ID   G4SWW9_META2            Unreviewed;       460 AA.
AC   G4SWW9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   04-NOV-2026, entry version 75.
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:CCE22035.1};
GN   OrderedLocusNames=MEALZ_0335 {ECO:0000313|EMBL:CCE22035.1};
OS   Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS   B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Methylococcales; Methylococcaceae; Methylotuvimicrobium.
OX   NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE22035.1, ECO:0000313|Proteomes:UP000008315};
RN   [1] {ECO:0000313|EMBL:CCE22035.1, ECO:0000313|Proteomes:UP000008315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC   {ECO:0000313|Proteomes:UP000008315};
RX   PubMed=22207753; DOI=10.1128/JB.06392-11;
RA   Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA   Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA   Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA   Trotsenko Y.A., Kalyuzhnaya M.G.;
RT   "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT   Methylomicrobium alcaliphilum 20Z.";
RL   J. Bacteriol. 194:551-552(2012).
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, ECO:0000256|PROSITE-
CC         ProRule:PRU10106};
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:0000256|HAMAP-Rule:MF_01347}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01347}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01347}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral
CC       membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC       subfamily. {ECO:0000256|ARBA:ARBA00024342}.
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DR   EMBL; FO082060; CCE22035.1; -; Genomic_DNA.
DR   RefSeq; WP_014146844.1; NC_016112.1.
DR   AlphaFoldDB; G4SWW9; -.
DR   STRING; 1091494.MEALZ_0335; -.
DR   KEGG; mah:MEALZ_0335; -.
DR   PATRIC; fig|271065.3.peg.347; -.
DR   HOGENOM; CLU_022398_0_2_6; -.
DR   OMA; AACHFQQ; -.
DR   Proteomes; UP000008315; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:InterPro.
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   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:000003; 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; 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   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}; Cell inner membrane {ECO:0000256|HAMAP-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|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01347}; Hydrolase {ECO:0000313|EMBL:CCE22035.1};
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:UP000008315};
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          6..71
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          128..340
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          349..424
FT                   /note="ATP synthase A/B type C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF22919"
FT   BINDING         148..155
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
FT   SITE            338
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10106"
SQ   SEQUENCE   460 AA;  50157 MW;  A308E41F21F7F2CC CRC64;
     MSLGKIVQII GAVVDVEFPR ESLPKVYDAL KVEDKNLVLE VQQQLGDGVV RSIAMGSTDG
     LSRGLQVSNS GAPIAVPVGQ KTLGRIMNVL GEPIDEKGAI GEDERWAIHR EAPSYDEQAA
     SNELLETGIK VIDLVCPFAK GGKVGLFGGA GVGKTVNMME LIRNIAIEHS GFSVFAGVGE
     RTREGNDFYH EMTDSKVIDK VSLVYGQMNE PPGNRLRVAL TGLTMAEFFR EEGRDVLFFV
     DNIYRYTLAG TEVSALLGRM PSAVGYQPNL AEEMGVLQER ITSTKTGSIT SIQAVYVPAD
     DLTDPSPATT FAHLDATVVL SRQIAELGIY PAIDPLDSTS RQLDPLVIGH EHYNVARAVQ
     GTLQRYKELR DIIAILGMDE LSEEDKLIVS RARKIQRFLS QPFFVAEVFT GSPGKYVSLK
     DTIAGFKGII DGEYDHVPEQ AFYMVGTIDE ALEKAKGMKK
//