| IED ID | IndEnz0002016998 |
| Enzyme Type ID | protease016998 |
| Protein Name |
ATP-dependent Clp protease ATP-binding subunit ClpE ATPase ClpE Heat shock protein HSP1 |
| Gene Name | clpE BSU13700 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MRCQHCHQNEATIRLNMQINSVHKQMVLCETCYNELTRKPSMSMGPQSFGFPFEQAFQPKEQSAAKQSEKKGLLDELAQNITNGAKAGLIDPVIGRDDEVARVIEILNRRNKNNPVLIGEPGVGKTAIAEGLALKIAEGDVPNKLKNKELYLLDVASLVANTGIRGQFEERMKQLITELKERKNVILFIDEIHLLVGAGSAEGSMDAGNILKPALARGELQVIGATTLKEYRQIEKDAALERRFQPVMVQEPSIEQAILILQGIKDKYEAYHGVTFSDEAIKACVTLSSRYIQDRHLPDKAIDLLDEAGSKANLLIDELNDEDAAERLTAIEAEKTKALEEENYELAAKLRDEELALEKKLNSSSAHTAVTVEAEHIQEIVEQKTGIPVGKLQADEQTKMKELEAKLHERVIGQEAAVQKVAKAVRRSRAGLKSKNRPVGSFLFVGPTGVGKTELSKTLADELFGTKDAIIRLDMSEYMEKHAVSKIIGSPPGYVGHEEAGQLTEKVRRNPYSIVLLDEIEKAHPDVQHMFLQIMEDGRLTDSQGRTVSFKDTVIIMTSNAGAGEKQTKVGFQSDDSVIEEQTLIDSLSMFFKPEFLNRFDSIIEFRSLEKEHLVKIVSLLLGELEETLAERGISLNVTDEAKEKIAELGYHPSFGARPLRRTIQEWVEDEMTDLLLDNGEITSFHVILEDDKIKVRAK |
| Enzyme Length | 699 |
| Uniprot Accession Number | O31673 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. {ECO:0000269|PubMed:16788169}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 119..126; /note=ATP; /evidence=ECO:0000255; NP_BIND 446..453; /note=ATP; /evidence=ECO:0000255 |
| Features | Chain (1); Domain (1); Mutagenesis (1); Nucleotide binding (2); Zinc finger (1) |
| Keywords | ATP-binding;Chaperone;Metal-binding;Nucleotide-binding;Reference proteome;Stress response;Zinc;Zinc-finger |
| Interact With | |
| Induction | INDUCTION: By heat shock via the relief of repression carried out by the transcriptional regulator CtsR. {ECO:0000269|PubMed:10320580, ECO:0000269|PubMed:14679237}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: ClpE is a very short-lived protein, that is, at least in the soluble cell fraction, degraded mainly by ClpCP. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,906 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |