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)
function
septum placement
product
cell-division initiation protein
Genomic Context
categories
[category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.8|Cell division] → [category|SW 1.1.8.1|The Min system][category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.8|Cell division] → [category|SW 1.1.8.2|Other genes][category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.1|Phosphorylation on an Arg residue][SW|Categories] containing this gene/protein
[SW|cell division], [SW|membrane proteins], [SW|phosphoproteins], [SW|sporulation/ other]This gene is a member of the following [SW|regulons]
[SW|Spo0A regulon]Gene
Coordinates on the chromosome (coding sequence)
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|9219999]A ''divIVA'' mutant has a moderate [(Pubmed)|26735940] to severe [(Pubmed)|11445541] [SW|sporulation] defect.The protein
Catalyzed reaction/ biological activity
curvature sensitive membrane binding protein that recruits other proteins to the poles and the division septumDivIVA is required for polar localisation of [protein|search|MinC]-[protein|search|MinD] via [protein|search|MinJ]. [Pubmed|19019154]It also recruits [protein|search|RacA] to the distal pole of the prespore [Pubmed|12493822].DivIVA may anchor [SW|SpoIIE] briefly to the assembling polar septum before [SW|SpoIIE] is subsequently released into the forespore membrane and recaptured at the polar septum [Pubmed|25101664]required for the compartment-specific activation of [protein|search|SigF] [Pubmed|25101664]activates [protein|search|PrkC] [Pubmed|25845974]required for oriC placement during spore development [Pubmed|27059541]Protein family
gpsB family (according to Swiss-Prot)Paralogous protein(s)
[protein|search|GpsB][SW|Domains]
the first 60 amino acids constitute a conserved lipid binding domain. [Pubmed|19478798]the C-terminal domain is less conservedmultimerisation involves two coiled-coil motifs, one in the lipid binding domain, and the other one being present in the helical C-terminal domain [Pubmed|18388125] [Pubmed|23264578]Modification
phosphorylated on Arg-102 [Pubmed|22517742]The ''Mycobacterium'' DivIVA homologue Wag31 is phosphorylated at T73 [Pubmed|15985609]DivIVA from ''Streptococcus pneumoniae'' is phosphorylated at Threonine 201 by the Ser/Thr protein kinase Sktp1. [Pubmed|20453092][Pubmed|22211696][SW|Cofactors]
not knownEffectors of protein activity
not knownStructure
[PDB|2WUJ] (N-terminal domain) [Pubmed|20502438][SW|Localization]
DivIVA forms a ring underneath the invaginating membrane at the site of cell division and is enriched at both cell poles [Pubmed|9219999].forms rings at the division septum and patches at the cell poles [Pubmed|22108385]membrane targeting requires [protein|search|SecA] [Pubmed|24592260]assembles into a ring-like structure at the polar septum during [SW|sporulation] [Pubmed|25101664][SW|Interactions]
([protein|search|MinC]-[protein|search|MinD])-[protein|search|MinJ]-[SW|DivIVA] [Pubmed|20352045], [protein|search|MinJ] binds to the N-terminal lipid-binding domain of [SW|DivIVA] [Pubmed|23264578][SW|DivIVA]-[protein|search|RacA], [protein|search|RacA] binds to the C-terminal domain of [SW|DivIVA] [Pubmed|23264578][SW|DivIVA]-[SW|DivIVA] [Pubmed|23264578][protein|search|Maf]-[SW|DivIVA] [Pubmed|21564336][SW|DivIVA]-[protein|search|ComN] [Pubmed|22582279][SW|DivIVA]-[protein|search|SecA] [Pubmed|24592260][SW|DivIVA]-[SW|SpoIIE] [Pubmed|25101664]Expression and Regulation
Operon
''divIVA'' [Pubmed|16420366]Regulation
repressed under conditions that trigger sporulation ([SW|Spo0A]) [Pubmed|14651647]constitutively expressed [Pubmed|23701187]Regulatory mechanism
[SW|Spo0A]: transcription repression [Pubmed|14651647]Biological materials
Mutant
4041 (''divIVA''::''tet''), available in [SW|Leendert Hamoen]'s, [SW|Jörg Stülke]'s, and [SW|Sven Halbedel] 's labGP1482 (chromosomal ''divIVA''-Strep fusion, ''aphA''3), purification from ''B. subtilis'', for [SW|SPINE], available in [SW|Jörg Stülke]'s labExpression vector
DivIVA-Strep available [http://www.rki.de/DE/Content/Institut/OrgEinheiten/Abt1/FG11/AG_LM.html here]pGP1497 (N-terminal Strep-tag fused to C-terminus of ''divIVA'', TEV-site, purification from ''E. coli'', in [SW|pGP172]), available in [SW|Jörg Stülke]'s labGFP fusion
divIVA-gfp fusions available from the [http://subtiwiki.uni-goettingen.de/wiki/index.php/Leendert_Hamoen Hamoen] Labtwo-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Sven Halbedel]'s and [SW|Jörg Stülke]'s labsAntibody
A polyclonal anti-DivIVA antiserum generated in rabbit is described here [Pubmed|11445541].Labs working on this gene/protein
[SW|Leendert Hamoen], Centre for Bacterial Cell Biology, Newcastle upon Tyne, United Kingdom [http://www.ncl.ac.uk/camb/staff/profile/l.hamoen x][SW|Imrich Barak], Slovak Academy of Science, Bratislava, Slovakia [http://imb.savba.sk/~barak/ homepage][SW|Sven Halbedel], Robert Koch Institute [http://www.rki.de/DE/Content/Institut/OrgEinheiten/Abt1/FG11/AG_LM.html homepage]References
Reviews
19654604,19884039,22722244,23182676 Original Publications
22582279,19654604,19666580,9219999,19019154,15554965,12368265,11445541,10835369,12511520,14651647,19478798,19429628,11445541,9219999,9045828,20352045,20502438,11886553,21564336,22108385,22457634,22517742,22661688,23264578,23701187,23927765,24391905,24592260,24600441,25101664,25845974,27059541,26735940 
