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Protein

Elongation factor Tu

Gene

tufA

more
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.UniRule annotation
May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 26GTPUniRule annotation8
Nucleotide bindingi81 – 85GTPUniRule annotation5
Nucleotide bindingi136 – 139GTPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Antibiotic resistance, Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciECOL199310:C4935-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor TuUniRule annotation
Short name:
EF-TuUniRule annotation
Alternative name(s):
P-43
Gene namesi
Name:tufAUniRule annotation
Ordered Locus Names:c4111
AND
Name:tufBUniRule annotation
Ordered Locus Names:c4935
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001410 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm
  • Cell inner membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000913222 – 394Elongation factor TuAdd BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei57N6-methylated lysineBy similarity1
Modified residuei314N6-acetyllysineBy similarity1
Modified residuei383PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRIDEiP0A6N2.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi199310.c4935.

Structurei

3D structure databases

ProteinModelPortaliP0A6N2.
SMRiP0A6N2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 204tr-type GAdd BLAST195

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 26G1By similarity8
Regioni60 – 64G2By similarity5
Regioni81 – 84G3By similarity4
Regioni136 – 139G4By similarity4
Regioni174 – 176G5By similarity3

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CGV. Bacteria.
COG0050. LUCA.
HOGENOMiHOG000229290.
KOiK02358.

Family and domain databases

CDDicd03697. EFTU_II. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR033720. EFTU_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6N2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI
60 70 80 90 100
DNAPEEKARG ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD
110 120 130 140 150
GAILVVAATD GPMPQTREHI LLGRQVGVPY IIVFLNKCDM VDDEELLELV
160 170 180 190 200
EMEVRELLSQ YDFPGDDTPI VRGSALKALE GDAEWEAKIL ELAGFLDSYI
210 220 230 240 250
PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG EEVEIVGIKE
260 270 280 290 300
TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK
310 320 330 340 350
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM
360 370 380 390
VMPGDNIKMV VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS
Length:394
Mass (Da):43,314
Last modified:January 23, 2007 - v2
Checksum:i6EDA60255F43358F
GO

Sequence cautioni

The sequence AAN82549 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti394S → G in tufA. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN82549.1. Different initiation.
AE014075 Genomic DNA. Translation: AAN83363.1.
RefSeqiWP_000031784.1. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN82549; AAN82549; c4111.
AAN83363; AAN83363; c4935.
KEGGiecc:c4111.
ecc:c4935.
PATRICi18285976. VBIEscCol75197_3864.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN82549.1. Different initiation.
AE014075 Genomic DNA. Translation: AAN83363.1.
RefSeqiWP_000031784.1. NC_004431.1.

3D structure databases

ProteinModelPortaliP0A6N2.
SMRiP0A6N2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi199310.c4935.

Proteomic databases

PRIDEiP0A6N2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN82549; AAN82549; c4111.
AAN83363; AAN83363; c4935.
KEGGiecc:c4111.
ecc:c4935.
PATRICi18285976. VBIEscCol75197_3864.

Phylogenomic databases

eggNOGiENOG4105CGV. Bacteria.
COG0050. LUCA.
HOGENOMiHOG000229290.
KOiK02358.

Enzyme and pathway databases

BioCyciECOL199310:C4935-MONOMER.

Family and domain databases

CDDicd03697. EFTU_II. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR033720. EFTU_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEFTU_ECOL6
AccessioniPrimary (citable) accession number: P0A6N2
Secondary accession number(s): O68929
, P02990, Q8X4S9, Q8XED3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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.Curated

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.