HAMAP rule MF_00444
General rule information
[?]
Accession | MF_00444 |
Dates | 1-JUN-2001 (Created)
28-NOV-2023 (Last updated, Version 54) |
Name | ClpP |
Scope(s) |
Bacteria Plastid |
Template(s) | P0A6G7 (CLPP_ECOLI); [ Recover all ] |
Triggered by |
HAMAP; MF_00444 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Identifier | CLPP |
Protein name | RecName: Full=ATP-dependent Clp protease proteolytic subunit; EC=3.4.21.92; AltName: Full=Endopeptidase Clp; |
Gene name | Name=clpP; |
Comments
[?]
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 | Reaction=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; |
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
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. Component of the ClpAP and ClpXP complexes. |
else case <OC:Bacteria> | |
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. |
else case <OC:Viridiplantae> | |
SUBUNIT | Component of the chloroplastic Clp protease core complex. |
end case | |
case <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Plastid, chloroplast stroma. |
end case | |
case not <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Cytoplasm. |
end case | |
SIMILARITY | Belongs to the peptidase S14 family. |
Keywords
[?]
case not <OG:Chloroplast> | |
Cytoplasm | |
end case | |
Hydrolase | |
Protease | |
Serine protease |
Gene Ontology
[?]
GO:0004252; Molecular function:serine-type endopeptidase activity | |
GO:0006508; Biological process:proteolysis | |
case <OG:Chloroplast> | |
GO:0009570; Cellular component:chloroplast stroma | |
end case | |
case not <OG:Chloroplast> | |
GO:0005737; Cellular component:cytoplasm | |
end case |
Cross-references
[?]
Pfam | PF00574; CLP_protease; 1; |
PRINTS | PR00127; CLPPROTEASEP; 1; |
NCBIfam | TIGR00493; ClpP; 1; |
PROSITE | PS00381; CLP_PROTEASE_SER; 1; |
PROSITE | PS00382; CLP_PROTEASE_HIS; 1; |
Features
[?]
From: CLPP_ECOLI (P0A6G7) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 111 | 111 | /note="Nucleophile" | S | ||||||||
ACT_SITE | 136 | 136 | H |
Additional information
[?]
Size range | 180-249 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |
Comments | In Bacillus subtilis and also probably in some other Bacillaceae, ClpXP plays a major role in the third proteolytic step of stress-induced degradation of anti-sigma-W factor RsiW (PubMed=16899079). A number of possible inactive clpP-like protein have not been shown in the alignment (clpP4 from STRCO, clpR from SYNY3, etc.). Inteins deleted in CHLEU (not shown in alignment). Weird insert in CHLRE (not shown in alignment). |