1TIL

Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA:Poised for phosphorylation complex with ATP, crystal form II

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)
B	d1tilb1	Alpha and beta proteins (a/b)	SpoIIaa-like	SpoIIaa-like	Anti-sigma factor antagonist SpoIIaa	Anti-sigma factor antagonist SpoIIaa	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
B	d1tilb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
D	d1tild1	Alpha and beta proteins (a/b)	SpoIIaa-like	SpoIIaa-like	Anti-sigma factor antagonist SpoIIaa	Anti-sigma factor antagonist SpoIIaa	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
D	d1tild2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
F	d1tilf1	Alpha and beta proteins (a/b)	SpoIIaa-like	SpoIIaa-like	Anti-sigma factor antagonist SpoIIaa	Anti-sigma factor antagonist SpoIIaa	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
F	d1tilf2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
A	d1tila_	Alpha and beta proteins (a+b)	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	Histidine kinase	Anti-sigma factor spoIIab	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
C	d1tilc_	Alpha and beta proteins (a+b)	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	Histidine kinase	Anti-sigma factor spoIIab	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
E	d1tile_	Alpha and beta proteins (a+b)	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	Histidine kinase	Anti-sigma factor spoIIab	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	SpoIIaa-like	8040208	3001065	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SpoIIaa-like	8040208	3001065	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	SpoIIaa-like	8040208	3001065	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GHKL (Gyrase Hsp90 Histidine Kinase MutL) domain-like	8040207	3000091	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	GHKL (Gyrase Hsp90 Histidine Kinase MutL) domain-like	8040207	3000091	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	GHKL (Gyrase Hsp90 Histidine Kinase MutL) domain-like	8040207	3000091	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)
B	STAS	e1tilB1	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: STAS	ECOD (1.6)
D	STAS	e1tilD1	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: STAS	ECOD (1.6)
F	STAS	e1tilF1	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: STAS	ECOD (1.6)
A	HATPase_c_2	e1tilA1	A: a+b two layers	X: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase-like	H: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase (From Topology)	T: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	F: HATPase_c_2	ECOD (1.6)
C	HATPase_c_2	e1tilC1	A: a+b two layers	X: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase-like	H: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase (From Topology)	T: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	F: HATPase_c_2	ECOD (1.6)
E	HATPase_c_2	e1tilE1	A: a+b two layers	X: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase-like	H: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase (From Topology)	T: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	F: HATPase_c_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.750.24	Alpha Beta	2-Layer Sandwich	Transcription Regulator spoIIAA	STAS domain	CATH (4.3.0)
D	3.30.750.24	Alpha Beta	2-Layer Sandwich	Transcription Regulator spoIIAA	STAS domain	CATH (4.3.0)
F	3.30.750.24	Alpha Beta	2-Layer Sandwich	Transcription Regulator spoIIAA	STAS domain	CATH (4.3.0)
A	3.30.565.10	Alpha Beta	2-Layer Sandwich	Heat Shock Protein 90	Histidine kinase-like ATPase, C-terminal domain	CATH (4.3.0)
C	3.30.565.10	Alpha Beta	2-Layer Sandwich	Heat Shock Protein 90	Histidine kinase-like ATPase, C-terminal domain	CATH (4.3.0)
E	3.30.565.10	Alpha Beta	2-Layer Sandwich	Heat Shock Protein 90	Histidine kinase-like ATPase, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, D, F	PF01740	STAS domain (STAS)	STAS domain	The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding ...	The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function [2].	Domain
A, C, E	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (HATPase_c)	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase	This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B, D, F	Anti-sigma F factor antagonist	transcription regulator activity anti-sigma factor antagonist activity protein binding binding antisigma factor binding	sporulation resulting in formation of a cellular spore developmental process anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development sporulation	-
A, C, E	Anti-sigma F factor	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding protein serine/threonine kinase activity catalytic activity, acting on a protein kinase activity protein kinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups protein serine kinase activity sigma factor antagonist activity transcription corepressor activity transcription regulator activity transcription coregulator activity protein-macromolecule adaptor activity molecular adaptor activity	phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process developmental process asexual sporulation reproductive process sporulation developmental process involved in reproduction asexual reproduction sporulation resulting in formation of a cellular spore anatomical structure morphogenesis phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process developmental process asexual sporulation reproductive process sporulation developmental process involved in reproduction asexual reproduction sporulation resulting in formation of a cellular spore anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development regulation of biological process regulation of developmental process negative regulation of sporulation resulting in formation of a cellular spore negative regulation of developmental process biological regulation negative regulation of biological process negative regulation of sporulation regulation of sporulation resulting in formation of a cellular spore regulation of sporulation	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, D, F	IPR036513	STAS domain superfamily	Homologous Superfamily
B, D, F	IPR014237	Anti-sigma F factor antagonist	Family
B, D, F	IPR002645	STAS domain	Domain
B, D, F	IPR003658	Anti-sigma factor antagonist	Family
A, C, E	IPR003594	Histidine kinase/HSP90-like ATPase	Domain
A, C, E	IPR010194	Anti-sigma F factor	Family
A, C, E	IPR036890	Histidine kinase/HSP90-like ATPase superfamily	Homologous Superfamily

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.