Difference between revisions of "SpoVD"

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* '''Operon:''' ''[[spoVD]]'' {{PubMed|8436954}}
 
* '''Operon:''' ''[[spoVD]]'' {{PubMed|8436954}}
  
* '''[[Sigma factor]]:''' [[SigE]] {{PubMed|15699190,15758244}}  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spoVD_1584214_1586154_1 spoVD] {{PubMed|22383849}}
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* '''Sigma factor:''' [[SigE]] {{PubMed|15699190,15758244}}  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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** [[SpoIIID]]: transcription repression {{PubMed|9006059}}
 
** [[SpoIIID]]: transcription repression {{PubMed|9006059}}
  
* '''Additional information:'''  
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* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =

Revision as of 08:25, 13 April 2012

Gene name spoVD
Synonyms
Essential no
Product penicillin-binding protein (spore cortex)
Function spore morphogenesis
Interactions involving this protein in SubtInteract: SpoVD
MW, pI 71 kDa, 8.85
Gene length, protein length 1935 bp, 645 aa
Immediate neighbours pbpB, murE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SpoVD context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell wall synthesis, sporulation proteins, membrane proteins

This gene is a member of the following regulons

SigE regulon, SpoIIID regulon

The gene

Basic information

  • Locus tag: BSU15170

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: protects SpoVE from proteolytic degradation PubMed
  • Protein family:
  • Paralogous protein(s): PbpB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: intramolecular disulfide bonds between two Cys residues are reduced by StoA, this is rquired for activity of SpoVD PubMed

Database entries

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

Additional information

Expression and regulation

  • Regulation:
    • expressed during sporulation in the mother cell (SigE) 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

Reviews

Original Publications

Allison Fay, Pablo Meyer, Jonathan Dworkin
Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation.
J Mol Biol: 2010, 399(4);547-61
[PubMed:20417640] [WorldCat.org] [DOI] (I p)

Yiming Liu, Mirja Carlsson Möller, Lise Petersen, Christopher A G Söderberg, Lars Hederstedt
Penicillin-binding protein SpoVD disulphide is a target for StoA in Bacillus subtilis forespores.
Mol Microbiol: 2010, 75(1);46-60
[PubMed:19919673] [WorldCat.org] [DOI] (I p)

Dirk-Jan Scheffers
Dynamic localization of penicillin-binding proteins during spore development in Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 3);999-1012
[PubMed:15758244] [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)

B Zhang, R A Daniel, J Errington, L Kroos
Bacillus subtilis SpoIIID protein binds to two sites in the spoVD promoter and represses transcription by sigmaE RNA polymerase.
J Bacteriol: 1997, 179(3);972-5
[PubMed:9006059] [WorldCat.org] [DOI] (P p)

R A Daniel, S Drake, C E Buchanan, R Scholle, J Errington
The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis.
J Mol Biol: 1994, 235(1);209-20
[PubMed:8289242] [WorldCat.org] [DOI] (P p)

R A Daniel, J Errington
DNA sequence of the murE-murD region of Bacillus subtilis 168.
J Gen Microbiol: 1993, 139(2);361-70
[PubMed:8436954] [WorldCat.org] [DOI] (P p)