Difference between revisions of "PcrB"

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(Categories containing this gene/protein)
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* '''[[SubtInteract|Interactions]]:'''
 
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** forms dimers  {{PubMed|22614947}}
  
 
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Revision as of 09:17, 23 May 2012

  • Description: heptaprenylglyceryl phosphate synthase

Gene name pcrB
Synonyms yerE
Essential no
Product heptaprenylglyceryl phosphate synthase
Function unknown
MW, pI 24 kDa, 4.204
Gene length, protein length 684 bp, 228 aa
Immediate neighbours yerD, pcrA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PcrB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PcrB expression.png
























Categories containing this gene/protein

lipid metabolism/ other

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU06600

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • 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

David Peterhoff, Hermann Zellner, Harald Guldan, Rainer Merkl, Reinhard Sterner, Patrick Babinger
Dimerization determines substrate specificity of a bacterial prenyltransferase.
Chembiochem: 2012, 13(9);1297-303
[PubMed:22614947] [WorldCat.org] [DOI] (I p)

Harald Guldan, Frank-Michael Matysik, Marco Bocola, Reinhard Sterner, Patrick Babinger
Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria.
Angew Chem Int Ed Engl: 2011, 50(35);8188-91
[PubMed:21761520] [WorldCat.org] [DOI] (I p)

Harald Guldan, Reinhard Sterner, Patrick Babinger
Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.
Biochemistry: 2008, 47(28);7376-84
[PubMed:18558723] [WorldCat.org] [DOI] (I p)

M A Petit, E Dervyn, M Rose, K D Entian, S McGovern, S D Ehrlich, C Bruand
PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication.
Mol Microbiol: 1998, 29(1);261-73
[PubMed:9701819] [WorldCat.org] [DOI] (P p)