IED ID | IndEnz0002000064 |
Enzyme Type ID | protease000064 |
Protein Name |
Lipoprotein signal peptidase EC 3.4.23.36 Prolipoprotein signal peptidase Signal peptidase II SPase II |
Gene Name | lspA Sbal_1055 |
Organism | Shewanella baltica (strain OS155 / ATCC BAA-1091) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Alteromonadales Shewanellaceae Shewanella Shewanella baltica Shewanella baltica (strain OS155 / ATCC BAA-1091) |
Enzyme Sequence | MPLTWKDSGLRWYWVAVLVFFADQLSKQWVLANFDLHESLNLLPFFNFTYVRNYGAAFSFLSDAGGWQRWLFTIVAVGFSTLLTVWLRRQSASLLKLNLAYTLVIGGALGNLVDRLMHGFVVDFIDFFWAKSHYPAFNIADSAICIGAVLIIWDAFLSGKSETDSAEGVKK |
Enzyme Length | 171 |
Uniprot Accession Number | A3D1G6 |
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;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 | 19,358 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |