clpB ClpB80;chaperone protein ClpB [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: clpB
Official Full Name: ClpB80;chaperone protein ClpB
Primary source: ECOCYC:EG10157
Locus tag: b2592
See related: ASAP:ABE-0008527
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK2590; htpM
Summary: clpB is required for growth below 8C, which is enabled by transgenic Oleispira antarctica Cpn10/60. [More information is available at EcoGene: EG10157]. ClpB belongs to the superfamily of AAA+ ("ATPase associated with a variety of cellular activities") proteins. [More information is available at EcoCyc: EG10157].
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Genomic context

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Sequence:: NC_000913.3 (2731600..2734173, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

ClpB activation reduces ATPase cooperativity and induces a sequential mode of ATP hydrolysis in the AAA2 ring, the main ATPase motor.
Title: Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.
Suggest possible role of E. coli ClpB in the molecular signaling cascade of protein-induced satiety.
Title: Effects of Macronutrients on the In Vitro Production of ClpB, a Bacterial Mimetic Protein of α-MSH and Its Possible Role in Satiety Signaling.
The authors find that large aggregates or bulky, native-like substrates activate the DnaK-ClpB complex, whereas a smaller, permanently unfolded protein or extended, short peptides fail to stimulate it.
Title: Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate.
The authors show here that both Escherichia coli ClpB and Saccharomyces cerevisiae Hsp104 cooperation with their cognate Hsp70 is crucial for efficient protein disaggregation and, in contrast to earlier claims, cannot be circumvented by activating M-domain mutations.
Title: Bacterial and Yeast AAA+ Disaggregases ClpB and Hsp104 Operate through Conserved Mechanism Involving Cooperation with Hsp70.
This unit describes the procedure for following reactivation of an aggregated enzyme glucose-6-phosphate dehydrogenase mediated by ClpB from Escherichia coli in cooperation with another molecular chaperone, DnaK.
Title: Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.
Studied the dynamic assembly equilibrium for E. coli ClpB
Title: Examination of the dynamic assembly equilibrium for E. coli ClpB.
Data show that E coli can propagate the Sup35 prion, which requires disaggregase activity of the heat shock protein ClpB chaperone.
Title: Prion propagation can occur in a prokaryote and requires the ClpB chaperone.
ClpB hexamers remain associated during several ATP hydrolysis events required to translocate substrates through the protein central channel.
Title: ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins.
E. coli DnaK variants with substitutions in subdomains IB and IIB of the nucleotide-binding domain are defective for in vivo and in vitro interactions with ClpB.
Title: Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.
Data indicate that ClpB requires DnaK more stringently than Hsp104 requires Hsp70 for protein disaggregation.
Title: Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP hydrolysis activity	IDA Inferred from Direct Assay more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to heat	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein refolding	IEA Inferred from Electronic Annotation more info
involved_in response to heat	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within response to heat	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	HDA more info	PubMed

General protein information

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Preferred Names: ClpB80;chaperone protein ClpB

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

2731600..2734173 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_417083.1 chaperone protein ClpB [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_417083.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A376M3V4, A0A5B9AFF4

Conserved Domains (1) summary

PRK10865
Location:1 → 857

PRK10865; ATP-dependent chaperone ClpB
YP_010051194.1 ClpB80 [Escherichia coli str. K-12 substr. MG1655]

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A828U5D1

Conserved Domains (1) summary

PRK10865
Location:1 → 709

PRK10865; ATP-dependent chaperone ClpB