7VHQ

Structural insights into the membrane microdomain organization by SPFH family proteins

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	FtsH N-domain-like	8053578	3002207	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	FtsH N-domain-like	8053578	3002207	SCOP2B (2022-06-29)
C	SCOP2 Family	FtsH N-domain	8106063	4006040	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	FtsH N-domain-like	8106064	3002207	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	FtsH N-domain-like	8053578	3002207	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	FtsH N-domain-like	8053578	3002207	SCOP2B (2022-06-29)
K [auth e]	SCOP2B Superfamily	FtsH N-domain-like	8053578	3002207	SCOP2B (2022-06-29)
L [auth f]	SCOP2B Superfamily	FtsH N-domain-like	8053578	3002207	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	PF06480	e7vhqA1	A: a+b two layers	X: TTHA1528-like	H: FtsH Periplasmic Domain (From Topology)	T: FtsH Periplasmic Domain	F: PF06480	ECOD (1.6)
B	PF06480	e7vhqB1	A: a+b two layers	X: TTHA1528-like	H: FtsH Periplasmic Domain (From Topology)	T: FtsH Periplasmic Domain	F: PF06480	ECOD (1.6)
C	PF06480	e7vhqC1	A: a+b two layers	X: TTHA1528-like	H: FtsH Periplasmic Domain (From Topology)	T: FtsH Periplasmic Domain	F: PF06480	ECOD (1.6)
D	PF06480	e7vhqD1	A: a+b two layers	X: TTHA1528-like	H: FtsH Periplasmic Domain (From Topology)	T: FtsH Periplasmic Domain	F: PF06480	ECOD (1.6)
K [auth e]	PF06480	e7vhqe1	A: a+b two layers	X: TTHA1528-like	H: FtsH Periplasmic Domain (From Topology)	T: FtsH Periplasmic Domain	F: PF06480	ECOD (1.6)
L [auth f]	PF06480	e7vhqf1	A: a+b two layers	X: TTHA1528-like	H: FtsH Periplasmic Domain (From Topology)	T: FtsH Periplasmic Domain	F: PF06480	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	PF06480	FtsH Extracellular (FtsH_ext)	FtsH Extracellular	-	Family
E, F, J [auth U]	PF01145	SPFH domain / Band 7 family (Band_7)	SPFH domain / Band 7 family	-	Family
G, H, I	PF01145	SPFH domain / Band 7 family (Band_7)	SPFH domain / Band 7 family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	ATP-dependent zinc metalloprotease FtsH	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 peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase 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 cation binding transition metal ion binding zinc ion binding metal ion binding ATP-dependent peptidase activity	organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process metabolic process protein metabolic process macromolecule metabolic process organic substance catabolic process proteolysis	protein-containing complex membrane membrane protein complex cellular anatomical entity cell periphery plasma membrane protein complex plasma membrane
E, F, J [auth U]	Protein HflK	-	response to stimulus response to stress response to heat response to abiotic stimulus response to temperature stimulus	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol protein-containing complex membrane membrane protein complex cell periphery plasma membrane plasma membrane protein complex
G, H, I	Modulator of FtsH protease HflC	-	response to stimulus response to stress response to heat response to abiotic stimulus response to temperature stimulus	protein-containing complex membrane membrane protein complex cellular anatomical entity cell periphery plasma membrane protein complex plasma membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR000642	Peptidase M41	Domain
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR037219	Peptidase M41-like	Homologous Superfamily
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR041569	AAA ATPase, AAA+ lid domain	Domain
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR011546	Peptidase M41, FtsH extracellular	Domain
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR003960	ATPase, AAA-type, conserved site	Conserved Site
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR003593	AAA+ ATPase domain	Domain
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR005936	ATP-dependent zinc metalloprotease, FtsH	Family
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR003959	ATPase, AAA-type, core	Domain
A, B, C, D, K [auth e], A, B, C, D, K [auth e], L [auth f]	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
E, F, J [auth U]	IPR036013	Band 7/SPFH domain superfamily	Homologous Superfamily
E, F, J [auth U]	IPR001972	Stomatin/HflK family	Family
E, F, J [auth U]	IPR020980	Menbrane protein HflK, N-terminal	Domain
E, F, J [auth U]	IPR001107	Band 7 domain	Domain
E, F, J [auth U]	IPR010201	HflK	Family
G, H, I	IPR036013	Band 7/SPFH domain superfamily	Homologous Superfamily
G, H, I	IPR001107	Band 7 domain	Domain
G, H, I	IPR010200	HflC	Family

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J [auth U], K [auth e], L [auth f]	OPM	Transmembrane	Alpha-helical polytopic	AAA-ATPase superfamily, transmembrane	FtsH zinc metalloprotease

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B, C, D, E A, B, C, D, E, F, G, H, I, J [auth U], K [auth e], L [auth f]	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B, C, D, E A, B, C, D, E, F, G, H, I, J [auth U], K [auth e], L [auth f]	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B, C, D, E A, B, C, D, E, F, G, H, I, J [auth U], K [auth e], L [auth f]	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH) Family Proteins	Supramolecular complex comprised of HflK, HflC, & FtsH

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 R01GM133198.