Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5SHN5 (EFG_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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:
Elongation factor G

Short name=EF-G
Gene names
Name:fusA
Synonyms:fus
Ordered Locus Names:TTHA1695
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length691 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. HAMAP-Rule MF_00054_B

Subcellular location

Cytoplasm HAMAP-Rule MF_00054_B.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 691691Elongation factor G HAMAP-Rule MF_00054_B
PRO_0000091249

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding83 – 875GTP By similarity
Nucleotide binding137 – 1404GTP By similarity

Secondary structure

........................................................................................................................................... 691
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SHN5 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 8F0063EE8123470E

FASTA69176,879
        10         20         30         40         50         60 
MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA TMDFMEQERE 

        70         80         90        100        110        120 
RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV LDGAIVVFDS SQGVEPQSET 

       130        140        150        160        170        180 
VWRQAEKYKV PRIAFANKMD KTGADLWLVI RTMQERLGAR PVVMQLPIGR EDTFSGIIDV 

       190        200        210        220        230        240 
LRMKAYTYGN DLGTDIREIP IPEEYLDQAR EYHEKLVEVA ADFDENIMLK YLEGEEPTEE 

       250        260        270        280        290        300 
ELVAAIRKGT IDLKITPVFL GSALKNKGVQ LLLDAVVDYL PSPLDIPPIK GTTPEGEVVE 

       310        320        330        340        350        360 
IHPDPNGPLA ALAFKIMADP YVGRLTFIRV YSGTLTSGSY VYNTTKGRKE RVARLLRMHA 

       370        380        390        400        410        420 
NHREEVEELK AGDLGAVVGL KETITGDTLV GEDAPRVILE SIEVPEPVID VAIEPKTKAD 

       430        440        450        460        470        480 
QEKLSQALAR LAEEDPTFRV STHPETGQTI ISGMGELHLE IIVDRLKREF KVDANVGKPQ 

       490        500        510        520        530        540 
VAYRETITKP VDVEGKFIRQ TGGRGQYGHV KIKVEPLPRG SGFEFVNAIV GGVIPKEYIP 

       550        560        570        580        590        600 
AVQKGIEEAM QSGPLIGFPV VDIKVTLYDG SYHEVDSSEM AFKIAGSMAI KEAVQKGDPV 

       610        620        630        640        650        660 
ILEPIMRVEV TTPEEYMGDV IGDLNARRGQ ILGMEPRGNA QVIRAFVPLA EMFGYATDLR 

       670        680        690 
SKTQGRGSFV MFFDHYQEVP KQVQEKLIKG Q 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Thermus thermophilus HB8 gene coding for elongation factor G."
Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.
Nucleic Acids Res. 17:8863-8863(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Nucleotide sequence of the Thermus thermophilus HB8 rps12 and rps7 genes coding for the ribosomal proteins S12 and S7."
Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.
Nucleic Acids Res. 18:3659-3659(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[4]"The crystal structure of elongation factor G complexed with GDP, at 2.7-A resolution."
Czworkowski J., Wang J., Steitz T.A., Moore P.B.
EMBO J. 13:3661-3668(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[5]"Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus."
Aevarsson A., Brazhnikov E., Garber M., Zheltonosova J., Chirgadze Y., Al-Karadaghi S., Svensson L.A., Liljas A.
EMBO J. 13:3669-3677(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16278 Genomic DNA. Translation: CAA34354.1.
AP008226 Genomic DNA. Translation: BAD71518.1.
X52165 Genomic DNA. Translation: CAA36420.1.
PIREFTWG. S15928.
RefSeqYP_144961.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DARX-ray2.40A1-691[»]
1EFGX-ray2.70A1-691[»]
1ELOX-ray2.80A1-691[»]
1ZN0electron microscopy15.50B6-688[»]
2EFGX-ray2.60A1-691[»]
2WRIX-ray3.60Y1-691[»]
2WRKX-ray3.60Y1-691[»]
2XSYelectron microscopy7.80Y1-691[»]
2XUYelectron microscopy7.60Y1-691[»]
4B8FX-ray3.70Y1-691[»]
4B8HX-ray3.70Y1-691[»]
4BTCX-ray2.95Y1-691[»]
4JUWX-ray2.86Y10-689[»]
ProteinModelPortalQ5SHN5.
SMRQ5SHN5. Positions 4-689.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1695.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71518; BAD71518; BAD71518.
GeneID3169680.
KEGGttj:TTHA1695.
PATRIC23958345. VBITheThe93045_1665.

Phylogenomic databases

eggNOGCOG0480.
HOGENOMHOG000231587.
KOK02355.
OMAKGIQEAM.
OrthoDBEOG6X6RBF.
ProtClustDBPRK00007.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1734-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_00054_B. EF_G_EF_2_B.
InterProIPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SMARTSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsTIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5SHN5.
PROQ5SHN5.

Entry information

Entry nameEFG_THET8
AccessionPrimary (citable) accession number: Q5SHN5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 75 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