Detail Information for IndEnz0002012718
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