Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Nucleotide bindingi158 – 165ATPUniRule annotation8

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001444221 – 473ATP synthase subunit betaAdd BLAST473

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

1473
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Beta strandi13 – 19Combined sources7
Beta strandi28 – 34Combined sources7
Beta strandi44 – 55Combined sources12
Beta strandi58 – 65Combined sources8
Beta strandi75 – 82Combined sources8
Beta strandi84 – 86Combined sources3
Helixi89 – 91Combined sources3
Beta strandi104 – 106Combined sources3
Beta strandi115 – 118Combined sources4
Helixi125 – 127Combined sources3
Helixi140 – 145Combined sources6
Beta strandi153 – 157Combined sources5
Beta strandi160 – 162Combined sources3
Helixi164 – 178Combined sources15
Beta strandi183 – 190Combined sources8
Helixi192 – 204Combined sources13
Helixi207 – 210Combined sources4
Beta strandi211 – 216Combined sources6
Helixi222 – 242Combined sources21
Beta strandi246 – 252Combined sources7
Helixi255 – 268Combined sources14
Helixi274 – 276Combined sources3
Helixi281 – 289Combined sources9
Beta strandi295 – 297Combined sources3
Beta strandi299 – 305Combined sources7
Beta strandi313 – 315Combined sources3
Helixi316 – 322Combined sources7
Beta strandi326 – 331Combined sources6
Helixi335 – 338Combined sources4
Turni346 – 348Combined sources3
Helixi356 – 387Combined sources32
Helixi395 – 409Combined sources15
Turni415 – 417Combined sources3
Helixi418 – 421Combined sources4
Helixi430 – 441Combined sources12
Turni442 – 447Combined sources6
Helixi450 – 452Combined sources3
Beta strandi456 – 459Combined sources4
Helixi460 – 466Combined sources7
Turni467 – 469Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SKYX-ray3.20E1-473[»]
ProteinModelPortaliP07677.
SMRiP07677.
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.
IPR005722. ATP_synth_F1_bsu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1/V1_bsu_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]
SUPFAMiSSF50615. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SKYX-ray3.20E1-473[»]
ProteinModelPortaliP07677.
SMRiP07677.
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.
IPR005722. ATP_synth_F1_bsu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1/V1_bsu_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]
SUPFAMiSSF50615. 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: November 30, 2016
This is version 122 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.