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Protein

Trigger factor

Gene

tig

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 4 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). Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24, PubMed:16271892), exposing a hydrophobic crevice that is probably important for its chaperone activity (PubMed:16091460 and PubMed:16271892).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-HAMAP
  2. rRNA binding Source: UniProtKB-KW

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

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-1981-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:DR_1948
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524: Chromosome I

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
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 465464Trigger factorPRO_0000179344Add
BLAST

Interactioni

Subunit structurei

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 (PubMed:16091460 and PubMed:16271892).2 Publications

Protein-protein interaction databases

STRINGi243230.DR_1948.

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 165Combined sources
Helixi20 – 223Combined sources
Helixi24 – 3512Combined sources
Helixi53 – 564Combined sources
Turni57 – 604Combined sources
Helixi63 – 8119Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi104 – 1085Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AARX-ray3.5072-114[»]
2D3OX-ray3.3511-112[»]
ProteinModelPortaliQ9RT21.
SMRiQ9RT21. Positions 10-109.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RT21.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 23576PPIase 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.
HOGENOMiHOG000099671.
InParanoidiQ9RT21.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9RT21-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAELISKEGN KVEFKVSVPA AEVNRAYDQV WAGLARDVRV PGFRPGKAPR
60 70 80 90 100
KVIENRVGKG YVESQVRDRL LETHYSQGLR ELGLNLVDAT VDPQDVQSGQ
110 120 130 140 150
AFEFTVKGET YPEVKLGDWQ GLKVSAQAPE ITDEVLEQTL SDLRERNASF
160 170 180 190 200
EKAERPIEAA DQVTIQELGE GDSEEGGSYP IYLDMAEEHV RNALLGKSAG
210 220 230 240 250
DVVDITVPAH QHGDHEHAEH TVRVKVVEVS SKKLQDLNDE FATSLNYESM
260 270 280 290 300
DKLRTDLREE LERRAQQEGD NLRREELVGH LVEGMTVEIP QALIDRRREG
310 320 330 340 350
MMSEIQDDLR RQGVQWKEYE AFMQEQGKLD EFEADLTKNA ETRVRRDLAL
360 370 380 390 400
EQLATDLNAQ VNEAEFNQTL MNLAQANGMN VQQLVQQLGQ DGVQSYYISL
410 420 430 440 450
LRERGLQRAL AQLSGEGQST EAASPKATGT EAAGTEQSEP AQTETAQNDA
460
GQTETAQSEG EQQSE
Length:465
Mass (Da):51,847
Last modified:January 23, 2007 - v3
Checksum:i475E073690C8E006
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11500.1.
PIRiD75334.
RefSeqiNP_295671.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF11500; AAF11500; DR_1948.
GeneIDi1798866.
KEGGidra:DR_1948.
PATRICi21631548. VBIDeiRad64572_2168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11500.1.
PIRiD75334.
RefSeqiNP_295671.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AARX-ray3.5072-114[»]
2D3OX-ray3.3511-112[»]
ProteinModelPortaliQ9RT21.
SMRiQ9RT21. Positions 10-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_1948.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF11500; AAF11500; DR_1948.
GeneIDi1798866.
KEGGidra:DR_1948.
PATRICi21631548. VBIDeiRad64572_2168.

Phylogenomic databases

eggNOGiCOG0544.
HOGENOMiHOG000099671.
InParanoidiQ9RT21.
KOiK03545.
OMAiPRIIDQR.
OrthoDBiEOG63VBX3.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-1981-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RT21.

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

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiTIG_DEIRA
AccessioniPrimary (citable) accession number: Q9RT21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.