Q94B60 · CLPP4_ARATH
- ProteinATP-dependent Clp protease proteolytic subunit 4, chloroplastic
- GeneCLPP4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids292 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (By similarity).
Essential protein required for chloroplast development and integrity (PubMed:16705403, PubMed:17241447).
Essential for Embryogenesis (PubMed:23548781).
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).
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 158 | Nucleophile | |||
Active site | 183 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | chloroplast stroma | |
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | chloroplastic endopeptidase Clp complex | |
Cellular Component | plastid | |
Cellular Component | plastid stroma | |
Cellular Component | thylakoid | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | chloroplast organization | |
Biological Process | proteolysis | |
Biological Process | regulation of timing of transition from vegetative to reproductive phase |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent Clp protease proteolytic subunit 4, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ94B60
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
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.
PTM/Processing
Features
Showing features for transit peptide, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-65 | Chloroplast | |||
Modified residue | 66 | N-acetylserine | |||
Chain | PRO_0000308979 | 66-292 | ATP-dependent Clp protease proteolytic subunit 4, chloroplastic | ||
Post-translational modification
Ubiquitinated by CHIP.
Keywords
- PTM
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).
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
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length292
- Mass (Da)31,498
- Last updated2001-12-01 v1
- Checksum227B514CF1C1CE4C
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 1-3 | in Ref. 2; CAA04393 | |||
Sequence conflict | 57 | in Ref. 2; CAA04393 | |||
Sequence conflict | 171 | in Ref. 2; CAA04393 | |||
Sequence conflict | 193 | in Ref. 6; AAM65254 | |||
Sequence conflict | 279 | in Ref. 6; AAM65254 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |