5AHW

Crystal structure of universal stress protein MSMEG_3811 in complex with cAMP

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	d5ahwa_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	Universal stress protein-like	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)
E	d5ahwe_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	Universal stress protein-like	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)
F	d5ahwf_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	Universal stress protein-like	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)
B	d5ahwb_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	Universal stress protein-like	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)
C	d5ahwc_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	Universal stress protein-like	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)
D	d5ahwd_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	Universal stress protein-like	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Universal stress protein-like	8083862	4003850	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Adenine nucleotide alpha hydrolases-like	8083863	3001593	SCOP2 (2022-06-29)
E	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8083863	3001593	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8083863	3001593	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8083863	3001593	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8083863	3001593	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8083863	3001593	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	Usp	e5ahwA1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Usp	ECOD (1.6)
E	Usp	e5ahwE1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Usp	ECOD (1.6)
F	Usp	e5ahwF1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Usp	ECOD (1.6)
B	Usp	e5ahwB1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Usp	ECOD (1.6)
C	Usp	e5ahwC1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Usp	ECOD (1.6)
D	Usp	e5ahwD1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Usp	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
E	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
F	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
B	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
C	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
D	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00582	Universal stress protein family (Usp)	Universal stress protein family	The universal stress protein UspA Swiss:P28242 [1] is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditio ...	The universal stress protein UspA Swiss:P28242 [1] is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA [3] reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP [2], though UspA lacks ATP-binding activity.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	UNIVERSAL STRESS PROTEIN	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR006015	Universal stress protein A family	Family
A, B, C, D, E A, B, C, D, E, F	IPR006016	UspA	Domain
A, B, C, D, E A, B, C, D, E, F	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.