A1AUF5 · HSLO_PELPD

Function

function

Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.

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 Functionprotein folding chaperone
Molecular Functionunfolded protein binding
Biological Processprotein refolding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    33 kDa chaperonin
  • Alternative names
    • Heat shock protein 33 homolog
      (HSP33
      )

Gene names

    • Name
      hslO
    • Ordered locus names
      Ppro_3383

Organism names

Accessions

  • Primary accession
    A1AUF5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_10000155531-30433 kDa chaperonin
Disulfide bond236↔238Redox-active
Disulfide bond269↔272Redox-active

Post-translational modification

Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.

Keywords

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the HSP33 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    304
  • Mass (Da)
    32,453
  • Last updated
    2007-01-23 v1
  • Checksum
    3D38290FB8F8D5BF
MGDHIIRSLSVSGGIRILVCDVALLTREICRLHGASPTVSIALGRGLAGGALMGALLKPGQRLALKFEANGPLRKMIVEADSDGAVRASVANPTAEAEPLEGRWNVAGVLGRAGFLTVSKDLGLGGQPYQGTVQLCSSEIGDDLAYYLADSEQTPSAVGLGAALDEDGLISVCGGFLVQALPGVDEAERDRVTDNIASLPPLSSLLREGGTQKLLELLFDSVAYTRLETRELFFRCGCGREKVERALLSLGGAELWDMGTREGEARVTCEFCRQSYQFDADELKALAETATLTRIHEEHEHLQQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000482
EMBL· GenBank· DDBJ
ABL00976.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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