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P13551 (EFG_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Elongation factor G
Short name=EF-G
Gene names
Name:fusA
Synonyms:fus
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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.

Caution

The sequence shown here has been extracted from PDB entry 1KTV.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: HAMAP

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: 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_0000091248

Regions

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

Secondary structure

1 ........................................................................................................................................ 691
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13551 [UniParc].

Last modified January 1, 1990. 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

[1]"The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange."
Al-Karadaghi S., Aevarsson A., Garber M., Zheltonosova J., Liljas A.
Structure 4:555-565(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[2]"Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site."
Laurberg M., Kristensen O., Martemyanov K., Gudkov A.T., Nagaev I., Hughes D., Liljas A.
J. Mol. Biol. 303:593-603(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-573.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNMX-ray2.80A1-691[»]
1IP8model-H5-689[»]
1IPMmodel-H5-689[»]
1IPOmodel-F5-689[»]
1IPRmodel-F5-689[»]
1JQMelectron microscopy-B1-691[»]
1JQSelectron microscopy-B220-251[»]
C606-673[»]
1KTVX-ray3.80A/B1-691[»]
1PN6electron microscopy10.80A1-691[»]
2BCWelectron microscopy11.20C200-257[»]
2BM0X-ray2.40A1-691[»]
2BM1X-ray2.60A1-691[»]
2BV3X-ray2.50A1-691[»]
2J7KX-ray2.90A1-691[»]
2OM7electron microscopy7.30L1-691[»]
3IZPelectron microscopy-E1-688[»]
DisProtDP00021.
ProteinModelPortalP13551.
SMRP13551. Positions 4-689.
ModBaseSearch...

Protein-protein interaction databases

STRING262724.TTC1331.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.70.240. 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.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
PfamPF00679. EFG_C. 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]
SUPFAMSSF54980. EFG_III_V. 2 hits.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF50447. Translat_factor. 1 hit.
TIGRFAMsTIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13551.

Entry information

Entry nameEFG_THETH
AccessionPrimary (citable) accession number: P13551
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 29, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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