Detail Information for IndEnz0002004044
IED ID IndEnz0002004044
Enzyme Type ID protease004044
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA OB1485
Organism Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Oceanobacillus Oceanobacillus iheyensis Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Enzyme Sequence MIMYYLIAIALVIIDQLTKWLVVSRMELGESISVIDNFFYITSHRNTGAAWGILEGQMLLFYIITTIVIIGIIYFLHTHAKGDKLLSVALVVILGGAIGNFIDRIFRQEVVDFANFYIFDYNFPIFNVADSSLTIGVILFLIATILEEKRQKGKSKS
Enzyme Length 157
Uniprot Accession Number Q8ER40
Absorption
Active Site ACT_SITE 112; /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 17,774
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda