Difference between revisions of "DivIVA"

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(Categories containing this gene/protein)
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Multimerisation involves two coiled-coil motifs, one in the lipid binding domain, and the other one being present in the helical C-terminal domain [http://www.ncbi.nlm.nih.gov/sites/entrez/18388125 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/18388125 PubMed].
  
* '''Modification:''' The Mycobacterium DivIVA homologue Wag31 is phosphorylated at T73 [http://www.ncbi.nlm.nih.gov/sites/entrez/15985609 PubMed].
+
* '''Modification:'''  
The DivIVA from Streptococcus pneumoniae is phosphorylated at a threonine side chain by the Ser/Thr protein kinase Sktp1. [http://www.ncbi.nlm.nih.gov/sites/entrez/20453092 PubMed]
+
** phosphorylated on Arg-102 {{PubMed|22517742}}
 +
** The ''Mycobacterium'' DivIVA homologue Wag31 is phosphorylated at T73 [http://www.ncbi.nlm.nih.gov/sites/entrez/15985609 PubMed]
 +
** DivIVA from ''Streptococcus pneumoniae'' is phosphorylated at a threonine side chain by the Ser/Thr protein kinase Sktp1. [http://www.ncbi.nlm.nih.gov/sites/entrez/20453092 PubMed]
  
 
* '''Cofactor(s):''' not known
 
* '''Cofactor(s):''' not known
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<pubmed> 19654604, 19884039 </pubmed>
 
<pubmed> 19654604, 19884039 </pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>19654604, 19666580,9219999,19019154,15554965, 12368265,11445541,10835369,12511520,14651647, 19478798 ,19429628, 11445541, 9219999, 9045828 20352045 20502438 11886553 21564336 22108385 22457634</pubmed>
+
<pubmed>19654604, 19666580,9219999,19019154,15554965, 12368265,11445541,10835369,12511520,14651647, 19478798 ,19429628, 11445541, 9219999, 9045828 20352045 20502438 11886553 21564336 22108385 22457634 22517742</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:23, 21 April 2012

  • Description: 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
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
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: 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:
    • phosphorylated on Arg-102 PubMed
    • The Mycobacterium DivIVA homologue Wag31 is phosphorylated at T73 PubMed
    • 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
  • 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

  • Sigma factor:
  • 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: 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

Your additional remarks

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)

Original Publications