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P0A6N3

- EFTU_ECO57

UniProt

P0A6N3 - EFTU_ECO57

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Protein

Elongation factor Tu

Gene

tufA

more
Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 4 out of 5- 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.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

BioCyciECOL386585:GJFA-4159-MONOMER.
ECOL386585:GJFA-4902-MONOMER.
ECOO157:TUFA-MONOMER.
ECOO157:TUFB-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:Z4697, ECs4190
AND
Name:tufBUniRule annotation
Ordered Locus Names:Z5553, ECs4903
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
  2. plasma membrane Source: UniProtKB-KW
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_0000091321Add
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

PRIDEiP0A6N3.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

MINTiMINT-1234032.
STRINGi155864.Z4697.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 209
Helixi21 – 233
Helixi25 – 3915
Beta strandi68 – 714
Beta strandi76 – 816
Helixi85 – 939
Beta strandi94 – 963
Beta strandi100 – 1078
Turni108 – 1103
Helixi116 – 12611
Beta strandi131 – 1366
Helixi138 – 1403
Helixi144 – 16017
Turni165 – 1673
Beta strandi170 – 1723
Turni176 – 1805
Helixi183 – 19816
Helixi206 – 2083
Beta strandi212 – 2143
Beta strandi217 – 2215
Turni222 – 2243
Beta strandi225 – 2317
Beta strandi234 – 2385
Beta strandi242 – 2509
Beta strandi252 – 2609
Beta strandi265 – 2706
Beta strandi274 – 2818
Helixi284 – 2863
Beta strandi292 – 2954
Turni296 – 2983
Beta strandi301 – 31111
Helixi314 – 3163
Beta strandi330 – 3323
Beta strandi334 – 3363
Beta strandi337 – 3437
Beta strandi358 – 36811
Beta strandi374 – 3796
Beta strandi382 – 39211

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AGPX-ray2.80A1-394[»]
3AGQX-ray3.22A1-394[»]
3AVTX-ray2.61A1-394[»]
3AVUX-ray2.91A1-394[»]
3AVVX-ray3.12A1-394[»]
3AVWX-ray2.60A1-394[»]
3AVXX-ray2.41A1-394[»]
3AVYX-ray2.62A1-394[»]
3VNUX-ray3.20A1-394[»]
3VNVX-ray2.60A1-394[»]
4FWTX-ray3.20A1-394[»]
ProteinModelPortaliP0A6N3.
SMRiP0A6N3. Positions 9-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6N3.

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

eggNOGiCOG0050.
HOGENOMiHOG000229290.
KOiK02358.
OMAiGTEMCMP.
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.

P0A6N3-1 [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

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
AE005174 Genomic DNA. Translation: AAG58446.1.
AE005174 Genomic DNA. Translation: AAG59176.1.
BA000007 Genomic DNA. Translation: BAB37613.1.
BA000007 Genomic DNA. Translation: BAB38326.1.
PIRiB85998.
G91241.
RefSeqiNP_289886.1. NC_002655.2.
NP_290611.1. NC_002655.2.
NP_312217.1. NC_002695.1.
NP_312930.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG58446; AAG58446; Z4697.
AAG59176; AAG59176; Z5553.
BAB37613; BAB37613; BAB37613.
BAB38326; BAB38326; BAB38326.
GeneIDi914959.
915957.
958801.
960150.
KEGGiece:Z4697.
ece:Z5553.
ecs:ECs4190.
ecs:ECs4903.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG58446.1 .
AE005174 Genomic DNA. Translation: AAG59176.1 .
BA000007 Genomic DNA. Translation: BAB37613.1 .
BA000007 Genomic DNA. Translation: BAB38326.1 .
PIRi B85998.
G91241.
RefSeqi NP_289886.1. NC_002655.2.
NP_290611.1. NC_002655.2.
NP_312217.1. NC_002695.1.
NP_312930.1. NC_002695.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AGP X-ray 2.80 A 1-394 [» ]
3AGQ X-ray 3.22 A 1-394 [» ]
3AVT X-ray 2.61 A 1-394 [» ]
3AVU X-ray 2.91 A 1-394 [» ]
3AVV X-ray 3.12 A 1-394 [» ]
3AVW X-ray 2.60 A 1-394 [» ]
3AVX X-ray 2.41 A 1-394 [» ]
3AVY X-ray 2.62 A 1-394 [» ]
3VNU X-ray 3.20 A 1-394 [» ]
3VNV X-ray 2.60 A 1-394 [» ]
4FWT X-ray 3.20 A 1-394 [» ]
ProteinModelPortali P0A6N3.
SMRi P0A6N3. Positions 9-394.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1234032.
STRINGi 155864.Z4697.

Proteomic databases

PRIDEi P0A6N3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG58446 ; AAG58446 ; Z4697 .
AAG59176 ; AAG59176 ; Z5553 .
BAB37613 ; BAB37613 ; BAB37613 .
BAB38326 ; BAB38326 ; BAB38326 .
GeneIDi 914959.
915957.
958801.
960150.
KEGGi ece:Z4697.
ece:Z5553.
ecs:ECs4190.
ecs:ECs4903.

Phylogenomic databases

eggNOGi COG0050.
HOGENOMi HOG000229290.
KOi K02358.
OMAi GTEMCMP.
OrthoDBi EOG6R5C6X.

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-4159-MONOMER.
ECOL386585:GJFA-4902-MONOMER.
ECOO157:TUFA-MONOMER.
ECOO157:TUFB-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6N3.

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: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB).
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiEFTU_ECO57
AccessioniPrimary (citable) accession number: P0A6N3
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: October 29, 2014
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

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3