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P0A850 (TIG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trigger factor

Short name=TF
EC=5.2.1.8
Alternative name(s):
PPIase
Gene names
Name:tig
Ordered Locus Names:b0436, JW0426
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 (Ref.14). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. Ref.8 Ref.11 Ref.16

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). HAMAP-Rule MF_00303

Subunit structure

Homodimer and monomer. In vivo most of the ribosomes are in complex with monomeric TF (Ref.13); binding as a dimer has also been suggested (Ref.17). 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 (Ref.18). Contacts ribosomal proteins L23 and L29 (Ref.14). Ref.13

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. Ref.8

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. Ref.16

Disruption phenotype

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. Ref.16

Sequence similarities

Belongs to the FKBP-type PPIase family. Tig subfamily.

Contains 1 PPIase FKBP-type domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Trigger factor HAMAP-Rule MF_00303
PRO_0000179347

Regions

Domain161 – 24686PPIase FKBP-type
Region148 – 251104Dispensable for chaperone activity HAMAP-Rule MF_00303

Experimental info

Mutagenesis44 – 463FRK → AAA: Decreases association with ribosomes. Ref.14
Sequence conflict1181Q → E in AAA62791. Ref.1
Sequence conflict279 – 2879KSAIRNRVK → RAPSVTALS in AAA62791. Ref.1

Secondary structure

................................................................ 432
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A850 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 42C3E3C335074164

FASTA43248,193
        10         20         30         40         50         60 
MQVSVETTQG LGRRVTITIA ADSIETAVKS ELVNVAKKVR IDGFRKGKVP MNIVAQRYGA 

        70         80         90        100        110        120 
SVRQDVLGDL MSRNFIDAII KEKINPAGAP TYVPGEYKLG EDFTYSVEFE VYPEVELQGL 

       130        140        150        160        170        180 
EAIEVEKPIV EVTDADVDGM LDTLRKQQAT WKEKDGAVEA EDRVTIDFTG SVDGEEFEGG 

       190        200        210        220        230        240 
KASDFVLAMG QGRMIPGFED GIKGHKAGEE FTIDVTFPEE YHAENLKGKA AKFAINLKKV 

       250        260        270        280        290        300 
EERELPELTA EFIKRFGVED GSVEGLRAEV RKNMERELKS AIRNRVKSQA IEGLVKANDI 

       310        320        330        340        350        360 
DVPAALIDSE IDVLRRQAAQ RFGGNEKQAL ELPRELFEEQ AKRRVVVGLL LGEVIRTNEL 

       370        380        390        400        410        420 
KADEERVKGL IEEMASAYED PKEVIEFYSK NKELMDNMRN VALEEQAVEA VLAKAKVTEK 

       430 
ETTFNELMNQ QA 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"L23 protein functions as a chaperone docking site on the ribosome."
Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B.
Nature 419:171-174(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRD64773.
RefSeqNP_414970.1. NC_000913.3.
YP_488728.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0A850.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36226N.
IntActP0A850. 125 interactions.
MINTMINT-1225982.
STRING511145.b0436.

2D gel databases

SWISS-2DPAGEP0A850.

Proteomic databases

PaxDbP0A850.
PRIDEP0A850.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73539; AAC73539; b0436.
BAE76216; BAE76216; BAE76216.
GeneID12930847.
945081.
KEGGecj:Y75_p0424.
eco:b0436.
PATRIC32116025. VBIEscCol129921_0454.

Organism-specific databases

EchoBASEEB0996.
EcoGeneEG11003. tig.

Phylogenomic databases

eggNOGCOG0544.
HOGENOMHOG000218239.
KOK03545.
OMAMQVSVEN.
OrthoDBEOG63VBX3.
PhylomeDBP0A850.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0A850.

Family and domain databases

Gene3D1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPMF_00303. Trigger_factor_Tig.
InterProIPR001179. PPIase_FKBP_dom.
IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamPF00254. FKBP_C. 1 hit.
PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view]
PIRSFPIRSF003095. Trigger_factor. 1 hit.
SUPFAMSSF102735. SSF102735. 1 hit.
SSF109998. SSF109998. 1 hit.
TIGRFAMsTIGR00115. tig. 1 hit.
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A850.
PROP0A850.

Entry information

Entry nameTIG_ECOLI
AccessionPrimary (citable) accession number: P0A850
Secondary accession number(s): P15299 expand/collapse secondary AC list , P22257, P77603, Q2MBZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: June 11, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene