ATPA_MOOTA
ID ATPA_MOOTA Reviewed; 507 AA.
AC Q2RFX7; O05431;
DT 30-MAY-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 alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=Moth_2380;
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 alpha chain is a regulatory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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_01346};
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_01346, 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_01346}.
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DR EMBL; U64318; AAB51464.1; -; Genomic_DNA.
DR EMBL; CP000232; ABC20662.1; -; Genomic_DNA.
DR RefSeq; WP_011393857.1; NC_007644.1.
DR RefSeq; YP_431205.1; NC_007644.1.
DR AlphaFoldDB; Q2RFX7; -.
DR SMR; Q2RFX7; -.
DR STRING; 264732.Moth_2380; -.
DR PRIDE; Q2RFX7; -.
DR EnsemblBacteria; ABC20662; ABC20662; Moth_2380.
DR KEGG; mta:Moth_2380; -.
DR PATRIC; fig|264732.11.peg.2593; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_9; -.
DR OMA; LQAPGVM; -.
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 CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 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..507
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000238288"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 363
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT CONFLICT 221
FT /note="T -> I (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> P (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="R -> G (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="A -> P (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="N -> T (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="G -> A (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="G -> A (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="G -> A (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="A -> G (in Ref. 1; AAB51464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 55639 MW; D4D12EB63E72FC3A CRC64;
MSIRPDEITS ILKNQIEQYQ LEVEMAEVGT VTQVGDGIAR IYGLDRAMAG ELLEFPGDIY
GMVLNLEEDN VGAVILGPYT HIKEGDQVKR TGRIVEVPVG EALIGRVVNA MGQPIDGKGP
IQTDKFRPVE SPAPGVVYRQ PVNTPLQTGL KAIDSMVPIG RGQRELIIGD RQTGKTAIAV
DTIINQKGQN VICIYVAIGQ KASTVAGVVQ RLEEAGAMEY TIVVMATASE PAPMLYIAPY
AGCTMGEYFM YEQHRDVLCV YDDLSKHAAA YRELSLLLRR PPGREAYPGD VFYLHSRLLE
RAARLNDSLG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLESDLF YAGQRPAINV
GLSVSRVGGA AQIKAMKQVA GRLRLDLAQY RELAAFAQFG SDLDKATQAR LARGERMMEI
LKQDQYQPMP VEEQVVVLYA AVNGFLDDLP VARVRAFEKD FLRFLRNERP EVLAGIREKR
QLDDNLQEQL KKSIEDFKGS FTAAGES
