Reviewed, UniProtKB/Swiss-Prot P57125 (ATPE_BUCAI)

Names and origin

Protein names

Recommended name:
    ATP synthase epsilon chain
Alternative name(s):
    ATP synthase F1 sector epsilon subunit
    F-ATPase epsilon subunit

Gene names

Name:	atpC
Ordered Locus Names:	BU009

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	138 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane. HAMAP MF_00530
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. HAMAP MF_00530
Subcellular location	Cell membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the ATPase epsilon chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell membrane Membrane
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 138	138	ATP synthase epsilon chain HAMAP MF_00530		PRO_0000188111

Sequences

	Sequence		Length	Mass (Da)
	P57125-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: C5F19B4C8FF89ADB	FASTA	138	15,463
	10 20 30 40 50 60 MNFYLDVVSL TKTIFSGFVE KIRVSGSEGE LGIYPGHAQL LSILKPGMVY IFHKKDKKEE 70 80 90 100 110 120 CIYISGGILE VQPSVVSILA DVAIHAIDLD RSRILKTKKN AEESIKSNNT KINKDAILLQ 130 ISKEIAKLRV LEVMDKFK

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB12737.1.
RefSeq	NP_239851.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1109518.
GenomeReviews	Gene locus BU009 in contig BA000003_GR.
KEGG	buc:BU009.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG663981.
OMA	ARAELME.
Enzyme and pathway databases
BioCyc	BSP107806:BU009-MON.
Family and domain databases
HAMAP	MF_00530. [Tree]
InterPro	IPR001469. ATPase_F1-cplx_dsu/esu. IPR020547. ATPase_F1-cplx_dsu/esu_C. IPR020546. ATPase_F1-cplx_dsu/esu_N. [Graphical view]
Gene3D	G3DSA:1.20.5.440. ATPase_F1_d/e. 1 hit. G3DSA:2.60.15.10. ATPase_F1_d/e. 1 hit.
PANTHER	PTHR13822. ATPase_F1_d/e. 1 hit.
Pfam	PF02823. ATP-synt_DE_N. 1 hit. [Graphical view]
ProDom	PD000944. ATPase_F1-cplx_dsu/esu. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

ATPE_BUCAI

Accession

Primary (citable) accession number: P57125

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	December 15, 2009
This is version 61 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)