mreC

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
Protein length
Gene length
Function
cell shape determation
Product
cell shape-determining protein
Essential
yes
Synonyms
mreC

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
trans-membrane protein PubMed
during logarithmic growth, MreD 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
reports on helical structures formed by MreC PubMed seem to be misinterpretation of data PubMed
Expression and Regulation
Operons
Description
Regulation
constitutively expressed PubMed
Regulatory mechanism
ComK: activation, PubMed, in comK regulon
Sigma factors
SigA: sigma factor, promoter p1, upstream of Maf PubMed, in sigA regulon
SigM: sigma factor, promoter p2, within Maf PubMed, in sigM regulon
SigH: sigma factor, promoter p4, upstream of MinC PubMed, in sigH regulon
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mreBminD

2025-04-03 04:42:23

ghost

150

df866addcf0a1b269336e8d5bd5fbd5f95fab5a3

37AF85C74BFE779D7BD018F30628D4588CACE9D3

Description
Regulation
constitutively expressed PubMed
Regulatory mechanism
ComK: activation, PubMed, in comK regulon
Sigma factors
SigM: sigma factor, promoter p2 within Maf PubMed, in sigM regulon
SigA: sigma factor, promoter p1, upstream of Maf PubMed, in sigA regulon
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mafminD

2025-04-03 12:26:20

ghost

139

5cb36570cb9eb74ac55107ce2bd7f07e7d2d5c0b

EE31E7A5D1B0C8BDC56B004AA68A1C721D4DA9CC

Biological materials
Mutant
A non-polar inframe deletion strain named 3481 and a xylose dependent conditional mutant named 3461 is avaliable from the Errington lab PubMed.
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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6A14D0C7FD94A838BAB3B74AA100EA678F1E4E34

Page visits: 7190

Time of last update: 2025-04-04 06:46:53

Author of last update: Jstuelk