A0A481YLC8 · A0A481YLC8_9CHRO

Function

function

An RbcL-specific chaperone. The central cleft of the RbcX homodimer (RbcX2) binds the C-terminus of an RbcL monomer, stabilizing the C-terminus and probably preventing its reassociation with chaperonin GroEL-ES. At the same time the peripheral region of RbcX2 binds a second RbcL monomer, bridging the RbcL homodimers in the correct orientation. The RbcX22-bound RbcL dimers then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of RbcX2.

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 Componentcarboxysome
Cellular Componentcytoplasm
Molecular Functionprotein folding chaperone
Biological Processcarbon fixation
Biological Processphotosynthesis
Biological Processribulose bisphosphate carboxylase complex assembly

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    RuBisCO chaperone RbcX

Gene names

    • Name
      rbcX

Organism names

  • Taxonomic identifier
  • Strain
    • CCAP1430/3
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Chroococcales > Aphanothecaceae > Gloeothece

Accessions

  • Primary accession
    A0A481YLC8

Subcellular Location

Carboxysome
Cytoplasm
Note: Most protein is cytoplasmic, but some is in the carboxysome.

Keywords

Interaction

Subunit

Homodimer. Interacts with the exposed C-terminal peptide of RbcL via its central cleft, contacts a second RbcL monomer via its peripheral polar surface.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region109-135Disordered

Domain

The homodimer has 2 functional domains, a central cleft essential for production of soluble RbcL in which the RbcL peptide binds, and a polar surface which plays a role in correct RbcL subunit arrangement.

Sequence similarities

Belongs to the RbcX family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    135
  • Mass (Da)
    15,360
  • Last updated
    2019-06-05 v1
  • Checksum
    6BDD357271F9973A
MYPKKIAADTAKVLQSYLTYQAVRTIIDQLSETNPTQAIWLTQYSSTHKIQDGEAYLEGLMAENKELVLRIMTVREHLAETVLDFLPEMVKTGISQANMEHRRQLLERLTQSQPANSAPQIETSESELDLDNPLN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MH507583
EMBL· GenBank· DDBJ
QBK82207.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp