| IED ID | IndEnz0002015083 |
| Enzyme Type ID | protease015083 |
| Protein Name |
ATP-dependent protease subunit HslV EC 3.4.25.2 Heat shock protein HslV |
| Gene Name | hslV SF4010 S3737 |
| Organism | Shigella flexneri |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella flexneri |
| Enzyme Sequence | MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVVQPENDLIAIGSGGPYAQAAARALLENTELSAREIAEKALDIAGDICIYTNHFHTIEELSYKA |
| Enzyme Length | 176 |
| Uniprot Accession Number | P0A7C1 |
| Absorption | |
| Active Site | ACT_SITE 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00248 |
| Activity Regulation | ACTIVITY REGULATION: Allosterically activated by HslU binding. {ECO:0000255|HAMAP-Rule:MF_00248}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP-dependent cleavage of peptide bonds with broad specificity.; EC=3.4.25.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00248}; |
| DNA Binding | |
| EC Number | 3.4.25.2 |
| Enzyme Function | FUNCTION: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. {ECO:0000255|HAMAP-Rule:MF_00248}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Initiator methionine (1); Metal binding (3) |
| Keywords | Allosteric enzyme;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome;Sodium;Stress response;Threonine protease |
| Interact With | |
| Induction | INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_00248}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00248}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 19,093 |
| Kinetics | |
| Metal Binding | METAL 157; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248; METAL 160; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248; METAL 163; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00248 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.25.2; |