mreC
168
MreC is a cell shape determining protein, it couples the cytosolic MreB and MreB-like proteins to the extracellular peptidoglycan-synthesizing machinery, part of the Rod complex for lateral cell wall synthesis and control of cell diameter
Locus
BSU_28020
Molecular weight
32.00 kDa
Isoelectric point
6.25
Function
cell shape determation
Product
cell shape-determining protein
Essential
yes
Synonyms
mreC
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG1792 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
2,859,832 2,860,704
Phenotypes of a mutant
mreC is essential under normal conditions PubMed.
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 ''rodA and the redundant gene pair pbpA and pbpH''.
Electron microscopy of cells depleted of MreC shows regions of the cell where a thick and irregular cell wall has accumulated PubMed.
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.
The protein
Catalyzed reaction/ biological activity
None/ structural protein
Protein family
mreC family (single member, according to UniProt)
Intracellular N-terminus, transmembrane domain, Coiled coil domain and C-terminal beta-sheet domain.
Structure
2J5U (PDB): MreC from Listeria monocytogenes PubMed
2QF4 (PDB): MreC monomer from Streptococcus pneumoniae PubMed
2QF5 (PDB): MreC dimer from Streptococcus pneumoniae PubMed
Expression and Regulation
Operons
Description
Regulation
constitutively expressed PubMed
Regulatory mechanism
Sigma factors
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Description
Regulation
constitutively expressed PubMed
Regulatory mechanism
Sigma factors
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Biological materials
Mutant
Antibody
antisera raised in rabit is avaliable from the Errington lab.
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.
Labs working on this gene/protein
Jeff Errington, Newcastle University, UK homepage
Peter Graumann, Freiburg University, Germany homepage
References
Reviews
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Original Publications
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Time of last update: 2025-04-04 04:52:58
Author of last update: Jstuelk