Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9RT21

- TIG_DEIRA

UniProt

Q9RT21 - TIG_DEIRA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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: 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-KW
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:
PDBe
RCSB PDB
PDBj
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.
OMAiFKVKVHE.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF11500.1 .
PIRi D75334.
RefSeqi NP_295671.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AAR X-ray 3.50 7 2-114 [» ]
2D3O X-ray 3.35 1 1-112 [» ]
ProteinModelPortali Q9RT21.
SMRi Q9RT21. Positions 10-109.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243230.DR_1948.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF11500 ; AAF11500 ; DR_1948 .
GeneIDi 1798866.
KEGGi dra:DR_1948.
PATRICi 21631548. VBIDeiRad64572_2168.

Phylogenomic databases

eggNOGi COG0544.
HOGENOMi HOG000099671.
InParanoidi Q9RT21.
KOi K03545.
OMAi FKVKVHE.
OrthoDBi EOG63VBX3.

Enzyme and pathway databases

BioCyci DRAD243230:GH46-1981-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9RT21.

Family and domain databases

Gene3Di 1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPi MF_00303. Trigger_factor_Tig.
InterProi IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view ]
Pfami PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF003095. Trigger_factor. 1 hit.
SUPFAMi SSF102735. SSF102735. 1 hit.
SSF109998. SSF109998. 1 hit.
TIGRFAMsi TIGR00115. tig. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 99 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