Difference between revisions of "SdpC"
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<pubmed>,12817086,16469701,16629676,13129613,14651647,15687200,15743949,15687200,17720793,12107147, </pubmed> | <pubmed>,12817086,16469701,16629676,13129613,14651647,15687200,15743949,15687200,17720793,12107147, </pubmed> | ||
− | + | '''Additional publications:''' {{PubMed|20805502}} | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:22, 8 October 2010
- Description: toxin, kills non-sporulating cells, induces activity of SigW
Gene name | sdpC |
Synonyms | yvaY |
Essential | no |
Product | toxin, kills non-sporulating cells |
Function | killing of non-sporulating sister cells |
MW, pI | 22 kDa, 9.611 |
Gene length, protein length | 609 bp, 203 aa |
Immediate neighbours | sdpB, sdpI |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU33770
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: the meture SDP is a 42-residue peptide with one disulfide bridge PubMed
- Cofactor(s):
- Effectors of protein activity:
- Localization: secreted (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O34344
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- 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
Mark A Strauch, Benjamin G Bobay, John Cavanagh, Fude Yao, Angelo Wilson, Yoann Le Breton
Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.
J Bacteriol: 2007, 189(21);7720-32
[PubMed:17720793]
[WorldCat.org]
[DOI]
(P p)
Bronwyn G Butcher, John D Helmann
Identification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacilli.
Mol Microbiol: 2006, 60(3);765-82
[PubMed:16629676]
[WorldCat.org]
[DOI]
(P p)
Craig D Ellermeier, Errett C Hobbs, Jose E Gonzalez-Pastor, Richard Losick
A three-protein signaling pathway governing immunity to a bacterial cannibalism toxin.
Cell: 2006, 124(3);549-59
[PubMed:16469701]
[WorldCat.org]
[DOI]
(P p)
Mark Albano, Wiep Klaas Smits, Linh T Y Ho, Barbara Kraigher, Ines Mandic-Mulec, Oscar P Kuipers, David Dubnau
The Rok protein of Bacillus subtilis represses genes for cell surface and extracellular functions.
J Bacteriol: 2005, 187(6);2010-9
[PubMed:15743949]
[WorldCat.org]
[DOI]
(P p)
Masaya Fujita, José Eduardo González-Pastor, Richard Losick
High- and low-threshold genes in the Spo0A regulon of Bacillus subtilis.
J Bacteriol: 2005, 187(4);1357-68
[PubMed:15687200]
[WorldCat.org]
[DOI]
(P p)
Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647]
[WorldCat.org]
[DOI]
(P p)
Dirk Linde, Rudolf Volkmer-Engert, Sandra Schreiber, Jörg P Müller
Interaction of the Bacillus subtilis chaperone CsaA with the secretory protein YvaY.
FEMS Microbiol Lett: 2003, 226(1);93-100
[PubMed:13129613]
[WorldCat.org]
[DOI]
(P p)
José E González-Pastor, Errett C Hobbs, Richard Losick
Cannibalism by sporulating bacteria.
Science: 2003, 301(5632);510-3
[PubMed:12817086]
[WorldCat.org]
[DOI]
(I p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)
Additional publications: PubMed