Difference between revisions of "TuaD"

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Revision as of 14:43, 16 May 2013

  • Description: UDP glucose 6-dehydrogenase

Gene name tuaD
Synonyms yvhD
Essential no
Product UDP glucose 6-dehydrogenase
Function biosynthesis of teichuronic acid
Gene expression levels in SubtiExpress: tuaD
Interactions involving this protein in SubtInteract: TuaD
MW, pI 49 kDa, 6.107
Gene length, protein length 1383 bp, 461 aa
Immediate neighbours tuaE, tuaC
Sequences Protein DNA DNA_with_flanks
Genetic context
TuaD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TuaD expression.png
























Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components

This gene is a member of the following regulons

PhoP regulon

The gene

Basic information

  • Locus tag: BSU35580

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH (according to Swiss-Prot)
  • Protein family: UDP-glucose/GDP-mannose dehydrogenase family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Cofactor(s):
  • Effectors of protein activity: PtkA-dependent phosphorylation stimulates TuaD activity PubMed

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expressed under conditions of phosphate limitation (PhoP) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Ivan Mijakovic, Lucia Musumeci, Lutz Tautz, Dina Petranovic, Robert A Edwards, Peter Ruhdal Jensen, Tomas Mustelin, Josef Deutscher, Nunzio Bottini
In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE.
J Bacteriol: 2005, 187(10);3384-90
[PubMed:15866923] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Sandrine Poncet, Grégory Boël, Alain Mazé, Sylvie Gillet, Emmanuel Jamet, Paulette Decottignies, Christophe Grangeasse, Patricia Doublet, Pierre Le Maréchal, Josef Deutscher
Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.
EMBO J: 2003, 22(18);4709-18
[PubMed:12970183] [WorldCat.org] [DOI] (P p)

H Antelmann, C Scharf, M Hecker
Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.
J Bacteriol: 2000, 182(16);4478-90
[PubMed:10913081] [WorldCat.org] [DOI] (P p)

Maryam Lahooti, Colin R Harwood
Transcriptional analysis of the Bacillus subtilis teichuronic acid operon.
Microbiology (Reading): 1999, 145 ( Pt 12);3409-3417
[PubMed:10627039] [WorldCat.org] [DOI] (P p)

Marco Pagni, Vladimir Lazarevic, Blazenka Soldo, Dimitri Karamata
Assay for UDPglucose 6-dehydrogenase in phosphate-starved cells: gene tuaD of Bacillus subtilis 168 encodes the UDPglucose 6-dehydrogenase involved in teichuronic acid synthesis.
Microbiology (Reading): 1999, 145 ( Pt 5);1049-1053
[PubMed:10376820] [WorldCat.org] [DOI] (P p)

B Soldo, V Lazarevic, M Pagni, D Karamata
Teichuronic acid operon of Bacillus subtilis 168.
Mol Microbiol: 1999, 31(3);795-805
[PubMed:10048024] [WorldCat.org] [DOI] (P p)

Wei Liu, F Marion Hulett
Comparison of PhoP binding to the tuaA promoter with PhoP binding to other Pho-regulon promoters establishes a Bacillus subtilis Pho core binding site.
Microbiology (Reading): 1998, 144 ( Pt 5);1443-1450
[PubMed:9611818] [WorldCat.org] [DOI] (P p)