DB code: M00122

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 Catalytic domain
E.C. 3.4.21.92
CSA 1tyf
M-CSA 1tyf
MACiE

CATH domain Related DB codes (homologues)
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 M00145 S00849 D00254

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0A6G7 ATP-dependent Clp protease proteolytic subunit
EC 3.4.21.92
Endopeptidase Clp
Caseinolytic protease
Protease Ti
Heat shock protein F21.5
NP_414971.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488729.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00574 (CLP_protease)
[Graphical View]

KEGG enzyme name
endopeptidase Clp
endopeptidase Ti
caseinolytic protease
protease Ti
ATP-dependent Clp protease
endopeptidase Ti
caseinolytic protease
ClpP
Clp protease

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A6G7 CLPP_ECOLI 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). 14 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. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00012 C00001 C00012 I00087 I00085 I00086
E.C.
Compound Peptide H2O Peptide Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type peptide/protein H2O peptide/protein
ChEBI 15377
 15377
PubChem 22247451
 962
 22247451
 962
1tyfA Unbound Unbound Unbound Unbound Unbound
1tyfB Unbound Unbound Unbound Unbound Unbound
1tyfC Unbound Unbound Unbound Unbound Unbound
1tyfD Unbound Unbound Unbound Unbound Unbound
1tyfE Unbound Unbound Unbound Unbound Unbound
1tyfF Unbound Unbound Unbound Unbound Unbound
1tyfG Unbound Unbound Unbound Unbound Unbound
1tyfH Unbound Unbound Unbound Unbound Unbound
1tyfI Unbound Unbound Unbound Unbound Unbound
1tyfJ Unbound Unbound Unbound Unbound Unbound
1tyfK Unbound Unbound Unbound Unbound Unbound
1tyfL Unbound Unbound Unbound Unbound Unbound
1tyfM Unbound Unbound Unbound Unbound Unbound
1tyfN Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1tyfA SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfB SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfC SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfD SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfE SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfF SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfG SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfH SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfI SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfJ SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfK SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfL SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfM SER 97;HIS 122;ASP 171 GLY 68;MET 98
1tyfN SER 97;HIS 122;ASP 171 GLY 68;MET 98

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.448-452
[3]
p.156-159
[4]
Fig.8

References
[1]
Resource
Comments X-ray crystallography
Medline ID 96428678
PubMed ID 8831780
Journal J Mol Biol
Year 1996
Volume 262
Pages 71-6
Authors Shin DH, Lee CS, Chung CH, Suh SW
Title Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome.
Related PDB
Related UniProtKB P0A6G7
[2]
Resource
Comments X-ray crystallography (2.3 Angstroms)
Medline ID
PubMed ID 9390554
Journal Cell
Year 1997
Volume 91
Pages 447-56
Authors Wang J, Hartling JA, Flanagan JM
Title The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis.
Related PDB 1tyf
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10049803
Journal J Struct Biol
Year 1998
Volume 124
Pages 151-63
Authors Wang J, Hartling JA, Flanagan JM
Title Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10555973
Journal Biochemistry
Year 1999
Volume 38
Pages 14906-15
Authors Singh SK, Guo F, Maurizi MR
Title ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10922052
Journal Proc Natl Acad Sci U S A
Year 2000
Volume 97
Pages 8898-903
Authors Singh SK, Grimaud R, Hoskins JR, Wickner S, Maurizi MR
Title Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11923310
Journal J Biol Chem
Year 2002
Volume 277
Pages 21095-102
Authors Kang SG, Ortega J, Singh SK, Wang N, Huang NN, Steven AC, Maurizi MR
Title Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12203011
Journal J Biol Inorg Chem
Year 2002
Volume 7
Pages 750-6
Authors Amici M, Forti K, Nobili C, Lupidi G, Angeletti M, Fioretti E, Eleuteri AM
Title Effect of neurotoxic metal ions on the proteolytic activities of the 20S proteasome from bovine brain.
Related PDB
Related UniProtKB
[8]
Resource
Comments Crystal structure of ClpA (6-subunits of ATPase domains in a two-tiered hexagonal ring)
Medline ID
PubMed ID 12205096
Journal J Biol Chem
Year 2002
Volume 277
Pages 46743-52
Authors Guo F, Maurizi MR, Esser L, Xia D
Title Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease.
Related PDB
Related UniProtKB
[9]
Resource
Comments Crystal structure of the adaptor protein, ClpS
Medline ID
PubMed ID 12235156
Journal J Biol Chem
Year 2002
Volume 277
Pages 46753-62
Authors Guo F, Esser L, Singh SK, Maurizi MR, Xia D
Title Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA.
Related PDB
Related UniProtKB
[10]
Resource
Comments Crystal structure of ClpS in complex with ClpA
Medline ID
PubMed ID 12426582
Journal Nat Struct Biol
Year 2002
Volume 9
Pages 906-11
Authors Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA
Title Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 12576022
Journal J Struct Biol
Year 2003
Volume 141
Pages 77-83
Authors Lupas AN, Koretke KK
Title Bioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation.
Related PDB
Related UniProtKB

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.

Created Updated
2002-07-04 2011-02-21