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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
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 bindingi155 – 1628ATPUniRule 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

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
Ordered Locus Names:BCE_5430
OrganismiBacillus cereus (strain ATCC 10987 / NRS 248)
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000002527 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 – 468468ATP synthase subunit betaPRO_0000254206Add
BLAST

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

Structurei

3D structure databases

ProteinModelPortaliQ72XE8.
SMRiQ72XE8. Positions 1-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000009605.
KOiK02112.
OMAiFKESGVI.
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]
PfamiPF00006. ATP-synt_ab. 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.

Q72XE8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKGRVTQIM GPVVDVKFDG GKLPEIYNAL TVKQSNENGE LNLTFEVALH
60 70 80 90 100
LGDDTVRTVA MSSTDGLVRG TEVEDTGKAI SVPVGDATLG RVFNVLGDAI
110 120 130 140 150
DLDGEVPADV RRDPIHRQAP AFEELSTKVE ILETGIKVVD LLAPYIKGGK
160 170 180 190 200
IGLFGGAGVG KTVLIQELIN NIAQEHGGIS VFAGVGERTR EGNDLYHEMS
210 220 230 240 250
DSGVIKKTAM VFGQMNEPPG ARQRVALTGL TMAEYFRDEQ GQDVLLFIDN
260 270 280 290 300
IFRFTQAGSE VSALLGRMPS AVGYQPTLAT EMGQLQERIT STNKGSITSI
310 320 330 340 350
QAVYVPADDY TDPAPATTFA HLDATTNLER RLTQMGIYPA VDPLASTSRA
360 370 380 390 400
LSPEIVGEEH YEVARQVQQT LQRYKELQDI IAILGMDELS EEDKLVVHRA
410 420 430 440 450
RRIQFFLSQN FHVAEQFTGQ KGSYVPVKDT VRGFKEILEG KYDDLPEDAF
460
RLVGGIEEVI ENAKKMMA
Length:468
Mass (Da):51,147
Last modified:July 5, 2004 - v1
Checksum:iA147AFC52E8C7CC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS44330.1.
RefSeqiWP_001032591.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS44330; AAS44330; BCE_5430.
KEGGibca:BCE_5430.
PATRICi18859460. VBIBacCer118379_5199.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS44330.1.
RefSeqiWP_001032591.1. NC_003909.8.

3D structure databases

ProteinModelPortaliQ72XE8.
SMRiQ72XE8. Positions 1-466.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS44330; AAS44330; BCE_5430.
KEGGibca:BCE_5430.
PATRICi18859460. VBIBacCer118379_5199.

Phylogenomic databases

HOGENOMiHOG000009605.
KOiK02112.
OMAiFKESGVI.
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]
PfamiPF00006. ATP-synt_ab. 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

  1. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
    Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
    Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10987 / NRS 248.

Entry informationi

Entry nameiATPB_BACC1
AccessioniPrimary (citable) accession number: Q72XE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.