Difference between revisions of "MraZ"

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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mraZ_1580121_1580552_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:mraZ_expression.png|500px]]
 
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Revision as of 08:55, 19 April 2012

  • Description: Putative DNA-binding protein

Gene name mraZ
Synonyms yllB
Essential no
Product unknown
Function unknown
MW, pI 16 kDa, 4.969
Gene length, protein length 429 bp, 143 aa
Immediate neighbours bshC, mraW
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YllB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MraZ expression.png
























Categories containing this gene/protein

proteins of unknown function

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU15130

Phenotypes of a mutant

Database entries

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

Additional information

the E.coli homolog: mraZ

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: mraZ family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • 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

Melanie A Adams, Christian M Udell, Gour Pada Pal, Zongchao Jia
MraZ from Escherichia coli: cloning, purification, crystallization and preliminary X-ray analysis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2005, 61(Pt 4);378-80
[PubMed:16511046] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

R A Daniel, A M Williams, J Errington
A complex four-gene operon containing essential cell division gene pbpB in Bacillus subtilis.
J Bacteriol: 1996, 178(8);2343-50
[PubMed:8636036] [WorldCat.org] [DOI] (P p)

A Yanouri, R A Daniel, J Errington, C E Buchanan
Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis.
J Bacteriol: 1993, 175(23);7604-16
[PubMed:8244929] [WorldCat.org] [DOI] (P p)