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Protein

Trigger factor

Gene

tig

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates (PubMed:24812405). Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.4 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).1 Publication

GO - Molecular functioni

  • peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc
  • protein binding involved in protein folding 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-HAMAP
  • protein unfolding Source: EcoCyc
  • response to heat Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciEcoCyc:EG11003-MONOMER.
ECOL316407:JW0426-MONOMER.
MetaCyc:EG11003-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Trigger factor (EC:5.2.1.81 Publication)
Short name:
TF
Alternative name(s):
PPIase
Gene namesi
Name:tig
Ordered Locus Names:b0436, JW0426
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11003. tig.

Subcellular locationi

  • 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

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Non-essential; synthetic lethality is seen in a triple tig-dnaK-dnaJ disruption, although this depends on temperature (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at all at 43 degrees) and strain background.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44 – 46FRK → AAA: Decreases association with ribosomes. 1 Publication3
Mutagenesisi140M → E: Significantly decreases antiaggregation activity. 1 Publication1
Mutagenesisi374 – 387MASAY…EVIEF → AASAAEDPKEAIEA: Significantly decreased affinity for substrate PhoA, significantly decreases antiaggregation activity. 1 PublicationAdd BLAST14

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001793471 – 432Trigger factorAdd BLAST432

Proteomic databases

EPDiP0A850.
PaxDbiP0A850.
PRIDEiP0A850.

2D gel databases

SWISS-2DPAGEP0A850.

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 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-544862,EBI-544862
ompAP0A9103EBI-544862,EBI-371347
rpsGP023593EBI-544862,EBI-543074

GO - Molecular functioni

  • protein binding involved in protein folding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259841. 463 interactors.
DIPiDIP-36226N.
IntActiP0A850. 125 interactors.
MINTiMINT-1225982.
STRINGi511145.b0436.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Beta strandi12 – 19Combined sources8
Helixi21 – 36Combined sources16
Helixi42 – 44Combined sources3
Beta strandi46 – 48Combined sources3
Helixi51 – 81Combined sources31
Beta strandi87 – 94Combined sources8
Beta strandi99 – 101Combined sources3
Beta strandi103 – 110Combined sources8
Turni120 – 122Combined sources3
Beta strandi127 – 129Combined sources3
Helixi134 – 147Combined sources14
Beta strandi155 – 157Combined sources3
Beta strandi163 – 166Combined sources4
Beta strandi168 – 174Combined sources7
Beta strandi183 – 188Combined sources6
Helixi198 – 201Combined sources4
Beta strandi202 – 204Combined sources3
Beta strandi210 – 216Combined sources7
Turni224 – 226Combined sources3
Beta strandi230 – 236Combined sources7
Helixi250 – 253Combined sources4
Turni254 – 257Combined sources4
Helixi263 – 297Combined sources35
Helixi304 – 319Combined sources16
Turni320 – 323Combined sources4
Helixi334 – 336Combined sources3
Helixi338 – 357Combined sources20
Helixi364 – 375Combined sources12
Helixi381 – 390Combined sources10
Helixi392 – 412Combined sources21
Beta strandi419 – 421Combined sources3
Helixi424 – 427Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L1PNMR-A148-249[»]
1OMSX-ray2.30A/B/C1-118[»]
1P9YX-ray2.15A/B1-118[»]
1W26X-ray2.70A/B1-432[»]
1W2BX-ray3.5051-144[»]
2MLXNMR-A1-432[»]
2MLYNMR-A1-432[»]
2MLZNMR-A1-432[»]
2VRHelectron microscopy19.00A1-432[»]
4URDelectron microscopy7.70A1-115[»]
ProteinModelPortaliP0A850.
SMRiP0A850.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A850.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini161 – 246PPIase FKBP-typeAdd BLAST86

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 112Ribosome-binding1 PublicationAdd BLAST112
Regioni148 – 251Dispensable for chaperone activity, although its removal significantly decreases antiaggregation activity2 PublicationsAdd BLAST104

Domaini

Consists of 3 domains; the N-terminus (residues 1-112) binds the ribosome, the middle domain (residues 150-246) has PPIase activity, while the discontinuous C-terminus (residues 113-149 and 247-432) binds substrate and has intrinsic chaperone activity on its own.2 Publications

Sequence similaritiesi

Belongs to the FKBP-type PPIase family. Tig subfamily.Curated
Contains 1 PPIase FKBP-type domain.Curated

Phylogenomic databases

eggNOGiENOG4105DEA. Bacteria.
COG0544. LUCA.
HOGENOMiHOG000218239.
InParanoidiP0A850.
KOiK03545.
OMAiKAQNDDK.
PhylomeDBiP0A850.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig. 1 hit.
InterProiIPR001179. PPIase_FKBP_dom.
IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003095. Trigger_factor. 1 hit.
SUPFAMiSSF102735. SSF102735. 1 hit.
SSF109998. SSF109998. 1 hit.
TIGRFAMsiTIGR00115. tig. 1 hit.
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A850-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:432
Mass (Da):48,193
Last modified:June 7, 2005 - v1
Checksum:i42C3E3C335074164
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti118Q → E in AAA62791 (PubMed:2211496).Curated1
Sequence conflicti279 – 287KSAIRNRVK → RAPSVTALS in AAA62791 (PubMed:2211496).Curated9

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.
PIRiD64773.
RefSeqiNP_414970.1. NC_000913.3.
WP_001198386.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73539; AAC73539; b0436.
BAE76216; BAE76216; BAE76216.
GeneIDi945081.
KEGGiecj:JW0426.
eco:b0436.
PATRICi32116025. VBIEscCol129921_0454.

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.
PIRiD64773.
RefSeqiNP_414970.1. NC_000913.3.
WP_001198386.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L1PNMR-A148-249[»]
1OMSX-ray2.30A/B/C1-118[»]
1P9YX-ray2.15A/B1-118[»]
1W26X-ray2.70A/B1-432[»]
1W2BX-ray3.5051-144[»]
2MLXNMR-A1-432[»]
2MLYNMR-A1-432[»]
2MLZNMR-A1-432[»]
2VRHelectron microscopy19.00A1-432[»]
4URDelectron microscopy7.70A1-115[»]
ProteinModelPortaliP0A850.
SMRiP0A850.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259841. 463 interactors.
DIPiDIP-36226N.
IntActiP0A850. 125 interactors.
MINTiMINT-1225982.
STRINGi511145.b0436.

2D gel databases

SWISS-2DPAGEP0A850.

Proteomic databases

EPDiP0A850.
PaxDbiP0A850.
PRIDEiP0A850.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73539; AAC73539; b0436.
BAE76216; BAE76216; BAE76216.
GeneIDi945081.
KEGGiecj:JW0426.
eco:b0436.
PATRICi32116025. VBIEscCol129921_0454.

Organism-specific databases

EchoBASEiEB0996.
EcoGeneiEG11003. tig.

Phylogenomic databases

eggNOGiENOG4105DEA. Bacteria.
COG0544. LUCA.
HOGENOMiHOG000218239.
InParanoidiP0A850.
KOiK03545.
OMAiKAQNDDK.
PhylomeDBiP0A850.

Enzyme and pathway databases

BioCyciEcoCyc:EG11003-MONOMER.
ECOL316407:JW0426-MONOMER.
MetaCyc:EG11003-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A850.
PROiP0A850.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig. 1 hit.
InterProiIPR001179. PPIase_FKBP_dom.
IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003095. Trigger_factor. 1 hit.
SUPFAMiSSF102735. SSF102735. 1 hit.
SSF109998. SSF109998. 1 hit.
TIGRFAMsiTIGR00115. tig. 1 hit.
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTIG_ECOLI
AccessioniPrimary (citable) accession number: P0A850
Secondary accession number(s): P15299
, P22257, P77603, Q2MBZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.