MinC

• Description: cell-division inhibitor (septum placement), destabilizes FtsZ-rings at new cell poles, part of the Min system (with DivIVA, MinD, MinJ), Noc and the Min system ensure the efficient utilization of the division site at midcell in by ensuring Z ring placement
  
  

Gene name	minC
Synonyms
Essential	no
Product	cell-division inhibitor
Function	septum placement
Gene expression levels in SubtiExpress: minC
Interactions involving this protein in SubtInteract: MinC
MW, pI	24 kDa, 6.262
Gene length, protein length	678 bp, 226 aa
Immediate neighbours	minD, mreD
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell division, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins

This gene is a member of the following regulons

SigH regulon, SigM regulon

The gene

Basic information

• Locus tag: BSU28000

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • The Min system prevents minicell formation adjacent to recently completed division sites by promoting the disassembly of the cytokinetic ring, thereby ensuring that cell division occurs only once per cell cycle PubMed
  • binds the C-terminal domain of FtsZ to inhibit its polymerization PubMed

• Protein family: minC family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • (MinC-MinD)-MinJ-DivIVA PubMed
  • FtsZ (C-terminal domain)-MinC PubMed

• Localization:
  • polar/ septal at the cell membrane PubMed
  • membrane binding/ polar localization depends on the proton motive force PubMed

Database entries

• Structure:

• UniProt: Q01463

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • radC-mreB-mreC-mreD-minC-minD PubMed
  • mreB-mreC-mreD-minC-minD PubMed
  • minC-minD PubMed

• Expression browser: minC PubMed

• Sigma factor:
  • radC: SigM PubMed
  • minC: SigH PubMed

• Regulation:
  • expression is reduced in a SigV mutant PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

Additional publications: PubMed

Valdir Blasios, Alexandre W Bisson-Filho, Patricia Castellen, Maria Luiza C Nogueira, Jefferson Bettini, Rodrigo V Portugal, Ana Carolina M Zeri, Frederico J Gueiros-Filho
Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
PLoS One: 2013, 8(4);e60690
[PubMed:23577149] [WorldCat.org] [DOI] (I p)

Christopher D A Rodrigues, Elizabeth J Harry
The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization.
PLoS Genet: 2012, 8(3);e1002561
[PubMed:22457634] [WorldCat.org] [DOI] (I p)

Inês Filipa Fernandes de Oliveira, Anabela de Sousa Borges, Viola Kooij, Jeremy Bartosiak-Jentys, Joen Luirink, Dirk-Jan Scheffers
Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.
PLoS One: 2010, 5(8);e12048
[PubMed:20711458] [WorldCat.org] [DOI] (I e)

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)

Suey van Baarle, Marc Bramkamp
The MinCDJ system in Bacillus subtilis prevents minicell formation by promoting divisome disassembly.
PLoS One: 2010, 5(3);e9850
[PubMed:20352045] [WorldCat.org] [DOI] (I e)

James A Gregory, Eric C Becker, Kit Pogliano
Bacillus subtilis MinC destabilizes FtsZ-rings at new cell poles and contributes to the timing of cell division.
Genes Dev: 2008, 22(24);3475-88
[PubMed:19141479] [WorldCat.org] [DOI] (P p)

Marc Bramkamp, Robyn Emmins, Louise Weston, Catriona Donovan, Richard A Daniel, Jeff Errington
A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD.
Mol Microbiol: 2008, 70(6);1556-69
[PubMed:19019154] [WorldCat.org] [DOI] (I p)

Dirk-Jan Scheffers
The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA.
FEBS Lett: 2008, 582(17);2601-8
[PubMed:18588879] [WorldCat.org] [DOI] (P p)

Warawan Eiamphungporn, John D Helmann
The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses.
Mol Microbiol: 2008, 67(4);830-48
[PubMed:18179421] [WorldCat.org] [DOI] (P p)

David E Anderson, Frederico J Gueiros-Filho, Harold P Erickson
Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.
J Bacteriol: 2004, 186(17);5775-81
[PubMed:15317782] [WorldCat.org] [DOI] (P p)

A L Marston, J Errington
Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC.
Mol Microbiol: 1999, 33(1);84-96
[PubMed:10411726] [WorldCat.org] [DOI] (P p)

S Lee, C W Price
The minCD locus of Bacillus subtilis lacks the minE determinant that provides topological specificity to cell division.
Mol Microbiol: 1993, 7(4);601-10
[PubMed:8459776] [WorldCat.org] [DOI] (P p)

P A Levin, P S Margolis, P Setlow, R Losick, D Sun
Identification of Bacillus subtilis genes for septum placement and shape determination.
J Bacteriol: 1992, 174(21);6717-28
[PubMed:1400224] [WorldCat.org] [DOI] (P p)