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Literature summary for 5.2.1.8 extracted from

  • Reffuveille, F.; Connil, N.; Sanguinetti, M.; Posteraro, B.; Chevalier, S.; Auffray, Y.; Rince, A.
    Involvement of peptidylprolyl cis/trans isomerases in Enterococcus faecalis virulence (2012), Infect. Immun., 80, 1728-1735.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.2.1.8

Protein Variants

Protein Variants Comment Organism
additional information generation of genes ef2898, ef0685, and ef1534 deletion mutants Enterococcus faecalis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface enzymes EF0685 and EF1534 Enterococcus faecalis 9986
-
intracellular enzyme EF2898 Enterococcus faecalis 5622
-

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis Q82ZZ9 gene ef2898
-
Enterococcus faecalis Q834U8 gene ef1534
-
Enterococcus faecalis Q837Y9 gene ef0685
-

Synonyms

Synonyms Comment Organism
EF0685
-
 Enterococcus faecalis
EF1534
-
 Enterococcus faecalis
EF2898
-
 Enterococcus faecalis
peptidylprolyl cis/trans isomerase
-
 Enterococcus faecalis
PPIase
-
 Enterococcus faecalis

General Information

General Information Comment Organism
malfunction a DELTAef0685/DELTAef1534 mutant is more resistant to oxidative stress, is able to grow under a high manganese concentration, and shows altered resistance to ampicillin and quinolone antibiotics Enterococcus faecalis
additional information EF0685, EF1534, and EF2898 protein sequence comparisons, overview Enterococcus faecalis
physiological function peptidylprolyl cis/trans isomerases are enzymes involved in protein folding. The parvulin family rotamase EF0685 and the cyclophilin family member EF1534 are important for virulence and resistance to NaCl, while EF2898 is not important for the Enterococcus faecalis stress response or virulence Enterococcus faecalis