Reviewed, UniProtKB/Swiss-Prot O51874 (ATPA_BUCAP)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit alpha
      Short name(s)=ATPase subunit alpha
    EC=3.6.3.14
Alternative name(s):
    ATP synthase F1 sector subunit alpha

Gene names

Name:	atpA
Ordered Locus Names:	BUsg_006

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	510 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. The alpha chain is a regulatory subunit.
Catalytic activity	ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
Subunit structure	F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) 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; Peripheral membrane proteinBy similarity.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 510	510	ATP synthase subunit alpha
Regions
	Nucleotide binding	169 – 176	8	ATP Potential
Sites
	Site	373	1	Required for activity
Experimental info
	Sequence conflict	269	1	A → R Ref.1 Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O51874-1 [UniParc]. Last modified August 30, 2002. Version 2. Checksum: EE2884411AFB5E3A	FASTA	510	56,391
	10 20 30 40 50 60 MQLNSTEISQ LIKERIAQFE VFNQSYNEGT IISVNDGIIK IYGLSDVMLG EMILLPDNEY 70 80 90 100 110 120 AIALNIERDT IGAVVMGPYI HITEGTKVRC TGKILEVPVG VALLGRIVNA LGFPIDGKGS 130 140 150 160 170 180 IEHDIYLPVE ADAPGVIERE SINEPIQTGY KAIDAMVPIG RGQRELIIGD RQTGKTALAI 190 200 210 220 230 240 DTIINQKKIN LPCVYVAIGQ KLSTIINVVK KLDEHDALLN TIVVVASASE AASLQYLAPY 250 260 270 280 290 300 SGCAMGEYFR DRGKDALIVY DDLSKHAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER 310 320 330 340 350 360 ASRVSKEHVK NVTKGKITGK TGSLTALPII ETQSGDVSAF VPTNVISITD GQIFLESNLF 370 380 390 400 410 420 NSGIRPAVNA GISVSRVGSA AQTKIIKKLS SGIRTALAQY HELAAFSQFA SDLDQTTRKQ 430 440 450 460 470 480 LIYGQKITEL LKQKQYRPMS ISEQGLMFFI AENNFLDDIS VENIIQFEKE ILTYAYNYHL 490 500 510 DLMEEINKDG NFNDIIKKKF IELINNFKNS

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: AAC38112.1. AE013218 Genomic DNA. Translation: AAM67578.1.
RefSeq	NP_660367.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1005804.
GenomeReviews	Gene locus BUsg_006 in contig AE013218_GR.
KEGG	bas:BUsg006.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O51874.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG006-MON.
Family and domain databases
HAMAP	MF_01346. [Tree]
InterPro	IPR000793. ATPase_a_b_C. IPR004100. ATPase_a_b_N. IPR000194. ATPase_a_b_nl_bd. IPR005294. ATPase_F1_a. IPR017458. ATPase_F1_asu_C. [Graphical view]
PANTHER	PTHR15184:SF3. ATPase_F1_a. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProDom	O51874. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ATPA_BUCAP

Accession

Primary (citable) accession number: O51874

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 30, 2002
Last modified:	July 22, 2008
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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