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Search results 101 to 153 out of 153 for Clpb

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0.025s

Type

Details

Score

Publication

- | J:85324

First Author:	Mouse Genome Informatics Group
Year:	2003
Journal:	Database Procedure
Title:	Automatic Encodes (AutoE) Reference

•

Publication

- | J:53168

First Author:	Bairoch A
Year:	1999
Journal:	Database Release
Title:	SWISS-PROT Annotated protein sequence database

•

Publication

- | J:91388

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations

•

Publication

- | J:90438

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and loading genome assembly coordinates from NCBI annotations

•

Publication

15037241 | -

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

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Protein Domain

IPR017730 | Chaperonin_ClpB

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

108707588 | clpb.L

Type:	gene
Organism:	frog, African clawed

•

Publication

10986262 | -

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

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Allele

Clpb<+> | MGI:2434968

Name:	ClpB caseinolytic peptidase B; wild type

•

Publication

28824920 | -

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

Clpb<Gt(OST350716)Lex> | MGI:4290079

Name:	ClpB caseinolytic peptidase B; gene trap OST350716, Lexicon Genetics
Allele Type:	Gene trapped

•

Allele

Clpb<em5Gpt> | MGI:7297134

Name:	ClpB caseinolytic peptidase B; endonuclease-mediated mutation 5, GemPharmatech Co., Ltd
Allele Type:	Endonuclease-mediated
Attribute String:	Null/knockout

•

Allele

Clpb<em1Cya> | MGI:7792771

Name:	ClpB caseinolytic peptidase B; endonuclease-mediated mutation 1, Cyagen Biosciences
Allele Type:	Endonuclease-mediated
Attribute String:	Null/knockout

•

Allele

Clpb<em3Cya> | MGI:7792772

Name:	ClpB caseinolytic peptidase B; endonuclease-mediated mutation 3, Cyagen Biosciences
Allele Type:	Endonuclease-mediated
Attribute String:	Null/knockout

•

Allele

Clpb<em2Cya> | MGI:7792773

Name:	ClpB caseinolytic peptidase B; endonuclease-mediated mutation 2, Cyagen Biosciences
Allele Type:	Endonuclease-mediated
Attribute String:	Conditional ready, No functional change

•

Allele

Clpb<Gt(CC0288)Wtsi> | MGI:3870341

Name:	ClpB caseinolytic peptidase B; gene trap CC0288, Wellcome Trust Sanger Institute
Allele Type:	Gene trapped

•

Allele

Clpb<Gt(G076F01)Wrst> | MGI:4349588

Name:	ClpB caseinolytic peptidase B; gene trap G076F01, German Gene Trap Consortium
Allele Type:	Gene trapped

•

Allele

Clpb<Gt(M079E06)Wrst> | MGI:4349864

Name:	ClpB caseinolytic peptidase B; gene trap M079E06, German Gene Trap Consortium
Allele Type:	Gene trapped

•

Allele

Clpb<tm1a(EUCOMM)Wtsi> | MGI:4432713

Name:	ClpB caseinolytic peptidase B; targeted mutation 1a, Wellcome Trust Sanger Institute
Allele Type:	Targeted
Attribute String:	Conditional ready, Null/knockout, Reporter

•

Allele

Clpb<tm1e(EUCOMM)Wtsi> | MGI:4434026

Name:	ClpB caseinolytic peptidase B; targeted mutation 1e, Wellcome Trust Sanger Institute
Allele Type:	Targeted
Attribute String:	Null/knockout, Reporter

•

Allele

Clpb<em1(IMPC)Bay> | MGI:6257767

Name:	ClpB caseinolytic peptidase B; endonuclease-mediated mutation 1, Baylor College of Medicine
Allele Type:	Endonuclease-mediated
Attribute String:	Null/knockout

•

Strain

MGI:7835431 | C57BL/6JCya-Clpb<em1Cya>/Cya

Attribute String:

coisogenic, endonuclease-mediated mutation, mutant strain

•

Strain

MGI:7837509 | C57BL/6N-Clpb<em3Cya>/Cya

Attribute String:

coisogenic, endonuclease-mediated mutation, mutant strain

•

Strain

MGI:7839209 | C57BL/6JCya-Clpb<em2Cya>/Cya

Attribute String:

coisogenic, endonuclease-mediated mutation, mutant strain

•

DO Term

DOID:0081134 | 3-methylglutaconic aciduria type 7b

•

DO Term

DOID:0110003 | 3-methylglutaconic aciduria with cataracts, neurologic involvement and neutropenia

•

DO Term

DOID:0081133 | 3-methylglutaconic aciduria type 7a

•

Protein Domain

IPR022848 | HSP20_IbpB

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

16307477 | -

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

IPR017729 | ATPase_T6SS_ClpV1

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

25305017 | -

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

12055295 | -

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

IPR023728 | HSP20_IbpA

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

8413229 | -

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

IPR028299 | ClpA/B_CS2

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

IPR001270 | ClpA/B

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.

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Publication

1896074 | -

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

2185473 | -

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

12071954 | -

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

H3BK73

Organism:	Mus musculus/domesticus
Length:	268
Fragment?:	true

•

Publication

27288401 | -

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

31379775 | -

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

Q8BH02

Organism:	Mus musculus/domesticus
Length:	426
Fragment?:	false

•

Protein

Q9ER38

Organism:	Mus musculus/domesticus
Length:	385
Fragment?:	false

•

Protein

Q8R1J9

Organism:	Mus musculus/domesticus
Length:	321
Fragment?:	false

•

Protein

Q3UA06

Organism:	Mus musculus/domesticus
Length:	432
Fragment?:	false

•

Protein

Q60649

Organism:	Mus musculus/domesticus
Length:	677
Fragment?:	false

•

Protein

Q8CCN6

Organism:	Mus musculus/domesticus
Length:	678
Fragment?:	false

•

Protein

Q3U3U6

Organism:	Mus musculus/domesticus
Length:	677
Fragment?:	false

•

Protein

Q3URM1

Organism:	Mus musculus/domesticus
Length:	677
Fragment?:	false

•

Protein

E9PY58

Organism:	Mus musculus/domesticus
Length:	707
Fragment?:	false

•

Protein

Q3UGS9

Organism:	Mus musculus/domesticus
Length:	598
Fragment?:	true

•

Protein

Q3TXD4

Organism:	Mus musculus/domesticus
Length:	677
Fragment?:	false

•

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