P56760 (ATPH_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit c, chloroplastic

Alternative name(s):
ATP synthase F(0) sector subunit c
ATPase subunit III
F-type ATPase subunit c
Short name=F-ATPase subunit c
Lipid-binding protein

Gene names

Name:	atpH
Ordered Locus Names:	AtCg00140

Encoded on

Plastid; Chloroplast

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	81 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation By similarity. HAMAP MF_01396 Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits By similarity. HAMAP MF_01396
Subunit structure	F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has four main subunits: a1, b1, b'1 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains By similarity.
Subcellular location	Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein By similarity HAMAP MF_01396.
Miscellaneous	In plastids the F-type ATPase is also known as CF1CF0. HAMAP MF_01396 Dicyclohexylcarbodiimide (DCDD) inhibits ATPase. HAMAP MF_01396
Sequence similarities	Belongs to the ATPase C chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Chloroplast Membrane Plastid Thylakoid
Domain	Transmembrane Transmembrane helix
Ligand	Lipid-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 81	81	ATP synthase subunit c, chloroplastic HAMAP MF_01396		PRO_0000112183
Regions
	Transmembrane	7 – 27	21	Helical; Potential
	Transmembrane	57 – 77	21	Helical; Potential
Sites
	Site	61	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56760 [UniParc]. Last modified May 30, 2000. Version 1. Checksum: 2EA40BC2265B3CB9	FASTA	81	7,976
	10 20 30 40 50 60 MNPLVSAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM 70 80 EALTIYGLVV ALALLFANPF V

References

[1]	"Complete structure of the chloroplast genome of Arabidopsis thaliana." Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S. DNA Res. 6:283-290(1999) [PubMed: 10574454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP000423 Genomic DNA. Translation: BAA84372.1.
IPI	IPI00548397.
RefSeq	NP_051046.1. NC_000932.1.
3D structure databases
ProteinModelPortal	P56760.
SMR	P56760. Positions 2-79.
ModBase	Search...
Protein-protein interaction databases
IntAct	P56760. 1 interaction.
STRING	P56760.
Proteomic databases
PRIDE	P56760.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	ATCG00140.1; ATCG00140.1; ATCG00140.
GeneID	844788.
GenomeReviews	Gene locus ATCG00140 in contig AP000423_GR.
KEGG	ath:ArthCp009.
NMPDR	fig|3702.1.peg.8.
Organism-specific databases
TAIR	AtCg00140.
Phylogenomic databases
eggNOG	KOG0232.
GeneTree	EPGT00050000013715.
HOGENOM	HBG753983.
PhylomeDB	P56760.
ProtClustDB	CHL00061.
Gene expression databases
Genevestigator	P56760.
GermOnline	ATCG00140. Arabidopsis thaliana.
Family and domain databases
HAMAP	MF_01396. ATP_synth_c_bact. [Tree]
InterPro	IPR000454. ATPase_F0-cplx_csu. IPR005953. ATPase_F0-cplx_csu_bac/chlpt. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_F0/V0-cplx_csu. [Graphical view]
Gene3D	G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.
KO	K02110.
Pfam	PF00137. ATP-synt_C. 1 hit. [Graphical view]
PRINTS	PR00124. ATPASEC.
SUPFAM	SSF81333. ATPase_F0/V0_c. 1 hit.
TIGRFAMs	TIGR01260. ATP_synt_c. 1 hit.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPH_ARATH

Accession

Primary (citable) accession number: P56760

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program