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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.UniRule annotation

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi156 – 1638ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-8-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit betaUniRule annotation (EC:3.6.3.14UniRule annotation)
Alternative name(s):
ATP synthase F1 sector subunit betaUniRule annotation
F-ATPase subunit betaUniRule annotation
Gene namesi
Name:atpDUniRule annotation
Synonyms:uncD
Ordered Locus Names:BUsg_008
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, CF(1), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466ATP synthase subunit betaPRO_0000144427Add
BLAST

Proteomic databases

PRIDEiQ07232.

Interactioni

Subunit structurei

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.UniRule annotation

Protein-protein interaction databases

STRINGi198804.BUsg008.

Structurei

3D structure databases

ProteinModelPortaliQ07232.
SMRiQ07232. Positions 5-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0055.
KOiK02112.
OMAiRWPIHRK.
OrthoDBiEOG6HQSP3.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF8. PTHR15184:SF8. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07232-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIATGKIIQI IGAVVDVEFD QNSVPKIYNA LEVKNKKIQL ILEVQQQLGA
60 70 80 90 100
GIVRTIAMGS TNGLKRGLIV IDLGHYIKVP VGQATLGRII NVLGKTIDNK
110 120 130 140 150
GPLKNLDNSK LEYWEIHRSA PSYQEQASSQ EILETGIKVI DLICPFSKGG
160 170 180 190 200
KVGLFGGAGV GKTVNMMELI RNIAIEHSGY SVFTGVGERT REGNDFYHEM
210 220 230 240 250
KDSKVLDKVS LVYGQMNEPP GNRLRVAFTG LTIAEKFRDE GRDVLLFIDN
260 270 280 290 300
IYRYTLAGTE VSALLGRMPS AVGYQPTLAE EMGLLQERIT STKEGSITSV
310 320 330 340 350
QAVYVPADDL TDPSPATTFA HLDSTVTLSR QIAALGIYPA IDPLNSTSRQ
360 370 380 390 400
LDPYIVGDEH YDTARGVQSI LQRYQELKDI IAILGMDELS QEDKILVSRA
410 420 430 440 450
RKIQRFLSQP FFVAEVFTGF PGKYVSLKDN IRAFKGIIGG EFDNLPEQAF
460
YMVGTIEEVI KKAKLL
Length:466
Mass (Da):51,349
Last modified:December 15, 1998 - v2
Checksum:iF0A1570A2DA470D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2801E → G (PubMed:7763501).Curated
Sequence conflicti280 – 2801E → G (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008210 Genomic DNA. Translation: AAC38110.1.
AE013218 Genomic DNA. Translation: AAM67580.1.
Z15147 Genomic DNA. Translation: CAA78853.1.
AJ247128 Genomic DNA. Translation: CAB95753.1.
PIRiS37647.
RefSeqiNP_660369.1. NC_004061.1.
WP_011053546.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67580; AAM67580; BUsg_008.
KEGGibas:BUsg008.
PATRICi21246771. VBIBucAph100086_0008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008210 Genomic DNA. Translation: AAC38110.1.
AE013218 Genomic DNA. Translation: AAM67580.1.
Z15147 Genomic DNA. Translation: CAA78853.1.
AJ247128 Genomic DNA. Translation: CAB95753.1.
PIRiS37647.
RefSeqiNP_660369.1. NC_004061.1.
WP_011053546.1. NC_004061.1.

3D structure databases

ProteinModelPortaliQ07232.
SMRiQ07232. Positions 5-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198804.BUsg008.

Proteomic databases

PRIDEiQ07232.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM67580; AAM67580; BUsg_008.
KEGGibas:BUsg008.
PATRICi21246771. VBIBucAph100086_0008.

Phylogenomic databases

eggNOGiCOG0055.
KOiK02112.
OMAiRWPIHRK.
OrthoDBiEOG6HQSP3.

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-8-MONOMER.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF8. PTHR15184:SF8. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiATPB_BUCAP
AccessioniPrimary (citable) accession number: Q07232
Secondary accession number(s): O51872, Q93V14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 15, 1998
Last modified: April 29, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.