4CBK

The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

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
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
D	ATP-synt_C	e4cbkD1	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: ATP-synt_C	ECOD (1.6)
J	ATP-synt_C	e4cbkJ1	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: ATP-synt_C	ECOD (1.6)
L	ATP-synt_C	e4cbkL1	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: ATP-synt_C	ECOD (1.6)
A	ATP-synt_C	e4cbkA1	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: ATP-synt_C	ECOD (1.6)
B	ATP-synt_C	e4cbkB1	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: ATP-synt_C	ECOD (1.6)
C	ATP-synt_C	e4cbkC1	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: ATP-synt_C	ECOD (1.6)
E	ATP-synt_C	e4cbkE1	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: ATP-synt_C	ECOD (1.6)
F	ATP-synt_C	e4cbkF1	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: ATP-synt_C	ECOD (1.6)
G	ATP-synt_C	e4cbkG1	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: ATP-synt_C	ECOD (1.6)
H	ATP-synt_C	e4cbkH1	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: ATP-synt_C	ECOD (1.6)
I	ATP-synt_C	e4cbkI1	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: ATP-synt_C	ECOD (1.6)
K	ATP-synt_C	e4cbkK1	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: ATP-synt_C	ECOD (1.6)
M	ATP-synt_C	e4cbkM1	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: ATP-synt_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
D	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
J	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
L	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)
C	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)
F	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
G	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
H	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
I	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
K	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
M	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 A, B, C, D, E, F, G, H, I, J, K, L, M	PF00137	ATP synthase subunit C (ATP-synt_C)	ATP synthase subunit C	This domain is found in the subunit c of ATP synthases and similar sequences from all cellular organisms. It forms two alpha-helices [1-4].	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, G, H, I, J, K, L, M	ATP SYNTHASE SUBUNIT C	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	-	cell periphery cellular anatomical structure plasma membrane membrane respiratory chain complex protein-containing complex catalytic complex proton-transporting ATP synthase complex membrane protein complex cation channel complex transporter complex proton-transporting two-sector ATPase complex, proton-transporting domain proton-transporting two-sector ATPase complex transmembrane transporter complex cell periphery cellular anatomical structure plasma membrane membrane respiratory chain complex protein-containing complex catalytic complex proton-transporting ATP synthase complex membrane protein complex cation channel complex transporter complex proton-transporting two-sector ATPase complex, proton-transporting domain proton-transporting two-sector ATPase complex transmembrane transporter complex proton-transporting ATP synthase complex, coupling factor F(o) monoatomic ion channel complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M	IPR035921	F/V-ATP synthase subunit C superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M	IPR005953	ATP synthase, F0 complex, subunit C, bacterial/chloroplast	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M	IPR038662	F1F0 ATP synthase subunit C superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M	IPR020537	ATP synthase, F0 complex, subunit C, DCCD-binding site	Binding Site
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M	IPR000454	ATP synthase, F0 complex, subunit C	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M	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 A, B, C, D, E, F, G, H, I, J, K, L, M	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, K, L, M	MemProtMD	Annotated as membrane protein by MemProtMD

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M	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 R01GM157729.