3STA

Crystal structure of ClpP in tetradecameric form from Staphylococcus aureus

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth V]	d3stav_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
B [auth A]	d3staa_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
C [auth B]	d3stab_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
D [auth C]	d3stac_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
E	d3stae_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
F	d3staf_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
G	d3stag_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
H [auth I]	d3stai_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
I [auth K]	d3stak_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
J [auth L]	d3stal_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
K [auth M]	d3stam_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
L [auth N]	d3stan_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
M [auth S]	d3stas_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)
N [auth T]	d3stat_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	(Staphylococcus aureus subsp. aureus MW2 ) [TaxId: 196620 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth V]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
B [auth A]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
D [auth C]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
H [auth I]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
I [auth K]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
J [auth L]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
K [auth M]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
L [auth N]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
M [auth S]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)
N [auth T]	SCOP2B Superfamily	ClpP/crotonase	8068481	3000033	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth V]	CLP_protease	e3staV1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
B [auth A]	CLP_protease	e3staA1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
C [auth B]	CLP_protease	e3staB1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
D [auth C]	CLP_protease	e3staC1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
E	CLP_protease	e3staE1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
F	CLP_protease	e3staF1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
G	CLP_protease	e3staG1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
H [auth I]	CLP_protease	e3staI1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
I [auth K]	CLP_protease	e3staK1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
J [auth L]	CLP_protease	e3staL1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
K [auth M]	CLP_protease	e3staM1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
L [auth N]	CLP_protease	e3staN1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
M [auth S]	CLP_protease	e3staS1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)
N [auth T]	CLP_protease	e3staT1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: CLP_protease	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth V]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
B [auth A]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
C [auth B]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
D [auth C]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
E	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
F	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
G	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
H [auth I]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
I [auth K]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
J [auth L]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
K [auth M]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
L [auth N]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
M [auth S]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
N [auth T]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth V], B [auth A], C [auth B], D [auth C], E, A [auth V], B [auth A], C [auth B], D [auth C], E, F, G, H [auth I], I [auth K], J [auth L], K [auth M], L [auth N], M [auth S], N [auth T]	PF00574	Clp protease (CLP_protease)	Clp protease	The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large in ...	The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large insertions, Swiss:P42380 contains one large insertion.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth V], B [auth A], C [auth B], D [auth C], E, A [auth V], B [auth A], C [auth B], D [auth C], E, F, G, H [auth I], I [auth K], J [auth L], K [auth M], L [auth N], M [auth S], N [auth T]	ATP-dependent Clp protease proteolytic subunit	peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity ATP-dependent peptidase activity ATP-dependent activity identical protein binding protein binding binding	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth V], B [auth A], C [auth B], D [auth C], E, A [auth V], B [auth A], C [auth B], D [auth C], E, F, G, H [auth I], I [auth K], J [auth L], K [auth M], L [auth N], M [auth S], N [auth T]	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
A [auth V], B [auth A], C [auth B], D [auth C], E, A [auth V], B [auth A], C [auth B], D [auth C], E, F, G, H [auth I], I [auth K], J [auth L], K [auth M], L [auth N], M [auth S], N [auth T]	IPR001907	ATP-dependent Clp protease proteolytic subunit	Family
A [auth V], B [auth A], C [auth B], D [auth C], E, A [auth V], B [auth A], C [auth B], D [auth C], E, F, G, H [auth I], I [auth K], J [auth L], K [auth M], L [auth N], M [auth S], N [auth T]	IPR018215	ClpP, Ser active site	Active Site
A [auth V], B [auth A], C [auth B], D [auth C], E, A [auth V], B [auth A], C [auth B], D [auth C], E, F, G, H [auth I], I [auth K], J [auth L], K [auth M], L [auth N], M [auth S], N [auth T]	IPR033135	ClpP, histidine active site	Active Site
A [auth V], B [auth A], C [auth B], D [auth C], E, A [auth V], B [auth A], C [auth B], D [auth C], E, F, G, H [auth I], I [auth K], J [auth L], K [auth M], L [auth N], M [auth S], N [auth T]	IPR023562	Clp protease proteolytic subunit /Translocation-enhancing protein TepA	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.