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P0A6N2

- EFTU_ECOL6

UniProt

P0A6N2 - EFTU_ECOL6

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Protein
Elongation factor Tu
Gene
tufA, c4111
tufB, c4935
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed - 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 By similarity.UniRule annotation
May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation By similarity.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 268GTP By similarity
Nucleotide bindingi81 – 855GTP By similarity
Nucleotide bindingi136 – 1394GTP By similarity

GO - Molecular functioni

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

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 Tu
Short name:
EF-Tu
Alternative name(s):
P-43
Gene namesi
Name:tufA
Ordered Locus Names:c4111
AND
Name:tufB
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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 394393Elongation factor TuUniRule annotation
PRO_0000091322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei57 – 571N6-methylated lysine By similarity
Modified residuei314 – 3141N6-acetyllysine By similarity
Modified residuei383 – 3831Phosphothreonine By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRIDEiP0A6N2.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi199310.c4111.

Structurei

3D structure databases

ProteinModelPortaliP0A6N2.
SMRiP0A6N2. Positions 9-394.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 268G1 By similarity
Regioni60 – 645G2 By similarity
Regioni81 – 844G3 By similarity
Regioni136 – 1394G4 By similarity
Regioni174 – 1763G5 By similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000229290.
KOiK02358.
OMAiKEECENH.
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

MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI    50
DNAPEEKARG ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD 100
GAILVVAATD GPMPQTREHI LLGRQVGVPY IIVFLNKCDM VDDEELLELV 150
EMEVRELLSQ YDFPGDDTPI VRGSALKALE GDAEWEAKIL ELAGFLDSYI 200
PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG EEVEIVGIKE 250
TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK 300
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM 350
VMPGDNIKMV VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS 394
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.

Natural variant

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE014075 Genomic DNA. Translation: AAN82549.1 . Different initiation.
AE014075 Genomic DNA. Translation: AAN83363.1 .
RefSeqi NP_755975.2. NC_004431.1.
NP_756789.1. NC_004431.1.

3D structure databases

ProteinModelPortali P0A6N2.
SMRi P0A6N2. Positions 9-394.
ModBasei Search...

Protein-protein interaction databases

STRINGi 199310.c4111.

Proteomic databases

PRIDEi P0A6N2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN82549 ; AAN82549 ; c4111 .
AAN83363 ; AAN83363 ; c4935 .
GeneIDi 1036191.
1039881.
KEGGi ecc:c4111.
ecc:c4935.
PATRICi 18285976. VBIEscCol75197_3864.

Phylogenomic databases

HOGENOMi HOG000229290.
KOi K02358.
OMAi KEECENH.
OrthoDBi EOG6R5C6X.

Enzyme and pathway databases

BioCyci ECOL199310:C4935-MONOMER.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00118_B. EF_Tu_B.
InterProi IPR000795. 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 ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 76 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.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi