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Q9RT21 (TIG_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 96. 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·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:DR_1948
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24, Ref.4), exposing a hydrophobic crevice that is probably important for its chaperone activity (Ref.3 and Ref.4). HAMAP-Rule MF_00303

Catalytic activity

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

Subunit structure

Binds to the 50S ribosomal subunit via interactions with ribosomal protein L23. Also interacts with 23S rRNA and proteins L24 and L29 when complexed with the ribosome (Ref.3 and Ref.4). Ref.3 Ref.4

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
   LigandRNA-binding
rRNA-binding
   Molecular functionChaperone
Isomerase
Rotamase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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

rRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 465464Trigger factor HAMAP-Rule MF_00303
PRO_0000179344

Regions

Domain160 – 23576PPIase FKBP-type

Secondary structure

................ 465
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9RT21 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 475E073690C8E006

FASTA46551,847
        10         20         30         40         50         60 
MAELISKEGN KVEFKVSVPA AEVNRAYDQV WAGLARDVRV PGFRPGKAPR KVIENRVGKG 

        70         80         90        100        110        120 
YVESQVRDRL LETHYSQGLR ELGLNLVDAT VDPQDVQSGQ AFEFTVKGET YPEVKLGDWQ 

       130        140        150        160        170        180 
GLKVSAQAPE ITDEVLEQTL SDLRERNASF EKAERPIEAA DQVTIQELGE GDSEEGGSYP 

       190        200        210        220        230        240 
IYLDMAEEHV RNALLGKSAG DVVDITVPAH QHGDHEHAEH TVRVKVVEVS SKKLQDLNDE 

       250        260        270        280        290        300 
FATSLNYESM DKLRTDLREE LERRAQQEGD NLRREELVGH LVEGMTVEIP QALIDRRREG 

       310        320        330        340        350        360 
MMSEIQDDLR RQGVQWKEYE AFMQEQGKLD EFEADLTKNA ETRVRRDLAL EQLATDLNAQ 

       370        380        390        400        410        420 
VNEAEFNQTL MNLAQANGMN VQQLVQQLGQ DGVQSYYISL LRERGLQRAL AQLSGEGQST 

       430        440        450        460 
EAASPKATGT EAAGTEQSEP AQTETAQNDA GQTETAQSEG EQQSE 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1."
White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. expand/collapse author list , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Science 286:1571-1577(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[2]"Protein recycling is a major component of post-irradiation recovery in Deinococcus radiodurans strain R1."
Joshi B.S., Schmid R., Altendorf K., Apte S.K.
Biochem. Biophys. Res. Commun. 320:1112-1117(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[3]"Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action."
Baram D., Pyetan E., Sittner A., Auerbach-Nevo T., Bashan A., Yonath A.
Proc. Natl. Acad. Sci. U.S.A. 102:12017-12022(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-114 IN COMPLEX WITH THE 50S RIBOSOMAL SUBUNIT.
[4]"The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction."
Schluenzen F., Wilson D.N., Tian P., Harms J.M., McInnes S.J., Hansen H.A.S., Albrecht R., Buerger J., Wilbanks S.M., Fucini P.
Structure 13:1685-1694(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 1-112 IN COMPLEX WITH THE 50S RIBOSOMAL SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF11500.1.
PIRD75334.
RefSeqNP_295671.1. NC_001263.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AARX-ray3.5072-114[»]
2D3OX-ray3.3511-112[»]
ProteinModelPortalQ9RT21.
SMRQ9RT21. Positions 10-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_1948.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF11500; AAF11500; DR_1948.
GeneID1798866.
KEGGdra:DR_1948.
PATRIC21631548. VBIDeiRad64572_2168.

Phylogenomic databases

eggNOGCOG0544.
HOGENOMHOG000099671.
KOK03545.
OMAFKVKVHE.
OrthoDBEOG63VBX3.

Enzyme and pathway databases

BioCycDRAD243230:GH46-1981-MONOMER.

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

EvolutionaryTraceQ9RT21.

Entry information

Entry nameTIG_DEIRA
AccessionPrimary (citable) accession number: Q9RT21
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 96 of the entry and version 3 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