ID   ATPB_STRLI              Reviewed;         478 AA.
AC   P0A301; P50004;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 83.
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};
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RC   STRAIN=66 / 1326;
RX   PubMed=7828915; DOI=10.1016/0378-1119(95)00673-t;
RA   Hensel M., Lill H., Schmid R., Deckers-Hebestreit G., Altendorf K.;
RT   "The ATP synthase (F1F0) of Streptomyces lividans: sequencing of the atp
RT   operon and phylogenetic considerations with subunit beta.";
RL   Gene 152:11-17(1995).
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; Z22606; CAA80327.1; -; Genomic_DNA.
DR   PIR; S37547; S37547.
DR   AlphaFoldDB; P0A301; -.
DR   SMR; P0A301; -.
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   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1);
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7828915"
FT   CHAIN           2..478
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000144479"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   478 AA;  52178 MW;  1E1C0A6C5B92EF56 CRC64;
     MTTTVETATA TGRVARVIGP VVDVEFPVDA MPEIYNALHV EVADPAKEGE LKTLTLEVAQ
     HLGDGLVRTI SMQPTDGLIR QAPVTDTGAA ISVPVGDFTK GKVFNTLGEV LNVDEQYTGE
     RWPIHRKAPN FDELESKTEM FETGVKVIDL LTPYVKGGKI GLFGGAGVGK TVLIQEMIYR
     VANNHDGVSV FAGVGERTRE GNDLIDEMSE SGVIDKTALV FGQMDEPPGT RLRVALAGLT
     MAEYFRDVQK QDVLFFIDNI FRFTQAGSEV STLLGRMPSA VGYQPNLADE MGLLQERITS
     TRGHSITSMQ AIYVPADDLT DPAPATTFAH LDATTVLSRP ISEKGIYPAV DPLDSTSRIL
     DPRYIAAEHY NAAMRVKNIL QKYKDLQDII AILGIDELGE EDKLVVHRAR RVERFLSQNT
     HVAKQFTGVD GSDVPLDESI AAFNAICDGE YDHFPEQAFF MCGGIEDLKN NAKELGVS