Detail Information for IndEnz0002016093
IED ID IndEnz0002016093
Enzyme Type ID protease016093
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA VP0535
Organism Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio harveyi group Vibrio parahaemolyticus Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Enzyme Sequence MSEKALTLKQSGVRWLWLAIVIFLADIGIKYVVMNNMGYGWANRIEILPFFNLLYVHNYGAAFSFLSDQAGWQRWLFTGIAFVVTGLLTYWMSKLPAKEKWNNIAYAMIIGGAVGNVFDRVIHGFVVDYLDFYWGNYHWPAFNLADMAICLGAAMIILDGFRKKDTAKA
Enzyme Length 169
Uniprot Accession Number Q87S89
Absorption
Active Site ACT_SITE 128; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 146; /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 (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 19,266
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda