ATPB_MOOTA
ID ATPB_MOOTA Reviewed; 462 AA.
AC Q2RFX9; O05433;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
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}; OrderedLocusNames=Moth_2378;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND OPERON STRUCTURE.
RX PubMed=9171425; DOI=10.1128/jb.179.11.3746-3755.1997;
RA Das A., Ljungdahl L.G.;
RT "Composition and primary structure of the F1F0 ATP synthase from the
RT obligately anaerobic bacterium Clostridium thermoaceticum.";
RL J. Bacteriol. 179:3746-3755(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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 (By similarity). In this bacterium the a and b subunits are transcribed
CC but do not seem to be translated, thus the ATP synthase consists of the
CC alpha, beta, gamma, delta, epsilon and c subunits. {ECO:0000255|HAMAP-
CC Rule:MF_01347, ECO:0000269|PubMed:9171425}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; U64318; AAB51466.1; -; Genomic_DNA.
DR EMBL; CP000232; ABC20660.1; -; Genomic_DNA.
DR RefSeq; WP_011393855.1; NC_007644.1.
DR RefSeq; YP_431203.1; NC_007644.1.
DR AlphaFoldDB; Q2RFX9; -.
DR SMR; Q2RFX9; -.
DR STRING; 264732.Moth_2378; -.
DR PRIDE; Q2RFX9; -.
DR EnsemblBacteria; ABC20660; ABC20660; Moth_2378.
DR GeneID; 61291101; -.
DR KEGG; mta:Moth_2378; -.
DR PATRIC; fig|264732.11.peg.2591; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_9; -.
DR OMA; GFNMIMD; -.
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 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..462
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000254300"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 228
FT /note="A -> P (in Ref. 1; AAB51466)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..236
FT /note="AEG -> PEA (in Ref. 1; AAB51466)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="A -> P (in Ref. 1; AAB51466)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="G -> A (in Ref. 1; AAB51466)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> P (in Ref. 1; AAB51466)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="A -> P (in Ref. 1; AAB51466)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="A -> V (in Ref. 1; AAB51466)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="E -> D (in Ref. 1; AAB51466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50451 MW; E5A874B6E620E96D CRC64;
MNEGQVVQVI GPVVDVEFAS DRLPDLYNAI TIKTDKINIT MEAMQHLGNN TVRCVALSST
DGLQRGMKAV DTGQPITVPV GRATLGRLFN VLGEPIDNQG PVETTERLPI HRPAPSFEEQ
QPSTEVLETG IKVVDLLAPY AKGGKIGLFG GAGVGKTVLI MELIRNIAYE HGGFSVFSGV
GERTREGNDL YLEMKESGVL EKTALVFGQM NEPPGARLRV GLTGLTMAEY FRDAEGQDVL
LFIDNIFRFV QAGSEVSALL GRMPSAVGYQ PTLATEMGAL QERITSTKKG SITSVQAIYV
PADDLTDPAP ATTFAHLDAT TVLSRQIAEL GIYPAVDPLD STSRILDPRV LGEEHYQVAR
GVQQVLQRYK ELQDIIAILG MDELSEEDKL IVARARKIQR FLSQPFHVAE AFTGQPGVYV
PLKETIRGFK EILEGRHDNL PEQAFYMVGT IDEAVKKGQE LM
