ID   ATPB_FUSBL              Reviewed;         478 AA.
AC   P05440;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 116.
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   Fuscovulum blasticum (Rhodobacter blasticus) (Rhodopseudomonas blastica).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Fuscovulum.
OX   NCBI_TaxID=1075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6209404; DOI=10.1016/0022-2836(84)90465-0;
RA   Tybulewicz V.L.J., Falk G., Walker J.E.;
RT   "Rhodopseudomonas blastica atp operon. Nucleotide sequence and
RT   transcription.";
RL   J. Mol. Biol. 179:185-214(1984).
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z00018; CAA77303.1; -; Genomic_DNA.
DR   PIR; S04675; S04675.
DR   AlphaFoldDB; P05440; -.
DR   SMR; P05440; -.
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 inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Translocase; Transport.
FT   CHAIN           1..478
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000144462"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   478 AA;  50803 MW;  5540A1AE9B6C8947 CRC64;
     MTMATTVSKG KVTQVIGAVV DVQFEGVLPA ILNALETTNN GKKLILEVAQ HLGENTVRCI
     AMDATEGLVR GAPVSDSGTP ISVPVGNATL GRILNVVGEP IDERGPIAAT EKRAIHQKAP
     DFQSQSTESQ ILVTGIKVID LLAPYSKGGK IGLFGGAGVG KTVLIQELIN NIAKVHSGYS
     VFAGVGERTR EGNDLYHEFI ESGVINIDDL EKSKVALVYG QMNEPPGARA RVALTGLTLA
     EQFRDQSGTD VLFFVDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG QLQERITSTK
     AGSITSVQAI YVPADDLTDP APATSFAHLD ATTTLSRAIS ELGIYPAVDP LDSTSRLMDP
     QILGEEHYNT ARAVQGILQR YKSLQDIIAI LGMDELSEED KLTVARARKI QRFLSQPFDV
     AQVFTGSPGV QVPLDKTIAS FKAVVAGEYD HLPEAAFYMV GDIEEAKAKA AKLAAAAA