ID   A0A5J4JDS4_9BACI        Unreviewed;       473 AA.
AC   A0A5J4JDS4;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   05-FEB-2025, entry version 19.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
GN   Name=atpD {ECO:0000256|HAMAP-Rule:MF_01347,
GN   ECO:0000313|EMBL:GER69469.1};
GN   ORFNames=BpJC7_07720 {ECO:0000313|EMBL:GER69469.1};
OS   Weizmannia acidilactici.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Heyndrickxia.
OX   NCBI_TaxID=2607726 {ECO:0000313|EMBL:GER69469.1, ECO:0000313|Proteomes:UP000391919};
RN   [1] {ECO:0000313|EMBL:GER69469.1, ECO:0000313|Proteomes:UP000391919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC-7 {ECO:0000313|EMBL:GER69469.1,
RC   ECO:0000313|Proteomes:UP000391919};
RA   Tanaka N., Shiwa Y., Fujita N., Tanasupawat S.;
RT   "Draft genome sequence of Bacillus sp. JC-7.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out);
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:0000256|HAMAP-Rule:MF_01347};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01347}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GER69469.1}.
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DR   EMBL; BKZQ01000007; GER69469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J4JDS4; -.
DR   Proteomes; UP000391919; Unassembled WGS sequence.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR   CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR   CDD; cd01133; F1-ATPase_beta_CD; 1.
DR   FunFam; 1.10.1140.10:FF:000001; ATP synthase subunit beta; 1.
DR   FunFam; 2.40.10.170:FF:000005; ATP synthase subunit beta; 1.
DR   FunFam; 3.40.50.300:FF:000004; ATP synthase subunit beta; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 1.10.1140.10; Bovine Mitochondrial F1-atpase, Atp Synthase Beta Chain, Chain D, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR055190; ATP-synt_VA_C.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR050053; ATPase_alpha/beta_chains.
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   NCBIfam; TIGR01039; atpD; 1.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF22919; ATP-synt_VA_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01347}; Reference proteome {ECO:0000313|Proteomes:UP000391919};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}.
FT   DOMAIN          150..413
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         158..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   473 AA;  51663 MW;  B9EF4450DBCFD349 CRC64;
     MSIGHVLQVM GPVVDVKFEN GQLPDIYNAL KINYKAKSSD EVDINVTLEV ALHLGDDAVR
     TVAMSSTDGI RRGMEVVDTG APISVPVGEA TLGRVFNVLG EVIDLDGELK GDVRRDPIQK
     PAPSFEQLST QVEILETGIK VVDLLAPYIK GGKIGLFGGA GVGKTVLIQE LIHNVAQEHG
     GISVFAGVGE RTREGNDLYY EMKDSGVINK TAMVFGQMNE PPGARMRVAL TGLTMAEYFR
     DEQGQDVLLF IDNIFRFTQA GSEVSALLGR MPSAVGYQPT LATEMGQLQE RITSTTKGSI
     TSIQAIYVPA DDYTDPAPAT TFAHLDATTN LERRLSEMGI YPAVDPLAST SRALAPEIVG
     EEHYKVARQV QATLQRYREL QDIIAILGMD ELSEDDKLVV HRARRIQFFL SQNFHVAEQF
     TGQPGSYVPV KETVRGFKEI LEGKYDHLPE DAFRLVGPIE DVVKKAEAMG VKV
//