ATP6_MOOTA
ID ATP6_MOOTA Reviewed; 218 AA.
AC Q2RFX3; O05428;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=Moth_2384;
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, TRANSCRIPT, AND OPERON
RP 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: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
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_01393, ECO:0000269|PubMed:9171425}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51460.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U64318; AAB51460.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000232; ABC20666.1; -; Genomic_DNA.
DR RefSeq; WP_011393861.1; NC_007644.1.
DR RefSeq; YP_431209.1; NC_007644.1.
DR AlphaFoldDB; Q2RFX3; -.
DR SMR; Q2RFX3; -.
DR STRING; 264732.Moth_2384; -.
DR EnsemblBacteria; ABC20666; ABC20666; Moth_2384.
DR KEGG; mta:Moth_2384; -.
DR PATRIC; fig|264732.11.peg.2597; -.
DR eggNOG; COG0356; Bacteria.
DR HOGENOM; CLU_041018_2_2_9; -.
DR OMA; FTHAVRL; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..218
FT /note="ATP synthase subunit a"
FT /id="PRO_0000362350"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 218 AA; 24723 MW; E83F4F294FA575F5 CRC64;
MTHVRPVEIF HLGPIPIYST VVNTWIIMIL LLAGIFLATR KLSFIPRGAQ HVLEMFLEFF
YGLLEEIIGK EGRRYLPLVA TLFIFILSLN LSWFIPGMKP PTMDLSTTAA FAVTTIILVQ
IFGIRKLGLR GYIRHFFQPA PFLFPLNVIE ELVKPVSLSL RLFGNLFGEE MVVTILFLMI
PFLLPTPIML LGVLMGTIQA FVFTLLTITY IANFVHGH
