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Literature summary for 5.2.1.8 extracted from

  • Hyyrylaeinen, H.L.; Marciniak, B.C.; Dahncke, K.; Pietiaeinen, M.; Courtin, P.; Vitikainen, M.; Seppala, R.; Otto, A.; Becher, D.; Chapot-Chartier, M.P.; Kuipers, O.P.; Kontinen, V.P.
    Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis (2010), Mol. Microbiol., 77, 108-127.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Bacillus subtilis 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
x * 33000, SDS-PAGE Bacillus subtilis
65000
-
the cross-linking of cells expressing either wild-type PrsA or PrsA-Myc revealed, in addition to the 33 kDa PrsA or PrsA-Myc monomers, two other PrsA-containing bands of higher molecular weights, one migrating (in SDS-PAGE) at approximately 65 kDa and the other one slightly above it (about 68 kDa) Bacillus subtilis
68000
-
the cross-linking of cells expressing either wild-type PrsA or PrsA-Myc revealed, in addition to the 33 kDa PrsA or PrsA-Myc monomers, two other PrsA-containing bands of higher molecular weights, one migrating (in SDS-PAGE) at approximately 65 kDa and the other one slightly above it (about 68 kDa) Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis IH8478
-
-
-

Subunits

Subunits Comment Organism
oligomer x * 33000, SDS-PAGE Bacillus subtilis

Synonyms

Synonyms Comment Organism
Peptidyl-prolyl cis-trans isomerase
-
Bacillus subtilis
PPIase
-
Bacillus subtilis
PrsA
-
Bacillus subtilis

General Information

General Information Comment Organism
malfunction Bacillus subtilis cells depleted of the PrsA protein are able to grow in the presence of a high concentration of magnesium (20 mM). PrsA depletion destabilizes penicillin-binding proteins Bacillus subtilis
physiological function PrsA catalyses the post-translocational folding of exported proteins and is essential for normal growth of Bacillus subtilis. PrsA is involved in the biosynthesis of the cylindrical lateral wall. PrsA is required for the folding of penicillin-binding protein 2a Bacillus subtilis