SpoVD

• Description: mother-cell specific penicillin-binding protein (spore cortex)
  
  

Gene name	spoVD
Synonyms
Essential	no
Product	penicillin-binding protein (spore cortex)
Function	spore morphogenesis
Gene expression levels in SubtiExpress: spoVD
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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Interactions:
  • SpoVD-StoA PubMed
  • SpoVD-SpoVE PubMed

• Localization: intermembrane space that separates forespores from mother cells PubMed

Database entries

• Structure:

• UniProt: Q03524

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: spoVD PubMed

• Expression browser: spoVD PubMed

• Sigma factor: SigE PubMed

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

• Regulatory mechanism:

• • SpoIIID: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:
  • 1A975 ( spoVD::cat), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Patrick Eichenberger
The red-ox status of a penicillin-binding protein is an on/off switch for spore peptidoglycan synthesis in Bacillus subtilis.
Mol Microbiol: 2010, 75(1);10-2
[PubMed:19919674] [WorldCat.org] [DOI] (I p)

Original Publications

Ewa Bukowska-Faniband, Lars Hederstedt
Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD.
FEMS Microbiol Lett: 2013, 346(1);65-72
[PubMed:23789716] [WorldCat.org] [DOI] (I p)

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)