| IED ID | IndEnz0002008119 |
| Enzyme Type ID | protease008119 |
| Protein Name |
Ribonuclease Y RNase Y EC 3.1.-.- Conserved virulence factor A |
| Gene Name | rny cvfA SAOUHSC_01263 |
| Organism | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Enzyme Sequence | MNLLSLLLILLGIILGVVGGYVVARNLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVDKTAKELLATAVQRLAADHTSESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRREIARTALVNLVSDGRIHPGRIEDMVEKARKEVDDIIREAGEQATFEVNAHNMHPDLVKIVGRLNYRTSYGQNVLKHSIEVAHLASMLAAELGEDETLAKRAGLLHDVGKAIDHEVEGSHVEIGVELAKKYGENETVINAIHSHHGDVEPTSIISILVAAADALSAARPGARKETLENYIRRLERLETLSESYDGVEKAFAIQAGREIRVIVSPEEIDDLKSYRLARDIKNQIEDELQYPGHIKVTVVRETRAVEYAK |
| Enzyme Length | 519 |
| Uniprot Accession Number | Q2FZ08 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.-.- |
| Enzyme Function | FUNCTION: Endoribonuclease that initiates mRNA decay (By similarity). In vitro, catalyzes the hydrolysis of both 2',3'-cyclic AMP and 2',3'-cyclic GMP into 3'-AMP and 3'-GMP, respectively, at the 3'-terminal of RNA. Activates sarZ and agr operon resulting in the expression of virulence genes such as hemolysin, DNase and protease. Contributes to virulence in both silkworm-infection model and mice. {ECO:0000250, ECO:0000269|PubMed:15853881, ECO:0000269|PubMed:17087772, ECO:0000269|PubMed:17951247}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:17951247}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (2); Mutagenesis (7); Transmembrane (1) |
| Keywords | Cell membrane;Endonuclease;Hydrolase;Membrane;Nuclease;RNA-binding;Reference proteome;Transmembrane;Transmembrane helix;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17951247}; Single-pass membrane protein {ECO:0000269|PubMed:17951247}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,512 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 mM for bis-p-nitrophenyl phosphate (bis-pNPP) {ECO:0000269|PubMed:17951247}; KM=17 mM for 2',3'-cAMP {ECO:0000269|PubMed:17951247}; KM=15 mM for 2',3'-cGMP {ECO:0000269|PubMed:17951247}; KM=1.1 uM for 2',3'-cGMP at the 3'-terminal of RNA {ECO:0000269|PubMed:17951247}; Vmax=0.75 umol/min/mg enzyme with bis-p-nitrophenyl phosphate (bis-pNPP) as substrate {ECO:0000269|PubMed:17951247}; Vmax=0.93 umol/min/mg enzyme with 2',3'-cAMP as substrate {ECO:0000269|PubMed:17951247}; Vmax=0.38 umol/min/mg enzyme with 2',3'-cGMP as substrate {ECO:0000269|PubMed:17951247}; Vmax=0.0015 umol/min/mg enzyme with 2',3'-cGMP at the 3'-terminal of RNA as substrate {ECO:0000269|PubMed:17951247}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |