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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Bacillus anthracis
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 bindingi156 – 163ATPUniRule 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:BA_5547, GBAA_5547, BAS5155
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome
  • UP000000427 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, CF(1), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002542051 – 469ATP synthase subunit betaAdd BLAST469

Proteomic databases

PRIDEiQ81JZ5

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

STRINGi260799.BAS5155

Structurei

3D structure databases

ProteinModelPortaliQ81JZ5
SMRiQ81JZ5
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.

Q81JZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKGRVTQIM GPVVDVKFDG GKLPEIYNAL TVKQSNENGT SINLTFEVAL
60 70 80 90 100
HLGDDTVRTV AMSSTDGLVR GTEVEDTGKA ISVPVGDATL GRVFNVLGDA
110 120 130 140 150
IDLDGEVPAD VRRDPIHRQA PAFEELSTKV EILETGIKVV DLLAPYIKGG
160 170 180 190 200
KIGLFGGAGV GKTVLIQELI NNIAQEHGGI SVFAGVGERT REGNDLYHEM
210 220 230 240 250
SDSGVIKKTA MVFGQMNEPP GARQRVALTG LTMAEHFRDE QGQDVLLFID
260 270 280 290 300
NIFRFTQAGS EVSALLGRMP SAVGYQPTLA TEMGQLQERI TSTNKGSITS
310 320 330 340 350
IQAVYVPADD YTDPAPATTF AHLDATTNLE RRLTQMGIYP AVDPLASTSR
360 370 380 390 400
ALSPEIVGEE HYEVARQVQQ TLQRYKELQD IIAILGMDEL SEEDKLVVHR
410 420 430 440 450
ARRIQFFLSQ NFHVAEQFTG QKGSYVPVKE TVRGFKEILE GKYDDLPEDA
460
FRLVGGIEEV IENAKKMMA
Length:469
Mass (Da):51,194
Last modified:June 1, 2003 - v1
Checksum:iA4EEA00A9B1E6E9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA Translation: AAP29191.1
AE017225 Genomic DNA Translation: AAT57444.1
AE017334 Genomic DNA Translation: AAT34691.1
RefSeqiNP_847705.1, NC_003997.3
WP_001032600.1, NZ_NVHS01000019.1
YP_031394.1, NC_005945.1

Genome annotation databases

EnsemblBacteriaiAAP29191; AAP29191; BA_5547
AAT34691; AAT34691; GBAA_5547
AAT57444; AAT57444; BAS5155
GeneIDi1085230
2852682
KEGGiban:BA_5547
bar:GBAA_5547
bat:BAS5155
PATRICifig|198094.11.peg.5507

Similar proteinsi

Entry informationi

Entry nameiATPB_BACAN
AccessioniPrimary (citable) accession number: Q81JZ5
Secondary accession number(s): Q6HQJ4, Q6KJW9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2003
Last modified: April 25, 2018
This is version 129 of the entry and version 1 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