Difference between revisions of "PpiB"

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(Extended information on the protein)
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=== Database entries ===
 
=== Database entries ===

Revision as of 20:20, 8 December 2011

  • Description: peptidyl-prolyl isomerase

Gene name ppiB
Synonyms cypBS
Essential no
Product peptidyl-prolyl isomerase
Function protein folding
MW, pI 15 kDa, 5.472
Gene length, protein length 429 bp, 143 aa
Immediate neighbours ypzD, ypuA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PpiB context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

chaperones/ protein folding

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU23360

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Peptidylproline (omega=180) = peptidylproline (omega=0) (according to Swiss-Prot)
  • Protein family: cyclophilin-type PPIase 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

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

S F Göthel, C Scholz, F X Schmid, M A Marahiel
Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions.
Biochemistry: 1998, 37(38);13392-9
[PubMed:9748346] [WorldCat.org] [DOI] (P p)

T V Achenbach, S F Göthel, M A Marahiel
Histidine 109 in peptidyl-prolyl cis-trans isomerase of Bacillus subtilis plays an important role in catalysis and in cyclosporin A binding.
FEMS Microbiol Lett: 1997, 154(1);139-44
[PubMed:9297832] [WorldCat.org] [DOI] (P p)

S F Göthel, M Herrler, M A Marahiel
Peptidyl-prolyl cis-trans isomerase of Bacillus subtilis: identification of residues involved in cyclosporin A affinity and catalytic efficiency.
Biochemistry: 1996, 35(11);3636-40
[PubMed:8639516] [WorldCat.org] [DOI] (P p)

M Herrler, H Bang, M A Marahiel
Cloning and characterization of ppiB, a Bacillus subtilis gene which encodes a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase.
Mol Microbiol: 1994, 11(6);1073-83
[PubMed:8022278] [WorldCat.org] [DOI] (P p)

M Herrler, H Bang, K Brune, G Fischer, M A Marahiel
Peptidyl-prolyl cis-trans isomerase from Bacillus subtilis. A prokaryotic enzyme that is highly sensitive to cyclosporin A.
FEBS Lett: 1992, 309(3);231-4
[PubMed:1516692] [WorldCat.org] [DOI] (P p)