ID   ATPE_STRSA              Reviewed;         139 AA.
AC   Q9ZJ00;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 91.
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}; Synonyms=uncC;
OS   Streptococcus sanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=10904;
RX   PubMed=12591869; DOI=10.1128/jb.185.5.1525-1533.2003;
RA   Kuhnert W.L., Quivey R.G. Jr.;
RT   "Genetic and biochemical characterization of the F-ATPase operon from
RT   Streptococcus sanguis 10904.";
RL   J. Bacteriol. 185:1525-1533(2003).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}.
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:0000255|HAMAP-Rule:MF_00530};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR   EMBL; AF001955; AAD00919.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZJ00; -.
DR   SMR; Q9ZJ00; -.
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; 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; 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; Transport.
FT   CHAIN           1..139
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188223"
SQ   SEQUENCE   139 AA;  15668 MW;  789D854CBFC5C79F CRC64;
     MAQMTVQIVT PDGLIYDHHA AFVSVKTIDG ELGILPRHIN TIAVLEVDQV KVRRVDDDKH
     IDWIAVNGGI IEIADNVITI VADSAERARD IDISRAERAK RRAELEIEEA HDKHLIDQER
     RAKIALQRAI NRINVGTRI