ID   ATPE_PRIM1              Reviewed;         134 AA.
AC   P12699; D5DWG0;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=ATP synthase epsilon chain;
DE   AltName: Full=ATP synthase F1 sector epsilon subunit;
DE   AltName: Full=F-ATPase epsilon subunit;
GN   Name=atpC; OrderedLocusNames=BMQ_5147;
OS   Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=545693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2894831; DOI=10.1016/s0006-291x(88)80370-x;
RA   Hawthorne C.A., Brusilow W.S.A.;
RT   "Sequence of the genes for the beta and epsilon subunits of the ATP
RT   synthase of Bacillus megaterium QM B1551.";
RL   Biochem. Biophys. Res. Commun. 151:926-931(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551;
RX   PubMed=21705586; DOI=10.1128/jb.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000250}.
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.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; M20255; AAA82527.1; -; Genomic_DNA.
DR   EMBL; CP001983; ADE72125.1; -; Genomic_DNA.
DR   PIR; B28599; PWBSEM.
DR   RefSeq; WP_013059798.1; NC_014019.1.
DR   AlphaFoldDB; P12699; -.
DR   SMR; P12699; -.
DR   STRING; 545693.BMQ_5147; -.
DR   EnsemblBacteria; ADE72125; ADE72125; BMQ_5147.
DR   GeneID; 64144395; -.
DR   KEGG; bmq:BMQ_5147; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_1_3_9; -.
DR   OMA; MGGFAEI; -.
DR   OrthoDB; 1696893at2; -.
DR   Proteomes; UP000000935; 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   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   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..134
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188096"
SQ   SEQUENCE   134 AA;  14645 MW;  FF281609FEE4F8AC CRC64;
     MKTIHVSVVT PDGPVYESEV EMVSTRAQSG ELGILHGHIP MVAPLQIGAV RLKKASSTEL
     VAVSGGFLEV RPDKVTILAQ AAETAEEIDV ARAEEAKKRA EMRLDSKQDD VDVKRAEIAL
     KRAVNRLDIS QRKF