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Entry version 140 (26 Feb 2020)
Sequence version 2 (23 Jan 2007)
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Protein

Elongation factor Ts

Gene

tsf

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

Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.UniRule annotation
(Microbial infection) In case of infection by bacteriophage Qbeta (and related Leviviruses), part of the viral RNA-dependent RNA polymerase complex. With EF-Tu may provide a stabilizing scaffold for the beta (catalytic) subunit, implicated in the elongation step of viral RNA synthesis where it fixes EF-Tu in an open conformation.6 Publications
(Microbial infection) Promotes the tRNase activity of CdiA-CT from E.coli strain EC869 (CdiA-CT-EC869); required in vivo but less so in vitro. Probably loads charged tRNA onto EF-Tu, making more ternary GTP-EF-Tu-aa-tRNA complexes. The guanine nucleotide exchange factor capacity of this protein does not seem to be needed as no GTP hydrolysis occurs during tRNA cleavage. Also required in vivo for toxic activity of CdiA-CT from E.coli strains NC101 and CdiA-CT-96.154. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Ts interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500).2 Publications
(Microbial infection) Promotes the tRNase activity of CdiA-CT from E.coli strain NC101 (CdiA-CT-NC101); required in vivo and in vitro. Probably loads charged tRNA onto EF-Tu, making more ternary GTP-EF-Tu-aa-tRNA complexes. The guanine nucleotide exchange factor capacity of this protein does not seem to be needed as no GTP hydrolysis occurs during tRNA cleavage. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28973472). EF-Ts interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500).2 Publications

Miscellaneous

In order to produce high amounts of bacteriophage Qbeta RNA polymerase catalytic core, a fusion protein consisting of tsf-tufB-replicase with a cleavable linker between tufB and the viral replicase subunit is frequently used.5 Publications

<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

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
Biological processProtein biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11033-MONOMER
ECOL316407:JW0165-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%5Fand%5Ftaxonomy%5Fsection">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 TsUniRule annotation
Short name:
EF-TsUniRule annotation
Alternative name(s):
Bacteriophage Q beta RNA-directed RNA polymerase subunit IV1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:tsfUniRule annotation
Ordered Locus Names:b0170, JW0165
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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

Cytoplasm

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi24K → A: No change in binding to EF-Tu and in promoting GDP exchange. 1 Publication1
Mutagenesisi81D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. 1 Publication1
Mutagenesisi82F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. 1 Publication1
Mutagenesisi148H → A: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. 1 Publication1
Mutagenesisi186 – 225VSAEV…KKFTG → EPGGEA: Resistant to toxins CdiA-CT-EC869, CdiA-CT-NC101 and CdiA-CT-96.154, but not other CdiA toxins in growth competition experiments, in vitro prevents CdiA-CT-EC869 from digesting tRNA(GUG-Gln). Resistant to bacteriophage R17. 1 PublicationAdd BLAST40
Mutagenesisi188 – 227Missing : Still associates with EF-Tu, no longer forms the Qbeta viral RNA polymerase complex. 1 PublicationAdd BLAST40
Mutagenesisi202A → E: Resistant to toxin CdiA-CT-EC869, partially resistant to toxins CdiA-CT-NC101 and CdiA-CT-96.154, but not resistant to other CdiA toxins in growth competition experiments, in vitro prevents CdiA-CT-EC869 from digesting tRNA(GUG-Gln). Partially resistant to bacteriophage R17. 1 Publication1
Mutagenesisi219R → P: Resistant to toxin CdiA-CT-EC869, partially resistant to toxins CdiA-CT-NC101 and CdiA-CT-96.154, but not resistant to other CdiA toxins in growth competition experiments. Resistant to bacteriophage R17. 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%5Fprocessing%5Fsection">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 methionineiRemoved3 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_00001611172 – 283Elongation factor TsAdd BLAST282

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A6P1

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A6P1

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

More...
PaxDbi
P0A6P1

PRoteomics IDEntifications database

More...
PRIDEi
P0A6P1

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A6P1

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P0A6P1

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes.

1 Publication

(Microbial infection) 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-Tu (PubMed:816798).

6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260795, 54 interactors

Database of interacting proteins

More...
DIPi
DIP-31835N

Protein interaction database and analysis system

More...
IntActi
P0A6P1, 12 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0170

<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

1283
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P0A6P1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A6P1

<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

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>Regioni80 – 83Involved in Mg(2+) ion dislocation from EF-TuUniRule annotation4

<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

Belongs to the EF-Ts family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CU7 Bacteria
COG0264 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_047155_0_2_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A6P1

KEGG Orthology (KO)

More...
KOi
K02357

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A6P1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.479.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00050 EF_Ts, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036402 EF-Ts_dimer_sf
IPR001816 Transl_elong_EFTs/EF1B
IPR014039 Transl_elong_EFTs/EF1B_dimer
IPR018101 Transl_elong_Ts_CS
IPR009060 UBA-like_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11741 PTHR11741, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00889 EF_TS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46934 SSF46934, 1 hit
SSF54713 SSF54713, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00116 tsf, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01126 EF_TS_1, 1 hit
PS01127 EF_TS_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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0A6P1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA
60 70 80 90 100
KKAGNVAADG VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA
110 120 130 140 150
VAGKITDVEV LKAQFEEERV ALVAKIGENI NIRRVAALEG DVLGSYQHGA
160 170 180 190 200
RIGVLVAAKG ADEELVKHIA MHVAASKPEF IKPEDVSAEV VEKEYQVQLD
210 220 230 240 250
IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK TVGQLLKEHN
260 270 280
AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS
Length:283
Mass (Da):30,423
Last modified:January 23, 2007 - v2
<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:i0B9D21E928A5051C
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 30294±6 Da. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
V00343 Genomic DNA Translation: CAA23632.1
D13334 Genomic DNA Translation: BAA02597.1
U00096 Genomic DNA Translation: AAC73281.1
AP009048 Genomic DNA Translation: BAB96746.1
U70214 Genomic DNA Translation: AAB08599.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A03525 EFECS

NCBI Reference Sequences

More...
RefSeqi
NP_414712.1, NC_000913.3
WP_000818114.1, NZ_STEB01000032.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73281; AAC73281; b0170
BAB96746; BAB96746; BAB96746

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
944866

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0165
eco:b0170

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2110

<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
V00343 Genomic DNA Translation: CAA23632.1
D13334 Genomic DNA Translation: BAA02597.1
U00096 Genomic DNA Translation: AAC73281.1
AP009048 Genomic DNA Translation: BAB96746.1
U70214 Genomic DNA Translation: AAB08599.1
PIRiA03525 EFECS
RefSeqiNP_414712.1, NC_000913.3
WP_000818114.1, NZ_STEB01000032.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EFUX-ray2.50B/D2-283[»]
3AGPX-ray2.80A1-283[»]
3AGQX-ray3.22A1-283[»]
3AVTX-ray2.61A1-283[»]
3AVUX-ray2.91A1-283[»]
3AVVX-ray3.12A1-283[»]
3AVWX-ray2.60A1-283[»]
3AVXX-ray2.41A1-283[»]
3AVYX-ray2.62A1-283[»]
3MMPX-ray2.50A/C1-283[»]
3VNUX-ray3.20A1-283[»]
3VNVX-ray2.60A1-283[»]
4FWTX-ray3.20A1-283[»]
4PC3X-ray1.83C/D2-283[»]
4PC7X-ray3.60C2-283[»]
4Q7JX-ray2.90A/E2-283[»]
4R71X-ray3.21A/C1-283[»]
SMRiP0A6P1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4260795, 54 interactors
DIPiDIP-31835N
IntActiP0A6P1, 12 interactors
STRINGi511145.b0170

PTM databases

CarbonylDBiP0A6P1

2D gel databases

SWISS-2DPAGEiP0A6P1

Proteomic databases

EPDiP0A6P1
jPOSTiP0A6P1
PaxDbiP0A6P1
PRIDEiP0A6P1

Genome annotation databases

EnsemblBacteriaiAAC73281; AAC73281; b0170
BAB96746; BAB96746; BAB96746
GeneIDi944866
KEGGiecj:JW0165
eco:b0170
PATRICifig|1411691.4.peg.2110

Organism-specific databases

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

More...
EchoBASEi
EB1026

Phylogenomic databases

eggNOGiENOG4105CU7 Bacteria
COG0264 LUCA
HOGENOMiCLU_047155_0_2_6
InParanoidiP0A6P1
KOiK02357
PhylomeDBiP0A6P1

Enzyme and pathway databases

BioCyciEcoCyc:EG11033-MONOMER
ECOL316407:JW0165-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A6P1

Protein Ontology

More...
PROi
PR:P0A6P1

Family and domain databases

Gene3Di3.30.479.20, 1 hit
HAMAPiMF_00050 EF_Ts, 1 hit
InterProiView protein in InterPro
IPR036402 EF-Ts_dimer_sf
IPR001816 Transl_elong_EFTs/EF1B
IPR014039 Transl_elong_EFTs/EF1B_dimer
IPR018101 Transl_elong_Ts_CS
IPR009060 UBA-like_sf
PANTHERiPTHR11741 PTHR11741, 1 hit
PfamiView protein in Pfam
PF00889 EF_TS, 1 hit
SUPFAMiSSF46934 SSF46934, 1 hit
SSF54713 SSF54713, 2 hits
TIGRFAMsiTIGR00116 tsf, 1 hit
PROSITEiView protein in PROSITE
PS01126 EF_TS_1, 1 hit
PS01127 EF_TS_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiEFTS_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: P0A6P1
Secondary accession number(s): P02997
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 26, 2020
This is version 140 of the entry and version 2 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, 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
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