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P0A6N2 (EFTU_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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
Alternative name(s):
P-43
Gene names
Name:tufA
Ordered Locus Names:c4111
AND
Name:tufB
Ordered Locus Names:c4935
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation By similarity. HAMAP-Rule MF_00118

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00118

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00118.

Miscellaneous

This chain is also used in bacteriophage Q-beta RNA polymerase By similarity.

The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome By similarity.

The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu By similarity.

The sequence of the tufB gene is shown. TufA differs in a single position By similarity.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Sequence caution

The sequence AAN82549.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 394393Elongation factor Tu HAMAP-Rule MF_00118
PRO_0000091322

Regions

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

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue571N6-methylated lysine By similarity
Modified residue3141N6-acetyllysine By similarity
Modified residue3831Phosphothreonine By similarity

Natural variations

Natural variant3941S → G in tufA.

Sequences

Sequence LengthMass (Da)Tools
P0A6N2 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6EDA60255F43358F

FASTA39443,314
        10         20         30         40         50         60 
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG 

        70         80         90        100        110        120 
ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI 

       130        140        150        160        170        180 
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE 

       190        200        210        220        230        240 
GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG 

       250        260        270        280        290        300 
EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK 

       310        320        330        340        350        360 
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV 

       370        380        390 
VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB).
Strain: CFT073 / ATCC 700928 / UPEC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN82549.1. Different initiation.
AE014075 Genomic DNA. Translation: AAN83363.1.
RefSeqNP_755975.2. NC_004431.1.
NP_756789.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0A6N2.
SMRP0A6N2. Positions 9-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c4111.

Proteomic databases

PRIDEP0A6N2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN82549; AAN82549; c4111.
AAN83363; AAN83363; c4935.
GeneID1036191.
1039881.
KEGGecc:c4111.
ecc:c4935.
PATRIC18285976. VBIEscCol75197_3864.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229290.
KOK02358.
OMAVTPHTEF.
OrthoDBEOG6R5C6X.
ProtClustDBPRK12735.

Enzyme and pathway databases

BioCycECOL199310:C4935-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_ECOL6
AccessionPrimary (citable) accession number: P0A6N2
Secondary accession number(s): O68929 expand/collapse secondary AC list , P02990, Q8X4S9, Q8XED3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 74 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