IED ID | IndEnz0002011251 |
Enzyme Type ID | protease011251 |
Protein Name |
Zinc metalloproteinase EC 3.4.24.- Hemolysin |
Gene Name | hly |
Organism | Renibacterium salmoninarum |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Micrococcaceae Renibacterium Renibacterium salmoninarum |
Enzyme Sequence | MKKYYAVTGIALAVGMLCTTQLAGATQAADPSVGSLDSSNVVTEFSAQGNVEQITFKSAIKSAPMSSARSAQTSAIIPGLKNLFVSAPGSDFSLNDSSNNYIKRFTQNIAGIPVLGSSITEVLDGQGAVTSAIGAVTSATKGAFPADLAAGQAAALASATKIASAGKDASAISLVDQKAIWFDAVLIGKGATGSVAVPAYQFSFTTGFAESRVLTVAANDGAILNDRTDRKDINRVVCDANSKVIDLEASNADALLKCGKTQANKPTRIEGQAASSVADVNSVYNFLNDTASFYGANTKANDLTALIGNDEGDGLGKAMRAVVRICVTDSQNGEQCPFANAFWYNGQMTYGQGVTTDDITGHELTHGVTEKTNGLVYANESGAINESMSDVFGEFIDLSNGSSDDTAANRWAIGEGSSLGVIRSMKDPGKYGEPAIYKGSNWKPTATNPNDNNDQGGVHSNSGVGNKLAFLITDGQTFNGQTVTGIGIAKAAQLYWAAQRQLTANATYSSLGKALNSACSANVSNNVAGTTAANCTQVANAIKAVGIK |
Enzyme Length | 548 |
Uniprot Accession Number | P55111 |
Absorption | |
Active Site | ACT_SITE 363; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 459; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Zinc metalloprotease with hemolytic properties. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Hemolytic activity is observed from 6 to 37 degrees Celsius for mammalian erythrocytes.; |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Compositional bias (1); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1) |
Keywords | Calcium;Cell wall;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | INDUCTION: Expression of the hemolysin is modulated by the availability of iron. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall. Note=Not secreted, but probably remains attached or associated with the cell wall. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 56,379 |
Kinetics | |
Metal Binding | METAL 362; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 366; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 386; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |