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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Bacillus sp. (strain PS3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 bindingi158 – 1658ATPUniRule 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
OrganismiBacillus sp. (strain PS3)
Taxonomic identifieri2334 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

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 – 473473ATP synthase subunit betaPRO_0000144422Add
BLAST

Proteomic databases

PRIDEiP07677.

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 annotation1 Publication

Protein-protein interaction databases

DIPiDIP-6215N.
MINTiMINT-1526871.

Structurei

Secondary structure

1
473
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Beta strandi13 – 197Combined sources
Beta strandi28 – 347Combined sources
Beta strandi44 – 5512Combined sources
Beta strandi58 – 658Combined sources
Beta strandi75 – 828Combined sources
Beta strandi84 – 863Combined sources
Helixi89 – 913Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi115 – 1184Combined sources
Helixi125 – 1273Combined sources
Helixi140 – 1456Combined sources
Beta strandi153 – 1575Combined sources
Beta strandi160 – 1623Combined sources
Helixi164 – 17815Combined sources
Beta strandi183 – 1908Combined sources
Helixi192 – 20413Combined sources
Helixi207 – 2104Combined sources
Beta strandi211 – 2166Combined sources
Helixi222 – 24221Combined sources
Beta strandi246 – 2527Combined sources
Helixi255 – 26814Combined sources
Helixi274 – 2763Combined sources
Helixi281 – 2899Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi299 – 3057Combined sources
Beta strandi313 – 3153Combined sources
Helixi316 – 3227Combined sources
Beta strandi326 – 3316Combined sources
Helixi335 – 3384Combined sources
Turni346 – 3483Combined sources
Helixi356 – 38732Combined sources
Helixi395 – 40915Combined sources
Turni415 – 4173Combined sources
Helixi418 – 4214Combined sources
Helixi430 – 44112Combined sources
Turni442 – 4476Combined sources
Helixi450 – 4523Combined sources
Beta strandi456 – 4594Combined sources
Helixi460 – 4667Combined sources
Turni467 – 4693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKYX-ray3.20E1-473[»]
ProteinModelPortaliP07677.
SMRiP07677. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07677.

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact. 1 hit.
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.

P07677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRGRVIQVM GPVVDVKFEN GHLPAIYNAL KIQHKARNEN EVDIDLTLEV
60 70 80 90 100
ALHLGDDTVR TIAMASTDGL IRGMEVIDTG APISVPVGQV TLGRVFNVLG
110 120 130 140 150
EPIDLEGDIP ADARRDPIHR PAPKFEELAT EVEILETGIK VVDLLAPYIK
160 170 180 190 200
GGKIGLFGGA GVGKTVLIQE LIHNIAQEHG GISVFAGVGE RTREGNDLYH
210 220 230 240 250
EMKDSGVISK TAMVFGQMNE PPGARMRVAL TGLTMAEYFR DEQGQDGLLF
260 270 280 290 300
IDNIFRFTQA GSEVSALLGR MPSAIGYQPT LATEMGQLQE RITSTAKGSI
310 320 330 340 350
TSIQAIYVPA DDYTDPAPAT TFSHLDATTN LERKLAEMGI YPAVDPLVST
360 370 380 390 400
SRALAPEIVG EEHYQVARKV QQTLERYKEL QDIIAILGMD ELSDEDKLVV
410 420 430 440 450
HRARRIQFFL SQNFHVAEQF TGQPGSYVPV KETVRGFKEI LEGKYDHLPE
460 470
DRFRLVGRIE EVVEKAKAMG VEV
Length:473
Mass (Da):51,938
Last modified:April 1, 1988 - v1
Checksum:i3CFDE82E98D58DEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00113 Genomic DNA. Translation: BAA00066.1.
X04609 Genomic DNA. Translation: CAA28277.1.
X07804 Genomic DNA. Translation: CAA30655.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00113 Genomic DNA. Translation: BAA00066.1.
X04609 Genomic DNA. Translation: CAA28277.1.
X07804 Genomic DNA. Translation: CAA30655.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKYX-ray3.20E1-473[»]
ProteinModelPortaliP07677.
SMRiP07677. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6215N.
MINTiMINT-1526871.

Proteomic databases

PRIDEiP07677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP07677.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact. 1 hit.
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...

Entry informationi

Entry nameiATPB_BACP3
AccessioniPrimary (citable) accession number: P07677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: September 7, 2016
This is version 119 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.