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Q8KTB2 (EFG_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. 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
Ordered Locus Names:RT0121
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length699 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-Rule MF_00054

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00054.

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-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 – 699699Elongation factor G HAMAP-Rule MF_00054
PRO_0000091205

Regions

Nucleotide binding17 – 248GTP By similarity
Nucleotide binding81 – 855GTP By similarity
Nucleotide binding135 – 1384GTP By similarity

Experimental info

Sequence conflict2631F → L in AAM90925. Ref.1
Sequence conflict3061T → L in AAM90925. Ref.1
Sequence conflict6411S → K in AAM90925. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8KTB2 [UniParc].

Last modified November 9, 2004. Version 2.
Checksum: DAACBEB448B39C37

FASTA69977,652
        10         20         30         40         50         60 
MSKINKLEHI RNIGICAHID AGKTTTTERI LYYTGKSHKI GEVHEGGATM DWMEQEQERG 

        70         80         90        100        110        120 
ITITSAATTC KWQDKVINII DTPGHVDFTI EVERSLRVLD GAVAVFDGVA GVEPQSETVW 

       130        140        150        160        170        180 
RQADKYNVPR MCFVNKMDRM GADFYKCVDM IKDRLGAKSL ILQLPIGIEE NFKGIINLIK 

       190        200        210        220        230        240 
MKAVIWKDES LGAEYFEEDI PTDMQDKAAE YRARLLDMTV ELDDTIMERY LSGEEITEEE 

       250        260        270        280        290        300 
IKILIRKGTI EAKFYPVLCG SAFKNKGVQP LLDAIVDFLP SPIDIGIVKG IEVSTSEEKD 

       310        320        330        340        350        360 
FPISITEPFS ALAFKIMNDP FVGSLTFIRI YSGKITSGAS VVNTVKNKRE KIGRMLLMHA 

       370        380        390        400        410        420 
NNREDIKEAS AGDIVALAGL KDTSTGDTLS DIDTQVVLER MEFPEPVIEL AVEPKSTADQ 

       430        440        450        460        470        480 
EKMGLALSRL AAEDPSFKVS TDHETGQTVI KGMGELHLEI IIDRMRREFK VEANIGAPQV 

       490        500        510        520        530        540 
AYRETITTAC EIDYTHKKQS GGAGQFARVK IIFEPLKDVI DLKDEDKNKT FVFESKIVGG 

       550        560        570        580        590        600 
AVPKEYIPGV EKGLNNIRET GIVAGYPMID FKATLVDGAF HDVDSSVLAF EIAAKGAFRE 

       610        620        630        640        650        660 
GMQKGNPKLL EPIMKVEVIT PDEYMGDIIG DLNSRRGQIQ SMDPRGNAQV VTAYVPLAEM 

       670        680        690 
FGYVNTLRSL SQGRAQFSMI FSHYDQVPSQ VADIIKAKK 

« Hide

References

« Hide 'large scale' references
[1]"Proliferation and deterioration of Rickettsia palindromic elements."
Amiri H., Alsmark C.M., Andersson S.G.E.
Mol. Biol. Evol. 19:1234-1243(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF502176 Genomic DNA. Translation: AAM90925.1.
AE017197 Genomic DNA. Translation: AAU03607.1.
RefSeqYP_067089.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ8KTB2.
SMRQ8KTB2. Positions 5-694.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0121.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU03607; AAU03607; RT0121.
GeneID2958765.
KEGGrty:RT0121.
PATRIC17909414. VBIRicTyp34752_0128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0480.
HOGENOMHOG000231585.
KOK02355.
OMAEYIPSCD.
OrthoDBEOG6X6RBF.
ProtClustDBPRK12739.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-129-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...

Entry information

Entry nameEFG_RICTY
AccessionPrimary (citable) accession number: Q8KTB2
Secondary accession number(s): Q68XN5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: November 9, 2004
Last modified: April 16, 2014
This is version 77 of the entry and version 2 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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names