$VAR1 = undef;
Summary for peptidase S14.001: peptidase Clp (type 1)
| Names | |
|---|---|
| MEROPS Name | peptidase Clp (type 1) |
| Other names | caseinolytic protease, ClpP, endopeptidase Ti, LmCP2 (Listeria monocytogenes), protease Ti |
| Domain architecture |
|---|
| MEROPS Classification | |
|---|---|
| Classification | Clan SK >> Subclan (none) >> Family S14 >> Subfamily (none) >> S14.001 |
| Holotype | peptidase Clp (type 1) (Escherichia coli), Uniprot accession Q1RF98 (peptidase unit: 1-207), MERNUM MER0000474 |
| History | Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London. |
| Activity | |||
|---|---|---|---|
| Catalytic type | Serine | ||
| Peplist | Included in the Peplist with identifier PL00382 | ||
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.92 | ||
| Enzymology | BRENDA database | ||
| Structure | Proteolytically active Clp peptidase is a complex of the catalytic subunit, ClpP, with another subunit, commonly ClpA. ClpA has protein-unfolding and ATPase activities, and makes an essential contribution to proteolysis by the complex, which is termed ClpAP. ClpA can be replaced by other subunits with similar activites such as ClpX (Maurizi, 2004). The activities of ClpAP and ClpXP are not identical. ClpP subunits are arranged in seven-membered rings, and the native protein is formed of two such rings. In the presence of ATP, ClpA and ClpX assemble into six-membered rings that have a high affinity for the rings of ClpP. | ||
| Physiology | Thought to contribute to elimination of damaged proteins in heat shock. | ||
| Other databases | PANTHER | http://www.pantherdb.org/panther/familyList.do?searchType=basic&fieldName=all&listType=6&fieldValue=PTHR10381:SF11 | |
| Cleavage site specificity | Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here. | ||
| Cleavage pattern | A/p/-/ml ay/L/V/P (based on 15 cleavages) | ||
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