Detail Information for IndEnz0002016091
IED ID IndEnz0002016091
Enzyme Type ID protease016091
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA lsp MG210
Organism Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Tenericutes Mollicutes Mycoplasmatales Mycoplasmataceae Mycoplasma Mycoplasma genitalium Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Enzyme Sequence MKLRKTKFFSQLKHQVLTANQKPFLFYKLTMIGFVGFIILLQVFILRNALNGEMDNTMVANSGFINIYVIRNKGVGFSLLQNQTGLVYFLQGLLSVIALVFLVFMVKYSYIFWITTLAFGSLGNFFDRLTSANDSVLDYFIFQNGSSVFNFADCCITFGFIGLFFCFLIQMFKEFKHSKNQ
Enzyme Length 181
Uniprot Accession Number Q49401
Absorption
Active Site ACT_SITE 138; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 153; /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 (4)
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 20,841
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda