Difference between revisions of "SpoIIQ"
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || part of the transmembrane channel linking the mother cell and the forespore |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || forespore | + | |style="background:#ABCDEF;" align="center"|'''Function''' || forespore encasement by the spore coat |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/SpoIIQ SpoIIQ] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/SpoIIQ SpoIIQ] | ||
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__TOC__ | __TOC__ | ||
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<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
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=== Additional information=== | === Additional information=== | ||
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* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
+ | ** required for forespore encasement by the spore coat {{PubMed|22171814}} | ||
* '''Protein family:''' | * '''Protein family:''' | ||
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* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
− | ** forespore | + | ** membrane protein, forms a transmembrane channel linking the mother cell and the forespore (with [[SpoIIIAH]]) {{PubMed|22431604,22431613,22171814}} |
=== Database entries === | === Database entries === | ||
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=References= | =References= | ||
'''Additional publications:''' {{PubMed|22431604}} | '''Additional publications:''' {{PubMed|22431604}} | ||
− | <pubmed>18812514,15752199,18077456,18485064,15574594,15044948,15882622,19609349 ,9140963 20444098 17121846 18160039 21097616 16497325,15699190 22431613</pubmed> | + | <pubmed>18812514,15752199,18077456,18485064,15574594,15044948,15882622,19609349 ,9140963 20444098 17121846 18160039 21097616 16497325,15699190 22431613 22171814</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:59, 29 July 2012
- Description: component of the SpoIIIAH-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 | part of the transmembrane channel linking the mother cell and the forespore |
Function | forespore encasement by the spore coat |
Interactions involving this protein in SubtInteract: SpoIIQ | |
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
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
sporulation proteins, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU36550
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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:
Database entries
- UniProt: P71044
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: spoIIQ PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed
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)
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)
Pablo Meyer, Jennifer Gutierrez, Kit Pogliano, Jonathan Dworkin
Cell wall synthesis is necessary for membrane dynamics during sporulation of Bacillus subtilis.
Mol Microbiol: 2010, 76(4);956-70
[PubMed:20444098]
[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)
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)
Leif Steil, Mónica Serrano, Adriano O Henriques, Uwe Völker
Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 2);399-420
[PubMed:15699190]
[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)
J A Londoño-Vallejo, C Fréhel, P Stragier
SpoIIQ, a forespore-expressed gene required for engulfment in Bacillus subtilis.
Mol Microbiol: 1997, 24(1);29-39
[PubMed:9140963]
[WorldCat.org]
[DOI]
(P p)