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Protein

Trigger factor

Gene

tig

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

Cell cycle, Cell division

Names & Taxonomyi

Protein namesi
Recommended name:
Trigger factorUniRule annotation (EC:5.2.1.8UniRule annotation)
Short name:
TFUniRule annotation
Alternative name(s):
PPIaseUniRule annotation
Gene namesi
Name:tigUniRule annotation
Ordered Locus Names:BWG_0318
OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
Taxonomic identifieri595496 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Cytoplasm

  • Note: About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002049861 – 432Trigger factorAdd BLAST432

Proteomic databases

PRIDEiC4ZTJ3.

Interactioni

Subunit structurei

Homodimer and monomer. In vivo most of the ribosomes are in complex with monomeric TF. Uncomplexed TF, however, is in a monomer-dimer equilibrium with approximately two thirds of TF existing in a dimeric state.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
dmsDP698533EBI-4407188,EBI-4406374From a different organism.

Protein-protein interaction databases

IntActiC4ZTJ3. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliC4ZTJ3.
SMRiC4ZTJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

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.UniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000218239.
KOiK03545.
OMAiKAQNDDK.

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.

C4ZTJ3-1 [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:July 28, 2009 - v1
Checksum:i42C3E3C335074164
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR63987.1.
RefSeqiWP_001198386.1. NC_012759.1.

Genome annotation databases

EnsemblBacteriaiACR63987; ACR63987; BWG_0318.
KEGGiebw:BWG_0318.
PATRICi18269602. VBIEscCol60876_0357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR63987.1.
RefSeqiWP_001198386.1. NC_012759.1.

3D structure databases

ProteinModelPortaliC4ZTJ3.
SMRiC4ZTJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiC4ZTJ3. 1 interactor.

Proteomic databases

PRIDEiC4ZTJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACR63987; ACR63987; BWG_0318.
KEGGiebw:BWG_0318.
PATRICi18269602. VBIEscCol60876_0357.

Phylogenomic databases

HOGENOMiHOG000218239.
KOiK03545.
OMAiKAQNDDK.

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_ECOBW
AccessioniPrimary (citable) accession number: C4ZTJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: November 2, 2016
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.