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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: -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 bindingi150 – 157ATPUniRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandATP-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:Z5230, ECs4674
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(1), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001444382 – 460ATP synthase subunit betaAdd BLAST459

Proteomic databases

PRIDEiP0ABB6

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

Protein-protein interaction databases

STRINGi155864.Z5230

Structurei

3D structure databases

ProteinModelPortaliP0ABB6
SMRiP0ABB6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C4J Bacteria
COG0055 LUCA
HOGENOMiHOG000009605
KOiK02112
OMAiFNMIMDG

Family and domain databases

Gene3Di1.10.1140.10, 1 hit
HAMAPiMF_01347 ATP_synth_beta_bact, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005722 ATP_synth_F1_bsu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01039 atpD, 1 hit
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ABB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGKIVQVI GAVVDVEFPQ DAVPRVYDAL EVQNGNERLV LEVQQQLGGG
60 70 80 90 100
IVRTIAMGSS DGLRRGLDVK DLEHPIEVPV GKATLGRIMN VLGEPVDMKG
110 120 130 140 150
EIGEEERWAI HRAAPSYEEL SNSQELLETG IKVIDLMCPF AKGGKVGLFG
160 170 180 190 200
GAGVGKTVNM MELIRNIAIE HSGYSVFAGV GERTREGNDF YHEMTDSNVI
210 220 230 240 250
DKVSLVYGQM NEPPGNRLRV ALTGLTMAEK FRDEGRDVLL FVDNIYRYTL
260 270 280 290 300
AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTKTGS ITSVQAVYVP
310 320 330 340 350
ADDLTDPSPA TTFAHLDATV VLSRQIASLG IYPAVDPLDS TSRQLDPLVV
360 370 380 390 400
GQEHYDTARG VQSILQRYQE LKDIIAILGM DELSEEDKLV VARARKIQRF
410 420 430 440 450
LSQPFFVAEV FTGSPGKYVS LKDTIRGFKG IMEGEYDHLP EQAFYMVGSI
460
EEAVEKAKKL
Length:460
Mass (Da):50,325
Last modified:January 23, 2007 - v2
Checksum:i18DB33154B1AE6FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA Translation: AAG58935.1
BA000007 Genomic DNA Translation: BAB38097.1
PIRiB91213
C86059
RefSeqiNP_312701.1, NC_002695.1
WP_000190506.1, NZ_NOKN01000002.1

Genome annotation databases

EnsemblBacteriaiAAG58935; AAG58935; Z5230
BAB38097; BAB38097; BAB38097
GeneIDi915359
KEGGiece:Z5230
ecs:ECs4674
PATRICifig|386585.9.peg.4879

Similar proteinsi

Entry informationi

Entry nameiATPB_ECO57
AccessioniPrimary (citable) accession number: P0ABB6
Secondary accession number(s): P00824
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 99 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health