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Literature summary for 3.4.21.89 extracted from

  • Schallenberger, M.A.; Niessen, S.; Shao, C.; Fowler, B.J.; Romesberg, F.E.
    Type I signal peptidase and protein secretion in Staphylococcus aureus (2012), J. Bacteriol., 194, 2677-2686.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
arylomycin A-C16 secretion of proteins HtrA, PrsA, and SAOUHSC_01761 is induced by inhibitor treatment Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-
Staphylococcus aureus NCTC 8325
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lipoteichoic acid synthase + H2O
-
Staphylococcus aureus ? soluble C-terminal domain has a noncanonical, internal cleavage site ?
lipoteichoic acid synthase + H2O
-
Staphylococcus aureus NCTC 8325 ? soluble C-terminal domain has a noncanonical, internal cleavage site ?
additional information identification of 46 proteins whose extracellular accumulation requires signal peptidase activity. Forty-four possess identifiable Sec-type signal peptides and thus are likely canonically secreted proteins, while four also appear to possess cell wall retention signals. For three proteins, HtrA, PrsA, and SAOUHSC_01761, secretion is induced by inhibitor arylomycin treatment Staphylococcus aureus ?
-
?
additional information identification of 46 proteins whose extracellular accumulation requires signal peptidase activity. Forty-four possess identifiable Sec-type signal peptides and thus are likely canonically secreted proteins, while four also appear to possess cell wall retention signals. For three proteins, HtrA, PrsA, and SAOUHSC_01761, secretion is induced by inhibitor arylomycin treatment Staphylococcus aureus NCTC 8325 ?
-
?
O-acetyltransferase + H2O
-
Staphylococcus aureus ? soluble C-terminal domain has a noncanonical, internal cleavage site ?
O-acetyltransferase + H2O
-
Staphylococcus aureus NCTC 8325 ? soluble C-terminal domain has a noncanonical, internal cleavage site ?