| IED ID |
IndEnz0002016813 |
| Enzyme Type ID |
protease016813 |
| Protein Name |
Chaperone protein ClpB
|
| Gene Name |
clpB |
| Organism |
Dichelobacter nodosus (Bacteroides nodosus) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Cardiobacteriales
Cardiobacteriaceae
Dichelobacter
Dichelobacter nodosus (Bacteroides nodosus)
|
| Enzyme Sequence |
MEFMQMSKKFTARFQEALSAAQSLAVGKDHAYIEPLHIFSALLDQEGSSIIAIAQRAGGQIGAVRQAVMQALERLPRVKNPTGDVNISPESMRLLNLCDKYAQQNGDEYISSELFLRAVYDAKGDLEQLLRANGLEKAAVVAAIDAVRGGEAVTDEYAEDKRGALKKYTLDVTQRPLDGKIDPVIGRDEEIRRAMQILQRRSKNNPVLIGEPGVGKTAIVEGLAQRIADRAVPESLKGKRLLSLDLAALLAGTKYRGEFEERLKAVLDEITKADGQIILFIDEIHTMVGAGKSEGSLDAGNMLKPALARGDLHCIGATTLDEYRQYMEKDAALERRFQKVIVDEPSVEDTIAILRNLQERYEVHHGINITDPALVAAAQLSHRYISGRKLPDKAIDLMDEAAAQIRMELDSKPEVMDKIDRRLIQLQIERMALEKETDAASKRRLSDLEAEIAAQEKEYADLEEIWLAEKAGNAGAAEIKEQLDKLRVELEAAKRRGDFARASEIQYGLIPAKEKQLLENEQQTEQRPHRLMRNKVTAEEIAEIVSRWTGIPVAKMMEGEKERLLHLETVLNERVVGQKTAVEAVANAIRRNRAGLSDPKRPIGSFLFLGPTGVGKTELCRTLAQFLFDSEENMVRIDMSEFMEKHSVARLIGAPPGYVGYDQGGYLTEAVRRKPYSVVLFDEVEKAHSDVFNTLLQVLDEGRLTDGQGRTVDFRHTVIIMTSNLGSDMIQLLAEKSYEEMKSAVMEIVMAHFRPEFINRIDEAIVFHGLAKTHMYRIAQIQLERLRQRLQTRELLLSVEEDAINQLVELGYDPLFGARPLKRAIQNYIENPLAQALLAGQYLPQSTITIGFDGTNFTFH |
| Enzyme Length |
860 |
| Uniprot Accession Number |
P17422 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
|
| catalytic Activity |
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| DNA Binding |
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| EC Number |
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| 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
|
| nucleotide Binding |
NP_BIND 210..217; /note=ATP 1; /evidence=ECO:0000250; NP_BIND 610..617; /note=ATP 2; /evidence=ECO:0000250 |
| Features |
Chain (1); Coiled coil (1); Domain (1); Nucleotide binding (2); Region (6) |
| Keywords |
ATP-binding;Chaperone;Coiled coil;Cytoplasm;Nucleotide-binding;Repeat;Stress response |
| Interact With |
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| Induction |
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| Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue |
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| Post Translational Modification |
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| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
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| Gene Encoded By |
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| Mass |
96,271 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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