ATP synthase subunit beta - Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)

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Q07232 (ATPB_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. 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
Synonyms:	uncD
Ordered Locus Names:	BUsg_008

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length	466 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-Rule MF_01347
Catalytic activity	ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out). HAMAP-Rule 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-Rule 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
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
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: HAMAP proton-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

Feature identifier

Molecule processing

Chain

1 – 466

466

ATP synthase subunit beta HAMAP-Rule MF_01347

PRO_0000144427

Regions

Nucleotide binding

156 – 163

ATP By similarity

Experimental info

Sequence conflict

280

E → G Ref.4

Sequence conflict

280

E → G Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

Q07232 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: F0A1570A2DA470D9
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FASTA

466

51,349

        10         20         30         40         50         60 
MIATGKIIQI IGAVVDVEFD QNSVPKIYNA LEVKNKKIQL ILEVQQQLGA GIVRTIAMGS 

        70         80         90        100        110        120 
TNGLKRGLIV IDLGHYIKVP VGQATLGRII NVLGKTIDNK GPLKNLDNSK LEYWEIHRSA 

       130        140        150        160        170        180 
PSYQEQASSQ EILETGIKVI DLICPFSKGG KVGLFGGAGV GKTVNMMELI RNIAIEHSGY 

       190        200        210        220        230        240 
SVFTGVGERT REGNDFYHEM KDSKVLDKVS LVYGQMNEPP GNRLRVAFTG LTIAEKFRDE 

       250        260        270        280        290        300 
GRDVLLFIDN IYRYTLAGTE VSALLGRMPS AVGYQPTLAE EMGLLQERIT STKEGSITSV 

       310        320        330        340        350        360 
QAVYVPADDL TDPSPATTFA HLDSTVTLSR QIAALGIYPA IDPLNSTSRQ LDPYIVGDEH 

       370        380        390        400        410        420 
YDTARGVQSI LQRYQELKDI IAILGMDELS QEDKILVSRA RKIQRFLSQP FFVAEVFTGF 

       430        440        450        460 
PGKYVSLKDN IRAFKGIIGG EFDNLPEQAF YMVGTIEEVI KKAKLL

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.
[4]	"Aspects of energy-yielding metabolism in the aphid, Schizaphis graminum, and its endosymbiont: detection of gene fragments potentially coding for the ATP synthase beta-subunit and glyceraldehyde-3-phosphate dehydrogenase." Clark M.A., Baumann P. Curr. Microbiol. 26:233-237(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-314.
[5]	"Effect of selection and random drift in the evolution of aphids endosymbionts." Latorre A., Buades C., Sabater B., Moya A. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-314.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF008210 Genomic DNA. Translation: AAC38110.1. AE013218 Genomic DNA. Translation: AAM67580.1. Z15147 Genomic DNA. Translation: CAA78853.1. AJ247128 Genomic DNA. Translation: CAB95753.1.
PIR	S37647.
RefSeq	NP_660369.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q07232.
SMR	Q07232. Positions 5-466.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg008.
Proteomic databases
PRIDE	Q07232.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67580; AAM67580; BUsg_008.
GeneID	1005596.
KEGG	bas:BUsg008.
PATRIC	21246771. VBIBucAph100086_0008.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0055.
KO	K02112.
OMA	NNIAKGH.
ProtClustDB	PRK09280.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-81-MONOMER.
Family and domain databases
Gene3D	1.10.1140.10. 1 hit.
HAMAP	MF_01347. ATP_synth_beta_bact.
InterPro	IPR003593. AAA+_ATPase. IPR020003. ATPase_a/bsu_AS. IPR004100. ATPase_a/bsu_N. IPR005722. ATPase_F1-cplx_bsu. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR024034. ATPase_F1_bsu/V1_C. [Graphical view]
PANTHER	PTHR15184:SF8. PTHR15184:SF8. 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_BUCAP

Accession

Primary (citable) accession number: Q07232
Secondary accession number(s): O51872, Q93V14

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 15, 1998
Last modified:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents