Q37304 (ATPH_CHLRE) 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

Encoded on

Plastid; Chloroplast

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii)

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	82 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 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
PTM	Formylation
Technical term	Complete proteome Direct protein sequencing 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 – 82	82	ATP synthase subunit c, chloroplastic HAMAP MF_01396		PRO_0000112184
Regions
	Transmembrane	3 – 23	21	Helical; Potential
	Transmembrane	57 – 77	21	Helical; Potential
Sites
	Site	61	1	Reversibly protonated during proton transport By similarity
Amino acid modifications
	Modified residue	1	1	N-formylmethionine HAMAP MF_01396
Natural variations
	Natural variant	8	1	T → A in strain: CC-503.

Sequences

	Sequence		Length	Mass (Da)
	Q37304 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BFDC3BAF43E96A45	FASTA	82	8,093
	10 20 30 40 50 60 MNPIVAATSV VSAGLAVGLA AIGPGMGQGT AAGYAVEGIA RQPEAEGKIR GALLLSFAFM 70 80 ESLTIYGLVV ALALLFANPF AG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Disruption of the plastid ycf10 open reading frame affects uptake of inorganic carbon in the chloroplast of Chlamydomonas." Rolland N., Dorne A.-J., Amoroso G., Sueltemeyer D.F., Joyard J., Rochaix J.-D. EMBO J. 16:6713-6726(1997) [PubMed: 9362486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cw15.
[2]	"Nucleotide diversity in the chloroplast genome of Chlamydomonas reinhardtii." United States Department of Energy Joint Genome Institute Smith D.R. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CC-503.
[3]	"Isolation of CF0CF1 from Chlamydomonas reinhardtii cw15 and the N-terminal amino acid sequences of the CF0CF1 subunits." Fiedler H.R., Schmid R., Leu S., Shavit N., Strotmann H. FEBS Lett. 377:163-166(1995) [PubMed: 8543042] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32. Strain: cw15.
[4]	"The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats." Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., Stern D.B. Plant Cell 14:2659-2679(2002) [PubMed: 12417694] [Abstract] Cited for: IDENTIFICATION, COMPLETE PLASTID GENOME.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X90559 Genomic DNA. Translation: CAA62149.1. FJ423446 Genomic DNA. Translation: ACJ50140.1. BK000554 Genomic DNA. Translation: DAA00954.1.
PIR	S58349.
RefSeq	NP_958409.1. NC_005353.1.
3D structure databases
ProteinModelPortal	Q37304.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	DAA00954; DAA00954; DAA00954.
GeneID	2717044.
KEGG	cre:ChreCp053.
Phylogenomic databases
ProtClustDB	CHL00061.
Enzyme and pathway databases
BioCyc	CHLAMY:CHRECP053-MONOMER.
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_CHLRE

Accession

Primary (citable) accession number: Q37304
Secondary accession number(s): B7U1J3, Q9T2G4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program