ATPB_PRIM1
ID ATPB_PRIM1 Reviewed; 473 AA.
AC P12698; D5DWG1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=BMQ_5148;
OS Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=545693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2894831; DOI=10.1016/s0006-291x(88)80370-x;
RA Hawthorne C.A., Brusilow W.S.A.;
RT "Sequence of the genes for the beta and epsilon subunits of the ATP
RT synthase of Bacillus megaterium QM B1551.";
RL Biochem. Biophys. Res. Commun. 151:926-931(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12872 / QMB1551;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01347};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; M20255; AAA82526.1; -; Genomic_DNA.
DR EMBL; CP001983; ADE72126.1; -; Genomic_DNA.
DR PIR; A28599; PWBSBM.
DR RefSeq; WP_013059799.1; NC_014019.1.
DR AlphaFoldDB; P12698; -.
DR SMR; P12698; -.
DR STRING; 545693.BMQ_5148; -.
DR PRIDE; P12698; -.
DR EnsemblBacteria; ADE72126; ADE72126; BMQ_5148.
DR GeneID; 48015624; -.
DR GeneID; 64144394; -.
DR KEGG; bmq:BMQ_5148; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_9; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 430176at2; -.
DR Proteomes; UP000000935; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..473
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144421"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 401
FT /note="Q -> P (in Ref. 1; AAA82526)"
FT /evidence="ECO:0000305"
FT CONFLICT 413..415
FT /note="NFH -> TS (in Ref. 1; AAA82526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 51541 MW; 23D980190C644881 CRC64;
MTKGRVTQIM GPVVDVKFDN GHLPAIYNAL KISHKPSSAS EVAIELTLEV AIHLGDNTVR
TVAMSSTDGL VRGLEVEDTG AAISVPVGDV TLGRVFNVLG EKIDLDAPID AGARRDPIHR
QAPKFENLST QAEILETGIK VVDLLAPYIK GGKIGLFGGA GVGKTVLIQE LINNIAQEHG
GISVFAGVGE RTREGNDLYH EMTDSGVIKK TAMVFGQMNE PPGARQRVAL TGLTMAEYFR
DEQGQDVLFF IDNIFRFTQA GSEVSALLGR MPSAVGYQPT LATEMGQLQE RITSTSVGSV
TSIQAIYVPA DDYTDPAPAT TFAHLDATTN LERKLSEMGI YPAVDPLAST SRALSPEIVG
EEHYAIARQV QQTLQRYKEL QDIIAILGMD ELSDEDKLVV QRARRVQFFL SQNFHVAEQF
TGQKGSYVPV KETVKGFKEI LEGKYDHLPE DAFRLVGRIE EVIENAKRMG VEV
