tufA

168

elongation factor Tu, binds to charged tRNAs to form ternary complexes, brings charged tRNAs to empty ribosome A sites

Locus: BSU_01130

Molecular weight: 43.43 kDa

Isoelectric point: 4.72

Protein length: 396 aa

Gene length: 1191 bp

Function: translation

Product: elongation factor Tu

Essential: yes

E.C.: 3.6.5.3

Synonyms: tufA

Genomic Context

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List of homologs in different organisms, belongs to COG0050 (Galperin et al., 2021)

Gene

Coordinates: 132,882 134,072

Phenotypes of a mutant

• essential PubMed

The protein

Catalyzed reaction/ biological activity

• binds to charged tRNAs to form ternary complexes, brings charged tRNAs to empty ribosome A sites PubMed

Protein family

• TRAFAC class translation factor GTPase superfamily (according to UniProt)
• Classic translation factor GTPase family (according to UniProt)

Domains

• tr-type G domain (aa 10-205) (according to UniProt)

Structure

• 3U6B (PDB) (from E. coli , 77% identity) PubMed
• P33166 (AlphaFold)

Modification

• acetylated by RimI PubMed
• phosphorylated on Thr-384 by PrkC, dephosphorylated by PrpC PubMed, PubMed
• Cys83 is S-bacillithiolated in B. subtilis and other Bacillus species PubMed
• phosphorylated on Arg-265 PubMed
• phosphorylated on several Arg residues PubMed
• phosphorylated during sporulation on Thr-63 by YabT, dephosphorylated by PrpC PubMed
• phosphorylated on Tyr-270 PubMed

Effectors of protein activity

• phosphorylation by YabT results in inhibtion of GTP hydrolysis; as a result, EF-Tu remains stably bound
• to the ribosome, stalling protein translation PubMed

Localization

• EF-Tu localizes in a helical pattern underneath the cell membrane and colocalizes with MreB PubMed
• membrane PubMed
• cytoplasm (according to UniProt)

Additional information

• belongs to the 100 most abundant proteins PubMed

Expression and Regulation

Operons

• Genes: rplGB-rpsL-rpsG-fusA-tufA

  Description: PubMed

  Regulation

  • Rel dependent downregulation (Class I) during stringent response PubMed
  • the mRNA is processed between rplGB and rpsL by RNase Y, this requires the RicA-RicF-RicT complex PubMed

  Regulatory mechanism

  • stringent response: negative regulation, PubMed, in stringent response

Biological materials

Two-hybrid system

• B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

References

Reviews

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Original Publications

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