Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Elongation factor Tu 1

Gene

tufA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi19 – 26GTP8
Nucleotide bindingi81 – 85GTP5
Nucleotide bindingi136 – 139GTP4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-UniRule
  • translation elongation factor activity Source: GO_Central

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11036-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tufAUniRule annotation
Ordered Locus Names:b3339, JW3301
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG11036 tufA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000913202 – 394Elongation factor Tu 1Add BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine2 Publications1
Modified residuei57N6,N6-dimethyllysine; alternate4 Publications1
Modified residuei57N6-methyllysine; alternate4 Publications1
Modified residuei314N6-acetyllysine1 Publication1
Modified residuei383Phosphothreonine3 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
P0CE47

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0CE47

PRoteomics IDEntifications database

More...
PRIDEi
P0CE47

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P0CE47

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0CE47

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259390, 79 interactors
852150, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-6159N

Protein interaction database and analysis system

More...
IntActi
P0CE47, 162 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_3514

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0CE47

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0CE47

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0CE47

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini10 – 204tr-type GAdd BLAST195

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni19 – 26G1By similarity8
Regioni60 – 64G2By similarity5
Regioni81 – 84G3By similarity4
Regioni136 – 139G4By similarity4
Regioni174 – 176G5By similarity3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CGV Bacteria
COG0050 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0CE47

KEGG Orthology (KO)

More...
KOi
K02358

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0CE47

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03697 EFTU_II, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00118_B EF_Tu_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit
PF03143 GTP_EFTU_D3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00315 ELONGATNFCT

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50447 SSF50447, 1 hit
SSF50465 SSF50465, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00485 EF-Tu, 1 hit
TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00301 G_TR_1, 1 hit
PS51722 G_TR_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i731A60255F43358F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
A91475 EFECTA

NCBI Reference Sequences

More...
RefSeqi
NP_417798.1, NC_000913.3
WP_000031783.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76364; AAC76364; b3339
BAE77952; BAE77952; BAE77952

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947838

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3301
eco:b3339

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3392

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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...

Protein-protein interaction databases

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

PTM databases

CarbonylDBiP0CE47
iPTMnetiP0CE47

Proteomic databases

EPDiP0CE47
PaxDbiP0CE47
PRIDEiP0CE47

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1029
EcoGeneiEG11036 tufA

Phylogenomic databases

eggNOGiENOG4105CGV Bacteria
COG0050 LUCA
InParanoidiP0CE47
KOiK02358
PhylomeDBiP0CE47

Enzyme and pathway databases

BioCyciEcoCyc:EG11036-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0CE47

Protein Ontology

More...
PROi
PR:P0CE47

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEFTU1_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0CE47
Secondary accession number(s): O68929
, P02990, P0A6N1, Q2M704, Q2M8R6, Q8X4S9, Q8XED3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: November 7, 2018
This is version 73 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again