ZapA

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  • Description: positive modulator of FtsZ Z ring assembly and stability

Gene name zapA
Synonyms yshA
Essential no
Product Z-ring-associated protein
Function control of Z-ring formation
Gene expression levels in SubtiExpress: zapA
Interactions involving this protein in SubtInteract: ZapA
MW, pI 9 kDa, 7.17
Gene length, protein length 255 bp, 85 aa
Immediate neighbours yshB, rnhC
Sequences Protein DNA DNA_with_flanks
Genetic context
YshA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ZapA expression.png















Categories containing this gene/protein

cell division, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU28610

Phenotypes of a mutant

  • a zapA ezrA double mutant forms filamentous cells PubMed
  • a yvcL zapA double mutant grows poorly, and the cells are filamentous (due to a defect in Z ring assembly) PubMed
  • the defects of the yvcL zapA double mutant can be suppressed by inactivation of either gtaB, pgcA, or ugtP PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: Type 2 subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • constitutively expressed PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Erik Nico Trip, Jan-Willem Veening, Eric J Stewart, Jeff Errington, Dirk-Jan Scheffers
Balanced transcription of cell division genes in Bacillus subtilis as revealed by single cell analysis.
Environ Microbiol: 2013, 15(12);3196-209
[PubMed:23701187] [WorldCat.org] [DOI] (I p)

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)


Original Publications

Katarina Surdova, Pamela Gamba, Dennis Claessen, Tjalling Siersma, Martijs J Jonker, Jeff Errington, Leendert W Hamoen
The conserved DNA-binding protein WhiA is involved in cell division in Bacillus subtilis.
J Bacteriol: 2013, 195(24);5450-60
[PubMed:24097947] [WorldCat.org] [DOI] (I p)

Leigh G Monahan, Andrew Robinson, Elizabeth J Harry
Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria.
Mol Microbiol: 2009, 74(4);1004-17
[PubMed:19843223] [WorldCat.org] [DOI] (I p)

Pamela Gamba, Jan-Willem Veening, Nigel J Saunders, Leendert W Hamoen, Richard A Daniel
Two-step assembly dynamics of the Bacillus subtilis divisome.
J Bacteriol: 2009, 191(13);4186-94
[PubMed:19429628] [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)

Leendert W Hamoen, Jean-Christophe Meile, Wouter de Jong, Philippe Noirot, Jeff Errington
SepF, a novel FtsZ-interacting protein required for a late step in cell division.
Mol Microbiol: 2006, 59(3);989-99
[PubMed:16420366] [WorldCat.org] [DOI] (P p)

Harry H Low, Martin C Moncrieffe, Jan Löwe
The crystal structure of ZapA and its modulation of FtsZ polymerisation.
J Mol Biol: 2004, 341(3);839-52
[PubMed:15288790] [WorldCat.org] [DOI] (P p)

Frederico J Gueiros-Filho, Richard Losick
A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ.
Genes Dev: 2002, 16(19);2544-56
[PubMed:12368265] [WorldCat.org] [DOI] (P p)