SubtiBank SubtiBank
divIVA [2017-07-05 12:49:32]
You are currently viewing an outdated version of SubtiWiki. Please use the newest version!

divIVA [2017-07-05 12:49:32]

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 Z ring placement)
Locus
BSU15420
Isoelectric point
4.85
Molecular weight
19.20 kDa
Protein length
164 aa Sequence Blast
Gene length
492 bp Sequence Blast
Function
septum placement
Product
cell-division initiation protein
Essential
no
Synonyms
ylmJ

Genomic Context

      
Loading

Categories containing this gene/protein

Gene

Coordinates
1,612,521 → 1,613,015

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 moderate [(Pubmed)|26735940] to severe [(Pubmed)|11445541] sporulation defect.
  • The protein

    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.
  • DivIVA may anchor SpoIIE briefly to the assembling polar septum before SpoIIE is subsequently released into the forespore membrane and recaptured at the polar septum PubMed
  • required for the compartment-specific activation of SigF PubMed
  • activates PrkC PubMed
  • required for oriC placement during spore development PubMed
  • Protein family

  • gpsB family (according to Swiss-Prot)
  • Paralogous protein(s)

    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
  • Cofactors

  • not known
  • Effectors of protein activity

  • not known
  • Structure

  • 2WUJ (N-terminal domain) PubMed
  • 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
  • assembles into a ring-like structure at the polar septum during sporulation PubMed
  • Expression and Regulation

    Operons

    Genes
    Description

    Regulatory mechanism

  • Spo0A: repression, PubMed, in Spo0A regulon
  • Regulation

  • constitutively expressed PubMed
  • view in new tab

    Biological materials

    Mutant

  • 4041 (divIVA::tet), available in Leendert Hamoen's, Jörg Stülke's, and Sven Halbedel 's lab
  • GP1482 (chromosomal divIVA-Strep fusion, aphA3), purification from B. subtilis, for SPINE, available in Jörg Stülke's lab
  • Expression vector

  • DivIVA-Strep available here
  • pGP1497 (N-terminal Strep-tag fused to C-terminus of divIVA, TEV-site, purification from E. coli, in pGP172), available in Jörg Stülke's lab
  • GFP fusion

  • divIVA-gfp fusions available from the Hamoen Lab
  • Two-hybrid system

  • B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Sven Halbedel's and Jörg Stülke's labs
  • FLAG-tag construct

  • GP1776 (spc, based on pGP1331), available in Jörg Stülke's lab
  • Antibody

  • A polyclonal anti-DivIVA antiserum generated in rabbit is described here PubMed.
  • Labs working on this gene/protein

  • Leendert Hamoen, Centre for Bacterial Cell Biology, Newcastle upon Tyne, United Kingdom x
  • Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage
  • Sven Halbedel, Robert Koch Institute homepage
  • References

    Reviews

    Loading

    Original Publications

    Loading