A0A1I2T1M7 · A0A1I2T1M7_9FIRM

  • Protein
    ATP-dependent Clp protease ATP-binding subunit ClpX
  • Gene
    clpX
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

Features

Showing features for binding site.

143450100150200250300350400
TypeIDPosition(s)Description
Binding site11Zn2+ (UniProtKB | ChEBI)
Binding site14Zn2+ (UniProtKB | ChEBI)
Binding site34Zn2+ (UniProtKB | ChEBI)
Binding site37Zn2+ (UniProtKB | ChEBI)
Binding site117-124ATP (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 ComponentHslUV protease complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionpeptidase activity
Molecular Functionprotein dimerization activity
Molecular Functionunfolded protein binding
Molecular Functionzinc ion binding
Biological Processcell division
Biological Processproteolysis involved in protein catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent Clp protease ATP-binding subunit ClpX

Gene names

    • Name
      clpX
    • ORF names
      SAMN05216356_11368

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • WCC10
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Oribacterium

Accessions

  • Primary accession
    A0A1I2T1M7

Proteomes

Subcellular Location

Interaction

Subunit

Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-53ClpX-type ZB
Region415-434Disordered

Sequence similarities

Belongs to the ClpX chaperone family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    434
  • Mass (Da)
    47,874
  • Last updated
    2017-11-22 v1
  • Checksum
    176B5F040A286C49
MAMKPEDKIRCSFCGKSAKQVHKLIAGLNNTYICDECVDLCQEILDEENGSEETTTDTSDIRLLKPKEIKEFLDEFVIGQDEAKKVLSVAVYNHYKRITSKIKDIDVQKSNILMIGPTGTGKTYLAQTLAKILGVPFAIADATALTEAGYVGEDVENILLKLIQAADYDIKRAEIGIIYIDEIDKITKKSENVSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQELIQIDTTNILFICGGAFDGLEHIIEKRIASGSIGFGAEIVEKNKENYDDVLKEVQPEDLVKFGLIPEFIGRVPVDVTLQSHDVDTLKQILTTPKNALIKQYQKLFEIDGVNLEFTEDAVTAIAQKAVARKTGARGLRSIMEDMMTDIMYEIPSEPDISVVEITENVVNNSAEPVVTHKDEEALKSSIAHNGSPFFDKDEDQSA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FOPH01000013
EMBL· GenBank· DDBJ
SFG57067.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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