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Search results 101 to 146 out of 146 for Clpb

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0.02s
Type Details Score
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication
First Author: Lee S
Year: 2004
Journal: J Struct Biol
Title: The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine.
Volume: 146
Issue: 1-2
Pages: 99-105
Protein Domain
Type: Family
Description: Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family of ATPases associated with various cellular activities (). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins [, ].
Gene
Type: gene
Organism: frog, African clawed
Publication
First Author: Badger JL
Year: 2000
Journal: J Bacteriol
Title: Yersinia enterocolitica ClpB affects levels of invasin and motility.
Volume: 182
Issue: 19
Pages: 5563-71
Allele    
Name: ClpB caseinolytic peptidase B; wild type
Publication  
First Author: Duran EC
Year: 2017
Journal: Front Mol Biosci
Title: Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.
Volume: 4
Pages: 54
Allele  
Name: ClpB caseinolytic peptidase B; gene trap OST350716, Lexicon Genetics
Allele Type: Gene trapped
Allele
Name: ClpB caseinolytic peptidase B; endonuclease-mediated mutation 5, GemPharmatech Co., Ltd
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Allele  
Name: ClpB caseinolytic peptidase B; gene trap G076F01, German Gene Trap Consortium
Allele Type: Gene trapped
Allele
Name: ClpB caseinolytic peptidase B; targeted mutation 1e, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
Allele  
Name: ClpB caseinolytic peptidase B; gene trap M079E06, German Gene Trap Consortium
Allele Type: Gene trapped
Allele  
Name: ClpB caseinolytic peptidase B; gene trap CC0288, Wellcome Trust Sanger Institute
Allele Type: Gene trapped
Allele
Name: ClpB caseinolytic peptidase B; targeted mutation 1a, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Conditional ready, Null/knockout, Reporter
Allele
Name: ClpB caseinolytic peptidase B; endonuclease-mediated mutation 1, Baylor College of Medicine
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
DO Term
DO Term
DO Term
Protein Domain
Type: Family
Description: This entry represents IbpB, which belongs to the small heat shock protein (HSP20) family. IbpB associates with aggregated proteins, together with IbpA, to stabilise and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.
Publication
First Author: Schlieker C
Year: 2005
Journal: Biol Chem
Title: ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria.
Volume: 386
Issue: 11
Pages: 1115-27
Protein Domain
Type: Family
Description: The type VI secretion system (T6SS) is a supra-molecular bacterial complex that resembles phage tails. It is a toxin delivery systems which fires toxins into target cells upon contraction of its TssBC sheath []. Thirteen essential core proteins are conserved in all T6SSs: the membrane associated complex TssJ-TssL-TssM, the baseplate proteins TssE, TssF, TssG, and TssK, the bacteriophage-related puncturing complex composed of the tube (Hcp), the tip/puncturing device VgrG, and the contractile sheath structure (TssB and TssC). Finally, the starfish-shaped dodecameric protein, TssA, limits contractile sheath polymerization at its distal part when TagA captures TssA []. ClpV is an AAA(+) ATPase that disassembles the type VI secretion system contracted sheath, which resets the systems for reassembly of an extended sheath that is ready to fire again []. The ClpV proteins are most similar to ClpB proteins within the Hsp100/Clp family, but cluster in a separate phylogenetic tree with a remarkable distance to ClpB []. However, this entry also includes ClpB from Yersinia enterocolitica [].
Publication
First Author: Förster A
Year: 2014
Journal: J Biol Chem
Title: Coevolution of the ATPase ClpV, the sheath proteins TssB and TssC, and the accessory protein TagJ/HsiE1 distinguishes type VI secretion classes.
Volume: 289
Issue: 47
Pages: 33032-43
Publication
First Author: Kuczyńska-Wiśnik D
Year: 2002
Journal: Microbiology
Title: The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock.
Volume: 148
Issue: Pt 6
Pages: 1757-65
Protein Domain
Type: Family
Description: Small heat shock proteins IbpA associate with aggregated proteins, together with IbpB, to stabilise and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent[], [].These proteins form homomultimers of about 100-150 subunits at optimal growth temperatures. The conformation changes to monomers at high temperatures or high ionic concentrations. Proteins in this entry belong to the small heat shock protein (HSP20) family.
Publication
First Author: Leonhardt SA
Year: 1993
Journal: Mol Cell Biol
Title: HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.
Volume: 13
Issue: 10
Pages: 6304-13
Protein Domain
Type: Conserved_site
Description: The ClpA/B family of ATP-binding proteins includes the regulatory subunit of the ATP-dependent protease Clp, ClpA; heat shock proteins ClpB, 104 and 78; and chloroplast proteins CD4a (ClpC) and CD4b [, ]. The proteins are thought to protect cells from stress by controlling the aggregation and denaturation of vital cellular structures. They vary in size, but share two conserved regions of about 200 amino acids that each contains an ATP-binding site [].This entry represents a conserved site found in the second conserved region.Proteins containing this site are listed below:Escherichia coli clpA, which acts as the regulatory subunit of the ATP- dependent protease clp.Rhodopseudomonas blastica clpA homolog.Escherichia coli heat shock protein clpB and homologues in other bacteria.Bacillus subtilis protein mecB.Yeast heat shock protein 104 (gene HSP104), which is vital for tolerance to heat, ethanol and other stresses.Neurospora heat shock protein hsp98.Yeast mitochondrial heat shock protein 78 (gene HSP78) [].CD4A and CD4b, two highly related tomato proteins that seem to be located in the chloroplast.Trypanosoma brucei protein clp.Porphyra purpurea chloroplast encoded clpC.
Protein Domain
Type: Family
Description: This family belongs to the AAA+ (ATPase associated with diverse cellular activities) superfamily. Most of these proteins of this family (ClpA, ClpC, ClpD, ClpE, ClpX, HslU) are involved in proteolysis and associate with a separate proteolytic subunit (ClpP, HslV) to form the active protease. ClpB is not involved in proteolysis but rather acts in collaboration with the DnaK (Hsp70) chaperone system to disassemble and refold large protein aggregates.A group of ATP-binding proteins that includes the regulatory subunit of the ATP-dependent protease clpA; heat shock proteins clpB, 104 and 78; and chloroplast proteins CD4a (ClpC) and CD4b belong to this family [, ]. The proteins are thought to protect cells from stress by controlling the aggregation and denaturation of vital cellular structures. They vary in size, but share a domainwhich contains an ATP-binding site.These signatures which span the ATP binding region also identify the bacterial DNA polymerase III subunit tau (), ATP-dependent protease La () and the mitochondrial lon protease homologue (), both of which belong to MEROPS peptidase family S16.
Publication
First Author: Parsell DA
Year: 1991
Journal: Nature
Title: Hsp104 is a highly conserved protein with two essential nucleotide-binding sites.
Volume: 353
Issue: 6341
Pages: 270-3
Publication
First Author: Gottesman S
Year: 1990
Journal: Proc Natl Acad Sci U S A
Title: Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes.
Volume: 87
Issue: 9
Pages: 3513-7
Publication
First Author: Kitagawa M
Year: 2002
Journal: Eur J Biochem
Title: Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants.
Volume: 269
Issue: 12
Pages: 2907-17
Protein
Organism: Mus musculus/domesticus
Length: 268  
Fragment?: true
Publication
First Author: Planamente S
Year: 2016
Journal: EMBO J
Title: TssA forms a gp6-like ring attached to the type VI secretion sheath.
Volume: 35
Issue: 15
Pages: 1613-27
Publication  
First Author: Liebl D
Year: 2019
Journal: Front Microbiol
Title: Baseplate Component TssK and Spatio-Temporal Assembly of T6SS in Pseudomonas aeruginosa.
Volume: 10
Pages: 1615
Protein
Organism: Mus musculus/domesticus
Length: 426  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 321  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 677  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 678  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 677  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 677  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 707  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 598  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 677  
Fragment?: false