P27182 (ATPL_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit c

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

Gene names

Name:	atpE
Synonyms:	atpH
Ordered Locus Names:	ssl2615

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa)

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

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	Cellular thylakoid membrane; Multi-pass membrane protein By similarity 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) Membrane 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	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 thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro 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 HAMAP MF_01396		PRO_0000112173
Regions
	Transmembrane	6 – 26	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)
	P27182 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 30E2CAB3B963FF27	FASTA	81	7,968
	10 20 30 40 50 60 MDSTVAAASV IAAALAVGLG AIGPGIGQGN ASGQAVSGIA RQPEAEGKIR GTLLLTLAFM 70 80 ESLTIYGLVI ALVLLFANPF A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The atp1 and atp2 operons of the cyanobacterium Synechocystis sp. PCC 6803." Lill H., Nelson N. Plant Mol. Biol. 17:641-652(1991) [PubMed: 1832989] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58128 Genomic DNA. Translation: CAA41131.1. BA000022 Genomic DNA. Translation: BAA16739.1.
PIR	PWYBLB. S17747.
RefSeq	NP_440059.1. NC_000911.1.
3D structure databases
ProteinModelPortal	P27182.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27182. 4 interactions.
STRING	P27182.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	953358.
GenomeReviews	Gene locus ssl2615 in contig BA000022_GR.
KEGG	syn:ssl2615.
NMPDR	fig|1148.1.peg.160.
PATRIC	23837198. VBISynSp132158_0174.
Phylogenomic databases
eggNOG	COG0636.
HOGENOM	HBG753983.
OMA	IGQGNAS.
PhylomeDB	P27182.
ProtClustDB	PRK07354.
Enzyme and pathway databases
BioCyc	SSP1148:SSL2615-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

ATPL_SYNY3

Accession

Primary (citable) accession number: P27182

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program