Difference between revisions of "PonA"

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(Categories containing this gene/protein)
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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[cell wall synthesis]]}},
 
{{SubtiWiki category|[[cell wall synthesis]]}},
{{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, W, X, Y)]]}},
+
{{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, V, W, X, Y)]]}},
 
{{SubtiWiki category|[[membrane proteins]]}}
 
{{SubtiWiki category|[[membrane proteins]]}}
  

Revision as of 22:10, 24 August 2011

Gene name ponA
Synonyms
Essential no
Product penicillin-binding protein 1A/1B
Function bifunctional glucosyltransferase/ transpeptidase
MW, pI 99 kDa, 4.752
Gene length, protein length 2742 bp, 914 aa
Immediate neighbours recU, ypoC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PonA context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell wall synthesis, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins

This gene is a member of the following regulons

SigM regulon

The gene

Basic information

  • Locus tag: BSU22320

Phenotypes of a mutant

  • prevents bulging of the cells when grown at low Mg(2+) concentrations, suppresses the lethal effect of a mreB mutation PubMed
  • deletion of ponA restores growth and normal shape of a yvcK mutant on gluconeogenic carbon sources PubMed

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:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:
    • membrane associated PubMed
    • localizes to the spore septum during sporulation PubMed
    • localizes to the vegetative septum PubMed, this depends on YvcK PubMed

Database entries

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

Additional information

Expression and regulation

  • Regulation: constitutive during vegetative growth PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jeff Errington lab
  • Antibody:

Labs working on this gene/protein

Jeff Errington, Newcastle University, UK homepage

Your additional remarks

References

Reviews

PubMed

Original publications

Elodie Foulquier, Frédérique Pompeo, Alain Bernadac, Leon Espinosa, Anne Galinier
The YvcK protein is required for morphogenesis via localization of PBP1 under gluconeogenic growth conditions in Bacillus subtilis.
Mol Microbiol: 2011, 80(2);309-18
[PubMed:21320184] [WorldCat.org] [DOI] (I p)

Yoshikazu Kawai, Richard A Daniel, Jeffery Errington
Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix.
Mol Microbiol: 2009, 71(5);1131-44
[PubMed:19192185] [WorldCat.org] [DOI] (I p)

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)

Dennis Claessen, Robyn Emmins, Leendert W Hamoen, Richard A Daniel, Jeff Errington, David H Edwards
Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis.
Mol Microbiol: 2008, 68(4);1029-46
[PubMed:18363795] [WorldCat.org] [DOI] (I p)

Warawan Eiamphungporn, John D Helmann
The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses.
Mol Microbiol: 2008, 67(4);830-48
[PubMed:18179421] [WorldCat.org] [DOI] (P p)

Dirk-Jan Scheffers, Jeffery Errington
PBP1 is a component of the Bacillus subtilis cell division machinery.
J Bacteriol: 2004, 186(15);5153-6
[PubMed:15262952] [WorldCat.org] [DOI] (P p)

Dirk-Jan Scheffers, Laura J F Jones, Jeffery Errington
Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis.
Mol Microbiol: 2004, 51(3);749-64
[PubMed:14731276] [WorldCat.org] [DOI] (P p)

L B Pedersen, E R Angert, P Setlow
Septal localization of penicillin-binding protein 1 in Bacillus subtilis.
J Bacteriol: 1999, 181(10);3201-11
[PubMed:10322023] [WorldCat.org] [DOI] (P p)

T Murray, D L Popham, P Setlow
Bacillus subtilis cells lacking penicillin-binding protein 1 require increased levels of divalent cations for growth.
J Bacteriol: 1998, 180(17);4555-63
[PubMed:9721295] [WorldCat.org] [DOI] (P p)

D L Popham, P Setlow
Phenotypes of Bacillus subtilis mutants lacking multiple class A high-molecular-weight penicillin-binding proteins.
J Bacteriol: 1996, 178(7);2079-85
[PubMed:8606187] [WorldCat.org] [DOI] (P p)

D L Popham, P Setlow
Cloning, nucleotide sequence, and mutagenesis of the Bacillus subtilis ponA operon, which codes for penicillin-binding protein (PBP) 1 and a PBP-related factor.
J Bacteriol: 1995, 177(2);326-35
[PubMed:7814321] [WorldCat.org] [DOI] (P p)