Q94B60 · CLPP4_ARATH

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 (By similarity).
Essential protein required for chloroplast development and integrity (PubMed:16705403, PubMed:17241447).
Essential for Embryogenesis (PubMed:23548781).

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.

129220406080100120140160180200220240260280
TypeIDPosition(s)Description
Active site158Nucleophile
Active site183

GO annotations

AspectTerm
Cellular Componentchloroplast
Cellular Componentchloroplast envelope
Cellular Componentchloroplast stroma
Cellular Componentchloroplast thylakoid membrane
Cellular Componentchloroplastic endopeptidase Clp complex
Cellular Componentplastid
Cellular Componentplastid stroma
Cellular Componentthylakoid
Molecular FunctionATP-dependent peptidase activity
Molecular Functionserine-type endopeptidase activity
Biological Processchloroplast organization
Biological Processproteolysis
Biological Processregulation of timing of transition from vegetative to reproductive phase

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent Clp protease proteolytic subunit 4, chloroplastic
  • EC number
  • Alternative names
    • Endopeptidase ClpP4
      (nClpP4)
    • nClpP3

Gene names

    • Name
      CLPP4
    • Synonyms
      NCLPP3, NCLPP4
    • ORF names
      MFC19.5
    • Ordered locus names
      At5g45390

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q94B60
  • Secondary accessions
    • Q8LAN0
    • Q9FHJ7
    • Q9SXJ5
    • Q9ZS78

Proteomes

Organism-specific databases

Genome annotation databases

Phenotypes & Variants

Disruption phenotype

Embryo lethal when homozygous.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 21 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, modified residue, chain.

Type
IDPosition(s)Description
Transit peptide1-65Chloroplast
Modified residue66N-acetylserine
ChainPRO_000030897966-292ATP-dependent Clp protease proteolytic subunit 4, chloroplastic

Post-translational modification

Ubiquitinated by CHIP.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Mostly expressed in leaves. Also detected in stems, and to a lower extent, in roots (at protein level).

Induction

Repressed in darkness. Levels decrease in leaves during aging (at protein level). Slightly and transiently repressed by high light stress (at protein level).

Gene expression databases

Interaction

Subunit

Component of the chloroplastic Clp protease core complex which consist of at least 16 proteins: CLPP4 (3 copies), CLPP5 (3 copies), CLPR4 (2 copies), ClpP1 (1 copy), CLPP6 (1 copy), CLPR2 (1 copy), CLPT1 (1 copy), CLPT2 (1 copy) and 3 copies of CLPP3 and/or CLPR1 and/or CLPR3 (PubMed:11278690, PubMed:14593120, PubMed:16766689, PubMed:16980539).
Interacts with CHIP (PubMed:17241447).
The core complex is organized in two heptameric rings, one containing CLPP3,4,5,6 in a 1:2:3:1 ratio and the other CLPP1 and CLPR1,2,3,4 in a 3:1:1:1:1 ratio (PubMed:21712416).

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase S14 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    292
  • Mass (Da)
    31,498
  • Last updated
    2001-12-01 v1
  • Checksum
    227B514CF1C1CE4C
MGTLSLSSSLKPSLVSSRLNSSSSASSSSFPKPNNLYLKPTKLISPPLRTTSPSPLRFANASIEMSQTQESAIRGAESDVMGLLLRERIVFLGSSIDDFVADAIMSQLLLLDAKDPKKDIKLFINSPGGSLSATMAIYDVVQLVRADVSTIALGIAASTASIILGAGTKGKRFAMPNTRIMIHQPLGGASGQAIDVEIQAKEVMHNKNNVTSIIAGCTSRSFEQVLKDIDRDRYMSPIEAVEYGLIDGVIDGDSIIPLEPVPDRVKPRVNYEEISKDPMKFLTPEIPDDEIY

Sequence caution

The sequence BAA82068.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence BAB09167.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAA04393.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict1-3in Ref. 2; CAA04393
Sequence conflict57in Ref. 2; CAA04393
Sequence conflict171in Ref. 2; CAA04393
Sequence conflict193in Ref. 6; AAM65254
Sequence conflict279in Ref. 6; AAM65254

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB022329
EMBL· GenBank· DDBJ
BAA82068.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AJ000930
EMBL· GenBank· DDBJ
CAA04393.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AB018113
EMBL· GenBank· DDBJ
BAB09167.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002688
EMBL· GenBank· DDBJ
AED95243.1
EMBL· GenBank· DDBJ
Genomic DNA
AY042832
EMBL· GenBank· DDBJ
AAK68772.1
EMBL· GenBank· DDBJ
mRNA
BT006321
EMBL· GenBank· DDBJ
AAP13429.1
EMBL· GenBank· DDBJ
mRNA
AY087717
EMBL· GenBank· DDBJ
AAM65254.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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