MreB

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  • Description: cell shape-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex, required for LytE activity

Gene name mreB
Synonyms divIVB
Essential yes PubMed
Product cell shape-determining protein
Function cell shape determination
Gene expression levels in SubtiExpress: mreB
Interactions involving this protein in SubtInteract: MreB
MW, pI 35 kDa, 4.901
Gene length, protein length 1011 bp, 337 aa
Immediate neighbours mreC, radC
Sequences Protein DNA DNA_with_flanks
Genetic context
MreB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MreB expression.png















Categories containing this gene/protein

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

This gene is a member of the following regulons

SigM regulon

The gene

Basic information

  • Locus tag: BSU28030

Phenotypes of a mutant

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
    • involved in the organization of ϕ29 DNA replication machinery in peripheral helix-like structures PubMed
    • required for LytE activity PubMed
  • Protein family: ftsA/mreB family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:
  • Localization:
    • during logarithmic growth, MreB forms discrete patches thst move processively along peripheral tracks perpendicular to the cell axis PubMed
    • forms transverse bands as cells enter the stationary phase PubMed
    • forms antiparallel double filaments PubMed
    • close to the inner surface of the cytoplasmic membrane PubMed
    • reports on helical structures formed by MreB PubMed seem to be misinterpretation of data PubMed
    • normal localization depends on the presence of glucolipids, MreB forms irregular clusters in an ugtP mutant 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:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1045 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 2367 PubMed

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


Localization


Other original publications