SpoIIIAH

• Description: component of the SpoIIIA-SpoIIQ type III secretion system residing in the forespore membrane, required for SigG activation
  
  

Gene name	spoIIIAH
Synonyms
Essential	no
Product	part of the transmembrane channel linking the mother cell and the forespore
Function	activation of SigG, forespore encasement by the spore coat
Gene expression levels in SubtiExpress: spoIIIAH
Interactions involving this protein in SubtInteract: SpoIIIAH
MW, pI	23 kDa, 4.627
Gene length, protein length	654 bp, 218 aa
Immediate neighbours	accB, spoIIIAG
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

protein secretion, sporulation proteins, membrane proteins

This gene is a member of the following regulons

SigE regulon, SpoIIID regulon

The gene

Basic information

• Locus tag: BSU24360

Phenotypes of a mutant

• block of sporulation after engulfment

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • required for forespore encasement by the spore coat PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • SpoIIIAH-SpoIIQ (interaction between proteins membrane proteins expressed in the mother cell and the forespore, respectively; the complex forms a 60 Å channel made up of twelve subunits of each protein) PubMed

• Localization:
  • membrane protein, forms a transmembrane channel linking the mother cell and the forespore (with SpoIIQ) PubMed
  • proper recruitment to the sporulation septum on the mother cell side requires SpoIIQ PubMed

Database entries

• Structure:
  • 3UZO; 3TUF (the SpoIIQ-SpoIIIAH pore forming complex) PubMed

• UniProt: P49785

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • spoIIIAA-spoIIIAB-spoIIIAC-spoIIIAD-spoIIIAE-spoIIIAF-spoIIIAG-spoIIIAH PubMed
  • spoIIIAG-spoIIIAH PubMed

• Expression browser: spoIIIAH PubMed

• Sigma factor: SigE PubMed
  • both promoters: SigE PubMed

• Regulation:
  • both promoters: expressed during sporulation in the mother cell (SigE) PubMed, switched off by SpoIIID PubMed

• Regulatory mechanism: SpoIIID: transcription repression PubMed

• Additional information: the internal promoter is essential for sporulation, it is twice as active as the promoter in front of spoIIIAA, suggesting that SpoIIIAG and SpoIIIAH are required in larger amounts as compared to the other products of the operon PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Charles Moran, Emory University, NC, USA homepage

References

Christopher D A Rodrigues, Kathleen A Marquis, Jeffrey Meisner, David Z Rudner
Peptidoglycan hydrolysis is required for assembly and activity of the transenvelope secretion complex during sporulation in Bacillus subtilis.
Mol Microbiol: 2013, 89(6);1039-52
[PubMed:23834622] [WorldCat.org] [DOI] (I p)

Jeffrey Meisner, Tatsuya Maehigashi, Ingemar André, Christine M Dunham, Charles P Moran
Structure of the basal components of a bacterial transporter.
Proc Natl Acad Sci U S A: 2012, 109(14);5446-51
[PubMed:22431613] [WorldCat.org] [DOI] (I p)

Vladimir M Levdikov, Elena V Blagova, Amanda McFeat, Mark J Fogg, Keith S Wilson, Anthony J Wilkinson
Structure of components of an intercellular channel complex in sporulating Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(14);5441-5
[PubMed:22431604] [WorldCat.org] [DOI] (I p)

Peter T McKenney, Patrick Eichenberger
Dynamics of spore coat morphogenesis in Bacillus subtilis.
Mol Microbiol: 2012, 83(2);245-60
[PubMed:22171814] [WorldCat.org] [DOI] (I p)

Jeffrey Meisner, Charles P Moran
A LytM domain dictates the localization of proteins to the mother cell-forespore interface during bacterial endospore formation.
J Bacteriol: 2011, 193(3);591-8
[PubMed:21097616] [WorldCat.org] [DOI] (I p)

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)

Chris Guillot, Charles P Moran
Essential internal promoter in the spoIIIA locus of Bacillus subtilis.
J Bacteriol: 2007, 189(20);7181-9
[PubMed:17693505] [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)

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)

N Illing, J Errington
The spoIIIA operon of Bacillus subtilis defines a new temporal class of mother-cell-specific sporulation genes under the control of the sigma E form of RNA polymerase.
Mol Microbiol: 1991, 5(8);1927-40
[PubMed:1766372] [WorldCat.org] [DOI] (P p)