Detail Information for IndEnz0002016226
IED ID IndEnz0002016226
Enzyme Type ID protease016226
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA stu0521
Organism Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus thermophilus Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Enzyme Sequence MRKVAIPVAILALIGLDQWVKHWVVANISLNQVIKAIPGVFSLTYLQNRGAAFSILQNQKYFFVILTVLVIGAALFYLVKNYQKSLWLVLSLILIISGGIGNFIDRVHLGYVVDMVQLDFIDFAIFNVADSYLTVGVLLLILILWKEENGSHH
Enzyme Length 153
Uniprot Accession Number Q5M5G2
Absorption
Active Site ACT_SITE 114; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 130; /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 (3)
Keywords Aspartyl protease;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell 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 17,185
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda