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Protein

Elongation factor Tu 1

Gene

tufA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.
In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Ts may provide a stabilizing scaffold for the beta (catalytic) subunit. Helps separate the double-stranded RNA of the template and growing RNA during elongation. With the beta subunit helps form the exit tunnel for template RNA.Curated1 Publication
Plays a stimulatory role in trans-translation; binds tmRNA.1 Publication
Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D-aminoacyl-tRNA deacylase (dtd) (By similarity).By similarity

Miscellaneous

Present with about 70,000 molecules/cell.1 Publication
This chain is also used in bacteriophage Q-beta RNA polymerase.1 Publication
The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome.1 Publication
The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu.1 Publication

Caution

EF-Tu 1 and EF-Tu 2 differ in a single position and are no longer merged. However, many papers are found in both entries as it is not always possible to determine for each paper which of EF-Tu 1 or EF-Tu 2 was being worked upon.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 26GTP8
Nucleotide bindingi81 – 85GTP5
Nucleotide bindingi136 – 139GTP4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionElongation factor, RNA-binding
Biological processAntibiotic resistance, Protein biosynthesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11036-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Tu 1UniRule annotation
Short name:
EF-Tu 1UniRule annotation
Alternative name(s):
Bacteriophage Q beta RNA-directed RNA polymerase subunit III1 Publication
P-43
Gene namesi
Name:tufAUniRule annotation
Ordered Locus Names:b3339, JW3301
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11036 tufA

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20H → A: No change in binding GDP and 3-fold reduction in binding EF-Ts. 1 Publication1
Mutagenesisi21V → G: Lowers GTPase activity 5 to 10-fold. 1 Publication1
Mutagenesisi83P → T: Loss of GTPase activity and creation of an autophosphorylation site. 1 Publication1
Mutagenesisi115Q → A: Weaker binding for GDP and for EF-Ts. 1 Publication1
Mutagenesisi125Q → K: Kirromycin resistant. 1 Publication1
Mutagenesisi137K → R, Q, E or I: Reduces affinity for GDP. 1 Publication1
Mutagenesisi139D → N: Reduces affinity for GDP; increases affinity for XDP. 1 Publication1
Mutagenesisi223G → D: Inhibits codon-induced conformational changes leading to GTPase activation on the ribosome. 1 Publication1
Mutagenesisi231R → C: Pulvomycin resistant. 1 Publication1
Mutagenesisi317G → D: Kirromycin resistant. 1 Publication1
Mutagenesisi334R → C: Pulvomycin resistant. 1 Publication1
Mutagenesisi335T → A: Pulvomycin resistant. 1 Publication1
Mutagenesisi349E → A: No change in binding GDP but higher binding constant for EF-Ts. 1 Publication1
Mutagenesisi376A → T or V: Kirromycin resistant. 1 Publication1
Mutagenesisi383T → V: No longer phosphorylated by phage protein doc, has no effect on translation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000913202 – 394Elongation factor Tu 1Add BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine2 Publications1
Modified residuei57N6,N6-dimethyllysine; alternate4 Publications1
Modified residuei57N6-methyllysine; alternate4 Publications1
Modified residuei314N6-acetyllysine1 Publication1
Modified residuei383Phosphothreonine3 Publications1

Post-translational modificationi

The N-terminus is blocked.
Methylated in vivo on Lys-57 in response to nutrient starvation.4 Publications
Phosphorylated in vitro by phage protein doc on Thr-383.3 Publications
Phosphorylated in vitro by HipA on Thr-383 (PubMed:19150849), this has since been reported not to occur in vivo (PubMed:24095282).4 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP0CE47
PaxDbiP0CE47
PRIDEiP0CE47

PTM databases

CarbonylDBiP0CE47
iPTMnetiP0CE47

Interactioni

Subunit structurei

Monomer. In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex, the other subunits are the viral replicase catalytic subunit (AC P14647), host ribosomal protein S1 and EF-Ts (PubMed:816798).UniRule annotationCurated4 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4259390, 79 interactors
852150, 1 interactor
DIPiDIP-6159N
IntActiP0CE47, 162 interactors
STRINGi316385.ECDH10B_3514

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 7Combined sources4
Beta strandi12 – 19Combined sources8
Beta strandi20 – 24Combined sources5
Helixi25 – 40Combined sources16
Helixi47 – 51Combined sources5
Beta strandi55 – 60Combined sources6
Beta strandi62 – 64Combined sources3
Beta strandi68 – 71Combined sources4
Beta strandi76 – 81Combined sources6
Helixi85 – 94Combined sources10
Beta strandi95 – 97Combined sources3
Beta strandi100 – 107Combined sources8
Turni108 – 110Combined sources3
Helixi116 – 125Combined sources10
Beta strandi131 – 136Combined sources6
Helixi138 – 140Combined sources3
Helixi144 – 160Combined sources17
Turni165 – 167Combined sources3
Beta strandi170 – 172Combined sources3
Helixi175 – 179Combined sources5
Helixi183 – 199Combined sources17
Helixi206 – 208Combined sources3
Beta strandi212 – 214Combined sources3
Beta strandi217 – 221Combined sources5
Turni222 – 224Combined sources3
Beta strandi225 – 231Combined sources7
Beta strandi234 – 238Combined sources5
Beta strandi242 – 249Combined sources8
Beta strandi252 – 261Combined sources10
Beta strandi264 – 270Combined sources7
Beta strandi274 – 281Combined sources8
Helixi284 – 286Combined sources3
Beta strandi292 – 294Combined sources3
Turni296 – 298Combined sources3
Beta strandi301 – 311Combined sources11
Turni314 – 317Combined sources4
Beta strandi323 – 327Combined sources5
Beta strandi330 – 333Combined sources4
Beta strandi336 – 343Combined sources8
Beta strandi356 – 368Combined sources13
Beta strandi374 – 379Combined sources6
Beta strandi382 – 394Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8TX-ray2.35A/B2-394[»]
1EFCX-ray2.05A/B2-393[»]
1ETUX-ray2.90A2-394[»]
1MJ1electron microscopy13.00A8-389[»]
2FX3X-ray3.40A2-394[»]
2HCJX-ray2.12A9-45[»]
B60-394[»]
2HDNX-ray2.80A/C/E/G/I/K9-45[»]
B/D/F/H/J/L60-394[»]
3EP2electron microscopy-X2-393[»]
3EQ3electron microscopy-X2-393[»]
3EQ4electron microscopy-X2-393[»]
3U2QX-ray2.70A3-394[»]
3U6BX-ray2.12A/B3-394[»]
3U6KX-ray2.45A/B3-394[»]
4G5GX-ray2.30A3-394[»]
4PC3X-ray1.83A/B1-394[»]
4PC7X-ray3.60A1-394[»]
4Q7JX-ray2.90B/F2-394[»]
4V69electron microscopy6.70AZ2-393[»]
5I4QX-ray2.35C178-394[»]
5I4RX-ray3.30D/H60-394[»]
5JBQX-ray2.01A1-394[»]
5UYKelectron microscopy3.90Z2-393[»]
5UYLelectron microscopy3.60Z2-393[»]
5UYMelectron microscopy3.20Z2-393[»]
5UYNelectron microscopy4.00Z2-393[»]
5UYPelectron microscopy3.90Z2-393[»]
5UYQelectron microscopy3.80Z2-393[»]
ProteinModelPortaliP0CE47
SMRiP0CE47
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CE47

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
InParanoidiP0CE47
KOiK02358
PhylomeDBiP0CE47

Family and domain databases

CDDicd03697 EFTU_II, 1 hit
HAMAPiMF_00118_B EF_Tu_B, 1 hit
InterProiView protein in InterPro
IPR004161 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_sf
IPR009001 Transl_elong_EF1A/Init_IF2_C
IPR004541 Transl_elong_EFTu/EF1A_bac/org
IPR004160 Transl_elong_EFTu/EF1A_C
PfamiView protein in Pfam
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit
PF03143 GTP_EFTU_D3, 1 hit
PRINTSiPR00315 ELONGATNFCT
SUPFAMiSSF50447 SSF50447, 1 hit
SSF50465 SSF50465, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00485 EF-Tu, 1 hit
TIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS00301 G_TR_1, 1 hit
PS51722 G_TR_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0CE47-1 [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 KVLG
Length:394
Mass (Da):43,284
Last modified:March 23, 2010 - v1
Checksum:i731A60255F43358F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01690 Genomic DNA Translation: AAA50993.1
M10459 Genomic DNA Translation: AAA24702.1
U00096 Genomic DNA Translation: AAC76364.1
AP009048 Genomic DNA Translation: BAE77952.1
U18997 Genomic DNA Translation: AAA58136.1
AF058450 Genomic DNA Translation: AAC14286.1
PIRiA91475 EFECTA
RefSeqiNP_417798.1, NC_000913.3
WP_000031783.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76364; AAC76364; b3339
BAE77952; BAE77952; BAE77952
GeneIDi947838
KEGGiecj:JW3301
eco:b3339
PATRICifig|1411691.4.peg.3392

Similar proteinsi

Entry informationi

Entry nameiEFTU1_ECOLI
AccessioniPrimary (citable) accession number: P0CE47
Secondary accession number(s): O68929
, P02990, P0A6N1, Q2M704, Q2M8R6, Q8X4S9, Q8XED3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: February 28, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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