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Protein

Trigger factor

Gene

tig

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciECOO157:TIG-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:Z0541, ECs0490
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

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.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001793481 – 432Trigger factorAdd BLAST432

Proteomic databases

PRIDEiP0A851.

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 (By similarity).By similarity

Protein-protein interaction databases

MINTiMINT-1225967.
STRINGi155864.Z0541.

Structurei

3D structure databases

ProteinModelPortaliP0A851.
SMRiP0A851.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini161 – 246PPIase FKBP-typeAdd 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.By similarity

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.
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.

P0A851-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG54786.1.
BA000007 Genomic DNA. Translation: BAB33913.1.
PIRiB90690.
F85540.
RefSeqiNP_308517.1. NC_002695.1.
WP_001198386.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG54786; AAG54786; Z0541.
BAB33913; BAB33913; BAB33913.
GeneIDi914592.
KEGGiece:Z0541.
ecs:ECs0490.
PATRICi18349945. VBIEscCol44059_0493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG54786.1.
BA000007 Genomic DNA. Translation: BAB33913.1.
PIRiB90690.
F85540.
RefSeqiNP_308517.1. NC_002695.1.
WP_001198386.1. NZ_LPWC02000002.1.

3D structure databases

ProteinModelPortaliP0A851.
SMRiP0A851.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1225967.
STRINGi155864.Z0541.

Proteomic databases

PRIDEiP0A851.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG54786; AAG54786; Z0541.
BAB33913; BAB33913; BAB33913.
GeneIDi914592.
KEGGiece:Z0541.
ecs:ECs0490.
PATRICi18349945. VBIEscCol44059_0493.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciECOO157:TIG-MONOMER.

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_ECO57
AccessioniPrimary (citable) accession number: P0A851
Secondary accession number(s): P15299, P22257, P77603
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 74 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

Complete proteome

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.