ATP synthase subunit beta - Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)

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P57124 (ATPB_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATP synthase subunit beta
EC=3.6.3.14

Alternative name(s):
ATP synthase F1 sector subunit beta
F-ATPase subunit beta

Gene names

Name:	atpD
Ordered Locus Names:	BU008

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
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. HAMAP MF_01347
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 HAMAP MF_01347.
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 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	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell 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: UniProtKB-KW hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro 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

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P57124 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 89CB775CC8F8172B
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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

« Hide

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: APS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12736.1.
RefSeq	NP_239850.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57124.
SMR	P57124. Positions 4-465.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002962; EBBUCP00000002738; EBBUCG00000002962.
GeneID	1109517.
GenomeReviews	Gene locus BU008 in contig BA000003_GR.
KEGG	buc:BU008.
PATRIC	21243520. VBIBucAph127364_0021.
Phylogenomic databases
GeneTree	EBGT00050000007862.
HOGENOM	HBG565875.
OMA	IGQEHYD.
PhylomeDB	P57124.
ProtClustDB	PRK09280.
Enzyme and pathway databases
BioCyc	BSP107806:BU008-MONOMER.
Family and domain databases
HAMAP	MF_01347. ATP_synth_beta_bact. [Tree]
InterPro	IPR020003. ATPase_a/bsu_AS. 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. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR024034. ATPase_F1_bsu/V1_C. [Graphical view]
Gene3D	G3DSA:1.10.1140.10. G3DSA:1.10.1140.10. 1 hit.
KO	K02112.
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]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR01039. AtpD. 1 hit.
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:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents