Reviewed, UniProtKB/Swiss-Prot P57124 (ATPB_BUCAI)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit beta
    EC=3.6.3.14
Alternative name(s):
    F-ATPase subunit beta
    ATP synthase F1 sector subunit beta

Gene names

Name:	atpD
Ordered Locus Names:	BU008

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	465 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 catalytic sites are hosted primarily by the beta subunits By similarity.
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP MF_01347
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: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 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 protein By 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	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 hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro 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 – 465	465	ATP synthase subunit beta HAMAP MF_01347		PRO_0000144426
Regions
	Nucleotide binding	155 – 162	8	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57124-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 89CB775CC8F8172B	FASTA	465	51,311
	10 20 30 40 50 60 MATGKIIQII GAVVDVEFNQ DSVPKIYNAL EVKNKQYKLI LEVQQQLGSG VVRTIAMGSS 70 80 90 100 110 120 NGLKRGLIVT DLGHYIKVPV GEATLGRIIN VLGETIDNKG ALKNNQSDKI EYWEIHRSPP 130 140 150 160 170 180 SYRDQASCRE ILETGIKVID LICPFSKGGK VGLFGGAGVG KTVNMMELIR NIAVEHSGYS 190 200 210 220 230 240 VFTGVGERTR EGNDFYHEMN DSQVLDKVSL VYGQMNEPPG NRLRVAFTGL TIAEKFRDEG 250 260 270 280 290 300 KDVLLFIDNI YRYTLAGTEV SALLGRMPSA VGYQPTLAEE MGLLQERITS TKNGSITSVQ 310 320 330 340 350 360 AVYVPADDLT DPSPATTFAH LDSTVTLSRQ IASLGIYPAI DPLNSTSRQL DPYIVGDEHY 370 380 390 400 410 420 ETALGVQSIL QRYQELKDII AILGMDELAE KDKLLVSRAR KIQRFLSQPF FVAEVFTGFP 430 440 450 460 GKYVSLKDNI RAFKGIIKGE FDDLPEQAFY MVGSIEEVIE KAKKL

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: BAB12736.1.
RefSeq	NP_239850.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1109517.
GenomeReviews	Gene locus BU008 in contig BA000003_GR.
KEGG	buc:BU008.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG565875.
OMA	IGQEHYD.
Enzyme and pathway databases
BioCyc	BSP107806:BU008-MON.
Family and domain databases
HAMAP	MF_01347. [Tree]
InterPro	IPR003593. ATPase_AAA+_core. IPR005722. ATPase_F1-cplx_bsu. IPR018118. ATPase_F1/A1-cplx_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR020003. ATPase_F1/V1/A1_a/bsu_AS. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. [Graphical view]
PANTHER	PTHR15184:SF8. ATPase_F1_b. 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]
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPB_BUCAI

Accession

Primary (citable) accession number: P57124

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	December 15, 2009
This is version 64 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)