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Q9WZF8 (TIG_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:TM_0694
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length425 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 protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase By similarity. HAMAP-Rule MF_00303

Catalytic activity

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

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 By similarity. HAMAP-Rule MF_00303

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 By similarity. HAMAP-Rule MF_00303

Sequence similarities

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

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasm
   Molecular functionChaperone
Isomerase
Rotamase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

protein folding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein transport

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rpsGP385265EBI-2463534,EBI-2463521

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Trigger factor HAMAP-Rule MF_00303
PRO_0000179452

Regions

Domain158 – 23174PPIase FKBP-type

Secondary structure

.................................................................... 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WZF8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: BEC16F20ACFDD922

FASTA42549,898
        10         20         30         40         50         60 
MEVKELERDK NRVVLEYVFG AEEIAQAEDK AVRYLNQRVE IPGFRKGRIP KNVLKMKLGE 

        70         80         90        100        110        120 
EFQEYTLDFL MDLIPDTLKD RKLILSPIVT ERELKDVTAR VVVEVHEEPE VRIGDISKIE 

       130        140        150        160        170        180 
VEKVDEEKVL EKYVERRIED LRESHALLEP KEGPAEAGDL VRVNMEVYNE EGKKLTSREY 

       190        200        210        220        230        240 
EYVISEDEDR PFVKDLVGKK KGDVVEIERE YEGKKYTYKL EVEEVYKRTL PEIGDELAKS 

       250        260        270        280        290        300 
VNNEFETLEQ LKESLKKEGK EIYDVEMKES MREQLLEKLP EIVEIEISDR TLEILVNEAI 

       310        320        330        340        350        360 
NRLKREGRYE QIVSSYESEE KFREELKERI LDDIKRDRVI EVLAQEKGIS VNDEELEKEA 

       370        380        390        400        410        420 
EELAPFWGIS PDRAKSLVKA RQDLREELRW AILKRKVLDL LLQEVKVKVV EPKGEGDDSE 


GKEDN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35776.1.
PIRD72345.
RefSeqNP_228503.1. NC_000853.1.
YP_007977044.1. NC_021214.1.
YP_008990337.1. NC_023151.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NSAX-ray1.70A244-405[»]
2NSBX-ray3.20A1-109[»]
2NSCX-ray2.20A1-109[»]
3GTYX-ray3.40X1-425[»]
3GU0X-ray3.50A1-405[»]
ProteinModelPortalQ9WZF8.
SMRQ9WZF8. Positions 1-109, 244-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WZF8. 1 interaction.
STRING243274.TM0694.

Protocols and materials databases

DNASU898361.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35776; AAD35776; TM_0694.
GeneID15494297.
18092095.
898361.
KEGGtma:TM0694.
tmm:Tmari_0694.
PATRIC23936306. VBITheMar51294_0706.

Phylogenomic databases

eggNOGCOG0544.
KOK03545.
OMARIIDQRI.
OrthoDBEOG63VBX3.
ProtClustDBCLSK875303.

Family and domain databases

Gene3D1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPMF_00303. Trigger_factor_Tig.
InterProIPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamPF05698. 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.
ProtoNetSearch...

Other

EvolutionaryTraceQ9WZF8.

Entry information

Entry nameTIG_THEMA
AccessionPrimary (citable) accession number: Q9WZF8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 88 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