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MreC is a [SW|cell shape] determining protein, it couples the cytosolic [protein|A4C8719E06F774A6EB4D79757CC79CF89E453A54|MreB] and [protein|A4C8719E06F774A6EB4D79757CC79CF89E453A54|MreB]-like proteins to the extracellular peptidoglycan-synthesizing machinery, part of the [protein|search|Rod complex] for lateral [SW|cell wall synthesis] and control of cell diameter
32.00 kDa
protein length
290 aa Sequence Blast
gene length
873 bp Sequence Blast
[SW|cell shape] determation
[SW|cell shape]-determining protein

Genomic Context



  • [category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.2|Cell shape]
  • [category|SW 4|Lifestyles] → [category|SW 4.3|Coping with stress] → [category|SW 4.3.2|Cell envelope stress proteins (controlled by SigM, V, W, X, Y)]
  • [category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes]
  • [category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins]
  • Gene

    2,859,832 2,860,704

    Phenotypes of a mutant

  • ''mreC'' is essential under normal conditions [Pubmed|12682299].
  • Depletion of MreC leads to a progressive increase in the width and a decrease in the length of the cell. This shape defect is consistent with a role for ''mreC'' in cell wall synthesis during elongation and has a similar phenotype to other genes with roles in elongation like ''[gene|B405B3C21B464F904BBB2AFD5DA21ADE45B4DD96|rodA]'' and the redundant gene pair ''[gene|3B4F035535D6504405567E7C44E72902A11F7447|pbpA]'' and ''[gene|883DFF72888D280A102E53CC1D69A8B1C7BE2907|pbpH]''.
  • Electron microscopy of cells depleted of MreC shows regions of the cell where a thick and irregular cell wall has accumulated [Pubmed|12867458,16101995].
  • ''mreC'' can be deleted provided that 0.5 M sucrose and 20 mM Mg(2 ) is provided in the media, ''mreC'' is therefore conditionally essential. The phenotype of the ''mreC'' deletion in these conditions is one characterised by extreamly fat and bloated cells that tend to grow in clusters [Pubmed|16101995].
  • The protein

    Catalyzed reaction/ biological activity

  • None/ structural protein
  • Protein family

  • mreC family (single member, according to UniProt)
  • [SW|Domains]

  • Intracellular N-terminus, transmembrane domain, Coiled coil domain and C-terminal beta-sheet domain.
  • Structure

  • [PDB|2J5U]: MreC from ''Listeria monocytogenes'' [Pubmed|17427287]
  • [PDB|2QF4]: MreC monomer from ''Streptococcus pneumoniae'' [Pubmed|17707860]
  • [PDB|2QF5]: MreC dimer from ''Streptococcus pneumoniae'' [Pubmed|17707860]
  • [SW|Localization]

  • trans-membrane protein [Pubmed|21636744,16101995]
  • during logarithmic growth, [protein|231C30963AFB863424C087CB722446D319976D65|MreD] forms discrete patches thst move processively along peripheral tracks perpendicular to the cell axis [Pubmed|21636744]
  • forms transverse bands as cells enter the stationary phase [Pubmed|21636744]
  • reports on helical structures formed by MreC [Pubmed|16101995,20566861] seem to be misinterpretation of data [Pubmed|21636744]
  • Expression and Regulation



    sigma factors

  • [protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, promoter p1, upstream of [protein|49D996C9AED44A820A214C3DF60AB1B6E1508DEA|Maf] [Pubmed|26091431], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]
  • [protein|081DF3EE9FA56209D648C7677188C61CE3AA8E41|SigM]: sigma factor, promoter p2, within [protein|49D996C9AED44A820A214C3DF60AB1B6E1508DEA|Maf] [Pubmed|18179421], in [regulon|081DF3EE9FA56209D648C7677188C61CE3AA8E41|SigM regulon]
  • [protein|DC3449D5F195E5C2E9E14FEC95396C8F1FDF73B4|SigH]: sigma factor, promoter p4, upstream of [protein|8C94C9598A823A8405B3E1FA0124E21D90845B8E|MinC] [Pubmed|8459776], in [regulon|DC3449D5F195E5C2E9E14FEC95396C8F1FDF73B4|SigH regulon]
  • regulatory mechanism

  • [protein|08CFA2C72931A75532D4289BC1D18A826DE9F9CA|ComK]: activation, [Pubmed|26091431], in [regulon|08CFA2C72931A75532D4289BC1D18A826DE9F9CA|ComK regulon]
  • regulation

  • constitutively expressed [Pubmed|23701187]
  • view in new tab


    sigma factors

  • [protein|081DF3EE9FA56209D648C7677188C61CE3AA8E41|SigM]: sigma factor, promoter p2 within [protein|49D996C9AED44A820A214C3DF60AB1B6E1508DEA|Maf] [Pubmed|18179421], in [regulon|081DF3EE9FA56209D648C7677188C61CE3AA8E41|SigM regulon]
  • [protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, promoter p1, upstream of [protein|49D996C9AED44A820A214C3DF60AB1B6E1508DEA|Maf] [Pubmed|26091431], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]
  • regulatory mechanism

  • [protein|08CFA2C72931A75532D4289BC1D18A826DE9F9CA|ComK]: activation, [Pubmed|11948146,11918817,21564336], in [regulon|08CFA2C72931A75532D4289BC1D18A826DE9F9CA|ComK regulon]
  • regulation

  • constitutively expressed [Pubmed|23701187]
  • view in new tab

    Biological materials


  • A non-polar inframe deletion strain named 3481 and a xylose dependent conditional mutant named 3461 is avaliable from the [SW|Errington] lab [Pubmed|16101995].
  • GFP fusion

  • A functional N-terminal GFP fusion has been made where the fusion protein is the only copy of the gene in the cell: strain 3417 [Pubmed|16101995].
  • Antibody

  • antisera raised in rabit is avaliable from the [SW|Errington] lab.
  • labs

  • [SW|Jeff Errington], Newcastle University, UK [ homepage]
  • [SW|Peter Graumann], Freiburg University, Germany [ homepage]
  • References

  • 20566861,21636744,21636745,18363795,17427287,18179421,8459776,21926231,16101995,22383849,26091431,31086310