PpiB

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  • Description: peptidyl-prolyl isomerase

Gene name ppiB
Synonyms cypBS
Essential no
Product peptidyl-prolyl isomerase
Function protein folding
Gene expression levels in SubtiExpress: ppiB
MW, pI 15 kDa, 5.472
Gene length, protein length 429 bp, 143 aa
Immediate neighbours ypzD, ypuA
Sequences Protein DNA Advanced_DNA
Genetic context
PpiB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PpiB expression.png
























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)