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ECOLI:TIG

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) tig
Protein Name(s) Trigger factor

TF PPIase

External Links
UniProt P0A850
EMBL M34066
U00096
AP009048
U82664
X17642
J05534
PIR D64773
RefSeq NP_414970.1
YP_488728.1
PDB 1L1P
1OMS
1P9Y
1W26
1W2B
2VRH
PDBsum 1L1P
1OMS
1P9Y
1W26
1W2B
2VRH
ProteinModelPortal P0A850
SMR P0A850
DIP DIP-36226N
IntAct P0A850
MINT MINT-1225982
STRING 511145.b0436
SWISS-2DPAGE P0A850
PaxDb P0A850
PRIDE P0A850
EnsemblBacteria AAC73539
BAE76216
GeneID 12930847
945081
KEGG ecj:Y75_p0424
eco:b0436
PATRIC 32116025
EchoBASE EB0996
EcoGene EG11003
eggNOG COG0544
HOGENOM HOG000218239
InParanoid P0A850
KO K03545
OMA KITFIID
OrthoDB EOG63VBX3
PhylomeDB P0A850
BioCyc EcoCyc:EG11003-MONOMER
ECOL316407:JW0426-MONOMER
MetaCyc:EG11003-MONOMER
EvolutionaryTrace P0A850
PRO PR:P0A850
Proteomes UP000000318
UP000000625
Genevestigator P0A850
GO GO:0005829
GO:0016020
GO:0042802
GO:0003755
GO:0044183
GO:0043022
GO:0051083
GO:0007049
GO:0051301
GO:0000413
GO:0015031
GO:0009408
Gene3D 1.10.3120.10
3.30.70.1050
HAMAP MF_00303
InterPro IPR001179
IPR005215
IPR008880
IPR008881
IPR027304
Pfam PF00254
PF05698
PF05697
PIRSF PIRSF003095
SUPFAM SSF102735
SSF109998
TIGRFAMs TIGR00115
PROSITE PS50059

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0016020

membrane

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11003
PANTHER:PTN001254607

P

Seeded From UniProt

complete

involved_in

GO:0051083

'de novo' cotranslational protein folding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11003
PANTHER:PTN001254607

P

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11003
PANTHER:PTN001254607

F

Seeded From UniProt

complete

involved_in

GO:0043335

protein unfolding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11003
PANTHER:PTN001254607

P

Seeded From UniProt

complete

enables

GO:0043022

ribosome binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11003
PANTHER:PTN001254607

F

Seeded From UniProt

complete

enables

GO:0003755

peptidyl-prolyl cis-trans isomerase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11003
PANTHER:PTN001254607

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A850

F

occurs_in:(GO:0005737)

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:9009267[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:24812405[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051083

'de novo' cotranslational protein folding

PMID:8633085[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:8633085[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:24812405[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043335

protein unfolding

PMID:24812405[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043335

protein unfolding

PMID:22921937[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0043022

ribosome binding

PMID:12226666[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043022

ribosome binding

PMID:8633085[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043022

ribosome binding

PMID:7588623[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043022

ribosome binding

PMID:12226666[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:24580753[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:3299381[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003755

peptidyl-prolyl cis-trans isomerase activity

PMID:8633085[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003755

peptidyl-prolyl cis-trans isomerase activity

PMID:7588623[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000413

protein peptidyl-prolyl isomerization

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003755

P

Seeded From UniProt

complete

involved_in

GO:0000413

protein peptidyl-prolyl isomerization

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0003755

P

Seeded From UniProt

complete

involved_in

GO:0000413

protein peptidyl-prolyl isomerization

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0003755

P

Seeded From UniProt

complete

involved_in

GO:0000413

protein peptidyl-prolyl isomerization

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0003755

P

Seeded From UniProt

complete

involved_in

GO:0000413

protein peptidyl-prolyl isomerization

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003755

P

Seeded From UniProt

complete

involved_in

GO:0000413

protein peptidyl-prolyl isomerization

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003755

P

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008880
InterPro:IPR008881
InterPro:IPR036611
InterPro:IPR037041

P

Seeded From UniProt

complete

involved_in

GO:0015031

protein transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005215
InterPro:IPR008880
InterPro:IPR008881
InterPro:IPR036611
InterPro:IPR037041

P

Seeded From UniProt

complete

enables

GO:0003755

peptidyl-prolyl cis-trans isomerase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:5.2.1.8

F

Seeded From UniProt

complete

enables

GO:0003755

peptidyl-prolyl cis-trans isomerase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000058592

F

Seeded From UniProt

complete

involved_in

GO:0015031

protein transport

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000058592

P

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000058592

P

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0413

F

Seeded From UniProt

complete

enables

GO:0003755

peptidyl-prolyl cis-trans isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0697

F

Seeded From UniProt

complete

involved_in

GO:0007049

cell cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0131

P

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0132

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ Scholz, C et al. (1997) Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16 54-8 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 Saio, T et al. (2014) Structural basis for protein antiaggregation activity of the trigger factor chaperone. Science 344 1250494 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 5.3 Hesterkamp, T et al. (1996) Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc. Natl. Acad. Sci. U.S.A. 93 4437-41 PubMed GONUTS page
  6. ↑ Hoffmann, A et al. (2012) Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding. Mol. Cell 48 63-74 PubMed GONUTS page
  7. ↑ 7.0 7.1 Kramer, G et al. (2002) L23 protein functions as a chaperone docking site on the ribosome. Nature 419 171-4 PubMed GONUTS page
  8. ↑ 8.0 8.1 Stoller, G et al. (1995) A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J. 14 4939-48 PubMed GONUTS page
  9. ↑ Krisko, A et al. (2014) Inferring gene function from evolutionary change in signatures of translation efficiency. Genome Biol. 15 R44 PubMed GONUTS page
  10. ↑ Crooke, E & Wickner, W (1987) Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form. Proc. Natl. Acad. Sci. U.S.A. 84 5216-20 PubMed GONUTS page
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