ID   ATPB_MESH2              Reviewed;         471 AA.
AC   Q601Z5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=mhp055;
OS   Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=295358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232;
RX   PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA   Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA   Mahairas G.G.;
RT   "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT   swine mycoplasmosis.";
RL   J. Bacteriol. 186:7123-7133(2004).
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; AE017332; AAV27380.1; -; Genomic_DNA.
DR   RefSeq; WP_011205894.1; NC_006360.1.
DR   AlphaFoldDB; Q601Z5; -.
DR   SMR; Q601Z5; -.
DR   STRING; 295358.mhp055; -.
DR   EnsemblBacteria; AAV27380; AAV27380; mhp055.
DR   KEGG; mhy:mhp055; -.
DR   eggNOG; COG0055; Bacteria.
DR   HOGENOM; CLU_022398_0_2_14; -.
DR   OMA; GFNMIMD; -.
DR   PhylomeDB; Q601Z5; -.
DR   Proteomes; UP000006822; 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; Translocase; Transport.
FT   CHAIN           1..471
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000254302"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   471 AA;  51559 MW;  2E15183D32B2F5EC CRC64;
     MEKQENVGHI VQIFGPVIDV QFPNEHMPAI LSALEVKIND ESIIFEVAQH LGEGIVRAIA
     MSMTYNLSKG LEVYDTGSQI SVPVGKQVLS RMFNVLGQPI DGGKPLDSFI KNPIHANAPT
     YLEQKATSEI LVTGIKVIDL LIPFIKGGKI GLFGGAGVGK TVLVQELINN IASKHGGLSV
     FAGVGERSRE GNDLYFEMKK AGVLDKTALV FGQMNEPPGA RMRVALSALT MAEYFRDYEN
     QDVLLFIDNI FRFTQAGSEV STLLGRIPST VGYQPTLSTE MGQLQERITS TIRGSITSVQ
     AVYVPADDIT DPAPATTFSH LDAKTVLDRG IAALGIYPAV DPLASSSRAL EPNIVGKKHY
     LVAKKVVQIL QRFKELQDII AILGVDELSE SDKQVVARAR RIRNFLSQPF FVAQKFSGIQ
     GQFIKIQDTV NNFDELLSGK YDNIPEEAFL YVGTIDQALE KAKKMGWSEK N