Detail Information for IndEnz0002001447
IED ID IndEnz0002001447
Enzyme Type ID protease001447
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA SMU_853
Organism Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus mutans Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Enzyme Sequence MRKIVLAVTALLLVALDQLSKFFVVKYIRLGTIVEFIPNLVSLTYLRNTGAAFSILENQQWLFTVITFIVLGVAFYYLIKQMQTQNFWLLASLLLIISGGLGNFIDRLRLGYVVDMIHLDFVDFAIFNVADSYLSVGVALLIIALWKEEKNGN
Enzyme Length 153
Uniprot Accession Number Q8DUQ0
Absorption
Active Site ACT_SITE 115; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 131; /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 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 17,340
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.23.36;