IED ID | IndEnz0002008467 |
Enzyme Type ID | protease008467 |
Protein Name |
Putative signal peptide peptidase SppA EC 3.4.21.- |
Gene Name | sppA yteI BSU29530 |
Organism | Bacillus subtilis (strain 168) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
Enzyme Sequence | MNAKRWIALVIALGIFGVSIIVSISMSFFESVKGAQTDLTSLTDESQEKTLENGSPSSKIAVLEVSGTIQDNGDSSSLLGADGYNHRTFLKNLERAKDDKTVKGIVLKVNSPGGGVYESAEIHKKLEEIKKETKKPIYVSMGSMAASGGYYISTAADKIFATPETLTGSLGVIMESVNYSKLADKLGISFETIKSGAHKDIMSPSREMTKEEKNIMQSMVDNSYEGFVDVISKGRGMPKAEVKKIADGRVYDGRQAKKLNLVDELGFYDDTITAMKKDHKDLKNASVISYEESFGLGSLFSMGANKMFKSEIDFLNMREILSQSGSPRMMYLYAK |
Enzyme Length | 335 |
Uniprot Accession Number | O34525 |
Absorption | |
Active Site | ACT_SITE 147; /note=Nucleophile; /evidence=ECO:0000269|PubMed:22472423; ACT_SITE 199; /note=Proton donor/acceptor; /evidence=ECO:0000269|PubMed:22472423 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion. Has a preference for leucine-rich substrate peptides. {ECO:0000250, ECO:0000269|PubMed:10455123}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (12); Chain (1); Helix (10); Mutagenesis (2); Site (1); Transmembrane (1); Turn (1) |
Keywords | 3D-structure;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Serine protease;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456, ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:23651456}; Single-pass membrane protein. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. {ECO:0000269|PubMed:23651456}. |
Modified Residue | |
Post Translational Modification | PTM: Autocatalytically cleaves its own C-terminus. |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 3RST; 4KWB; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 36,673 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.23.B24; |