P12208 · CLPP_MARPO

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.

120320406080100120140160180200
TypeIDPosition(s)Description
Active site101Nucleophile
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 thylakoid
Cellular Componentchloroplastic endopeptidase Clp complex
Molecular FunctionATP-dependent peptidase activity
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group 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

Accessions

  • Primary accession
    P12208

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001797441-203ATP-dependent Clp protease proteolytic subunit

Interaction

Subunit

Component of the chloroplastic Clp protease core complex.

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase S14 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    203
  • Mass (Da)
    22,685
  • Last updated
    1989-10-01 v1
  • Checksum
    C0C30114F13CB89B
MPIGVPKVPFRLPGEEDAVWIDVYNRLYRERLLFLGQQVDDEIANQLIGIMMYLNGEDESKDMYLYINSPGGAVLAGISVYDAMQFVVPDVHTICMGLAASMGSFILTGGEITKRIALPHARVMIHQPASSYYDGQAGECIMEAEEVLKLRDCITKVYVQRTGKPLWVISEDMERDVFMSAKEAKLYGIVDLVAIENNSTIKN

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict184in Ref. 3

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X04465
EMBL· GenBank· DDBJ
CAA28109.1
EMBL· GenBank· DDBJ
Genomic DNA
X03661
EMBL· GenBank· DDBJ
CAA27296.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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