Structural highlights
Function
SPPA_ECOLI Digests cleaved signal peptides in vitro, its in vivo function is unknown. This activity is necessary to maintain proper secretion of mature proteins across the membrane.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Ichihara S, Suzuki T, Suzuki M, Mizushima S. Molecular cloning and sequencing of the sppA gene and characterization of the encoded protease IV, a signal peptide peptidase, of Escherichia coli. J Biol Chem. 1986 Jul 15;261(20):9405-11. PMID:3522590
- ↑ Wang P, Shim E, Cravatt B, Jacobsen R, Schoeniger J, Kim AC, Paetzel M, Dalbey RE. Escherichia coli signal peptide peptidase A is a serine-lysine protease with a lysine recruited to the nonconserved amino-terminal domain in the S49 protease family. Biochemistry. 2008 Jun 17;47(24):6361-9. doi: 10.1021/bi800657p. Epub 2008 May, 14. PMID:18476724 doi:http://dx.doi.org/10.1021/bi800657p
- ↑ Saito A, Hizukuri Y, Matsuo E, Chiba S, Mori H, Nishimura O, Ito K, Akiyama Y. Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria. Proc Natl Acad Sci U S A. 2011 Aug 16;108(33):13740-5. doi:, 10.1073/pnas.1108376108. Epub 2011 Aug 2. PMID:21810987 doi:http://dx.doi.org/10.1073/pnas.1108376108
- ↑ Kim AC, Oliver DC, Paetzel M. Crystal structure of a bacterial signal Peptide peptidase. J Mol Biol. 2008 Feb 15;376(2):352-66. Epub 2007 Dec 4. PMID:18164727 doi:10.1016/j.jmb.2007.11.080
