Signal peptide peptidase-and ClpP-like proteins of Bacillus subtilis required for efficient translocation and processing of secretory proteins
A Bolhuis, A Matzen, HL Hyyryläinen… - Journal of Biological …, 1999 - ASBMB
Signal peptides direct the export of secretory proteins from the cytoplasm. After processing
by signal peptidase, they are degraded in the membrane and cytoplasm. The resulting
fragments can have signaling functions. These observations suggest important roles for
signal peptide peptidases. The present studies show that the Gram-positive eubacterium
Bacillus subtilis contains two genes for proteins, denoted SppA and TepA, with similarity to
the signal peptide peptidase A of Escherichia coli. Notably, TepA also shows similarity to …
by signal peptidase, they are degraded in the membrane and cytoplasm. The resulting
fragments can have signaling functions. These observations suggest important roles for
signal peptide peptidases. The present studies show that the Gram-positive eubacterium
Bacillus subtilis contains two genes for proteins, denoted SppA and TepA, with similarity to
the signal peptide peptidase A of Escherichia coli. Notably, TepA also shows similarity to …
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