DivIVA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• Cofactors: not known

• Effectors of protein activity: not known

• Interactions:
  • (MinC-MinD)-MinJ-DivIVA PubMed, MinJ binds to the N-terminal lipid-binding domain of DivIVA PubMed
  • DivIVA-RacA, RacA binds to the C-terminal domain of DivIVA PubMed
  • DivIVA-DivIVA PubMed
  • Maf-DivIVA PubMed
  • DivIVA-ComN PubMed
  • DivIVA-SecA 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

Database entries

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

• UniProt: P71021

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: divIVA PubMed

• Expression browser: divIVA PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • Spo0A: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:
  • 4041 (divIVA::tet), available in Leendert Hamoen's, Jörg Stülke's, and Sven Halbedel 's lab

• Expression vector: DivIVA-Strep available here

• lacZ fusion:

• 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

• 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