Difference between revisions of "PonA"

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* '''Description:''' [[penicillin-binding protein]] 1A/1B <br/><br/>
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* '''Description:''' class A [[penicillin-binding protein]] 1A/1B <br/><br/>
  
 
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''

Revision as of 09:13, 5 March 2014

Gene name ponA
Synonyms
Essential no
Product penicillin-binding protein 1A/1B
Function bifunctional glucosyltransferase/ transpeptidase
Gene expression levels in SubtiExpress: ponA
Interactions involving this protein in SubtInteract: PonA
MW, pI 99 kDa, 4.752
Gene length, protein length 2742 bp, 914 aa
Immediate neighbours recU, ypoC
Sequences Protein DNA DNA_with_flanks
Genetic context
PonA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PonA expression.png















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:
  • Modification:
  • Effectors of protein activity:

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

Johann Mignolet, Patrick H Viollier
A sweet twist gets Bacillus into shape.
Mol Microbiol: 2011, 80(2);283-5
[PubMed:21371139] [WorldCat.org] [DOI] (I p)

Original publications

Elitza I Tocheva, Javier López-Garrido, H Velocity Hughes, Jennifer Fredlund, Erkin Kuru, Michael S Vannieuwenhze, Yves V Brun, Kit Pogliano, Grant J Jensen
Peptidoglycan transformations during Bacillus subtilis sporulation.
Mol Microbiol: 2013, 88(4);673-86
[PubMed:23531131] [WorldCat.org] [DOI] (I p)

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)