IED ID | IndEnz0002012718 |
Enzyme Type ID | protease012718 |
Protein Name |
Lipoprotein signal peptidase EC 3.4.23.36 Prolipoprotein signal peptidase Signal peptidase II SPase II |
Gene Name | lspA lsp b0027 JW0025 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MSQSICSTGLRWLWLVVVVLIIDLGSKYLILQNFALGDTVPLFPSLNLHYARNYGAAFSFLADSGGWQRWFFAGIAIGISVILAVMMYRSKATQKLNNIAYALIIGGALGNLFDRLWHGFVVDMIDFYVGDWHFATFNLADTAICVGAALIVLEGFLPSRAKKQ |
Enzyme Length | 164 |
Uniprot Accession Number | P00804 |
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 | ACTIVITY REGULATION: Enzyme activity is inhibited by globomycin, a cyclic peptide antibiotic. {ECO:0000269|PubMed:6368552}. |
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:6368552}; |
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:6368552, ECO:0000269|PubMed:6374664, ECO:0000269|PubMed:6378662}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-45 degrees Celsius. {ECO:0000269|PubMed:6368552}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:6368552}; |
Pathway | PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Topological domain (5); 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, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1894646, ECO:0000269|PubMed:6368552}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:1894646, ECO:0000269|PubMed:6368552}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 2993296; 3112119; 3282924; 6313636; 6347715; 6350278; 6373724; 7050113; 8051048; 8407783; |
Motif | |
Gene Encoded By | |
Mass | 18,156 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |