mreB
168

cell shape-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex, required for LytE activity, part of the Rod complex for lateral cell wall synthesis and control of cell diameter

Locus

BSU_28030

Molecular weight

35.79 kDa

Isoelectric point

4.9

Protein length

337 aaSequenceBlast

Gene length

1014 bpSequenceBlast

Function

cell shape determination

Product

cell shape-determining protein

Essential

yes

Synonyms

mreB, divIVB

Outlinks

BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Hide small RNAsZoom:

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG1077 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene

Coordinates

2,860,735 2,861,748

Phenotypes of a mutant

essential PubMed

the mutation can be suppressed by addition of 5 mM magnesium to the growth medium, this results in inhibition of peptidoglycan hydrolyses such as LytE PubMed

the mutation can be suppressed by inactivation of ''ponA, ptsI, ccpA'' PubMed, or by overexpression of GlmR PubMed

rougher, softer cell surfaces, loss of cell shape, cell lysis PubMed

The protein

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 29 DNA replication machinery in peripheral helix-like structures PubMed

required for LytE activity PubMed

Protein family

FtsA/MreB family (according to UniProt)

Structure

1JCF (PDB) (from Thermotoga maritima, 57% identity) PubMed

Q01465 (AlphaFold)

Modification

acetylated at Lys-240, this is important for restricting cell wall growth and cell diameter PubMed

Paralogous protein(s)

MreBH, Mbl

Localization

during logarithmic growth, MreB forms discrete patches that 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

during stationary phase: delocalized in the cytoplasm PubMed

during development of genetic competence: co-localizes with polar clusters of the late competence protein ComGA (ComGA sequesters MreB) PubMed

MreB patch speed depends on the growth rate, the faster growth, the higher the patch speed PubMed

MreB filament intensity increases with the growth rate and depends on the abundance of lipid II and MurAA due to increased RodZ phosphorylation by PrkC PubMed

Expression and Regulation

Operons

Genes

mreB-mreC-mreD-minC-minD

Description

PubMed

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