A1STI2 · HTPG_PSYIN

Function

function

Molecular chaperone. Has ATPase 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 Componentcytosol
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionunfolded protein binding
Biological ProcessDNA damage response
Biological Processresponse to heat

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chaperone protein HtpG
  • Alternative names
    • Heat shock protein HtpG
    • High temperature protein G

Gene names

    • Name
      htpG
    • Ordered locus names
      Ping_0956

Organism names

Accessions

  • Primary accession
    A1STI2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000149411-634Chaperone protein HtpG

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-345A; substrate-binding
Region346-562B
Region563-634C

Sequence similarities

Belongs to the heat shock protein 90 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    634
  • Mass (Da)
    71,501
  • Last updated
    2007-02-06 v1
  • Checksum
    FF00B7C9F8479F9D
MEHQQNHTFSADTGKLLKLMIHSLYSNKEIFLRELVSNAADAADKLRFKALSDGSLFENDGDLRVRLSFDADLKTITISDNGIGMSRDEVIEHLGTIAKSGTSDFFEQLSGDQVKDSQLIGQFGVGFYSSFIVADKVTVNTRKAGEPASQGTCWISTGESDYTVADIEKAGRGTEITLHLRDDETEFLNDYKLRGIVSKYSDHISIPVEMFKEATEESEGSDGEKVPATEATWEAVNKATALWSCSKSELKDEEYKEFYKHIANDFEDPLTWSHNKVEGEQAYTSLLYIPKRAPYDLWNREKAHGLKLYVQRVFVMDDAEQFMPTYLRFVKGVLDSNDLPLNVSREILQDTRVTAKLRSGCTKRVLDLLTKLAKKDDDAYNLFWKEFGQVLKEGPAEDSSNKEKIGKLFRFSSTETDSTEQTVSLDAYISRMTEGQDKIYYITADSFNAAKNSPHLEVLREKGIEVLLLSDRIDEWLLSHLPEYDGKTFTSVTQGDLDLGKLDSEEKKKEQEKQETEFASFVERVKAVLGDKVKDVRLTHRLTSTPSCIVADNDDMSTQMAKLMAQMGQPVPESKPVFELNPEHVMIVKLADMADEDLFAQWSELLLEQAILSEKGSLDDPSEFVGRINKLLLA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000510
EMBL· GenBank· DDBJ
ABM02797.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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