Difference between revisions of "PbpB"

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* '''Description:''' [[penicillin-binding protein]]  2B, Pbp2B <br/><br/>
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* '''Description:''' class B [[penicillin-binding protein]]  2B, Pbp2B <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || [[penicillin-binding protein]]  2B
 
|style="background:#ABCDEF;" align="center"| '''Product''' || [[penicillin-binding protein]]  2B
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || septation
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|style="background:#ABCDEF;" align="center"|'''Function''' || septation, [[cell division]]
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU15160 pbpB]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU15160 pbpB]
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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 division]]}},
 
{{SubtiWiki category|[[essential genes]]}},
 
{{SubtiWiki category|[[essential genes]]}},
 
{{SubtiWiki category|[[membrane proteins]]}}
 
{{SubtiWiki category|[[membrane proteins]]}}
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* '''[[Localization]]:'''  
 
* '''[[Localization]]:'''  
 
** cell membrane {{PubMed|23869552,20870765}}
 
** cell membrane {{PubMed|23869552,20870765}}
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** extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
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** division sites {{PubMed|23895585}}
 +
** extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
 
** localizes to the sporulation septum during sporulation [http://www.ncbi.nlm.nih.gov/sites/entrez/15758244 PubMed]
 
** localizes to the sporulation septum during sporulation [http://www.ncbi.nlm.nih.gov/sites/entrez/15758244 PubMed]
  
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=References=
 
=References=
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<pubmed>8636036,14731276,8244929,20487272,10652091, 19429628, 18957862 21219466 20870765 14734544 </pubmed>
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<pubmed>8636036,14731276,8244929,20487272,10652091, 19429628, 18957862 21219466 20870765 14734544 23895585 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:54, 5 March 2014

Gene name pbpB
Synonyms
Essential yes PubMed
Product penicillin-binding protein 2B
Function septation, cell division
Gene expression levels in SubtiExpress: pbpB
Interactions involving this protein in SubtInteract: PbpB
MW, pI 79 kDa, 9.234
Gene length, protein length 2148 bp, 716 aa
Immediate neighbours ftsL, spoVD
Sequences Protein DNA DNA_with_flanks
Genetic context
PbpB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PbpB expression.png















Categories containing this gene/protein

cell wall synthesis, cell division, essential genes, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU15160

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: transpeptidase family (according to Swiss-Prot)
  • Paralogous protein(s): SpoVD

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 1RP5 (PBP 2x from Streptococcus pneumoniae, 32% identity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • constitutively expressed 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

Marta Carolina Afonso Lages, Katrin Beilharz, Danae Morales Angeles, Jan-Willem Veening, Dirk-Jan Scheffers
The localization of key Bacillus subtilis penicillin binding proteins during cell growth is determined by substrate availability.
Environ Microbiol: 2013, 15(12);3272-81
[PubMed:23895585] [WorldCat.org] [DOI] (I p)

Tatsuya Fukushima, Isako Furihata, Robyn Emmins, Richard A Daniel, James A Hoch, Hendrik Szurmant
A role for the essential YycG sensor histidine kinase in sensing cell division.
Mol Microbiol: 2011, 79(2);503-22
[PubMed:21219466] [WorldCat.org] [DOI] (I p)

Susan L Rowland, Kimberly D Wadsworth, Scott A Robson, Carine Robichon, Jon Beckwith, Glenn F King
Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B.
J Bacteriol: 2010, 192(23);6116-25
[PubMed:20870765] [WorldCat.org] [DOI] (I p)

Hanne-Leena Hyyryläinen, Bogumila C Marciniak, Kathleen Dahncke, Milla Pietiäinen, Pascal Courtin, Marika Vitikainen, Raili Seppala, Andreas Otto, Dörte Becher, Marie-Pierre Chapot-Chartier, Oscar P Kuipers, Vesa P Kontinen
Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis.
Mol Microbiol: 2010, 77(1);108-27
[PubMed:20487272] [WorldCat.org] [DOI] (I p)

Pamela Gamba, Jan-Willem Veening, Nigel J Saunders, Leendert W Hamoen, Richard A Daniel
Two-step assembly dynamics of the Bacillus subtilis divisome.
J Bacteriol: 2009, 191(13);4186-94
[PubMed:19429628] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Lucile Pernot, Laurent Chesnel, Audrey Le Gouellec, Jacques Croizé, Thierry Vernet, Otto Dideberg, Andréa Dessen
A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics.
J Biol Chem: 2004, 279(16);16463-70
[PubMed:14734544] [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)

R A Daniel, E J Harry, J Errington
Role of penicillin-binding protein PBP 2B in assembly and functioning of the division machinery of Bacillus subtilis.
Mol Microbiol: 2000, 35(2);299-311
[PubMed:10652091] [WorldCat.org] [DOI] (P p)

R A Daniel, A M Williams, J Errington
A complex four-gene operon containing essential cell division gene pbpB in Bacillus subtilis.
J Bacteriol: 1996, 178(8);2343-50
[PubMed:8636036] [WorldCat.org] [DOI] (P p)

A Yanouri, R A Daniel, J Errington, C E Buchanan
Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis.
J Bacteriol: 1993, 175(23);7604-16
[PubMed:8244929] [WorldCat.org] [DOI] (P p)

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