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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Leuconostoc citreum (strain KM20)
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 bindingi153 – 160ATPUniRule 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:LCK_01627
OrganismiLeuconostoc citreum (strain KM20)
Taxonomic identifieri349519 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeLeuconostoc
Proteomesi
  • UP000002166 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_10001435221 – 466ATP synthase subunit betaAdd BLAST466

Proteomic databases

PRIDEiB1MW85

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

STRINGi349519.LCK_01627

Structurei

3D structure databases

ProteinModelPortaliB1MW85
SMRiB1MW85
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.

B1MW85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTGKVVQVI GPVVDVAFES GQQVPDINNA LKIDKGDGQT LTVEVSLALG
60 70 80 90 100
DGIVRTIAMD STDGLQRGMS VTDTGDAIKV PVGEATLGRV FNVLGEPVDN
110 120 130 140 150
NGEIAAETPR HSIHRDAPSY DDLANSTEIL ETGIKVIDLL APYVRGGKIG
160 170 180 190 200
LFGGAGVGKT VLIQELIHNI AQGHNGISVF TGVGERTREG NDMYHEMAES
210 220 230 240 250
GVLKQTAMVY GQMNEPPGAR MRVALTGLTM AENFRDSEGK DVLLFIDNIF
260 270 280 290 300
RFTQAGSEVS ALLGRIPSAV GYQPTLATEM GQLQERITST KKGSVTSIQA
310 320 330 340 350
VYVPADDYTD PAPATTFAHL DATTNLERAL TQQGIYPAVD PLASTSSALD
360 370 380 390 400
PQVVGQEHYE VATEVQRTLQ RYRELQDIIS ILGMDELSDE EKTTVNRARR
410 420 430 440 450
IQFFLSQPFS VAETFTGING EYVPVAETVR SFKEILDGKY DDLPEDAFRN
460
VGAIEQVVEK AKTMAQ
Length:466
Mass (Da):50,267
Last modified:April 29, 2008 - v1
Checksum:iAD46BC8ADDC5D231
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ489736 Genomic DNA Translation: ACA83450.1
RefSeqiWP_004902054.1, NC_010471.1

Genome annotation databases

EnsemblBacteriaiACA83450; ACA83450; LCK_01627
GeneIDi35826053
KEGGilci:LCK_01627

Similar proteinsi

Entry informationi

Entry nameiATPB_LEUCK
AccessioniPrimary (citable) accession number: B1MW85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: April 25, 2018
This is version 70 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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