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Protein

Trigger factor

Gene

tig

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. protein folding Source: UniProtKB-HAMAP
  4. protein transport Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

Cell cycle, Cell division

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:TM_0694
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: 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

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Trigger factorPRO_0000179452Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsGP385265EBI-2463534,EBI-2463521

Protein-protein interaction databases

IntActiQ9WZF8. 1 interaction.
STRINGi243274.TM0694.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Beta strandi12 – 187Combined sources
Helixi21 – 3616Combined sources
Beta strandi42 – 443Combined sources
Helixi51 – 588Combined sources
Helixi59 – 613Combined sources
Helixi62 – 7110Combined sources
Helixi74 – 774Combined sources
Turni78 – 803Combined sources
Beta strandi83 – 853Combined sources
Beta strandi88 – 947Combined sources
Beta strandi99 – 1079Combined sources
Beta strandi110 – 1123Combined sources
Helixi116 – 1183Combined sources
Beta strandi119 – 1246Combined sources
Helixi126 – 14419Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi159 – 16810Combined sources
Beta strandi174 – 18310Combined sources
Helixi193 – 1964Combined sources
Beta strandi204 – 2118Combined sources
Beta strandi214 – 22815Combined sources
Helixi235 – 2395Combined sources
Beta strandi241 – 2444Combined sources
Helixi248 – 2547Combined sources
Helixi259 – 2624Combined sources
Helixi267 – 27812Combined sources
Helixi279 – 2824Combined sources
Beta strandi284 – 2863Combined sources
Helixi289 – 30517Combined sources
Helixi309 – 3146Combined sources
Helixi319 – 34729Combined sources
Helixi353 – 36715Combined sources
Helixi371 – 38010Combined sources
Helixi382 – 40221Combined sources
Beta strandi405 – 4106Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NSAX-ray1.70A244-405[»]
2NSBX-ray3.20A1-109[»]
2NSCX-ray2.20A1-109[»]
3GTYX-ray3.40X1-425[»]
3GU0X-ray3.50A1-405[»]
ProteinModelPortaliQ9WZF8.
SMRiQ9WZF8. Positions 1-109, 244-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WZF8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini158 – 23174PPIase FKBP-typeAdd
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.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0544.
InParanoidiQ9WZF8.
KOiK03545.
OMAiPRIIDQR.
OrthoDBiEOG63VBX3.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig.
InterProiIPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF05698. 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.

Sequencei

Sequence statusi: Complete.

Q9WZF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVKELERDK NRVVLEYVFG AEEIAQAEDK AVRYLNQRVE IPGFRKGRIP
60 70 80 90 100
KNVLKMKLGE EFQEYTLDFL MDLIPDTLKD RKLILSPIVT ERELKDVTAR
110 120 130 140 150
VVVEVHEEPE VRIGDISKIE VEKVDEEKVL EKYVERRIED LRESHALLEP
160 170 180 190 200
KEGPAEAGDL VRVNMEVYNE EGKKLTSREY EYVISEDEDR PFVKDLVGKK
210 220 230 240 250
KGDVVEIERE YEGKKYTYKL EVEEVYKRTL PEIGDELAKS VNNEFETLEQ
260 270 280 290 300
LKESLKKEGK EIYDVEMKES MREQLLEKLP EIVEIEISDR TLEILVNEAI
310 320 330 340 350
NRLKREGRYE QIVSSYESEE KFREELKERI LDDIKRDRVI EVLAQEKGIS
360 370 380 390 400
VNDEELEKEA EELAPFWGIS PDRAKSLVKA RQDLREELRW AILKRKVLDL
410 420
LLQEVKVKVV EPKGEGDDSE GKEDN
Length:425
Mass (Da):49,898
Last modified:November 1, 1999 - v1
Checksum:iBEC16F20ACFDD922
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35776.1.
PIRiD72345.
RefSeqiNP_228503.1. NC_000853.1.
YP_007977044.1. NC_021214.1.
YP_008990337.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35776; AAD35776; TM_0694.
GeneIDi15494297.
18092095.
898361.
KEGGitma:TM0694.
tmi:THEMA_01195.
PATRICi23936306. VBITheMar51294_0706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35776.1.
PIRiD72345.
RefSeqiNP_228503.1. NC_000853.1.
YP_007977044.1. NC_021214.1.
YP_008990337.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NSAX-ray1.70A244-405[»]
2NSBX-ray3.20A1-109[»]
2NSCX-ray2.20A1-109[»]
3GTYX-ray3.40X1-425[»]
3GU0X-ray3.50A1-405[»]
ProteinModelPortaliQ9WZF8.
SMRiQ9WZF8. Positions 1-109, 244-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WZF8. 1 interaction.
STRINGi243274.TM0694.

Protocols and materials databases

DNASUi898361.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35776; AAD35776; TM_0694.
GeneIDi15494297.
18092095.
898361.
KEGGitma:TM0694.
tmi:THEMA_01195.
PATRICi23936306. VBITheMar51294_0706.

Phylogenomic databases

eggNOGiCOG0544.
InParanoidiQ9WZF8.
KOiK03545.
OMAiPRIIDQR.
OrthoDBiEOG63VBX3.

Miscellaneous databases

EvolutionaryTraceiQ9WZF8.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig.
InterProiIPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF05698. 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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Entry informationi

Entry nameiTIG_THEMA
AccessioniPrimary (citable) accession number: Q9WZF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: March 4, 2015
This is version 97 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.