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C1CXH0 (EFG_DEIDV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Ordered Locus Names:Deide_18990
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length697 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP MF_00054_B

Subcellular location

Cytoplasm By similarity HAMAP 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 termComplete proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 697697Elongation factor G HAMAP MF_00054_B
PRO_1000202298

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding89 – 935GTP By similarity
Nucleotide binding143 – 1464GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
C1CXH0 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 97CBE039BC3E3D33

FASTA69776,634
        10         20         30         40         50         60 
MTTKAQSYLT HFRNIGIAAH IDAGKTTTTE RILYYTGRTH NIGEVHDGAA TMDWMEQERE 

        70         80         90        100        110        120 
RGITITAAAT TAKWKRSGTD QEYVVNIIDT PGHVDFTIEV ERSMRVLDGA VAVFDSSQGV 

       130        140        150        160        170        180 
EPQSETVWRQ ADRYGVPRIA FSNKMDKTGA SFELVLTDIK ERLGAIPAPI QYPMGQENDF 

       190        200        210        220        230        240 
KGIIDIVRMR AHVYTNDLGT DIVESDIPAE FADKVAEMRA QLIEAAAEVD EDLMMMYLEG 

       250        260        270        280        290        300 
EEPSVEQLVS AIRKGTIEKK IFPVLCGSAL KNKGVQLLLD AVVDYLPSPL EVPAIRGKVE 

       310        320        330        340        350        360 
DSEDTVEFPA DPEGKLAALA FKIMADPYVG RLTFVRIYSG TLQSGSYVYN ASKDKRDRVG 

       370        380        390        400        410        420 
RLLKMHANSR EEVTELRAGE LGAVIGLKDA GTGNTLIADG EDRVLLESID VPEPVIKLAI 

       430        440        450        460        470        480 
EPKTKADQEK MGIGLQKLAE EDPTFRVESD QESGQTTISG MGELHLEILV DRLKREYKVE 

       490        500        510        520        530        540 
ANVGAPQVAY RETITKAVDV EGKFVRQSGG RGQFGHVKIK AEPLEPGAGF VFENIVVGGT 

       550        560        570        580        590        600 
VPREFIGPAQ KGIEEALQSG PMLGFPVVDM KVSLYDGSYH EVDSSEMAFK IAGSMALKEA 

       610        620        630        640        650        660 
VQKGAPAILE PIMRVEVTVP EDYMGDIIGD LNSRRGQIQG MEARGNAQIV KAFVPLSEMF 

       670        680        690 
GYATDMRSMT QGRASYSMFF DHYSQVPNNL AQQLMKK 

« Hide

References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed: 19370165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001114 Genomic DNA. Translation: ACO46887.1.
RefSeqYP_002786641.1. NC_012526.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC1CXH0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7737597.
GenomeReviewsGene locus Deide_18990 in contig CP001114_GR.
KEGGddr:Deide_18990.
PATRIC21617794. VBIDeiDes121019_2172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMACNEWREK.
ProtClustDBPRK00007.

Family and domain databases

HAMAPMF_00054_B. EF-G_EF-2_B.
[Tree]
InterProIPR009022. Elongation_fac_G/III/V.
IPR000795. ProtSyn_GTP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR004540. Transl_elong_EFG/EF2.
IPR000640. Transl_elong_EFG/EF2_C.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
Gene3DG3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
G3DSA:3.30.70.240. Transl_elong_EFG/EF2_C. 1 hit.
KOK02355.
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.
SSF50447. Translat_factor. 1 hit.
TIGRFAMsTIGR00484. EF-G. 1 hit.
TIGR00231. Small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEFG_DEIDV
AccessionPrimary (citable) accession number: C1CXH0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: January 25, 2012
This is version 20 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