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; |