Mbl
- Description: cell shape-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex
Gene name | mbl |
Synonyms | |
Essential | no |
Product | MreB-like protein |
Function | cell shape determination |
Interactions involving this protein in SubtInteract: Mbl | |
MW, pI | 35 kDa, 5.669 |
Gene length, protein length | 999 bp, 333 aa |
Immediate neighbours | flhO, spoIIID |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
cell shape, sporulation proteins, membrane proteins
This gene is a member of the following regulons
SigE regulon, stringent response
The gene
Basic information
- Locus tag: BSU36410
Phenotypes of a mutant
non-viable in the presence of low Mg(2+), readily accumulate rsgI suppressor mutants PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- forms helical filaments in a heterologous system PubMed
- 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, Mbl 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 Mbl PubMed seem to be misinterpretation of data PubMed
Database entries
- Structure:
- UniProt: P39751
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- An antisense RNA is predicted for mbl PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Görke lab
- Antibody: available in the Jeff Errington and Peter Graumann labs
Labs working on this gene/protein
Peter Graumann, Freiburg University, Germany homepage
Your additional remarks
References
Localization
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)
Ethan C Garner, Remi Bernard, Wenqin Wang, Xiaowei Zhuang, David Z Rudner, Tim Mitchison
Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis.
Science: 2011, 333(6039);222-5
[PubMed:21636745]
[WorldCat.org]
[DOI]
(I p)
Julia Domínguez-Escobar, Arnaud Chastanet, Alvaro H Crevenna, Vincent Fromion, Roland Wedlich-Söldner, Rut Carballido-López
Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria.
Science: 2011, 333(6039);225-8
[PubMed:21636744]
[WorldCat.org]
[DOI]
(I p)
Henrik Strahl, Leendert W Hamoen
Membrane potential is important for bacterial cell division.
Proc Natl Acad Sci U S A: 2010, 107(27);12281-6
[PubMed:20566861]
[WorldCat.org]
[DOI]
(I p)
Hervé Joël Defeu Soufo, Peter L Graumann
Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB.
Mol Microbiol: 2006, 62(5);1340-56
[PubMed:17064365]
[WorldCat.org]
[DOI]
(P p)
Other original publications