EzCatDB: M00122

DB codeM00122
RLCP classification1.13.30000.10
CATH domainDomain 13.90.226.10Catalytic domain
Domain 23.90.226.10Catalytic domain
Domain 33.90.226.10Catalytic domain
Domain 43.90.226.10Catalytic domain
Domain 53.90.226.10Catalytic domain
Domain 63.90.226.10Catalytic domain
Domain 73.90.226.10Catalytic domain
Domain 83.90.226.10Catalytic domain
Domain 93.90.226.10Catalytic domain
Domain 103.90.226.10Catalytic domain
Domain 113.90.226.10Catalytic domain
Domain 123.90.226.10Catalytic domain
Domain 133.90.226.10Catalytic domain
Domain 143.90.226.10Catalytic domain
E.C.3.4.21.92
CSA1tyf

CATH domainRelated DB codes (homologues)
3.90.226.10M00145,S00849,D00254

Enzyme Name
Swiss-protKEGG

P0A6G7
Protein nameATP-dependent Clp protease proteolytic subunitendopeptidase Clp
endopeptidase Ti
caseinolytic protease
protease Ti
ATP-dependent Clp protease
endopeptidase Ti
caseinolytic protease
ClpP
Clp protease
SynonymsEC 3.4.21.92
Endopeptidase Clp
Caseinolytic protease
Protease Ti
Heat shock protein F21.5


Swiss-prot:Accession NumberP0A6G7
Entry nameCLPP_ECOLI
ActivityHydrolysis 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).
Subunit14 clpP subunits assemble into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. In the presence of ATP, clpA or clpX subunits interact with the clpP structure to form a 750 kDa complex that exhibits ATP-dependent proteolytic activity.
Subcellular locationCytoplasm.
Cofactor


SubstratesProductsintermediates
KEGG-idC00012C00001C00012I00087I00085I00086
CompoundPeptideH2OPeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinH2Opeptide/protein


1tyfAUnbound
UnboundUnboundUnboundUnbound
1tyfBUnbound
UnboundUnboundUnboundUnbound
1tyfCUnbound
UnboundUnboundUnboundUnbound
1tyfDUnbound
UnboundUnboundUnboundUnbound
1tyfEUnbound
UnboundUnboundUnboundUnbound
1tyfFUnbound
UnboundUnboundUnboundUnbound
1tyfGUnbound
UnboundUnboundUnboundUnbound
1tyfHUnbound
UnboundUnboundUnboundUnbound
1tyfIUnbound
UnboundUnboundUnboundUnbound
1tyfJUnbound
UnboundUnboundUnboundUnbound
1tyfKUnbound
UnboundUnboundUnboundUnbound
1tyfLUnbound
UnboundUnboundUnboundUnbound
1tyfMUnbound
UnboundUnboundUnboundUnbound
1tyfNUnbound
UnboundUnboundUnboundUnbound

Active-site residues
resource
literature [2]
pdbCatalytic residuesMain-chain involved in catalysis
1tyfASER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfBSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfCSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfDSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfESER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfFSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfGSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfHSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfISER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfJSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfKSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfLSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfMSER 97;HIS 122;ASP 171
GLY 68;MET 98
1tyfNSER 97;HIS 122;ASP 171
GLY 68;MET 98

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.448-452
[3]p.156-159
[4]Fig.8

references
[1]
CommentsX-ray crystallography
Medline ID96428678
PubMed ID8831780
JournalJ Mol Biol
Year1996
Volume262
Pages71-6
AuthorsShin DH, Lee CS, Chung CH, Suh SW
TitleMolecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome.
Related Swiss-protP0A6G7
[2]
CommentsX-ray crystallography (2.3 Angstroms)
PubMed ID9390554
JournalCell
Year1997
Volume91
Pages447-56
AuthorsWang J, Hartling JA, Flanagan JM
TitleThe structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis.
Related PDB1tyf
[3]
PubMed ID10049803
JournalJ Struct Biol
Year1998
Volume124
Pages151-63
AuthorsWang J, Hartling JA, Flanagan JM
TitleCrystal structure determination of Escherichia coli ClpP starting from an EM-derived mask.
[4]
PubMed ID10555973
JournalBiochemistry
Year1999
Volume38
Pages14906-15
AuthorsSingh SK, Guo F, Maurizi MR
TitleClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease.
[5]
PubMed ID10922052
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages8898-903
AuthorsSingh SK, Grimaud R, Hoskins JR, Wickner S, Maurizi MR
TitleUnfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.
[6]
PubMed ID11923310
JournalJ Biol Chem
Year2002
Volume277
Pages21095-102
AuthorsKang SG, Ortega J, Singh SK, Wang N, Huang NN, Steven AC, Maurizi MR
TitleFunctional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP.
[7]
PubMed ID12203011
JournalJ Biol Inorg Chem
Year2002
Volume7
Pages750-6
AuthorsAmici M, Forti K, Nobili C, Lupidi G, Angeletti M, Fioretti E, Eleuteri AM
TitleEffect of neurotoxic metal ions on the proteolytic activities of the 20S proteasome from bovine brain.
[8]
CommentsCrystal structure of ClpA (6-subunits of ATPase domains in a two-tiered hexagonal ring)
PubMed ID12205096
JournalJ Biol Chem
Year2002
Volume277
Pages46743-52
AuthorsGuo F, Maurizi MR, Esser L, Xia D
TitleCrystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease.
[9]
CommentsCrystal structure of the adaptor protein, ClpS
PubMed ID12235156
JournalJ Biol Chem
Year2002
Volume277
Pages46753-62
AuthorsGuo F, Esser L, Singh SK, Maurizi MR, Xia D
TitleCrystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA.
[10]
CommentsCrystal structure of ClpS in complex with ClpA
PubMed ID12426582
JournalNat Struct Biol
Year2002
Volume9
Pages906-11
AuthorsZeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA
TitleStructural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA.
[11]
PubMed ID12576022
JournalJ Struct Biol
Year2003
Volume141
Pages77-83
AuthorsLupas AN, Koretke KK
TitleBioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation.

comments
This enzyme belongs to peptidase family S14.
This enzyme, ClpP, is a catalytic component of ClpAP protease. The ClpAP protease is a complex of two oligomeric proteins, ClpA and ClpP. Whilst ClpA is composed of six identical subunits arranged in a two-layered hexagonal ring, which consists of ATPase domains, ClpP is composed of two seven-membered rings, the junction of which forms a chamber that contains the catalytic active sites [3], [4].
According to the literature [2], its 14 catalytic triads (Ser97, His122, and Asp171) are located within the central chamber.

createdupdated
2002-07-042011-02-21
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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