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Literature summary for 3.4.21.89 extracted from

  • Renier, S.; Chafsey, I.; Chambon, C.; Caccia, N.; Charbit, A.; HÃebraud, M.; Desvaux, M.
    Contribution of the multiple Type I signal peptidases to the secretome of Listeria monocytogenes: Deciphering their specificity for secreted exoproteins by exoproteomic analysis (2015), J. Proteomics, 117, 95-105.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
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-
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Synonyms

Synonyms Comment Organism
SipX
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Listeria monocytogenes
SipY
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Listeria monocytogenes
SipZ
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Listeria monocytogenes

General Information

General Information Comment Organism
physiological function deletion of membrane-bound signal peptidases SipX, SipY and SipZ and construction of SipX/SipY and SipY/SipZ double mutants. The amounts of listeriolysin O, phosphatidylcholine phospholipase C and zinc metalloproteinase Mpl in the extracellular milieu are significantly decreased upon inactivation of SipZ. For the majority of the Sec-secreted exoproteins identified, protein secretion is not affected by the inactivation of one or two of the signal peptidases Listeria monocytogenes