fusA
168
elongation factor G, catalyzes translocation steps of the ribosome after peptide bond formation, facilitates movement of tRNA and mRNA by one codon
Locus
BSU_01120
Molecular weight
76.36 kDa
Isoelectric point
4.61
Function
translation
Product
elongation factor G
Essential
yes
Synonyms
fusA, fus
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG0480 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
130,684 132,762
Phenotypes of a mutant
The protein
Catalyzed reaction/ biological activity
hydrolyses GTP
catalyzes translocation steps of the ribosome after peptide bond formation, facilitates movement of tRNA and mRNA by one codon PubMed
Protein family
TRAFAC class translation factor GTPase superfamily (according to UniProt)
Classic translation factor GTPase family (according to UniProt)
tr-type G domain (aa 8-282) (according to UniProt)
Structure
2XEX (PDB) (from Staphylococcus aureus, 78.35% identity) PubMed
1ELO (PDB) (from Thermus thermophilus) PubMed
4BTC (PDB), 4BTD (PDB), the Thermus thermophilus EF-Gribosome complex in a pretranslocation state PubMed
Modification
phosphorylation on Ser-213 AND Ser-302 AND Ser-569 AND Ser-680 AND (Thr-24 OR Thr-25) AND (Thr-43 OR Ser 48) PubMed, PubMed
phosphorylated on Tyr-339 PubMed
cytoplasm (according to UniProt)
Additional information
belongs to the 100 most abundant proteins PubMed
Expression and Regulation
Operons
Description
Regulation
Regulatory mechanism
stringent response: negative regulation, PubMed, in stringent response
Biological materials
Expression vectors
References
Reviews
Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu.Quarterly reviews of biophysics. 2009 Aug; 42(3):159-200. PMID: 20025795
Original Publications
Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation.Nature communications. 2021 Jul 30; 12(1):4644. PMID: 34330903
Essentiality of c-di-AMP in Bacillus subtilis: Bypassing mutations converge in potassium and glutamate homeostasis.PLoS genetics. 2021 Jan 22; 17(1):e1009092. PMID: 33481774
Kinetics of Spontaneous and EF-G-Accelerated Rotation of Ribosomal Subunits.
Cell reports. 2016 Aug 23; 16(8):2187-96. doi:10.1016/j.celrep.2016.07.051. pii:S2211-1247(16)30982-2. PMID:27524615
Phosphoproteome dynamics mediate revival of bacterial spores.
BMC biology. 2015 Sep 17; 13:76. doi:10.1186/s12915-015-0184-7. PMID:26381121
Fluctuations between multiple EF-G-induced chimeric tRNA states during translocation on the ribosome.
Nature communications. 2015 Jun 15; 6:7442. doi:10.1038/ncomms8442. PMID:26072700
EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon-anticodon duplex.
Nature structural & molecular biology. 2014 Sep; 21(9):817-24. doi:10.1038/nsmb.2869. PMID:25108354
GTP hydrolysis by EF-G synchronizes tRNA movement on small and large ribosomal subunits.
The EMBO journal. 2014 May 02; 33(9):1073-85. doi:10.1002/embj.201387465. PMID:24614227
Structure of EF-G-ribosome complex in a pretranslocation state.
Nature structural & molecular biology. 2013 Sep; 20(9):1077-84. doi:10.1038/nsmb.2645. PMID:23912278
. . PMID: 20718859
Atomic mutagenesis reveals A2660 of 23S ribosomal RNA as key to EF-G GTPase activation.
Nature chemical biology. 2010 May; 6(5):344-51. doi:10.1038/nchembio.341. PMID:20348921
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics. 2007 Oct; 7(19):3509-26. . PMID:17726680
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Molecular & cellular proteomics : MCP. 2007 Apr; 6(4):697-707. . PMID:17218307
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics. 2004 Oct; 4(10):2849-76. . PMID:15378759
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
The EMBO journal. 1994 Aug 15; 13(16):3669-77. . PMID:8070397
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Time of last update: 2025-01-17 14:03:47
Author of last update: Jstuelk