2WIE

High-resolution structure of the rotor ring from a proton dependent ATP synthase

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C	PF00137	e2wieC1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: PF00137	ECOD (1.6)
D	PF00137	e2wieD1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: PF00137	ECOD (1.6)
E	PF00137	e2wieE1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: PF00137	ECOD (1.6)
A	PF00137	e2wieA1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: PF00137	ECOD (1.6)
B	PF00137	e2wieB1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: PF00137	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
D	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
E	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
A	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
B	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E	PF00137	ATP synthase subunit C (ATP-synt_C)	ATP synthase subunit C	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E	ATP SYNTHASE C CHAIN	binding lipid binding monoatomic cation transmembrane transporter activity proton transmembrane transporter activity monoatomic ion channel activity proton channel activity proton-transporting ATP synthase activity, rotational mechanism monoatomic cation channel activity passive transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity channel activity monoatomic ion transmembrane transporter activity transporter activity binding lipid binding monoatomic cation transmembrane transporter activity proton transmembrane transporter activity monoatomic ion channel activity proton channel activity proton-transporting ATP synthase activity, rotational mechanism monoatomic cation channel activity passive transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity channel activity monoatomic ion transmembrane transporter activity transporter activity transmembrane transporter activity catalytic activity ligase activity	-	intracellular anatomical structure plasma membrane-derived chromatophore membrane membrane plasma membrane plasma membrane-derived chromatophore cellular anatomical entity thylakoid membrane intracellular organelle cell periphery plasma membrane-derived thylakoid membrane organelle intracellular non-membrane-bounded organelle plasma membrane region bacterial thylakoid intracellular anatomical structure plasma membrane-derived chromatophore membrane membrane plasma membrane plasma membrane-derived chromatophore cellular anatomical entity thylakoid membrane intracellular organelle cell periphery plasma membrane-derived thylakoid membrane organelle intracellular non-membrane-bounded organelle plasma membrane region bacterial thylakoid cytoplasm photosynthetic membrane thylakoid non-membrane-bounded organelle membrane-bounded organelle intracellular membrane-bounded organelle protein-containing complex ATPase complex catalytic complex proton-transporting ATP synthase complex membrane protein complex proton-transporting two-sector ATPase complex, proton-transporting domain proton-transporting two-sector ATPase complex proton-transporting ATP synthase complex, coupling factor F(o)

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E	IPR035921	F/V-ATP synthase subunit C superfamily	Homologous Superfamily
A, B, C, D, E	IPR005953	ATP synthase, F0 complex, subunit C, bacterial/chloroplast	Family
A, B, C, D, E	IPR038662	F1F0 ATP synthase subunit C superfamily	Homologous Superfamily
A, B, C, D, E	IPR020537	ATP synthase, F0 complex, subunit C, DCCD-binding site	Binding Site
A, B, C, D, E	IPR000454	ATP synthase, F0 complex, subunit C	Family
A, B, C, D, E	IPR002379	V-ATPase proteolipid subunit C-like domain	Domain

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B, C, D, E	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B, C, D, E	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	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	F-type ATPase	Rotor (c₁₅) of H⁺-dependent F-ATP Synthase of an alkaliphilic cyanobacterium

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D, E	FME	Parent Component: MET RESID: AA0021 , AA0566 PSI-MOD : N-formyl-L-methionine residue MOD:00030 , N-formyl-L-methionine (Met) MOD:00482 , N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet) MOD:01890 , N-[(L-histidin-1'-yl)methyl]-L-methionine (Met) MOD:01891

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.