divIVA

divIVA
168

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
BSU_15420
Molecular weight
19.20 kDa
Isoelectric point
4.85
Protein length
Gene length
Function
division site selection, chromosome segregation and control of peptidoglycan homeostasis
Product
cell division initiation protein, member of the divisome
Essential
no
Synonyms
divIVA, ylmJ

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG3599 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,612,521  1,613,015
Phenotypes of a mutant
filamentation and polar divisions that in turn cause a minicell phenotype PubMed
moderate PubMed to severe PubMed 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
DivIVA family (single member, according to UniProt)
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
not known
Structure
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
Paralogous protein(s)
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 foreshore face of the polar septum during sporulation PubMed
mobility of DivIVA is reduced by its interaction with MinJ PubMed
Additional information
about 1,700 molecules per cell PubMed
Expression and Regulation
Operons
Genes
Description
Regulation
constitutively expressed PubMed
Regulatory mechanism
Spo0A: repression, PubMed, in spo0A regulon
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divIVA

2025-03-10 21:17:30

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B966EABA9A51355C0F0BD5882C0E3EC9A7ABDDE5

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
BKE15420 (divIVA::erm  trpC2) available at BGSCPubMed, upstream reverse: _UP1_CATGATGCCACCTCCATTTT,  downstream forward: _UP4_TAAATTCTCTGATTATCTTG
BKK15420 (divIVA::kan  trpC2) available at BGSCPubMed, upstream reverse: _UP1_CATGATGCCACCTCCATTTT,  downstream forward: _UP4_TAAATTCTCTGATTATCTTG
Expression vectors
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
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.
GFP fusion
divIVA-gfp fusions available from the Hamoen Lab
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
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Original Publications
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A8C0C2B7BCA6FFFF3811402D683FB7B99F7120A4

Page visits: 14507

Time of last update: 2025-04-04 05:29:39

Author of last update: Jstuelk