| IED ID | IndEnz0002001606 |
| Enzyme Type ID | protease001606 |
| Protein Name |
SPS-sensor serine protease component SSY5 Endoprotease SSY5 |
| Gene Name | SSY5 APF8 YJL156C J0570 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MVRFFGLNKKKNEEKENTDLPADNEQNAAETSSSNVSGNEERIDPNSHDTNPENANNDDASTTFGSSIQSSSIFSRGRMTYGTGASSSMATSEMRSHSSGHSGSKNSKNLQGFKDVGKPLRAVSFLSPVKEEESQDTQNTLDVSSSTSSTLATSENARENSFTSRRSITLEYIHKSLSELEENLVDIMDDIHQDVISISKAVIEAIEYFKEFLPTTRDRIPYRISLEKSSSLRKINKIVLHFLDNLLVSDAFSNSRSILLRRFYFFLKKLNLITDDDLISESGVLPCLSVFCIGSHCNLPSMDKLGMILDELTKMDSSIISDQEGAFIAPILRGITPKSSILTIMFGLPNLQHEHYEMIKVLYSLFPDVHMYCVKDYIKKAASAVGSIPSHTAATIDTIAPTKFQFSPPYAVSENPLELPISMSLSTETSAKITGTLGGYLFPQTGSDKKFSQFASCSFAITCAHVVLSEKQDYPNVMVPSNVLQTSYKKVLTKESDRYPDGSVEKTAFLEEVQRIDQNLNWQKSNKFGQVVWGERAIVDHRLSDFAIIKVNSSFKCQNTLGNGLKSFPDPTLRFQNLHVKRKIFKMKPGMKVFKIGASTGYTSGELNSTKLVYWADGKLQSSEFVVASPTPLFASAGDSGAWILTKLEDRLGLGLVGMLHSYDGEQRQFGLFTPIGDILERLHAVTKIQWDIDPQLDG |
| Enzyme Length | 699 |
| Uniprot Accession Number | P47002 |
| Absorption | |
| Active Site | ACT_SITE 465; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 545; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 640; /note=Charge relay system; /evidence=ECO:0000255 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Protease component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2. Catalyzes the activation of these transcription factors, which are synthesized as latent cytoplasmic precursors, by proteolytic removal of an N-terminal inhibitory domain containing cytoplasmic retention motifs. SSY5 binds as an inactive protease complex to STP1. In response to extracellular amino acids and dependent on the other SPS-sensor components, the inhibitory propeptide is induced to dissociate, and thereby enables the catalytic domain to process STP1. {ECO:0000269|PubMed:11154269, ECO:0000269|PubMed:11489133, ECO:0000269|PubMed:12502738, ECO:0000269|PubMed:15947203, ECO:0000269|PubMed:16524914, ECO:0000269|PubMed:16778074}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (4); Frameshift (1); Mutagenesis (8); Propeptide (1); Region (3) |
| Keywords | Autocatalytic cleavage;Cell membrane;Direct protein sequencing;Hydrolase;Membrane;Protease;Reference proteome;Zymogen |
| Interact With | |
| Induction | INDUCTION: Down-regulated after extracellular amino-acid addition. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11154269}; Peripheral membrane protein {ECO:0000269|PubMed:11154269}; Cytoplasmic side {ECO:0000269|PubMed:11154269}. |
| Modified Residue | |
| Post Translational Modification | PTM: The propeptide is autoproteolytically cleaved from the catalytic domain but remains associated, forming an inactive protease complex. This processing occurs even in the absence of signaling. {ECO:0000269|PubMed:15509782}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11679080; 12702263; 17603098; 17984223; 19270062; 20421414; 21127045; 21310956; 21653827; 21821114; 22419079; 22928083; 23447701; 23750217; 24483210; 25218923; 25253722; 25825491; 25988166; 26362128; 26703187; 27683589; 31461372; |
| Motif | |
| Gene Encoded By | |
| Mass | 77,527 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |