Detail Information for IndEnz0002002108
IED ID IndEnz0002002108
Enzyme Type ID protease002108
Protein Name Lipoprotein signal peptidase
EC 3.4.23.36
Prolipoprotein signal peptidase
Signal peptidase II
SPase II
Gene Name lspA ABSDF0026
Organism Acinetobacter baumannii (strain SDF)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Moraxellales Moraxellaceae Acinetobacter Acinetobacter calcoaceticus/baumannii complex Acinetobacter baumannii Acinetobacter baumannii (strain SDF)
Enzyme Sequence MPNSQAKKGLFQFYPHNLIWLGLSVLAIVLDQWTKWIASTHMNYADPVPVLPFLNWTLLHNYGAAFSFLSDAGGWQRYFFTSLAGLVSILFVFWLLRMPKKMVVLPVAIALILGGALGNLIDRITLGYVVDFIHVYYQNHHFPAFNIADSAITLGTILLLIDTFFLEKQRPKNSDA
Enzyme Length 176
Uniprot Accession Number B0VMM0
Absorption
Active Site ACT_SITE 131; /evidence=ECO:0000255|HAMAP-Rule:MF_00161; ACT_SITE 149; /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;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 19,929
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda