Reviewed, UniProtKB/Swiss-Prot O51877 (ATPL_BUCAP)

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
Ordered Locus Names:	BUsg_003

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	79 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. 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.
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 three main subunits: a1, b2 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 and b chains By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
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) Cell membrane Membrane
Domain	Transmembrane
Ligand	Lipid-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma 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	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP 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 – 79	79	ATP synthase subunit c HAMAP MF_01396		PRO_0000112141
Regions
	Transmembrane	11 – 31	21	Potential
	Transmembrane	53 – 73	21	Potential
Sites
	Site	61	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	O51877-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 1A9D8F7C9FD90AC6	FASTA	79	8,267
	10 20 30 40 50 60 MESLNVDMLY IAVAIMIGLA AIGAAIGIGI LGSKFLEGAA RQPDLVPLLR TQFFVVMGLV 70 DAIPMIAVGL GLYMLFAIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The (F1F0) ATP synthase of Buchnera aphidicola (endosymbiont of aphids): genetic analysis of the putative ATP operon." Clark M.A., Baumann P. Curr. Microbiol. 35:84-89(1997) [PubMed: 9216881] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon, gidA, and rho." Clark M.A., Baumann L., Baumann P. Curr. Microbiol. 36:158-163(1998) [PubMed: 9516544] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF008210 Genomic DNA. Translation: AAC38115.1. AE013218 Genomic DNA. Translation: AAM67575.1.
RefSeq	NP_660364.1.
3D structure databases
SMR	O51877. Positions 1-79.
ModBase	Search...
Genome annotation databases
GeneID	1005815.
GenomeReviews	Gene locus BUsg_003 in contig AE013218_GR.
KEGG	bas:BUsg003.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O51877.
OMA	FFIMMGL
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG003-MON.
Family and domain databases
HAMAP	MF_01396. [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.
Pfam	PF00137. ATP-synt_C. 1 hit. [Graphical view]
PRINTS	PR00124. ATPASEC.
TIGRFAMs	TIGR01260. ATP_synt_c. 1 hit.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPL_BUCAP

Accession

Primary (citable) accession number: O51877

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	November 24, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)