Difference between revisions of "DivIVA"

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(Extended information on the protein)
(Extended information on the protein)
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:''' The first 60 amino acids constitute a lipid binding domain. Multimerisation involves two coiled-coil motifs, one in the lipid binding domain, and the other one being present in the helical C-terminal domain.
+
* '''Domains:''' The first 60 amino acids constitute a lipid binding domain. [http://www.ncbi.nlm.nih.gov/sites/entrez/19478798 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.
  
 
* '''Modification:''' The Mycobacterium DivIVA homologue Wag31 is phosphorylated at T73.
 
* '''Modification:''' The Mycobacterium DivIVA homologue Wag31 is phosphorylated at T73.

Revision as of 14:59, 14 July 2009

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

Gene name divIVA
Synonyms ylmJ
Essential no
Product cell-division initiation protein
Function septum placement
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
DivIVA context.gif
This image was kindly provided by SubtiList



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. A divIVA mutant has a severe sporulation defect.

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: DivIVA is required for polar localisation of MinCD via MinJ. It also recruits RacA to the distal pole of the prespore.
  • 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.

  • Modification: The Mycobacterium DivIVA homologue Wag31 is phosphorylated at T73.
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: DivIVA forms a ring underneath the invaginating membrane at the site of cell division and is enriched at both cell poles.

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: one gene cistron
  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: divIVA::tet available from the Hamoen Lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • 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

Your additional remarks

References