Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A850

- TIG_ECOLI

UniProt

P0A850 - TIG_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Trigger factor

Gene

tig

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 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.3 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc
  3. protein binding involved in protein folding Source: EcoCyc
  4. ribosome binding Source: EcoCyc

GO - Biological processi

  1. 'de novo' cotranslational protein folding Source: EcoCyc
  2. cell cycle Source: UniProtKB-KW
  3. cell division Source: UniProtKB-KW
  4. protein peptidyl-prolyl isomerization Source: GOC
  5. protein transport Source: UniProtKB-HAMAP
  6. 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:5.2.1.8)
Short name:
TF
Alternative name(s):
PPIase
Gene namesi
Name:tig
Ordered Locus Names:b0436, JW0426
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: 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.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 463FRK → AAA: Decreases association with ribosomes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Trigger factorPRO_0000179347Add
BLAST

Proteomic databases

PaxDbiP0A850.
PRIDEiP0A850.

2D gel databases

SWISS-2DPAGEP0A850.

Expressioni

Gene expression databases

GenevestigatoriP0A850.

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. 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).4 Publications

Binary interactionsi

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

Protein-protein interaction databases

DIPiDIP-36226N.
IntActiP0A850. 125 interactions.
MINTiMINT-1225982.
STRINGi511145.b0436.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76
Beta strandi12 – 198
Helixi21 – 3616
Helixi42 – 443
Beta strandi46 – 483
Helixi51 – 8131
Beta strandi87 – 948
Beta strandi99 – 1013
Beta strandi103 – 1108
Turni120 – 1223
Beta strandi127 – 1293
Helixi134 – 14714
Beta strandi155 – 1573
Beta strandi163 – 1664
Beta strandi168 – 1747
Beta strandi183 – 1886
Helixi198 – 2014
Beta strandi202 – 2043
Beta strandi210 – 2167
Turni224 – 2263
Beta strandi230 – 2367
Helixi250 – 2534
Turni254 – 2574
Helixi263 – 29735
Helixi304 – 31916
Turni320 – 3234
Helixi334 – 3363
Helixi338 – 35720
Helixi364 – 37512
Helixi381 – 39010
Helixi392 – 41221
Beta strandi419 – 4213
Helixi424 – 4274

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
2VRHelectron microscopy19.00A1-432[»]
ProteinModelPortaliP0A850.
SMRiP0A850. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A850.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini161 – 24686PPIase FKBP-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 251104Dispensable for chaperone activityAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0544.
HOGENOMiHOG000218239.
InParanoidiP0A850.
KOiK03545.
OMAiMQVSVEN.
OrthoDBiEOG63VBX3.
PhylomeDBiP0A850.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181Q → E in AAA62791. (PubMed:2211496)Curated
Sequence conflicti279 – 2879KSAIRNRVK → RAPSVTALS in AAA62791. (PubMed:2211496)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_488728.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73539; AAC73539; b0436.
BAE76216; BAE76216; BAE76216.
GeneIDi12930847.
945081.
KEGGiecj:Y75_p0424.
eco:b0436.
PATRICi32116025. VBIEscCol129921_0454.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_488728.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2VRH electron microscopy 19.00 A 1-432 [» ]
ProteinModelPortali P0A850.
SMRi P0A850. Positions 1-432.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36226N.
IntActi P0A850. 125 interactions.
MINTi MINT-1225982.
STRINGi 511145.b0436.

2D gel databases

SWISS-2DPAGE P0A850.

Proteomic databases

PaxDbi P0A850.
PRIDEi P0A850.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73539 ; AAC73539 ; b0436 .
BAE76216 ; BAE76216 ; BAE76216 .
GeneIDi 12930847.
945081.
KEGGi ecj:Y75_p0424.
eco:b0436.
PATRICi 32116025. VBIEscCol129921_0454.

Organism-specific databases

EchoBASEi EB0996.
EcoGenei EG11003. tig.

Phylogenomic databases

eggNOGi COG0544.
HOGENOMi HOG000218239.
InParanoidi P0A850.
KOi K03545.
OMAi MQVSVEN.
OrthoDBi EOG63VBX3.
PhylomeDBi P0A850.

Enzyme and pathway databases

BioCyci EcoCyc:EG11003-MONOMER.
ECOL316407:JW0426-MONOMER.
MetaCyc:EG11003-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A850.
PROi P0A850.

Gene expression databases

Genevestigatori P0A850.

Family and domain databases

Gene3Di 1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPi MF_00303. Trigger_factor_Tig.
InterProi IPR001179. PPIase_FKBP_dom.
IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view ]
Pfami PF00254. FKBP_C. 1 hit.
PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF003095. Trigger_factor. 1 hit.
SUPFAMi SSF102735. SSF102735. 1 hit.
SSF109998. SSF109998. 1 hit.
TIGRFAMsi TIGR00115. tig. 1 hit.
PROSITEi PS50059. FKBP_PPIASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Trigger factor depletion or overproduction causes defective cell division but does not block protein export."
    Guthrie B., Wickner W.
    J. Bacteriol. 172:5555-5562(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene."
    Aldea M., Garrido T., Hernandez-Chico C., Vicente M., Kushner S.R.
    EMBO J. 8:3923-3931(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-145.
  6. "ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle."
    Crooke E., Guthrie B., Lecker S., Lill R., Wickner W.
    Cell 54:1003-1011(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-13.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-21 AND 38-58.
    Strain: K12 / EMG2.
  8. "Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains."
    Hesterkamp T., Hauser S., Lutcke H., Bukau B.
    Proc. Natl. Acad. Sci. U.S.A. 93:4437-4441(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-7, FUNCTION AS A PPIASE, SUBCELLULAR LOCATION, RIBOSOME-BINDING.
  9. "An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity."
    Stoller G., Tradler T., Ruecknagel K.P., Rahfeld J.-U., Fischer G.
    FEBS Lett. 384:117-122(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 145-174.
  10. "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli."
    Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B., Gottesman S.
    J. Biol. Chem. 265:12536-12545(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 390-432.
  11. "Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides."
    Valent Q.A., Kendall D.A., High S., Kusters R., Oudega B., Luirink J.
    EMBO J. 14:5494-5505(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  13. "Three-state equilibrium of Escherichia coli trigger factor."
    Patzelt H., Kramer G., Rauch T., Schonfeld H.J., Bukau B., Deuerling E.
    Biol. Chem. 383:1611-1619(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  14. Cited for: BINDING TO RIBOSOMAL PROTEINS L23 AND L29, MUTAGENESIS OF 44-PHE--LYS-46.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  15. "Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome."
    Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.
    J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKS TO NASCENT PROTEIN CHAINS.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  16. "In vivo analysis of the overlapping functions of DnaK and trigger factor."
    Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S., Hartl F.U., Georgopoulos C.
    EMBO Rep. 5:195-200(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, DISPENSABILITY OF PPIASE FOR CHAPERONE FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  17. "Localization of the trigger factor binding site on the ribosomal 50S subunit."
    Blaha G., Wilson D.N., Stoller G., Fischer G., Willumeit R., Nierhaus K.H.
    J. Mol. Biol. 326:887-897(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MAY BIND TO THE RIBOSOME AS A DIMER.
    Strain: MRE-600.
  18. "Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor."
    Buskiewicz I., Deuerling E., Gu S.-Q., Joeckel J., Rodnina M.V., Bukau B., Wintermeyer W.
    Proc. Natl. Acad. Sci. U.S.A. 101:7902-7906(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMULTANEOUS BINDING OF TRIGGER FACTOR AND SRP TO THE RIBOSOME.
    Strain: MRE-600.

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: October 29, 2014
This is version 96 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

External Data

Dasty 3