Difference between revisions of "SdpC"

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Revision as of 09:18, 23 April 2012

  • Description: toxin, collapses the proton motive force and induces autolysis, 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
Interactions involving this protein in SubtInteract: SdpC
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
YvaY context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SdpC expression.png
























Categories containing this gene/protein

toxins, antitoxins and immunity against toxins

This gene is a member of the following regulons

AbrB regulon, Rok regulon, Spo0A regulon

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:
    • toxin, collapses the proton motive force and induces autolysis PubMed
  • 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:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Additional information:
    • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original Publications

Additional publications: PubMed

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947

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)