Difference between revisions of "TufA"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fusA]]'', ''[[ybaC]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fusA]]'', ''[[ybaC]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU01130 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU01130 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU01130 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU01130 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU01130 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU01130 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:tufA_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:tufA_context.gif]]

Revision as of 09:15, 14 May 2013

  • Description: elongation factor Tu

Gene name tufA
Synonyms
Essential yes PubMed
Product elongation factor Tu
Function translation
Gene expression levels in SubtiExpress: tufA
Interactions involving this protein in SubtInteract: TufA
MW, pI 43 kDa, 4.723
Gene length, protein length 1188 bp, 396 aa
Immediate neighbours fusA, ybaC
Sequences Protein DNA DNA_with_flanks
Genetic context
TufA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TufA expression.png
























Categories containing this gene/protein

translation, essential genes, membrane proteins, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01130

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: EF-Tu/EF-1A subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on Thr-384 by PrkC, dephosphorylated by PrpC PubMed, PubMed
    • Cys83 is S-bacillithiolated in B. subtilis and other Bacillus species PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
    • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP839, available in Stülke lab
    • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP847, available in Stülke lab


  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038] [WorldCat.org] [DOI] (I p)

Hervé Joël Defeu Soufo, Christian Reimold, Uwe Linne, Tobias Knust, Johannes Gescher, Peter L Graumann
Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein.
Proc Natl Acad Sci U S A: 2010, 107(7);3163-8
[PubMed:20133608] [WorldCat.org] [DOI] (I p)

Cédric Absalon, Michal Obuchowski, Edwige Madec, Delphine Delattre, I Barry Holland, Simone J Séror
CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 3);932-943
[PubMed:19246764] [WorldCat.org] [DOI] (P p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)