1HT1 | pdb_00001ht1

Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth C]	d1ht1c_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	HslV (ClpQ) protease	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
B [auth D]	d1ht1d_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	HslV (ClpQ) protease	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
C [auth V]	d1ht1v_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	HslV (ClpQ) protease	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
D [auth X]	d1ht1x_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	HslV (ClpQ) protease	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
E [auth A]	d1ht1a_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	HslV (ClpQ) protease	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
F [auth B]	d1ht1b_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	HslV (ClpQ) protease	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
G [auth Z]	d1ht1z_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	HslV (ClpQ) protease	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
H [auth Y]	d1ht1y_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	HslV (ClpQ) protease	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
I [auth E]	d1ht1e1	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Extended AAA-ATPase domain	HslU	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
I [auth E]	d1ht1e2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
J [auth F]	d1ht1f1	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Extended AAA-ATPase domain	HslU	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
J [auth F]	d1ht1f2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
K [auth G]	d1ht1g1	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Extended AAA-ATPase domain	HslU	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
K [auth G]	d1ht1g2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
L [auth I]	d1ht1i1	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Extended AAA-ATPase domain	HslU	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)
L [auth I]	d1ht1i2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli BL21(DE3) ) [TaxId: 469008 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth C]	SCOP2B Superfamily	Class II glutamine amidotransferases	8036886	3000131	SCOP2B (2022-06-29)
B [auth D]	SCOP2B Superfamily	Class II glutamine amidotransferases	8036886	3000131	SCOP2B (2022-06-29)
C [auth V]	SCOP2B Superfamily	Class II glutamine amidotransferases	8036886	3000131	SCOP2B (2022-06-29)
D [auth X]	SCOP2B Superfamily	Class II glutamine amidotransferases	8036886	3000131	SCOP2B (2022-06-29)
E [auth A]	SCOP2B Superfamily	Class II glutamine amidotransferases	8036886	3000131	SCOP2B (2022-06-29)
F [auth B]	SCOP2B Superfamily	Class II glutamine amidotransferases	8036886	3000131	SCOP2B (2022-06-29)
G [auth Z]	SCOP2B Superfamily	Class II glutamine amidotransferases	8036886	3000131	SCOP2B (2022-06-29)
H [auth Y]	SCOP2B Superfamily	Class II glutamine amidotransferases	8036886	3000131	SCOP2B (2022-06-29)
I [auth E]	SCOP2B Superfamily	RecA-like P-loop NTPases	8044319	3002019	SCOP2B (2022-06-29)
J [auth F]	SCOP2B Superfamily	RecA-like P-loop NTPases	8044319	3002019	SCOP2B (2022-06-29)
K [auth G]	SCOP2B Superfamily	RecA-like P-loop NTPases	8044319	3002019	SCOP2B (2022-06-29)
L [auth I]	SCOP2B Superfamily	RecA-like P-loop NTPases	8044319	3002019	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 C]	Proteasome	e1ht1C1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
B [auth D]	Proteasome	e1ht1D1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
C [auth V]	Proteasome	e1ht1V1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
D [auth X]	Proteasome	e1ht1X1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
E [auth A]	Proteasome	e1ht1A1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
F [auth B]	Proteasome	e1ht1B1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
G [auth Z]	Proteasome	e1ht1Z1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
H [auth Y]	Proteasome	e1ht1Y1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
I [auth E]	ClpB_D2-small	e1ht1E2	A: alpha arrays	X: Histone-like	H: Histone-related	T: AAA+ ATPase lid domain	F: ClpB_D2-small	ECOD (1.6)
I [auth E]	Sigma54_activat	e1ht1E1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: Sigma54_activat	ECOD (1.6)
J [auth F]	ClpB_D2-small	e1ht1F2	A: alpha arrays	X: Histone-like	H: Histone-related	T: AAA+ ATPase lid domain	F: ClpB_D2-small	ECOD (1.6)
J [auth F]	Sigma54_activat	e1ht1F1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: Sigma54_activat	ECOD (1.6)
K [auth G]	ClpB_D2-small	e1ht1G2	A: alpha arrays	X: Histone-like	H: Histone-related	T: AAA+ ATPase lid domain	F: ClpB_D2-small	ECOD (1.6)
K [auth G]	Sigma54_activat	e1ht1G1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: Sigma54_activat	ECOD (1.6)
L [auth I]	ClpB_D2-small	e1ht1I2	A: alpha arrays	X: Histone-like	H: Histone-related	T: AAA+ ATPase lid domain	F: ClpB_D2-small	ECOD (1.6)
L [auth I]	Sigma54_activat	e1ht1I1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: Sigma54_activat	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth C]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
B [auth D]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
C [auth V]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
D [auth X]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
E [auth A]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
F [auth B]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
G [auth Z]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
H [auth Y]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
I [auth E]	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
I [auth E]	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
I [auth E]	1.10.8.60	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
J [auth F]	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
J [auth F]	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
J [auth F]	1.10.8.60	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
K [auth G]	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
K [auth G]	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
K [auth G]	1.10.8.60	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
L [auth I]	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
L [auth I]	1.10.8.10	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
L [auth I]	1.10.8.60	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], F [auth B], G [auth Z], H [auth Y]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
I [auth E], J [auth F], K [auth G], L [auth I]	PF00004	ATPase family associated with various cellular activities (AAA) (AAA)	ATPase family associated with various cellular activities (AAA)	AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], F [auth B], G [auth Z], H [auth Y]	HEAT SHOCK LOCUS HSLV	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding anion binding adenyl nucleotide binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding protein binding protein domain specific binding peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity identical protein binding	cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus cellular process response to temperature stimulus protein denaturation catabolic process metabolic process primary metabolic process protein catabolic process cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus cellular process response to temperature stimulus protein denaturation catabolic process metabolic process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process proteolysis involved in protein catabolic process proteolysis	protein-containing complex intracellular anatomical structure catalytic complex peptidase complex cytosolic proteasome complex HslUV protease complex cellular anatomical structure proteasome complex endopeptidase complex cytoplasm cytosol intracellular protein-containing complex proteasome core complex
I [auth E], J [auth F], K [auth G], L [auth I]	HEAT SHOCK LOCUS HSLU	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding anion binding adenyl nucleotide binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding protein binding protein domain specific binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity, acting on acid anhydrides ATP-dependent activity identical protein binding polypeptide conformation or assembly isomerase activity isomerase activity proteasome-activating activity macromolecular conformation isomerase activity	cellular process protein unfolding cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus response to temperature stimulus protein denaturation catabolic process metabolic process primary metabolic process cellular process protein unfolding cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus response to temperature stimulus protein denaturation catabolic process metabolic process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process proteolysis involved in protein catabolic process proteolysis	cellular anatomical structure membrane protein-containing complex intracellular anatomical structure catalytic complex peptidase complex cytosolic proteasome complex HslUV protease complex proteasome complex endopeptidase complex cytoplasm cytosol intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], F [auth B], G [auth Z], H [auth Y]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], F [auth B], G [auth Z], H [auth Y]	IPR023333	Proteasome B-type subunit	Family
A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], F [auth B], G [auth Z], H [auth Y]	IPR001353	Proteasome, subunit alpha/beta	Family
A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], A [auth C], B [auth D], C [auth V], D [auth X], E [auth A], F [auth B], G [auth Z], H [auth Y]	IPR022281	ATP-dependent protease subunit HslV	Family
I [auth E], J [auth F], K [auth G], L [auth I]	IPR050052	ATP-dependent Clp protease ATP-binding subunit ClpX	Family
I [auth E], J [auth F], K [auth G], L [auth I]	IPR003593	AAA+ ATPase domain	Domain
I [auth E], J [auth F], K [auth G], L [auth I]	IPR003959	ATPase, AAA-type, core	Domain
I [auth E], J [auth F], K [auth G], L [auth I]	IPR004491	Heat shock protein HslU	Family
I [auth E], J [auth F], K [auth G], L [auth I]	IPR019489	Clp ATPase, C-terminal	Domain
I [auth E], J [auth F], K [auth G], L [auth I]	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
E [auth A]	HslU---HslV peptidase M-CSA #678	HslVU is an ATP-dependent prokaryotic proteasome. It is a homolog of the eukaryotic 26S proteasome. It is responsible for the degradation of a majority of proteins in the cell, including regulatory protein factors and abnormally folded proteins. HslVU has two protein components, HslV and HslU. HslV is a protease. By itself, HslV has a low catalytic activity. Its activity is enhanced greatly by the interaction with HslU to form HslVU complex. HslU consists of ATPase and chaperone activities. It belongs to the Hsp100/Clp family of molecular chaperones, which is a member of the extended AAA(ATPase associated with a variety of cellular activities) family. It was found that the degradation of polypeptides by HslVU has an ATP requirement. For at least one substrate, SulA protein, ATP hydrolysis is required for degradation. Though ATP hydrolysis does not seem to be mandatory.	Defined by 4 residues: THR:E-1 [auth A-1]LYS:E-33 [auth A-33]GLY:E-45 [auth A-45]SER:E-124 [auth A-124] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.4.25.2 (UniProt) Search M-CSA Motif + EC 3.4.25.2