EC 3.4.21.92 - Endopeptidase Clp

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IntEnz Enzyme Nomenclature
EC 3.4.21.92

Names

Accepted name:
endopeptidase Clp
Other names:
ATP-dependent Clp protease
Clp protease
ClpP
caseinolytic protease
endopeptidase Ti
protease Ti
Systematic name:

Reaction

Comments:

An enzyme from bacteria that contains subunits of two types, ClpP, with peptidase activity, and ClpA, with ATPase activity. The ClpAP complex, which displays ATP-dependent endopeptidase activity, has the composition (ClpP14ClpA6)2 [4]. ClpP is the type example of peptidase family S14.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00358
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008462
CAS Registry Number: 110910-59-3
UniProtKB/Swiss-Prot: (757) [show] [UniProt]

References

  1. Gottesman, S., Clark, W.P. and Maurizi, M.R.
    The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate.
    J. Biol. Chem. 265: 7886-7893 (1990). [PMID: 2186030]
  2. Maurizi, M.R., Clark, W.P., Katayama, Y., Rudikoff, S., Pumphrey, J., Bowers, B. and Gottesman, S.
    Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.
    J. Biol. Chem. 265: 12536-12545 (1990). [PMID: 2197275]
  3. Maurizi, M.R., Thompson, M.W., Singh, S.K. and Kim, S.-H.
    Endopeptidase Clp: the ATP-dependent Clp protease from Escherichia coli.
    Methods Enzymol. 244: 314-331 (1994). [PMID: 7845217]
  4. Kessel, M., Maurizi,M.R., Kim, B., Kocsis, E., Trus, B., Singh, S.K. and Steven, A.C.
    Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome.
    J. Mol. Biol. 250: 587-594 (1995). [PMID: 7623377]

[EC 3.4.21.92 created 1996]