|Function||signal peptide peptidase SppA, 36K type|
|Domain Trusted Cutoff||155.45|
|Domain Noise Cutoff||97.75|
|Mainrole Category||Protein fate|
|Subrole Category||Degradation of proteins, peptides, and glycopeptides|
|Gene Ontology Term||GO:0006465: signal peptide processing biological_process|
| ||GO:0008981: protease IV activity molecular_function|
|Entry Date||Feb 1 2000 10:52AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||The related but duplicated, double-length protein SppA (protease IV) of E. coli was shown experimentally to degrade signal peptides as are released by protein processing and secretion. This protein shows stronger homology to the C-terminal region of SppA than to the N-terminal domain or to the related putative protease SuhB.
The member of this family from Bacillus subtilis was shown to have properties consistent with a role in degrading signal peptides after cleavage from precursor proteins, although it was not demonstrated conclusively.|
RT Signal peptide peptidase- and ClpP-like proteins of Bacillus subtilis required for efficient translocation and processing of secretory proteins.
RA Bolhuis A, Matzen A, Hyyrylainen HL, Kontinen VP, Meima R, Chapuis J, Venema G, Bron S, Freudl R, van Dijl JM
RL J Biol Chem 1999 Aug 27;274(35):24585-92|
|Genome Property||GenProp0205: signal recognition system, bacterial (HMM)|
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