View protein in Pfam PF00254, FKBP_C, 1 hit PF05698, Trigger_C, 1 hit PF05697, Trigger_N, 1 hit |
PIRSFi | PIRSF003095, Trigger_factor, 1 hit |
SUPFAMi | SSF102735, SSF102735, 1 hit SSF109998, SSF109998, 1 hit |
TIGRFAMsi | TIGR00115, tig, 1 hit |
PROSITEi | View protein in PROSITE PS50059, FKBP_PPIASE, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MQVSVETTQG LGRRVTITIA ADSIETAVKS ELVNVAKKVR IDGFRKGKVP
60 70 80 90 100
MNIVAQRYGA SVRQDVLGDL MSRNFIDAII KEKINPAGAP TYVPGEYKLG
110 120 130 140 150
EDFTYSVEFE VYPEVELQGL EAIEVEKPIV EVTDADVDGM LDTLRKQQAT
160 170 180 190 200
WKEKDGAVEA EDRVTIDFTG SVDGEEFEGG KASDFVLAMG QGRMIPGFED
210 220 230 240 250
GIKGHKAGEE FTIDVTFPEE YHAENLKGKA AKFAINLKKV EERELPELTA
260 270 280 290 300
EFIKRFGVED GSVEGLRAEV RKNMERELKS AIRNRVKSQA IEGLVKANDI
310 320 330 340 350
DVPAALIDSE IDVLRRQAAQ RFGGNEKQAL ELPRELFEEQ AKRRVVVGLL
360 370 380 390 400
LGEVIRTNEL KADEERVKGL IEEMASAYED PKEVIEFYSK NKELMDNMRN
410 420 430
VALEEQAVEA VLAKAKVTEK ETTFNELMNQ QA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 118 | Q → E in AAA62791 (PubMed:2211496).Curated | 1 | |
Sequence conflicti | 279 – 287 | KSAIRNRVK → RAPSVTALS in AAA62791 (PubMed:2211496).Curated | 9 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M34066 Genomic DNA Translation: AAA62791.1 U00096 Genomic DNA Translation: AAC73539.1 AP009048 Genomic DNA Translation: BAE76216.1 U82664 Genomic DNA Translation: AAB40192.1 X17642 Genomic DNA Translation: CAA35634.1 J05534 Genomic DNA Translation: AAA23587.1 |
PIRi | D64773 |
RefSeqi | NP_414970.1, NC_000913.3 WP_001198386.1, NZ_STEB01000007.1 |
Genome annotation databases
EnsemblBacteriai | AAC73539; AAC73539; b0436 BAE76216; BAE76216; BAE76216 |
GeneIDi | 58463319 945081 |
KEGGi | ecj:JW0426 eco:b0436 |
PATRICi | fig|1411691.4.peg.1840 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M34066 Genomic DNA Translation: AAA62791.1 U00096 Genomic DNA Translation: AAC73539.1 AP009048 Genomic DNA Translation: BAE76216.1 U82664 Genomic DNA Translation: AAB40192.1 X17642 Genomic DNA Translation: CAA35634.1 J05534 Genomic DNA Translation: AAA23587.1 |
PIRi | D64773 |
RefSeqi | NP_414970.1, NC_000913.3 WP_001198386.1, NZ_STEB01000007.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1L1P | NMR | - | A | 148-249 | [»] | |
1OMS | X-ray | 2.30 | A/B/C | 1-118 | [»] | |
1P9Y | X-ray | 2.15 | A/B | 1-118 | [»] | |
1W26 | X-ray | 2.70 | A/B | 1-432 | [»] | |
1W2B | X-ray | 3.50 | 5 | 1-144 | [»] | |
2MLX | NMR | - | A | 1-432 | [»] | |
2MLY | NMR | - | A | 1-432 | [»] | |
2MLZ | NMR | - | A | 1-432 | [»] | |
2VRH | electron microscopy | 19.00 | A | 1-432 | [»] | |
4URD | electron microscopy | 7.70 | A | 1-115 | [»] | |
5OWI | NMR | - | A/B | 1-432 | [»] | |
5OWJ | NMR | - | A/B | 1-432 | [»] | |
5ZR0 | NMR | - | A | 148-249 | [»] | |
6D6S | NMR | - | A/B | 1-432 | [»] | |
SMRi | P0A850 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259841, 557 interactors |
DIPi | DIP-36226N |
IntActi | P0A850, 130 interactors |
STRINGi | 511145.b0436 |
2D gel databases
SWISS-2DPAGEi | P0A850 |
Proteomic databases
jPOSTi | P0A850 |
PaxDbi | P0A850 |
PRIDEi | P0A850 |
Genome annotation databases
EnsemblBacteriai | AAC73539; AAC73539; b0436 BAE76216; BAE76216; BAE76216 |
GeneIDi | 58463319 945081 |
KEGGi | ecj:JW0426 eco:b0436 |
PATRICi | fig|1411691.4.peg.1840 |
Organism-specific databases
EchoBASEi | EB0996 |
Phylogenomic databases
eggNOGi | COG0544, Bacteria |
HOGENOMi | CLU_033058_2_0_6 |
InParanoidi | P0A850 |
PhylomeDBi | P0A850 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11003-MONOMER MetaCyc:EG11003-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A850 |
PROi | PR:P0A850 |
Family and domain databases
Gene3Di | 1.10.3120.10, 1 hit 3.30.70.1050, 1 hit |
HAMAPi | MF_00303, Trigger_factor_Tig, 1 hit |
InterProi | View protein in InterPro IPR001179, PPIase_FKBP_dom IPR005215, Trig_fac IPR008880, Trigger_fac_C IPR037041, Trigger_fac_C_sf IPR008881, Trigger_fac_ribosome-bd_bac IPR036611, Trigger_fac_ribosome-bd_sf IPR027304, Trigger_fact/SurA_dom_sf |
PANTHERi | PTHR30560, PTHR30560, 1 hit |
Pfami | View protein in Pfam PF00254, FKBP_C, 1 hit PF05698, Trigger_C, 1 hit PF05697, Trigger_N, 1 hit |
PIRSFi | PIRSF003095, Trigger_factor, 1 hit |
SUPFAMi | SSF102735, SSF102735, 1 hit SSF109998, SSF109998, 1 hit |
TIGRFAMsi | TIGR00115, tig, 1 hit |
PROSITEi | View protein in PROSITE PS50059, FKBP_PPIASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TIG_ECOLI | |
Accessioni | P0A850Primary (citable) accession number: P0A850 Secondary accession number(s): P15299 Q2MBZ0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 7, 2005 |
Last sequence update: | June 7, 2005 | |
Last modified: | April 7, 2021 | |
This is version 142 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families