PpiB

• 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 DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

chaperones/ protein folding

The gene

Basic information

• Locus tag: BSU23360

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P35137

• KEGG entry: [3]

• E.C. number: 5.2.1.8

Expression and regulation

• Operon: ppiB PubMed

• Expression browser: ppiB PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)