Detail Information for IndEnz0002011838
IED ID IndEnz0002011838
Enzyme Type ID protease011838
Protein Name Foldase protein PrsA
EC 5.2.1.8
Gene Name prsA BSU09950
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MKKIAIAAITATSILALSACSSGDKEVIAKTDAGDVTKGELYTNMKKTAGASVLTQLVQEKVLDKKYKVSDKEIDNKLKEYKTQLGDQYTALEKQYGKDYLKEQVKYELLTQKAAKDNIKVTDADIKEYWEGLKGKIRASHILVADKKTAEEVEKKLKKGEKFEDLAKEYSTDSSASKGGDLGWFAKEGQMDETFSKAAFKLKTGEVSDPVKTQYGYHIIKKTEERGKYDDMKKELKSEVLEQKLNDNAAVQEAVQKVMKKADIEVKDKDLKDTFNTSSTSNSTSSSSSNSK
Enzyme Length 292
Uniprot Accession Number P24327
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
DNA Binding
EC Number 5.2.1.8
Enzyme Function FUNCTION: Essential protein that plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Has PPIase activity but it is not essential for its function in vivo. {ECO:0000269|PubMed:12634326}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (4); Chain (1); Compositional bias (1); Domain (1); Helix (13); Lipidation (2); Mutagenesis (13); Region (1); Sequence caution (1); Signal peptide (1); Turn (3)
Keywords 3D-structure;Cell membrane;Isomerase;Lipoprotein;Membrane;Palmitate;Reference proteome;Rotamase;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000305}; Lipid-anchor {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}; Lipid-anchor {ECO:0000305}. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D NMR spectroscopy (1); X-ray crystallography (1)
Cross Reference PDB 1ZK6; 4WO7;
Mapped Pubmed ID 16516208; 16796675; 22512862; 25525259;
Motif
Gene Encoded By
Mass 32,510
Kinetics
Metal Binding
Rhea ID RHEA:16237
Cross Reference Brenda