ID   ATPE_MOOTA              Reviewed;         134 AA.
AC   O05434; Q2RFY0;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=ATP synthase epsilon chain {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=F-ATPase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
GN   Name=atpC {ECO:0000255|HAMAP-Rule:MF_00530}; OrderedLocusNames=Moth_2377;
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.
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, b and c (By similarity). In this bacterium the a and b
CC       subunits are transcribed but do not seem to be translated, thus the ATP
CC       synthase consists of the alpha, beta, gamma, delta, epsilon and c
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00530,
CC       ECO:0000269|PubMed:9171425}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U64318; AAB51467.1; -; Genomic_DNA.
DR   EMBL; CP000232; ABC20659.1; -; Genomic_DNA.
DR   RefSeq; WP_011393854.1; NC_007644.1.
DR   RefSeq; YP_431202.1; NC_007644.1.
DR   AlphaFoldDB; O05434; -.
DR   SMR; O05434; -.
DR   STRING; 264732.Moth_2377; -.
DR   EnsemblBacteria; ABC20659; ABC20659; Moth_2377.
DR   KEGG; mta:Moth_2377; -.
DR   PATRIC; fig|264732.11.peg.2590; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_2_0_9; -.
DR   OMA; MGGFAEI; -.
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   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 2.60.15.10; -; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR036794; ATP_F1_dsu/esu_C_sf.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020547; ATP_synth_F1_dsu/esu_C.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF00401; ATP-synt_DE; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF46604; SSF46604; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Transport.
FT   CHAIN           1..134
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188157"
SQ   SEQUENCE   134 AA;  14535 MW;  78F934A6E55AFC0E CRC64;
     MASLNLEIIT PERVVLQAEA ASVIAPGIQG YLGVLPEHAP LITPLQAGVV TCRRRERAEE
     RVAVSGGFLE AGPDQVIILA DTAERSEEID VEWARQARER AERRLRERPP GLDVARAEAA
     LRRAVARLKA AGAI