MinD

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

Gene name	minD
Synonyms	divIVB1
Essential	no
Product	cell-division inhibitor
Function	septum placement
Gene expression levels in SubtiExpress: minD
Interactions involving this protein in SubtInteract: MinD
MW, pI	29 kDa, 4.984
Gene length, protein length	804 bp, 268 aa
Immediate neighbours	spoIVFA, minC
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: BSU27990

Phenotypes of a mutant

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

Database entries

• BsubCyc: BSU27990

• DBTBS entry: [1]

• SubtiList entry: [2]

Additional information

• A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed

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

• Protein family: MinD subfamily (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

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

Database entries

• BsubCyc: BSU27990

• Structure:

• UniProt: Q01464

• 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: minD PubMed

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

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

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 716 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 813 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3544 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1500 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6195 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 Jörg Stülke's lab

• 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)