Chaperone protein ClpB
Details
- Name
- Chaperone protein ClpB
- Synonyms
- Not Available
- Gene Name
- clpB
- Organism
- Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
- Amino acid sequence
>lcl|BSEQ0017051|Chaperone protein ClpB MNLERWTQAAREALAQAQVLAQRMKHQAIDLPHLWAVLLKDERSLAWRLLEKAGADPKAL KELQERELARLPKVEGAEVGQYLTSRLSGALNRAEALMEELKDRYVAVDTLVLALAEATP GLPGLEALKGALKELRGGRTVQTEHAESTYNALEQYGIDLTRLAAEGKLDPVIGRDEEIR RVIQILLRRTKNNPVLIGEPGVGKTAIVEGLAQRIVKGDVPEGLKGKRIVSLQMGSLLAG AKYRGEFEERLKAVIQEVVQSQGEVILFIDELHTVVGAGKAEGAVDAGNMLKPALARGEL RLIGATTLDEYREIEKDPALERRFQPVYVDEPTVEETISILRGLKEKYEVHHGVRISDSA IIAAATLSHRYITERRLPDKAIDLIDEAAARLRMALESAPEEIDALERKKLQLEIEREAL KKEKDPDSQERLKAIEAEIAKLTEEIAKLRAEWEREREILRKLREAQHRLDEVRREIELA ERQYDLNRAAELRYGELPKLEAEVEALSEKLRGARFVRLEVTEEDIAEIVSRWTGIPVSK LLEGEREKLLRLEEELHKRVVGQDEAIRAVADAIRRARAGLKDPNRPIGSFLFLGPTGVG KTELAKTLAATLFDTEEAMIRIDMTEYMEKHAVSRLIGAPPGYVGYEEGGQLTEAVRRRP YSVILFDEIEKAHPDVFNILLQILDDGRLTDSHGRTVDFRNTVIILTSNLGSPLILEGLQ KGWPYERIRDEVFKVLQQHFRPEFLNRLDEIVVFRPLTKEQIRQIVEIQLSYLRARLAEK RISLELTEAAKDFLAERGYDPVFGARPLRRVIQRELETPLAQKILAGEVKEGDRVQVDVG PAGLVFAVPARVEA
- Number of residues
- 854
- Molecular Weight
- 96252.605
- Theoretical pI
- 5.57
- GO Classification
- FunctionsATP binding / identical protein bindingProcessesprotein processing / response to heatComponentscytoplasm
- General Function
- Identical protein binding
- Specific 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.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0017052|Chaperone protein ClpB (clpB) ATGAACCTGGAACGCTGGACCCAAGCCGCCCGCGAAGCCCTGGCCCAGGCGCAGGTCCTG GCGCAAAGGATGAAGCACCAGGCCATAGACCTGCCCCACCTCTGGGCTGTCCTCCTGAAG GACGAGAGAAGCCTCGCCTGGCGCCTCTTGGAGAAGGCGGGGGCCGACCCCAAGGCCCTT AAAGAGCTCCAGGAGCGGGAGCTTGCCCGCCTGCCCAAGGTGGAAGGGGCCGAGGTGGGC CAGTACCTCACGAGCCGCCTCTCCGGGGCCTTGAACCGGGCCGAGGCCCTGATGGAGGAG CTCAAGGACCGCTACGTGGCGGTGGACACCCTGGTCCTGGCCTTGGCGGAGGCCACGCCG GGGCTTCCGGGCCTGGAGGCCCTGAAGGGGGCGCTCAAGGAACTGAGGGGAGGGAGAACC GTGCAGACGGAACACGCGGAAAGCACCTACAACGCTTTGGAGCAGTACGGCATTGACCTC ACGCGGCTTGCCGCCGAGGGGAAGCTGGACCCCGTGATCGGCCGGGACGAGGAGATCCGG CGGGTGATCCAGATCCTCCTCCGGCGCACCAAGAACAACCCGGTGCTCATCGGCGAGCCC GGCGTGGGGAAGACGGCCATCGTGGAGGGCCTGGCCCAGCGCATCGTCAAGGGGGACGTG CCCGAAGGCCTCAAGGGCAAGCGGATCGTCTCCTTGCAGATGGGCTCCCTCCTCGCCGGG GCCAAGTACCGGGGCGAGTTTGAGGAGCGCTTGAAGGCGGTGATCCAGGAGGTGGTCCAG TCCCAAGGGGAAGTCATCCTCTTCATTGACGAGCTCCACACCGTGGTGGGGGCAGGCAAG GCCGAGGGCGCCGTGGACGCGGGCAACATGCTGAAGCCCGCCCTGGCCCGGGGGGAGCTC AGGCTCATCGGGGCCACCACCCTGGACGAGTACCGGGAGATTGAGAAGGACCCCGCCCTG GAGCGCCGCTTCCAGCCCGTGTACGTGGACGAGCCCACGGTGGAGGAGACCATCTCCATC CTCCGGGGCCTCAAGGAGAAGTACGAGGTCCACCACGGGGTGCGCATCTCCGACAGCGCC ATCATCGCCGCCGCCACCCTCTCCCACCGGTACATCACGGAAAGGCGCCTTCCCGACAAG GCCATTGACCTCATTGACGAGGCGGCGGCCCGCCTGCGCATGGCCCTGGAGAGCGCTCCC GAGGAGATTGACGCCCTGGAGCGCAAGAAGCTCCAGCTGGAGATTGAGCGGGAGGCCCTG AAGAAGGAGAAGGACCCGGACTCCCAGGAGCGCCTCAAGGCCATTGAGGCCGAGATCGCC AAGCTCACGGAGGAGATCGCCAAGCTCCGGGCCGAGTGGGAGAGGGAGCGGGAGATCCTG AGGAAGCTCCGCGAGGCCCAGCACCGCCTGGACGAGGTCAGGCGGGAGATTGAGCTCGCC GAGCGGCAGTACGACCTGAACCGGGCCGCCGAGCTCCGCTACGGGGAGCTTCCCAAGCTG GAGGCCGAGGTGGAGGCCCTTTCGGAAAAGCTCCGGGGCGCCCGCTTCGTCCGCCTCGAG GTCACCGAGGAGGACATCGCCGAGATCGTCTCCCGCTGGACCGGGATCCCTGTGTCCAAG CTCCTGGAAGGGGAGAGGGAGAAGCTTTTGAGGCTTGAGGAGGAGCTCCACAAGCGGGTG GTGGGGCAGGACGAGGCCATAAGGGCCGTGGCCGACGCCATCCGCCGGGCGAGGGCCGGC CTAAAGGACCCGAACCGGCCCATCGGAAGCTTCCTCTTCCTCGGGCCCACGGGGGTGGGG AAGACGGAGCTCGCCAAGACCCTGGCCGCCACCCTCTTTGACACCGAGGAGGCCATGATC CGCATTGACATGACGGAGTACATGGAGAAGCACGCCGTCTCCCGCCTCATCGGGGCCCCG CCCGGCTACGTGGGCTACGAGGAGGGGGGGCAGCTCACCGAGGCGGTGCGGAGGAGGCCC TACTCGGTCATCCTCTTTGACGAGATTGAGAAGGCCCACCCCGACGTCTTCAACATCCTC CTCCAGATCCTGGACGACGGCCGCCTCACCGACAGCCACGGCCGCACCGTGGACTTCCGC AACACCGTCATCATCCTCACCTCCAACCTGGGGAGCCCCTTGATCCTCGAGGGCCTCCAG AAGGGCTGGCCCTACGAGAGGATCCGGGACGAGGTCTTTAAGGTCTTGCAGCAGCACTTC CGCCCCGAGTTCCTGAACCGCCTGGACGAGATCGTGGTCTTCCGGCCCCTCACCAAGGAG CAGATCCGCCAGATCGTGGAGATCCAGCTCTCCTACCTCCGGGCCCGCCTCGCCGAGAAG CGCATCTCCCTGGAGCTCACCGAGGCCGCCAAGGACTTCCTGGCGGAAAGGGGCTACGAC CCCGTCTTCGGGGCAAGGCCCTTGCGGCGGGTCATCCAGCGGGAGCTGGAGACGCCCCTC GCCCAGAAGATCCTGGCCGGCGAGGTCAAGGAGGGGGACCGCGTGCAGGTGGACGTGGGG CCCGCGGGCCTCGTGTTTGCCGTCCCCGCCCGGGTGGAGGCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9RA63 UniProtKB Entry Name CLPB_THET8 GenBank Gene ID AB012390 - General References
- Motohashi K, Watanabe Y, Yohda M, Yoshida M: Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7184-9. [Article]
- Klostermeier D, Seidel R, Reinstein J: The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. J Mol Biol. 1999 Apr 2;287(3):511-25. [Article]
- Watanabe YH, Motohashi K, Taguchi H, Yoshida M: Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form. J Biol Chem. 2000 Apr 28;275(17):12388-92. [Article]
- Schlee S, Groemping Y, Herde P, Seidel R, Reinstein J: The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites. J Mol Biol. 2001 Mar 2;306(4):889-99. [Article]
- Watanabe YH, Motohashi K, Yoshida M: Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J Biol Chem. 2002 Feb 22;277(8):5804-9. Epub 2001 Dec 10. [Article]
- Schlee S, Beinker P, Akhrymuk A, Reinstein J: A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK. J Mol Biol. 2004 Feb 6;336(1):275-85. [Article]
- Lee S, Hisayoshi M, Yoshida M, Tsai FT: Crystallization and preliminary X-ray crystallographic analysis of the Hsp100 chaperone ClpB from Thermus thermophilus. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2334-6. Epub 2003 Nov 27. [Article]
- Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT: The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell. 2003 Oct 17;115(2):229-40. [Article]