ATPB_BUCAP
ID ATPB_BUCAP Reviewed; 466 AA.
AC Q07232; O51872; Q93V14;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 146.
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}; Synonyms=uncD;
GN OrderedLocusNames=BUsg_008;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9216881; DOI=10.1007/s002849900217;
RA Clark M.A., Baumann P.;
RT "The (F1F0) ATP synthase of Buchnera aphidicola (endosymbiont of aphids):
RT genetic analysis of the putative ATP operon.";
RL Curr. Microbiol. 35:84-89(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9516544; DOI=10.1007/pl00006760;
RA Clark M.A., Baumann L., Baumann P.;
RT "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT gidA, and rho.";
RL Curr. Microbiol. 36:158-163(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-314.
RX PubMed=7763501; DOI=10.1007/bf01577382;
RA Clark M.A., Baumann P.;
RT "Aspects of energy-yielding metabolism in the aphid, Schizaphis graminum,
RT and its endosymbiont: detection of gene fragments potentially coding for
RT the ATP synthase beta-subunit and glyceraldehyde-3-phosphate
RT dehydrogenase.";
RL Curr. Microbiol. 26:233-237(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-314.
RA Latorre A., Buades C., Sabater B., Moya A.;
RT "Effect of selection and random drift in the evolution of aphids
RT endosymbionts.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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; AF008210; AAC38110.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67580.1; -; Genomic_DNA.
DR EMBL; Z15147; CAA78853.1; -; Genomic_DNA.
DR EMBL; AJ247128; CAB95753.1; -; Genomic_DNA.
DR PIR; S37647; S37647.
DR AlphaFoldDB; Q07232; -.
DR SMR; Q07232; -.
DR STRING; 198804.BUsg_008; -.
DR PRIDE; Q07232; -.
DR EnsemblBacteria; AAM67580; AAM67580; BUsg_008.
DR KEGG; bas:BUsg_008; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_6; -.
DR OMA; GFNMIMD; -.
DR Proteomes; UP000000416; Chromosome.
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..466
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144427"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 280
FT /note="E -> G (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51349 MW; F0A1570A2DA470D9 CRC64;
MIATGKIIQI IGAVVDVEFD QNSVPKIYNA LEVKNKKIQL ILEVQQQLGA GIVRTIAMGS
TNGLKRGLIV IDLGHYIKVP VGQATLGRII NVLGKTIDNK GPLKNLDNSK LEYWEIHRSA
PSYQEQASSQ EILETGIKVI DLICPFSKGG KVGLFGGAGV GKTVNMMELI RNIAIEHSGY
SVFTGVGERT REGNDFYHEM KDSKVLDKVS LVYGQMNEPP GNRLRVAFTG LTIAEKFRDE
GRDVLLFIDN IYRYTLAGTE VSALLGRMPS AVGYQPTLAE EMGLLQERIT STKEGSITSV
QAVYVPADDL TDPSPATTFA HLDSTVTLSR QIAALGIYPA IDPLNSTSRQ LDPYIVGDEH
YDTARGVQSI LQRYQELKDI IAILGMDELS QEDKILVSRA RKIQRFLSQP FFVAEVFTGF
PGKYVSLKDN IRAFKGIIGG EFDNLPEQAF YMVGTIEEVI KKAKLL
