| IED ID | IndEnz0002006666 |
| Enzyme Type ID | protease006666 |
| Protein Name |
Lipoprotein signal peptidase EC 3.4.23.36 LspMrs Prolipoprotein signal peptidase Signal peptidase II SPase II |
| Gene Name | lspA SAUSA300_1089 |
| Organism | Staphylococcus aureus (strain USA300) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain USA300) |
| Enzyme Sequence | MHKKYFIGTSILIAVFVVIFDQVTKYIIATTMKIGDSFEVIPHFLNITSHRNNGAAWGILSGKMTFFFIITIIILIALVYFFIKDAQYNLFMQVAISLLFAGALGNFIDRILTGEVVDFIDTNIFGYDFPIFNIADSSLTIGVILIIIALLKDTSNKKEKEVK |
| Enzyme Length | 163 |
| Uniprot Accession Number | Q2FHP2 |
| Absorption | |
| Active Site | ACT_SITE 118; /evidence="ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:31919415"; ACT_SITE 136; /evidence="ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:31919415" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the antibiotics globomycin and myxovirescin. They act by blocking the catalytic dyad. {ECO:0000269|PubMed:31919415}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.; EC=3.4.23.36; Evidence={ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:31919415}; |
| DNA Binding | |
| EC Number | 3.4.23.36 |
| Enzyme Function | FUNCTION: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:31919415}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Mutagenesis (9); Topological domain (5); Transmembrane (4) |
| Keywords | 3D-structure;Aspartyl protease;Cell membrane;Hydrolase;Membrane;Protease;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:31919415}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:31919415}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 6RYO; 6RYP; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,342 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=47 uM for P.aeruginosa inhibitor of cysteine peptidase {ECO:0000269|PubMed:31919415}; Vmax=2.5 nmol/min/mg enzyme with P.aeruginosa inhibitor of cysteine peptidase as substrate {ECO:0000269|PubMed:31919415}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |