| IED ID | IndEnz0002016814 |
| Enzyme Type ID | protease016814 |
| Protein Name |
Chaperone protein ClpB Heat shock protein F84.1 |
| Gene Name | clpB htpM b2592 JW2573 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRLPQVEGTGGDVQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKIAIEQARRVGDLARMSELQYGKIPELEKQLEAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMMESEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNEDRIVAVQ |
| Enzyme Length | 857 |
| Uniprot Accession Number | P63284 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. {ECO:0000269|PubMed:10982797, ECO:0000269|PubMed:12624113, ECO:0000269|PubMed:14640692}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 206..213; /note=ATP 1; NP_BIND 605..612; /note=ATP 2 |
| Features | Alternative sequence (2); Beta strand (26); Chain (1); Coiled coil (1); Domain (1); Helix (46); Modified residue (3); Mutagenesis (22); Nucleotide binding (2); Region (6); Sequence conflict (2); Turn (10) |
| Keywords | 3D-structure;ATP-binding;Acetylation;Alternative initiation;Chaperone;Coiled coil;Cytoplasm;Direct protein sequencing;Nucleotide-binding;Reference proteome;Repeat;Stress response |
| Interact With | Itself; P0A6Y8; P33014 |
| Induction | INDUCTION: By heat shock and other environmental stresses. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8376377}. |
| Modified Residue | MOD_RES 96; /note=N6-acetyllysine; /evidence=ECO:0000269|PubMed:18723842; MOD_RES 176; /note=N6-acetyllysine; /evidence=ECO:0000269|PubMed:18723842; MOD_RES 640; /note=N6-acetyllysine; /evidence=ECO:0000269|PubMed:18723842 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (13); X-ray crystallography (3) |
| Cross Reference PDB | 1JBK; 1KHY; 4CIU; 4D2Q; 4D2U; 4D2X; 5OFO; 5OG1; 6OAX; 6OAY; 6OG1; 6OG2; 6OG3; 6QS6; 6QS7; 6QS8; |
| Mapped Pubmed ID | 1400361; 15690043; 16606699; 16858726; 19440203; 19698713; 20094032; 24561554; 24843029; 28798962; 31160557; 31216466; |
| Motif | |
| Gene Encoded By | |
| Mass | 95,585 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.6.4.10; |