Detail Information for IndEnz0002002242
IED ID IndEnz0002002242
Enzyme Type ID protease002242
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA CF0797
Organism Chlamydia felis (strain Fe/C-56) (Chlamydophila felis)
Taxonomic Lineage cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia felis Chlamydia felis (strain Fe/C-56) (Chlamydophila felis)
Enzyme Sequence MSNRSRSTLLTISFFVLIDWVTKLAVLLYRGNLPNANPILYQYSWGKLFFCICPTFNEGAAFGLFSKYKYFLLLIRIVIILGILAFLFLRKKKTSATTRFSLILLCSGAIGNVGDIFFYNHVIDFISIGYNRWSFPTFNFADIFISLGTLIFVYKLYFPTKQKIK
Enzyme Length 165
Uniprot Accession Number Q253G9
Absorption
Active Site ACT_SITE 124; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 142; /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 inner membrane;Cell membrane;Hydrolase;Membrane;Protease;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 19,070
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda