Difference between revisions of "DivIVA"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
−
Deletion of divIVA leads to filamentation and polar divisions that in turn cause a minicell phenotype. [http://www.ncbi.nlm.nih.gov/sites/entrez/9219999 PubMed] A divIVA mutant has a severe sporulation defect. [http://www.ncbi.nlm.nih.gov/sites/entrez/11445541 PubMed]
+
* Deletion of ''divIVA'' leads to filamentation and polar divisions that in turn cause a minicell phenotype. [http://www.ncbi.nlm.nih.gov/sites/entrez/9219999 PubMed]  
 +
* A ''divIVA'' mutant has a severe [[sporulation]] defect. [http://www.ncbi.nlm.nih.gov/sites/entrez/11445541 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
−
* '''Domains:'''  
+
* '''[[Domains]]:'''  
 
** the first 60 amino acids constitute a conserved lipid binding domain. [http://www.ncbi.nlm.nih.gov/sites/entrez/19478798 PubMed]
 
** the first 60 amino acids constitute a conserved lipid binding domain. [http://www.ncbi.nlm.nih.gov/sites/entrez/19478798 PubMed]
 
** the C-terminal domain is less conserved
 
** the C-terminal domain is less conserved
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** DivIVA from ''Streptococcus pneumoniae'' is phosphorylated at Threonine 201 by the Ser/Thr protein kinase Sktp1. [http://www.ncbi.nlm.nih.gov/sites/entrez/20453092 PubMed][http://www.ncbi.nlm.nih.gov/sites/entrez/22211696 PubMed]
 
** DivIVA from ''Streptococcus pneumoniae'' is phosphorylated at Threonine 201 by the Ser/Thr protein kinase Sktp1. [http://www.ncbi.nlm.nih.gov/sites/entrez/20453092 PubMed][http://www.ncbi.nlm.nih.gov/sites/entrez/22211696 PubMed]
  
−
* '''Cofactor(s):''' not known
+
* '''[[Cofactors]]:''' not known
  
 
* '''Effectors of protein activity:''' not known
 
* '''Effectors of protein activity:''' not known
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** [[Maf]]-[[DivIVA]] {{PubMed|21564336}}
 
** [[Maf]]-[[DivIVA]] {{PubMed|21564336}}
 
** [[DivIVA]]-[[ComN]] {{PubMed|22582279}}
 
** [[DivIVA]]-[[ComN]] {{PubMed|22582279}}
 +
** [[DivIVA]]-[[SecA]] {{PubMed|24592260}}
  
 
* '''[[Localization]]:'''  
 
* '''[[Localization]]:'''  
 
** DivIVA forms a ring underneath the invaginating membrane at the site of cell division and is enriched at both cell poles [http://www.ncbi.nlm.nih.gov/sites/entrez/9219999 PubMed].
 
** DivIVA forms a ring underneath the invaginating membrane at the site of cell division and is enriched at both cell poles [http://www.ncbi.nlm.nih.gov/sites/entrez/9219999 PubMed].
 
** forms rings at the division septum and patches at the cell poles {{PubMed|22108385}}
 
** forms rings at the division septum and patches at the cell poles {{PubMed|22108385}}
 +
** membrane targeting requires [[SecA]] {{PubMed|24592260}}
  
 
=== Database entries ===
 
=== Database entries ===
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==Original Publications==
 
==Original Publications==
−
<pubmed>22582279, 19654604, 19666580,9219999,19019154,15554965, 12368265,11445541,10835369,12511520,14651647, 19478798 ,19429628, 11445541, 9219999, 9045828 20352045 20502438 11886553 21564336 22108385 22457634 22517742 22661688 23264578 23701187 23927765 24391905 </pubmed>
+
<pubmed>22582279, 19654604, 19666580,9219999,19019154,15554965, 12368265,11445541,10835369,12511520,14651647, 19478798 ,19429628, 11445541, 9219999, 9045828 20352045 20502438 11886553 21564336 22108385 22457634 22517742 22661688 23264578 23701187 23927765 24391905 24592260 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:44, 5 March 2014

  • 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
  • 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
    • membrane targeting requires SecA 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

  • Expression vector: DivIVA-Strep available here
  • lacZ fusion:
  • GFP fusion: divIVA-gfp fusions available from the Hamoen Lab
  • 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

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