Detail Information for IndEnz0002012714
IED ID IndEnz0002012714
Enzyme Type ID protease012714
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA RPA4376
Organism Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Bradyrhizobiaceae Rhodopseudomonas Rhodopseudomonas palustris Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Enzyme Sequence MTPVRLGVLAGIVALVLDQVTKLWLLYGFELARKGVVQVLPFFDLVLAWNTGISYGWFSGQGPTGQILMLAFKAVAIVALAIWMARSTTKLATIGLGLIIGGAIGNAIDRLAYGAVVDFALLHAEIGGKIYNWYVFNIADVAIVVGVAALLYDSLIGLPAAKAP
Enzyme Length 164
Uniprot Accession Number Q6N1M9
Absorption
Active Site ACT_SITE 118; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 140; /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); Erroneous initiation (1); Transmembrane (5)
Keywords Aspartyl protease;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;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 17,330
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda