Detail Information for IndEnz0002008467
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;