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ATPB_ACIFI
ID   ATPB_ACIFI              Reviewed;         468 AA.
AC   P41168;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 113.
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   Acidithiobacillus ferridurans.
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=1232575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX   PubMed=7958772; DOI=10.1111/j.1574-6968.1994.tb07137.x;
RA   Brown L.D., Dennehy M.E., Rawlings D.E.;
RT   "The F1 genes of the F1F0 ATP synthase from the acidophilic bacterium
RT   Thiobacillus ferrooxidans complement Escherichia coli F1 unc mutants.";
RL   FEMS Microbiol. Lett. 122:19-26(1994).
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}.
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DR   EMBL; M81087; AAA53127.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41168; -.
DR   SMR; P41168; -.
DR   STRING; 380394.Lferr_2807; -.
DR   PRIDE; P41168; -.
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..468
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000144485"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   468 AA;  50610 MW;  A6039491D4390574 CRC64;
     MSERCKENAV GHIVQVIGPV IDVAFSRGQV PEIMEAIVVD ANNLTIEVQA QLGDGVARGI
     AMGPSEGLKR GLAVTRTGAP ISVPVGHATL GRIMNVLGEP VDGKGPVQTE DRQAIHRPAP
     AFDELAASTE VLETGIKVID LVCPFAKGGK VGLFGGAGVG KTVLMMELIR NIAIEHTGYS
     VFAGVGERTR EGNDFYHEMT DSGVLDKVAL VYGQMNEPPG NRLRAGLTGL TMAEHFRDEG
     RDILMFIDNI FRYPLAGTEV SALLGRMPSA VGYQPTLAEE MGQLQERITS TKVGSITSVQ
     AVYVPADDLT DPSPATTFAH LDATVVLSRQ IAELGIYPAL DPLDSFSRQL DPQIVGQEHY
     DVARSCQKTL QRYKELQDII AILGMDELSE DDKLLVSRAR KIQRYLSQPF FVAEVFTGSP
     GTYVSLKETI RAFKAIVAGE YDHLPEQAFY MVGTIDEALA KAQKLQQG
 
 
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