| IED ID | IndEnz0002010470 |
| Enzyme Type ID | protease010470 |
| Protein Name |
Lipoprotein signal peptidase EC 3.4.23.36 LspPae Prolipoprotein signal peptidase Signal peptidase II SPase II |
| Gene Name | lspA ls PA4559 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MPDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVSASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRMVLGHVVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMFRSKKSGEAAHG |
| Enzyme Length | 169 |
| Uniprot Accession Number | Q9HVM5 |
| Absorption | |
| Active Site | ACT_SITE 124; /evidence="ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896"; ACT_SITE 143; /evidence="ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by globomycin. {ECO:0000269|PubMed:26912896, 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:26912896, 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:26912896, 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); Beta strand (4); Chain (1); Helix (7); Mutagenesis (5); Topological domain (5); Transmembrane (4); Turn (3) |
| Keywords | 3D-structure;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, ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5DIR; 6FMS; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,997 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for inhibitor of cysteine peptidase {ECO:0000269|PubMed:31919415}; Vmax=107 nmol/min/mg enzyme with inhibitor of cysteine peptidase as substrate {ECO:0000269|PubMed:31919415}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |