Difference between revisions of "TuaD"

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= [[Categories]] containing this gene/protein =
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{{SubtiWiki category|[[cell wall synthesis]]}},
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{{SubtiWiki category|[[biosynthesis of cell wall components]]}}
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= This gene is a member of the following [[regulons]] =
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{{SubtiWiki regulon|[[PhoP regulon]]}}
  
 
=The gene=
 
=The gene=
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[cell wall synthesis]]}},
 
{{SubtiWiki category|[[biosynthesis of cell wall components]]}}
 
 
=The protein=
 
=The protein=
  

Revision as of 23:56, 8 December 2010

  • Description: UDP glucose 6-dehydrogenase

Gene name tuaD
Synonyms yvhD
Essential no
Product UDP glucose 6-dehydrogenase
Function biosynthesis of teichuronic acid
MW, pI 49 kDa, 6.107
Gene length, protein length 1383 bp, 461 aa
Immediate neighbours tuaE, tuaC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
TuaD context.gif
This image was kindly provided by SubtiList



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
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

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)