ID   ATPB_PECFR              Reviewed;         470 AA.
AC   Q03235;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 117.
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   Pectinatus frisingensis.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Pectinatus.
OX   NCBI_TaxID=865;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20465 / MKK 1;
RA   Klugbauer N., Ludwig W., Bauerlein E., Schleifer K.H.;
RT   "Subunit beta of adenosine triphosphate synthase of Pectinatus frisingensis
RT   and Lactobacillus casei.";
RL   Syst. Appl. Microbiol. 15:323-330(1992).
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; X64543; CAA45841.1; -; Genomic_DNA.
DR   PIR; S30598; S30598.
DR   AlphaFoldDB; Q03235; -.
DR   SMR; Q03235; -.
DR   PRIDE; Q03235; -.
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..470
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000144458"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   470 AA;  50983 MW;  1D8956B5CED01F2C CRC64;
     MAKGKIVQVI GPVVDIEFPA EELPSILNAI TIKGKSGDID INLTVEVMQH LGDGITRCIA
     MSSTDGLTRG MEAVDTGSPI KVPVGEETLG RVFNVLGQTV DHNPAPVGNK EFWPIHRPAP
     KFDEQETSTQ ILETGIKVVD LIAPYSRGGK IGLFGGAGVG KTVLIMELIH NIATQHGGYS
     VFSGVGERTR EGNDLWSEMT ESGVINKTAL VYGQMNEPPG ARMRVALTGL TMAEYFRDVQ
     HQDVLLFIDN IFRFIQAGSE VSALLGRMPS AVGYQPTLTT DVGALQERIT STKKGSITSV
     QAVYVPADDL TDPGPAATFT HLDATTVLSR QIAELGIYPA VDPLDSTSRI LDPHVIGEDH
     YEVARGVQAV LQKYKELQDI IAILGMEELS DADKLTVARA RKIQRFLSQP FFVAEQFTGS
     PGKYVPLKET IRGFKEILEG KYDDLPESAF YMVGSIDEAV EAAKKIKQEA