IED ID | IndEnz0001000372 |
Enzyme Type ID | amylase000372 |
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 |