| IED ID | IndEnz0002016146 |
| Enzyme Type ID | protease016146 |
| Protein Name |
ATP-dependent protease subunit HslV EC 3.4.25.2 Heat shock protein HslV |
| Gene Name | hslV htpO yiiC b3932 JW3903 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVVQPENDLIAIGSGGPYAQAAARALLENTELSAREIAEKALDIAGDICIYTNHFHTIEELSYKA |
| Enzyme Length | 176 |
| Uniprot Accession Number | P0A7B8 |
| Absorption | |
| Active Site | ACT_SITE 2; /evidence="ECO:0000255|HAMAP-Rule:MF_00248, ECO:0000269|PubMed:9257689" |
| Activity Regulation | ACTIVITY REGULATION: Allosterically activated by HslU binding. {ECO:0000305}. |
| 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, ECO:0000269|PubMed:10419524, ECO:0000269|PubMed:10452560, ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:9288941, ECO:0000269|PubMed:9393683}; |
| 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. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins. {ECO:0000255|HAMAP-Rule:MF_00248, ECO:0000269|PubMed:10419524, ECO:0000269|PubMed:10452560, ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:8662828, ECO:0000269|PubMed:9288941, ECO:0000269|PubMed:9393683}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:15696175}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Helix (5); Initiator methionine (1); Metal binding (3); Mutagenesis (9); Turn (4) |
| Keywords | 3D-structure;Allosteric enzyme;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;Sodium;Stress response;Threonine protease |
| Interact With | P0A6H5; Itself |
| Induction | INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_00248, ECO:0000269|PubMed:8244018}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (10) |
| Cross Reference PDB | 1E94; 1G4A; 1G4B; 1HQY; 1HT1; 1HT2; 1NED; 4G4E; 5JI3; 6PXI; |
| Mapped Pubmed ID | 12670962; 15690043; 16606699; 16858726; 19395483; 23707406; 24627523; 27667691; 33472065; |
| Motif | |
| Gene Encoded By | |
| Mass | 19,093 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius) {ECO:0000269|PubMed:15696175}; Note=Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.; |
| Metal Binding | METAL 157; /note=Sodium; via carbonyl oxygen; METAL 160; /note=Sodium; via carbonyl oxygen; METAL 163; /note=Sodium; via carbonyl oxygen |
| Rhea ID | |
| Cross Reference Brenda | 3.4.25.2; |