Difference between revisions of "MreB"

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(Expression and regulation)
(Other original publications)
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==Other original publications==
 
==Other original publications==
<pubmed>15752190,11290328,12809607,1400224,19192185,7836311, 16950129, 19192185, 19117023 19643765 19654094 19659933 8459776 11544518 20133608 21091501 21320184</pubmed>
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<pubmed>15752190,11290328,12809607,1400224,19192185,7836311, 16950129, 19192185, 19117023 19643765 19654094 19659933 8459776 11544518 20133608 21091501 21320184 18179421</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:33, 17 May 2011

  • Description: cell-shape determining protein, forms filaments

Gene name mreB
Synonyms divIVB
Essential yes PubMed
Product cell-shape determining protein
Function cell-shape determination
MW, pI 35 kDa, 4.901
Gene length, protein length 1011 bp, 337 aa
Immediate neighbours mreC, radC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MreB context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell shape, cell envelope stress proteins (controlled by SigM, W, X, Y), essential genes, membrane proteins

This gene is a member of the following regulons

SigH regulon, SigM regulon

The gene

Basic information

  • Locus tag: BSU28030

Phenotypes of a mutant

essential PubMed, the mutation can be suppressed by inactivation of ponA, ptsI, ccpA PubMed, by overexpression of YvcK PubMed, or by addition of 5 mM magnesium to the growth medium PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • forms straight filaments in a heterologous system PubMed
    • polymerizes in the presence of millimolar divalent cations, binds and hydrolyzes GTP and ATP PubMed
  • Protein family: ftsA/mreB family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • forms helical structures close to the inner surface of the cytoplasmic membrane PubMed
    • formation of helical clusters depends on the proton motive force PubMed

Database entries

  • Structure: 1JCE (from Thermotoga maritima) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:

Labs working on this gene/protein

Jeff Errington, Newcastle University, UK homepage

Peter Graumann, Freiburg University, Germany homepage

Your additional remarks

References

Reviews

Additional reviews: PubMed


Localization


Other original publications