ID   ATPB_FERIS              Reviewed;         472 AA.
AC   O50341;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
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   Fervidobacterium islandicum.
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=2423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49647 / DSM 5733 / H21;
RX   PubMed=9588802; DOI=10.1002/elps.1150190416;
RA   Ludwig W., Strunk O., Klugbauer S., Klugbauer N., Weizenegger M.,
RA   Neumaier J., Bachleitner M., Schleifer K.H.;
RT   "Bacterial phylogeny based on comparative sequence analysis.";
RL   Electrophoresis 19:554-568(1998).
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; Y15789; CAA75783.1; -; Genomic_DNA.
DR   RefSeq; WP_033191080.1; NZ_CP014334.1.
DR   AlphaFoldDB; O50341; -.
DR   SMR; O50341; -.
DR   STRING; 2423.NA23_0201480; -.
DR   eggNOG; COG0055; Bacteria.
DR   OrthoDB; 430176at2; -.
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..472
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000144441"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   472 AA;  51890 MW;  0A97381256CFDC70 CRC64;
     MSKKSVGKIV RIIGPVVDVK FQEGDLPDIY DALVVINPQT GKKLILEVEQ LIGDNIVRTV
     AMDSTDGLVR GLEVENTGEP IKAPVGRGVL GRMFNVIGEP IDEQGELKDI EYWPIHRPAP
     SMTEQKTEIE ILETGLKVID LLAPFPKGGK IGFFGGAGVG KTVLVMEMIR NIAIEHHGFS
     IFAGVGERTR EGNDLYLEMT EAGVLNNTVL VFGQMNEPPG ARFRVALTAL TIAEYFRDVE
     GRDVLLFIDN IFRFVQAGSE VSALLGRMPS AVGYQPTLST DMGELQERIT STKKGSITSV
     QAIYVPADDI TDPAPATTFT HLDATIVLSR QLAALGLYPA VDPLDSTSKI LDPNIVGKEH
     YEVARGVQEV LQRYKDLQDI IAILGMEELS EEDKLIVQRA RKIQRFLTQP THVAERFSGI
     PGVYVPIKET IRGFKEILEG RYDDLPEAAF YMVGTIDEAV EKAKKLMKSA VI