Detail Information for IndEnz0002006863
IED ID IndEnz0002006863
Enzyme Type ID protease006863
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA SYNW1079
Organism Parasynechococcus marenigrum (strain WH8102)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Prochlorococcaceae Parasynechococcus Parasynechococcus marenigrum Parasynechococcus marenigrum (strain WH8102)
Enzyme Sequence MTGSILRRAPLLGVAGLVVLVDQATKLLAASQLADGRIVQLLPGLINGQLVHNTGAAFSLFRGSVQWLGLLSLAVTTGLLIWVVRHRTPPFWQGMAVAFLLGGTLGNGIDRWRLGHVIDFLALVPINFPIFNPADIAINLAVLCFLVDLWSSRTSSRHG
Enzyme Length 159
Uniprot Accession Number Q7U7A6
Absorption
Active Site ACT_SITE 119; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 135; /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 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 17,083
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda