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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
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)DescriptionActionsGraphical viewLength
Nucleotide bindingi155 – 162ATPUniRule 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
Ordered Locus Names:SAHV_2087
OrganismiStaphylococcus aureus (strain Mu3 / ATCC 700698)
Taxonomic identifieri418127 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

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_10000551681 – 470ATP synthase subunit betaAdd BLAST470

Proteomic databases

PRIDEiA7X4U3.

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

ProteinModelPortaliA7X4U3.
SMRiA7X4U3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000009605.
KOiK02112.
OMAiFKESGVI.

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.

A7X4U3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIGRVTQVM GPVIDVRFEH NEVPKINNAL VIDVPKEEGT IQLTLEVALQ
60 70 80 90 100
LGDDVVRTIA MDSTDGVQRG MDVKDTGKEI SVPVGDETLG RVFNVLGETI
110 120 130 140 150
DLKEEISDSV RRDPIHRQAP AFDELSTEVQ ILETGIKVVD LLAPYIKGGK
160 170 180 190 200
IGLFGGAGVG KTVLIQELIN NIAQEHGGIS VFAGVGERTR EGNDLYFEMS
210 220 230 240 250
DSGVIKKTAM VFGQMNEPPG ARMRVALSGL TMAEYFRDEQ GQDVLLFIDN
260 270 280 290 300
IFRFTQAGSE VSALLGRMPS AVGYQPTLAT EMGQLQERIT STTKGSVTSI
310 320 330 340 350
QAVFVPADDY TDPAPATAFA HLDATTNLER KLTEMGIYPA VDPLASTSRA
360 370 380 390 400
LEPSIVGQEH YEVARDVQST LQKYRELQDI IAILGMDELS DEDKQTVERA
410 420 430 440 450
RRIQFFLSQN FHVAEQFTGQ KGSYVPVKTT VANFKDILDG KYDHIPEDAF
460 470
RLVGSMDDVI AKAKDMGVEV
Length:470
Mass (Da):51,400
Last modified:October 23, 2007 - v1
Checksum:iC388E63D87E7F488
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009324 Genomic DNA. Translation: BAF78970.1.
RefSeqiWP_000511135.1. NZ_CTYB01000015.1.

Genome annotation databases

EnsemblBacteriaiBAF78970; BAF78970; SAHV_2087.
GeneIDi28380311.
KEGGisaw:SAHV_2087.
PATRICi19559340. VBIStaAur127830_2145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009324 Genomic DNA. Translation: BAF78970.1.
RefSeqiWP_000511135.1. NZ_CTYB01000015.1.

3D structure databases

ProteinModelPortaliA7X4U3.
SMRiA7X4U3.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA7X4U3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF78970; BAF78970; SAHV_2087.
GeneIDi28380311.
KEGGisaw:SAHV_2087.
PATRICi19559340. VBIStaAur127830_2145.

Phylogenomic databases

HOGENOMiHOG000009605.
KOiK02112.
OMAiFKESGVI.

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_STAA1
AccessioniPrimary (citable) accession number: A7X4U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: November 30, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.