MreBH
- 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 | mreBH |
Synonyms | |
Essential | no |
Product | cell shape-determining protein |
Function | cell shape determation |
Gene expression levels in SubtiExpress: mreBH | |
Interactions involving this protein in SubtInteract: MreBH | |
MW, pI | 35 kDa, 5.239 |
Gene length, protein length | 1005 bp, 335 aa |
Immediate neighbours | ykpC, abh |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
cell shape, heat shock proteins, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU14470
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ftsA/mreB family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- during logarithmic growth, MreBH 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
- close to the inner surface of the cytoplasmic membrane PubMed
- reports on helical structures formed by MreBH 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:
- UniProt: P39763
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Peter Graumann, Freiburg University, Germany homepage
Your additional remarks
References
Localization
Other original publications
Katarína Muchová, Zuzana Chromiková, Imrich Barák
Control of Bacillus subtilis cell shape by RodZ.
Environ Microbiol: 2013, 15(12);3259-71
[PubMed:23879732]
[WorldCat.org]
[DOI]
(I p)
Patricia Domínguez-Cuevas, Ida Porcelli, Richard A Daniel, Jeff Errington
Differentiated roles for MreB-actin isologues and autolytic enzymes in Bacillus subtilis morphogenesis.
Mol Microbiol: 2013, 89(6);1084-98
[PubMed:23869552]
[WorldCat.org]
[DOI]
(I p)
Felix Dempwolff, Christian Reimold, Michael Reth, Peter L Graumann
Bacillus subtilis MreB orthologs self-organize into filamentous structures underneath the cell membrane in a heterologous cell system.
PLoS One: 2011, 6(11);e27035
[PubMed:22069484]
[WorldCat.org]
[DOI]
(I p)
Hervé Joël Defeu Soufo, Peter L Graumann
Bacillus subtilis MreB paralogues have different filament architectures and lead to shape remodelling of a heterologous cell system.
Mol Microbiol: 2010, 78(5);1145-58
[PubMed:21091501]
[WorldCat.org]
[DOI]
(I p)
Yoshikazu Kawai, Kei Asai, Jeffery Errington
Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis.
Mol Microbiol: 2009, 73(4);719-31
[PubMed:19659933]
[WorldCat.org]
[DOI]
(I p)
Kathrin Schirner, Jeff Errington
Influence of heterologous MreB proteins on cell morphology of Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 11);3611-3621
[PubMed:19643765]
[WorldCat.org]
[DOI]
(I p)
Chi-Ling Tseng, Gwo-Chyuan Shaw
Genetic evidence for the actin homolog gene mreBH and the bacitracin resistance gene bcrC as targets of the alternative sigma factor SigI of Bacillus subtilis.
J Bacteriol: 2008, 190(5);1561-7
[PubMed:18156261]
[WorldCat.org]
[DOI]
(I p)
Rut Carballido-López, Alex Formstone, Ying Li, S Dusko Ehrlich, Philippe Noirot, Jeff Errington
Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE.
Dev Cell: 2006, 11(3);399-409
[PubMed:16950129]
[WorldCat.org]
[DOI]
(P p)