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
Sequences	Protein DNA DNA_with_flanks
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

Phenotypes of a mutant

• a yvcL minC-minD mutant grows poorly, and the cells are filamentous PubMed

Database entries

• BsubCyc: BSU28000

• 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:

• Cofactors:

• 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

• BsubCyc: BSU28000

• 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
  • constitutively expressed PubMed

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 95 PubMed

Biological materials

• Mutant: BSN375 (minC::aphA3) (available in Leendert Hamoen's, Sven Halbedel's and Jörg Stülke's labs)

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Imrich Barák
Open questions about the function and evolution of bacterial Min systems.
Front Microbiol: 2013, 4;378
[PubMed:24367361] [WorldCat.org] [DOI] (P e)

Marc Bramkamp, Suey van Baarle
Division site selection in rod-shaped bacteria.
Curr Opin Microbiol: 2009, 12(6);683-8
[PubMed:19884039] [WorldCat.org] [DOI] (I p)

David W Adams, Jeff Errington
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
Nat Rev Microbiol: 2009, 7(9);642-53
[PubMed:19680248] [WorldCat.org] [DOI] (I p)