SpoIIQ

• Description: component of the SpoIIIA-SpoIIQ type III secretion system residing in the forespore membrane, required for anchoring of proteins on both sides of the sporulation septum
  
  

Gene name	spoIIQ
Synonyms	ywnI
Essential	no
Product	component of a type III secretion system
Function	forespore engulfment
MW, pI	30 kDa, 4.475
Gene length, protein length	849 bp, 283 aa
Immediate neighbours	ywnJ, ywnH
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU36550

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: SpoIIIAH-SpoIIQ, SpoIIQ-SpoIIE

• Localization: forespore membrane (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P71044

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor: SigF PubMed

• Regulation:
  • expressed early during sporulation in the forespore (SigF) PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Thierry Doan, Cecile Morlot, Jeffrey Meisner, Monica Serrano, Adriano O Henriques, Charles P Moran, David Z Rudner
Novel secretion apparatus maintains spore integrity and developmental gene expression in Bacillus subtilis.
PLoS Genet: 2009, 5(7);e1000566
[PubMed:19609349] [WorldCat.org] [DOI] (I p)

Jeffrey Meisner, Xin Wang, Monica Serrano, Adriano O Henriques, Charles P Moran
A channel connecting the mother cell and forespore during bacterial endospore formation.
Proc Natl Acad Sci U S A: 2008, 105(39);15100-5
[PubMed:18812514] [WorldCat.org] [DOI] (I p)

Amy H Camp, Richard Losick
A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels.
Mol Microbiol: 2008, 69(2);402-17
[PubMed:18485064] [WorldCat.org] [DOI] (I p)

Briana M Burton, Kathleen A Marquis, Nora L Sullivan, Tom A Rapoport, David Z Rudner
The ATPase SpoIIIE transports DNA across fused septal membranes during sporulation in Bacillus subtilis.
Cell: 2007, 131(7);1301-12
[PubMed:18160039] [WorldCat.org] [DOI] (P p)

Nathalie Campo, Kathleen A Marquis, David Z Rudner
SpoIIQ anchors membrane proteins on both sides of the sporulation septum in Bacillus subtilis.
J Biol Chem: 2008, 283(8);4975-82
[PubMed:18077456] [WorldCat.org] [DOI] (P p)

Shinobu Chiba, Kristina Coleman, Kit Pogliano
Impact of membrane fusion and proteolysis on SpoIIQ dynamics and interaction with SpoIIIAH.
J Biol Chem: 2007, 282(4);2576-86
[PubMed:17121846] [WorldCat.org] [DOI] (P p)

Stephanie T Wang, Barbara Setlow, Erin M Conlon, Jessica L Lyon, Daisuke Imamura, Tsutomu Sato, Peter Setlow, Richard Losick, Patrick Eichenberger
The forespore line of gene expression in Bacillus subtilis.
J Mol Biol: 2006, 358(1);16-37
[PubMed:16497325] [WorldCat.org] [DOI] (P p)

Jonathan Dworkin, Richard Losick
Developmental commitment in a bacterium.
Cell: 2005, 121(3);401-9
[PubMed:15882622] [WorldCat.org] [DOI] (P p)

Thierry Doan, Kathleen A Marquis, David Z Rudner
Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum.
Mol Microbiol: 2005, 55(6);1767-81
[PubMed:15752199] [WorldCat.org] [DOI] (P p)

Bill Blaylock, Xin Jiang, Aileen Rubio, Charles P Moran, Kit Pogliano
Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization.
Genes Dev: 2004, 18(23);2916-28
[PubMed:15574594] [WorldCat.org] [DOI] (P p)

Aileen Rubio, Kit Pogliano
Septal localization of forespore membrane proteins during engulfment in Bacillus subtilis.
EMBO J: 2004, 23(7);1636-46
[PubMed:15044948] [WorldCat.org] [DOI] (P p)