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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Bacillus subtilis (strain 168)
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

Enzyme and pathway databases

BioCyciBSUB:BSU36810-MONOMER.
SABIO-RKP37809.

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
Vegetative protein 31
Short name:
VEG31
Gene namesi
Name:atpDUniRule annotation
Ordered Locus Names:BSU36810
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 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 – 473473ATP synthase subunit betaPRO_0000144425Add
BLAST

Proteomic databases

PaxDbiP37809.
PRIDEiP37809.

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 (Probable). The F1F0 complex interacts with SpoIIIJ and YqjG; YqgA is found in the same complex.UniRule annotationCurated1 Publication

Protein-protein interaction databases

IntActiP37809. 3 interactions.
MINTiMINT-8365623.
STRINGi224308.Bsubs1_010100019901.

Structurei

3D structure databases

ProteinModelPortaliP37809.
SMRiP37809. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C4J. Bacteria.
COG0055. LUCA.
HOGENOMiHOG000009605.
InParanoidiP37809.
KOiK02112.
OMAiAEFGIYP.
PhylomeDBiP37809.

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.

P37809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKGRVSQVL GPVVDVRFED GHLPEIYNAI KISQPAASEN EVGIDLTLEV
60 70 80 90 100
ALHLGDDTVR TIAMASTDGV QRGMEAVDTG APISVPVGDV TLGRVFNVLG
110 120 130 140 150
ENIDLNEPVP ADAKKDPIHR QAPSFDQLST EVEILETGIK VVDLLAPYIK
160 170 180 190 200
GGKIGLFGGA GVGKTVLIQE LINNIAQEHG GISVFAGVGE RTREGNDLFY
210 220 230 240 250
EMSDSGVINK TAMVFGQMNE PPGARMRVAL TGLTMAEHFR DVQGQDVLFF
260 270 280 290 300
IDNIFRFTQA GSEVSALLGR MPSAVGYQPT LATEMGQLQE RITSTNVGSV
310 320 330 340 350
TSIQAIYVPA DDYTDPAPAT TFAHLDATTN LERKLTEMGI YPAVDPLAST
360 370 380 390 400
SRALAPEIVG EEHYAVAREV QSTLQRYKEL QDIIAILGMD ELGEEDKLVV
410 420 430 440 450
HRARRIQFFL SQNFHVAEQF TGQKGSYVPV KETVQGFKEI LAGKYDHLPE
460 470
DAFRLVGRIE EVVEKAKEMG VEV
Length:473
Mass (Da):51,420
Last modified:October 1, 1994 - v1
Checksum:iEF1EFB6B900A099A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28592 Genomic DNA. Translation: CAA82260.1.
AL009126 Genomic DNA. Translation: CAB15698.1.
PIRiI40368.
RefSeqiNP_391562.1. NC_000964.3.
WP_003227686.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15698; CAB15698; BSU36810.
GeneIDi936992.
KEGGibsu:BSU36810.
PATRICi18979396. VBIBacSub10457_3860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28592 Genomic DNA. Translation: CAA82260.1.
AL009126 Genomic DNA. Translation: CAB15698.1.
PIRiI40368.
RefSeqiNP_391562.1. NC_000964.3.
WP_003227686.1. NZ_JNCM01000034.1.

3D structure databases

ProteinModelPortaliP37809.
SMRiP37809. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP37809. 3 interactions.
MINTiMINT-8365623.
STRINGi224308.Bsubs1_010100019901.

Proteomic databases

PaxDbiP37809.
PRIDEiP37809.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15698; CAB15698; BSU36810.
GeneIDi936992.
KEGGibsu:BSU36810.
PATRICi18979396. VBIBacSub10457_3860.

Phylogenomic databases

eggNOGiENOG4105C4J. Bacteria.
COG0055. LUCA.
HOGENOMiHOG000009605.
InParanoidiP37809.
KOiK02112.
OMAiAEFGIYP.
PhylomeDBiP37809.

Enzyme and pathway databases

BioCyciBSUB:BSU36810-MONOMER.
SABIO-RKP37809.

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_BACSU
AccessioniPrimary (citable) accession number: P37809
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: September 7, 2016
This is version 129 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, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.