SdpB

• Description: membrane protein
  
  

Gene name	sdpB
Synonyms	yvaX
Essential	no
Product	unknown
Function	unknown
Gene expression levels in SubtiExpress: sdpB
MW, pI	37 kDa, 9.521
Gene length, protein length	969 bp, 323 aa
Immediate neighbours	sdpA, sdpC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

toxins, antitoxins and immunity against toxins, membrane proteins

This gene is a member of the following regulons

AbrB regulon, Rok regulon, Spo0A regulon

The gene

Basic information

• Locus tag: BSU33760

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:

• Localization:
  • cell membrane PubMed

Database entries

• Structure:

• UniProt: O34616

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sdpA-sdpB-sdpC PubMed

• Expression browser: sdpB PubMed

• Sigma factor:

• Regulation:
  • expressed under conditions that trigger sporulation (Spo0A) PubMed
  • repressed by Rok PubMed
  • repressed during logrithmic growth (AbrB) PubMed
  • strongly repressed in response to glucose starvation in M9 medium PubMed

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed
  • Rok: transcription repression PubMed
  • AbrB: transcription repression PubMed

• 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:

References

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

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

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)

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)

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)