A0AA42GU47 · A0AA42GU47_9HYPH

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

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

120920406080100120140160180200
TypeIDPosition(s)Description
Active site106
Active site106Nucleophile
Active site131

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
    • ORF names
      N7376_03485

Organism names

  • Taxonomic identifier
  • Strain
    • GD04153
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella

Accessions

  • Primary accession
    A0AA42GU47

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.

Family & Domains

Sequence similarities

Belongs to the peptidase S14 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    209
  • Mass (Da)
    23,429
  • Last updated
    2024-01-24 v1
  • Checksum
    381CAF9130400737
MRDPIETVMNLVPMVVEQTNRGERAYDIFSRLLKERIIFVNGPVEDGMSMLVCAQLLFLEAENPKKEINMYINSPGGVVTSGMAIYDTMQFIRPPVSTLCMGQAASMGSLLLTAGATGQRYALPNARIMVHQPSGGFQGQASDIERHAQDIIKMKRRLNEIYVKHTGRDYETIERTLDRDHFMTAQEALEFGLIDKVVEARDVSADESK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAODYY010000001
EMBL· GenBank· DDBJ
MDH0123046.1
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.
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