Elongation factor 2 - Saccharomyces cerevisiae (Baker's yeast)

Names and origin

Protein names

Recommended name:
    Elongation factor 2
      Short name=EF-2
Alternative name(s):
    Translation elongation factor 2
    Eukaryotic elongation factor 2
      Short name=eEF2
    Ribosomal translocase

Gene names

Name:	EFT1
Ordered Locus Names:	YOR133W
ORF Names:	O3317, YOR3317W
AND
Name:	EFT2
Ordered Locus Names:	YDR385W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	842 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site and of the deacylated tRNA from the P-site to the E-site of the ribosome during protein biosynthesis.
Enzyme regulation	Inhibited by fusidic acid and sordarin, which prevent the release of eEF2 from the ribosome after the translocation step. While fusidic acid acts on all eukaryotic eEF2, sordarin specifically binds and inhibits only selected fungal eEF2. Inhibited by diphtheria toxin and Pseudomonas aeruginosa exotoxin A (ETA), which ADP-ribosylate the diphthamide residue.
Pathway	Protein biosynthesis; polypeptide chain elongation.
Subunit structure	Binds to 80S ribosomes. Interacts directly with the 40S ribosomal subunit protein RPL9A, the 60S ribosomal subunit proteins RPL12A and RPS23A, as well as the 18S rRNA and the 25S rRNA. Interacts with RPL0.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 160782 molecules/cell in log phase SD medium. There are 2 genes for eEF2 in yeast.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=0.010 mM for GTP

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Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding RNA-binding rRNA-binding
Molecular function	Elongation factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	translational elongation Traceable author statement. Source: SGD
Cellular component	ribosome Traceable author statement. Source: SGD
Molecular function	protein binding Ref.13 Inferred from physical interaction. Source: IntAct ribonucleoprotein binding Inferred from physical interaction. Source: UniProtKB translation elongation factor activity Traceable author statement. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	P38332	1	EBI-6333,EBI-21094
RPP0	P05317	1	EBI-6333,EBI-15447
RPT6	Q01939	1	EBI-6333,EBI-13914
SKP1	P52286	1	EBI-6333,EBI-4090

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 842

842

Elongation factor 2

Regions

Nucleotide binding

26 – 33

8

GTP By similarity

Nucleotide binding

104 – 108

5

GTP By similarity

Nucleotide binding

158 – 161

4

GTP By similarity

Amino acid modifications

Modified residue

79

1

Phosphoserine

Modified residue

82

1

Phosphoserine

Modified residue

514

1

Phosphoserine

Modified residue

569

1

Phosphoserine

Modified residue

572

1

Phosphoserine

Modified residue

699

1

Diphthamide

Modified residue

763

1

Phosphothreonine

Experimental info

Mutagenesis

180

1

R → G: Causes resistance to fusidic acid and reduces sensitivity to sordarin

Mutagenesis

187

1

V → F: Causes resistance to fusidic acid and reduces sensitivity to sordarin

Mutagenesis

490

1

Q → E: Reduces sensitivity to sordarin

Mutagenesis

521

1

Y → D, N or S: Reduces sensitivity to fusidic acid and sordarin

Mutagenesis

523

1

S → F or P: Causes resistance to fusidic acid and sordarin

Mutagenesis

529

1

I → T: Reduces sensitivity to sordarin

Mutagenesis

559

1

P → L or R: Causes resistance to fusidic acid and sordarin

Mutagenesis

562

1

A → P: Reduces sensitivity to fusidic acid and causes resistance to sordarin

Mutagenesis

699

1

H → D, E, L or M: Prevents post-translational modification of this residue to diphthamide. Results in a functional protein that is resistant to diphtheria toxin

Mutagenesis

701

1

G → R: Prevents ADP-ribosylation of the diphthamide by diphtheria toxin

Mutagenesis

727

1

P → S: Causes resistance to sordarin

Mutagenesis

774

1

V → F: Causes resistance to sordarin

Mutagenesis

790

1

Missing: Causes resistance to fusidic acid and sordarin

Secondary structure

1

.

842

Helix Strand Turn

Details...

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure