DivIVA

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  • Description: curvature sensitive membrane binding protein that recruits other proteins to the poles and the division septum, cell-division initiation protein (septum placement), part of the Min system (with MinC, 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 divIVA
Synonyms ylmJ
Essential no
Product cell-division initiation protein
Function septum placement
Gene expression levels in SubtiExpress: divIVA
Interactions involving this protein in SubtInteract: DivIVA
MW, pI 19 kDa, 4.846
Gene length, protein length 492 bp, 164 aa
Immediate neighbours ylmH, ileS
Sequences Protein DNA DNA_with_flanks
Genetic context
DivIVA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DivIVA expression.png















Categories containing this gene/protein

cell division, membrane proteins, phosphoproteins

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

  • Locus tag: BSU15420

Phenotypes of a mutant

Deletion of divIVA leads to filamentation and polar divisions that in turn cause a minicell phenotype. PubMed A divIVA mutant has a severe sporulation defect. PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

Filamentation is suppressed by mutations in minCD PubMed.

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • curvature sensitive membrane binding protein that recruits other proteins to the poles and the division septum
    • DivIVA is required for polar localisation of MinC-MinD via MinJ. PubMed
    • It also recruits RacA to the distal pole of the prespore PubMed.
  • Protein family: gpsB family (according to Swiss-Prot)
  • Paralogous protein(s): GpsB

Extended information on the protein

  • Kinetic information:
  • Domains:
    • the first 60 amino acids constitute a conserved lipid binding domain. PubMed
    • the C-terminal domain is less conserved
    • multimerisation involves two coiled-coil motifs, one in the lipid binding domain, and the other one being present in the helical C-terminal domain PubMed PubMed
  • Modification:
    • phosphorylated on Arg-102 PubMed
    • The Mycobacterium DivIVA homologue Wag31 is phosphorylated at T73 PubMed
    • DivIVA from Streptococcus pneumoniae is phosphorylated at Threonine 201 by the Ser/Thr protein kinase Sktp1. PubMedPubMed
  • Cofactor(s): not known
  • Effectors of protein activity: not known
  • Localization:
    • DivIVA forms a ring underneath the invaginating membrane at the site of cell division and is enriched at both cell poles PubMed.
    • forms rings at the division septum and patches at the cell poles PubMed

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
    • constitutively expressed PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: divIVA::tet available from the Hamoen Lab
  • Expression vector: DivIVA-Strep available here
  • lacZ fusion:
  • GFP fusion: divIVA-gfp fusions available from the Hamoen Lab
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Leendert Hamoen, Centre for Bacterial Cell Biology, Newcastle upon Tyne, United Kingdom [4]

Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage

Sven Halbedel, Robert Koch Institute homepage

Your additional remarks

References

Reviews

Karan Gautam Kaval, Sven Halbedel
Architecturally the same, but playing a different game: the diverse species-specific roles of DivIVA proteins.
Virulence: 2012, 3(4);406-7
[PubMed:22722244] [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)

Jennifer R Juarez, William Margolin
Irresistible curves.
EMBO J: 2009, 28(15);2147-8
[PubMed:19654604] [WorldCat.org] [DOI] (I p)


Original Publications

Monika Vishnoi, Jatin Narula, Seram Nganbiton Devi, Hoang-Anh Dao, Oleg A Igoshin, Masaya Fujita
Triggering sporulation in Bacillus subtilis with artificial two-component systems reveals the importance of proper Spo0A activation dynamics.
Mol Microbiol: 2013, 90(1);181-94
[PubMed:23927765] [WorldCat.org] [DOI] (I p)

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)

Suey van Baarle, Ilkay Nazli Celik, Karan Gautam Kaval, Marc Bramkamp, Leendert W Hamoen, Sven Halbedel
Protein-protein interaction domains of Bacillus subtilis DivIVA.
J Bacteriol: 2013, 195(5);1012-21
[PubMed:23264578] [WorldCat.org] [DOI] (I p)

Joe Pogliano, Nicolas Pogliano, Jared A Silverman
Daptomycin-mediated reorganization of membrane architecture causes mislocalization of essential cell division proteins.
J Bacteriol: 2012, 194(17);4494-504
[PubMed:22661688] [WorldCat.org] [DOI] (I p)

Valquiria Tiago dos Santos, Alexandre W Bisson-Filho, Frederico J Gueiros-Filho
DivIVA-mediated polar localization of ComN, a posttranscriptional regulator of Bacillus subtilis.
J Bacteriol: 2012, 194(14);3661-9
[PubMed:22582279] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [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)

Prahathees Eswaramoorthy, Marcella L Erb, James A Gregory, Jared Silverman, Kit Pogliano, Joe Pogliano, Kumaran S Ramamurthi
Cellular architecture mediates DivIVA ultrastructure and regulates min activity in Bacillus subtilis.
mBio: 2011, 2(6);
[PubMed:22108385] [WorldCat.org] [DOI] (I e)

Kenneth Briley, Peter Prepiak, Miguel J Dias, Jeanette Hahn, David Dubnau
Maf acts downstream of ComGA to arrest cell division in competent cells of B. subtilis.
Mol Microbiol: 2011, 81(1);23-39
[PubMed:21564336] [WorldCat.org] [DOI] (I p)

Maria A Oliva, Sven Halbedel, Stefan M Freund, Pavel Dutow, Thomas A Leonard, Dmitry B Veprintsev, Leendert W Hamoen, Jan Löwe
Features critical for membrane binding revealed by DivIVA crystal structure.
EMBO J: 2010, 29(12);1988-2001
[PubMed:20502438] [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)

Kumaran S Ramamurthi, Richard Losick
Negative membrane curvature as a cue for subcellular localization of a bacterial protein.
Proc Natl Acad Sci U S A: 2009, 106(32);13541-5
[PubMed:19666580] [WorldCat.org] [DOI] (I p)

Jennifer R Juarez, William Margolin
Irresistible curves.
EMBO J: 2009, 28(15);2147-8
[PubMed:19654604] [WorldCat.org] [DOI] (I p)

Rok Lenarcic, Sven Halbedel, Loek Visser, Michael Shaw, Ling Juan Wu, Jeff Errington, Davide Marenduzzo, Leendert W Hamoen
Localisation of DivIVA by targeting to negatively curved membranes.
EMBO J: 2009, 28(15);2272-82
[PubMed:19478798] [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)

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)

S E Perry, D H Edwards
Identification of a polar targeting determinant for Bacillus subtilis DivIVA.
Mol Microbiol: 2004, 54(5);1237-49
[PubMed:15554965] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Leendert W Hamoen, Jeffery Errington
Polar targeting of DivIVA in Bacillus subtilis is not directly dependent on FtsZ or PBP 2B.
J Bacteriol: 2003, 185(2);693-7
[PubMed:12511520] [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)

M E Karoui, J Errington
Isolation and characterization of topological specificity mutants of minD in Bacillus subtilis.
Mol Microbiol: 2001, 42(5);1211-21
[PubMed:11886553] [WorldCat.org] [DOI] (P p)

H B Thomaides, M Freeman, M El Karoui, J Errington
Division site selection protein DivIVA of Bacillus subtilis has a second distinct function in chromosome segregation during sporulation.
Genes Dev: 2001, 15(13);1662-73
[PubMed:11445541] [WorldCat.org] [DOI] (P p)

D H Edwards, H B Thomaides, J Errington
Promiscuous targeting of Bacillus subtilis cell division protein DivIVA to division sites in Escherichia coli and fission yeast.
EMBO J: 2000, 19(11);2719-27
[PubMed:10835369] [WorldCat.org] [DOI] (P p)

D H Edwards, J Errington
The Bacillus subtilis DivIVA protein targets to the division septum and controls the site specificity of cell division.
Mol Microbiol: 1997, 24(5);905-15
[PubMed:9219999] [WorldCat.org] [DOI] (P p)

J H Cha, G C Stewart
The divIVA minicell locus of Bacillus subtilis.
J Bacteriol: 1997, 179(5);1671-83
[PubMed:9045828] [WorldCat.org] [DOI] (P p)

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