| IED ID | IndEnz0002004954 |
| Enzyme Type ID | protease004954 |
| Protein Name |
Lipoprotein signal peptidase EC 3.4.23.36 Prolipoprotein signal peptidase Signal peptidase II SPase II |
| Gene Name | lspA SF0023 S0026 |
| Organism | Shigella flexneri |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella flexneri |
| Enzyme Sequence | MSQSICSTGLRWLWLVVVVLIIDLGSKYLILQNFALGDTVPLFPSLNLHYARNYGAAFSFLADSGGWQRWFFAGIAIGISVLLAVMMYRSKATQKLNNIAYALIIGGALGNLFDRLWHGFVVDMIDFYVGDWHFATFNLADTAICVGAALIVLEGFLPSKAKKQ |
| Enzyme Length | 164 |
| Uniprot Accession Number | Q83MH1 |
| Absorption | |
| Active Site | ACT_SITE 123; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 141; /evidence=ECO:0000255|HAMAP-Rule:MF_00161 |
| Activity Regulation | |
| 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}; |
| 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}. |
| 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); Transmembrane (4) |
| Keywords | Aspartyl protease;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,128 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |