ID   ATPE_MYCLE              Reviewed;         121 AA.
AC   P45822;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   25-MAY-2022, entry version 131.
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=ML1146;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA63105.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U15186; AAA63105.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL583920; CAC31527.1; -; Genomic_DNA.
DR   PIR; D87052; D87052.
DR   RefSeq; NP_301840.1; NC_002677.1.
DR   RefSeq; WP_010908164.1; NC_002677.1.
DR   AlphaFoldDB; P45822; -.
DR   BMRB; P45822; -.
DR   SMR; P45822; -.
DR   STRING; 272631.ML1146; -.
DR   EnsemblBacteria; CAC31527; CAC31527; CAC31527.
DR   KEGG; mle:ML1146; -.
DR   PATRIC; fig|272631.5.peg.2068; -.
DR   Leproma; ML1146; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_4_0_11; -.
DR   OMA; MGGFAEI; -.
DR   Proteomes; UP000000806; 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; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   Pfam; PF02823; ATP-synt_DE_N; 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..121
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188161"
SQ   SEQUENCE   121 AA;  13338 MW;  629DF3A63F93603B CRC64;
     MDELNIEIVA VDRKIWSGKG TFLFTRTTAG EIGILPRHIP MVAQLVDDNM VRIEREGEKD
     LRVAVDGGFL SVTEERVSIL AESAEFDSEI DENAAKQDAE SDDPRIAARG RARLRAVGAI
     D