P46219 · THSA_SACSH

Function

function

Molecular chaperone; binds unfolded polypeptides in vitro, stimulates protein folding and has ATPase activity (Probable). One of the most abundant proteins in the cell at all temperatures (PubMed:7473746).

Catalytic activity

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
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionunfolded protein binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thermosome subunit alpha
  • EC number
  • Alternative names
    • Chaperonin subunit alpha
    • Ring complex subunit alpha
    • Thermophilic factor 55 alpha (TF55-alpha
      )
    • Thermophilic factor 56
    • Thermosome subunit 1

Gene names

    • Name
      thsA
    • Synonyms
      tf56
    • ORF names
      J5U23_02606

Organism names

Accessions

  • Primary accession
    P46219
  • Secondary accessions
    • A0A8F5GUD2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001284041-560Thermosome subunit alpha

Expression

Induction

Transcription is induced by heat shock (shift from 75 to 86 degrees Celsius). At 80 degrees Celsius and above ThsA and ThsB are the major proteins synthesized (at protein level).

Interaction

Subunit

Forms a heterooligomeric complex of two stacked nine-membered rings; one of alpha and the other of beta subunits (Probable). Sometimes called a 'rosettasome' (PubMed:7473746).

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region535-560Disordered

Sequence similarities

Belongs to the TCP-1 chaperonin family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    560
  • Mass (Da)
    59,733
  • Last updated
    2024-01-24 v2
  • Checksum
    5A147A8F87996AF7
MASPVLLLKEGTSRTTGRDALRNNILAAKTLAEMLRSSLGPKGLDKMLIDSFGDVTITNDGATIVKDMEIQHPAAKLLVEAAKAQDAEVGDGTTSAVVLAGALLEKAESLLDQNIHPTIIIEGYKKAYTKALELLPQLGTRIDIRDLNSSVARDTLRKIAFTTLASKFIAEGAELNKIIDMVIDAIVNVAEPLPNGGYNVSLDLIKIDKKKGGSIEDSVLVKGLVLDKEVVHPGMPRRVTKAKIAVLDAALEVEKPEISAKISITSPEQIKAFLDEESKYLKDMVDKLASIGANVVICQKGIDDIAQHFLAKKGILAVRRVKRSDIEKLEKALGARIISSIKDATPDDLGYAELVEERRVGNDKMVFIEGAKNLKAVNILLRGSNDMALDEAERSINDALHALRNILLEPVILPGGGAIELELAMKLREYARSVGGKEQLAIEAFADALEEIPMILAETAGLEAISALMDLRARHAKGLTNTGVDVIGGKIVDDVYALNIIEPIRVKAQVLKSATEAATAILKIDDLIAAAPLKSEKKGGEGSKEESGGEGGAGTPSLGD

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict454in Ref. 1; AAA87624

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L34691
EMBL· GenBank· DDBJ
AAA87624.1
EMBL· GenBank· DDBJ
Genomic DNA
CP077717
EMBL· GenBank· DDBJ
QXJ29731.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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