Q7UM33 · CLPB_RHOBA

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).

Features

Showing features for binding site.

1881100200300400500600700800
TypeIDPosition(s)Description
Binding site207-214ATP 1 (UniProtKB | ChEBI)
Binding site628-635ATP 2 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Biological Processcellular response to heat
Biological Processprotein refolding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chaperone protein ClpB

Gene names

    • Name
      clpB
    • Ordered locus names
      RB9103

Organism names

Accessions

  • Primary accession
    Q7UM33

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001911671-881Chaperone protein ClpB

Interaction

Subunit

Homohexamer. The oligomerization is ATP-dependent (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, coiled coil.

Type
IDPosition(s)Description
Domain5-147Clp R
Region8-73Repeat 1
Region84-147Repeat 2
Region160-341NBD1
Region342-568Linker
Coiled coil392-530
Region528-548Disordered
Region578-789NBD2
Region790-881C-terminal

Domain

The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).

Sequence similarities

Belongs to the ClpA/ClpB family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    881
  • Mass (Da)
    97,443
  • Last updated
    2004-10-11 v2
  • Checksum
    B1B09910EB4E36C7
MAFRIDKLTTQAQNVVAEAQAQATSAGNAEIDPLHVLSAAVNQRDGITTPLLEKINVDVPKLKSLLTSELEKLPHASGMGQARVSAKLQAALEASATSAESLKDEYVSTEHLLVGLARTDNKAKNLLSLLGVSDNDLLTAMSQIRGSARVTDPNAESTYQALEKFGIDLTQLAQSGKLDPVIGRDNEIRRVIQVLSRRTKNNPVLIGQPGVGKTAIAEGLALRIFEGDVPQSLKGKKVVSLDMGALVAGAKFRGDFEERLKSVLREVKDSDGKVILFIDELHLVVGAGNAEGSADAANLLKPELARGALRCIGATTLDEYRQHIEKDAALERRFQPVFVGEPNVEDTVAILRGLKPRYESHHGVRITDSALVAAANLSDRYIADRFLPDKAIDLIDEAASRLAMEKESVPEPIDRLQRRLRQLELVHRQLVDEQEASAVDKRVEVEEEMESAKAELASLKEQWETEKMGLDDVQSVRQEVDQLQHRFAQLDADAKEKQLRGESPEDAYSEMLQVQSRLRELQARIDEAEKHDDSADQTKEEPGDEKRRLLRKEVTEEEIAEVVSTWTGVPVTRMMETERAKLLVMEERLHQRVVGQDEAVTAVSDAVRRSRSGLQDPNRPIGSFLFLGPTGVGKTELCKALAEVMFDDESAMVRIDMSEFMERHSVSRLIGAPPGYVGYEEGGKLTEAVRRRPYAVILLDEMEKAHPDVFNVLLQVLDDGRLTDGQGRTVNFTNTVVVMTSNVGSQVIQRVTEEGGGEDEMRQAVEDALKARFLPEFLNRIDDTVIFHPLQQTQIRRIVQLQLEELRSRLAANGLSFEITDAAIDQIAEVGYDPAYGARPLKRVIQREVQNPLASAILKNSYAEGTTIKIDHDGDQFVFSG

Sequence caution

The sequence CAD76084.1 differs from that shown. Reason: Erroneous initiation

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX294148
EMBL· GenBank· DDBJ
CAD76084.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

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