ID   ATPE_ACIFI              Reviewed;         141 AA.
AC   P41171;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 99.
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;
OS   Acidithiobacillus ferridurans.
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=1232575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX   PubMed=7958772; DOI=10.1111/j.1574-6968.1994.tb07137.x;
RA   Brown L.D., Dennehy M.E., Rawlings D.E.;
RT   "The F1 genes of the F1F0 ATP synthase from the acidophilic bacterium
RT   Thiobacillus ferrooxidans complement Escherichia coli F1 unc mutants.";
RL   FEMS Microbiol. Lett. 122:19-26(1994).
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.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; M81087; AAA53128.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41171; -.
DR   SMR; P41171; -.
DR   STRING; 380394.Lferr_2806; -.
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 inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Transport.
FT   CHAIN           1..141
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188233"
SQ   SEQUENCE   141 AA;  15169 MW;  FB6A5A900C3681C4 CRC64;
     MAMTIDVRVV SAEGSIYAGV ADMVVAPGEM GELGILPRHA PLLTGLRPGE LRIIHGAETE
     YLFVNGGILE IQPDMVTVLA DSAERATDID EAKALAAKQA AEARMAGHTD QMEYAAAQAE
     LLEQIARLKT VQRLREQGFV R