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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 268GTPUniRule annotation
Nucleotide bindingi81 – 855GTPUniRule annotation
Nucleotide bindingi136 – 1394GTPUniRule annotation

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-HAMAP
  3. translation elongation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. response to antibiotic Source: UniProtKB-KW
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001410: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 394393Elongation factor TuPRO_0000091322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei57 – 571N6-methylated lysineBy similarity
Modified residuei314 – 3141N6-acetyllysineBy similarity
Modified residuei383 – 3831PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRIDEiP0A6N2.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi199310.c4111.

Structurei

3D structure databases

ProteinModelPortaliP0A6N2.
SMRiP0A6N2. Positions 9-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 204195tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 268G1By similarity
Regioni60 – 645G2By similarity
Regioni81 – 844G3By similarity
Regioni136 – 1394G4By similarity
Regioni174 – 1763G5By similarity

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

HOGENOMiHOG000229290.
KOiK02358.
OrthoDBiEOG6R5C6X.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B.
InterProiIPR000795. 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]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. 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 AAN82549.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti394 – 3941S → G in tufA.

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.
RefSeqiNP_755975.2. NC_004431.1.
NP_756789.1. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN82549; AAN82549; c4111.
AAN83363; AAN83363; c4935.
GeneIDi1036191.
1039881.
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.
RefSeqiNP_755975.2. NC_004431.1.
NP_756789.1. NC_004431.1.

3D structure databases

ProteinModelPortaliP0A6N2.
SMRiP0A6N2. Positions 9-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi199310.c4111.

Proteomic databases

PRIDEiP0A6N2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN82549; AAN82549; c4111.
AAN83363; AAN83363; c4935.
GeneIDi1036191.
1039881.
KEGGiecc:c4111.
ecc:c4935.
PATRICi18285976. VBIEscCol75197_3864.

Phylogenomic databases

HOGENOMiHOG000229290.
KOiK02358.
OrthoDBiEOG6R5C6X.

Enzyme and pathway databases

BioCyciECOL199310:C4935-MONOMER.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B.
InterProiIPR000795. 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]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. 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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB).
    Strain: CFT073 / ATCC 700928 / UPEC.

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: January 7, 2015
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.