Trigger factor - Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)

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Q9RT21 (TIG_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Trigger factor
Short name=TF
EC=5.2.1.8

Alternative name(s):
PPIase

Gene names

Name:	tig
Ordered Locus Names:	DR_1948

Organism

Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]

Taxonomic identifier

243230 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus ›

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cell cycle Cell division
Cellular component	Cytoplasm
Ligand	RNA-binding rRNA-binding
Molecular function	Chaperone Isomerase Rotamase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW protein folding Inferred from electronic annotation. Source: HAMAP protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC protein transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: HAMAP rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 465

464

Trigger factor HAMAP-Rule MF_00303

PRO_0000179344

Regions

Domain

160 – 235

PPIase FKBP-type

Secondary structure

465

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9RT21 [UniParc].

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

FASTA

465

51,847

        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' referencesShow '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. 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.

PIR

D75334.

RefSeq

NP_295671.1. NC_001263.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AAR	X-ray	3.50	7	2-114	[»]
2D3O	X-ray	3.35	1	1-112	[»]

ProteinModelPortal

Q9RT21.

SMR

Q9RT21. Positions 10-109.

ModBase

Search...

Protein-protein interaction databases

STRING

243230.DR_1948.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAF11500; AAF11500; DR_1948.

GeneID

1798866.

KEGG

dra:DR_1948.

PATRIC

21631548. VBIDeiRad64572_2168.

Phylogenomic databases

eggNOG

COG0544.

HOGENOM

HOG000099671.

K03545.

OMA

NARLIQY.

ProtClustDB

CLSK445324.

Enzyme and pathway databases

BioCyc

DRAD243230:GH46-2317-MONOMER.

Family and domain databases

Gene3D

1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.

HAMAP

MF_00303. Trigger_factor_Tig.

InterPro

IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]

Pfam

PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view]

PIRSF

PIRSF003095. Trigger_factor. 1 hit.

SUPFAM

SSF109998. Trigger_fac_C_bac. 1 hit.
SSF102735. Trigger_fac_ribosome-bd_bac. 1 hit.

TIGRFAMs

TIGR00115. tig. 1 hit.

PROSITE

PS50059. FKBP_PPIASE. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9RT21.

Entry information

Entry name

TIG_DEIRA

Accession

Primary (citable) accession number: Q9RT21

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents