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

B3QY22 (EFTU_CHLT3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 Tu

Short name=EF-Tu
Gene names
Name:tuf
Ordered Locus Names:Ctha_1086
OrganismChloroherpeton thalassium (strain ATCC 35110 / GB-78) [Complete proteome] [HAMAP]
Taxonomic identifier517418 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChloroherpeton

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis By similarity. HAMAP-Rule MF_00118

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00118

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00118.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A 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 – 393393Elongation factor Tu HAMAP-Rule MF_00118
PRO_1000095057

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding81 – 855GTP By similarity
Nucleotide binding136 – 1394GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3QY22 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: CACF0B3DD973902C

FASTA39342,990
        10         20         30         40         50         60 
MAKESYKREK PHVNIGTIGH VDHGKTTLTA AITKVLSEKG QAQKMDFDEI DKAPEEKERG 

        70         80         90        100        110        120 
ITISTSHVEY ETPSRHYAHI DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI 

       130        140        150        160        170        180 
LLAKQVNVPS IVVFMNKVDI ADPELIELVE MELRELLSSY GFPGDDIPII QGSALGALNG 

       190        200        210        220        230        240 
EAEWVGKIEE LMEAVDNYIP TPVRDVDKPF LMPVEDVFSI SGRGTVGTGR IERGVIKINE 

       250        260        270        280        290        300 
EVELVGIRPT KKSVVTGIEM FRKLLDQGEA GDNAGLLLRG VNKDELERGM VIAKPGSITP 

       310        320        330        340        350        360 
HTKFKAEVYI LKKEEGGRHT PFFNGYRPQF YFRTTDVTGS VNLPDGVEMV MPGDNLSIEA 

       370        380        390 
ELIAPIAMDE GLRFAIREGG RTVGAGTVTS IIE 

« Hide

References

[1]"Complete sequence of Chloroherpeton thalassium ATCC 35110."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35110 / GB-78.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001100 Genomic DNA. Translation: ACF13550.1.
RefSeqYP_001995997.1. NC_011026.1.

3D structure databases

ProteinModelPortalB3QY22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING517418.Ctha_1086.

Proteomic databases

PRIDEB3QY22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF13550; ACF13550; Ctha_1086.
GeneID6422142.
KEGGcts:Ctha_1086.
PATRIC21430927. VBIChlTha99257_1280.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMATGQITAF.
OrthoDBEOG6R5C6X.
ProtClustDBPRK00049.

Enzyme and pathway databases

BioCycCTHA517418:GHTO-1101-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00118_B. EF_Tu_B.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEFTU_CHLT3
AccessionPrimary (citable) accession number: B3QY22
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 39 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