A0A2I6C010 · A0A2I6C010_MOMCH

Function

function

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.

Catalytic activity

  • Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
    EC:3.4.21.92 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

119620406080100120140160180
TypeIDPosition(s)Description
Active site100
Active site100Nucleophile
Active site126

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchloroplast stroma
Cellular Componentendopeptidase Clp complex
Molecular FunctionATP-dependent peptidase activity
Molecular FunctionATPase binding
Molecular Functionserine-type endopeptidase activity
Biological Processprotein quality control for misfolded or incompletely synthesized proteins

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent Clp protease proteolytic subunit
  • EC number
  • Alternative names
    • Endopeptidase Clp

Gene names

    • Name
      clpP

Encoded on

  • Chloroplast

Organism names

  • Taxonomic identifier
  • Strain
    • OHB3-1
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Cucurbitales > Cucurbitaceae > Momordiceae > Momordica

Accessions

  • Primary accession
    A0A2I6C010

Subcellular Location

Keywords

Interaction

Subunit

Component of the chloroplastic Clp protease core complex.

Family & Domains

Sequence similarities

Belongs to the peptidase S14 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    196
  • Mass (Da)
    22,069
  • Last updated
    2018-03-28 v1
  • Checksum
    7B8B7E65B303EE25
MPIGVPKVPFRNPGEEDASWVDVNRLYRERLLFLGQEVDSQISNQLIGLMVYLSIEDDTKDLYLFINSPGGWVIPGVAIYDTMQFVRTNVQTICMGLAASMGSFILVGGEITKRLAFPHARRVMIHQPASSFYEAQTGEFILEAEELLKLRETITRVYVQRTGKPLWVVSEDMERDVFMSATEAQAHGIVDLVAVE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MG022622
EMBL· GenBank· DDBJ
AUJ21853.1
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