Detail Information for IndEnz0002003739
IED ID IndEnz0002003739
Enzyme Type ID protease003739
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA MLBr01199
Organism Mycobacterium leprae (strain Br4923)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium leprae Mycobacterium leprae (strain Br4923)
Enzyme Sequence MMGRVPDGPTGLAALVPSVEEAQAMLPPRRLRLLLSIAAVVLTLDIVTKVLAVKFLLPGKSVSIIGDTVTWTLVRNSGAAFSMATGYTWVLTLIATGVVIGIFWMGRRLVSSWWALGLGMILGGAMGNLVDRFFRAPAPLRGHVVDFLSIGWWPVFNVADPSVVVGAILLVVLSIFGFDFDTVGRRKAEFDIAGQRKAEQR
Enzyme Length 201
Uniprot Accession Number B8ZR76
Absorption
Active Site ACT_SITE 146; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 160; /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;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 21,691
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda