DivIVA

• Description: cell-division initiation protein (septum placement)
  
  

Gene name	divIVA
Synonyms	ylmJ
Essential	no
Product	cell-division initiation protein
Function	septum placement
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

cell division, membrane proteins

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: DivIVA is required for polar localisation of MinCD 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 lipid binding domain. PubMed

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.

• Modification: The Mycobacterium DivIVA homologue Wag31 is phosphorylated at T73 PubMed.

The DivIVA from Streptococcus pneumoniae is phosphorylated at a threonine side chain by the Ser/Thr protein kinase Sktp1. PubMed

• Cofactor(s): not known

• Effectors of protein activity: not known

• Interactions:
  • (MinC-MinD)-MinJ-DivIVA PubMed
  • DivIVA-RacA, DivIVA-DivIVA
  • Maf-DivIVA PubMed

• Localization: DivIVA forms a ring underneath the invaginating membrane at the site of cell division and is enriched at both cell poles PubMed.

Database entries

• Structure: 2WUJ (N-terminal domain) PubMed

• UniProt: P71021

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: divIVA PubMed

• Sigma factor:

• Regulation:
  • repressed under conditions that trigger sporulation (Spo0A) PubMed

• Regulatory mechanism:
  • Spo0A: transcription repression PubMed

• Additional information:

Biological materials

• Mutant: divIVA::tet available from the Hamoen Lab

• Expression vector:

• 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

References

Reviews

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)