ID   ATPE_RHOCA              Reviewed;         132 AA.
AC   P72248;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 105.
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   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=9440534; DOI=10.1128/jb.180.2.416-421.1998;
RA   Borghese R., Crimi M., Fava L., Melandri B.A.;
RT   "The ATP synthase atpHAGDC (F1) operon from Rhodobacter capsulatus.";
RL   J. Bacteriol. 180:416-421(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=GA;
RA   Gabellini N., Gao Z., Eckerskorn C., Lottspeich F., Oesterhelt D.;
RT   "Purification of the H+-ATPase from Rhodobacter capsulatus, identification
RT   of the F1F0 components and reconstitution of the active enzyme.";
RL   Biochim. Biophys. Acta 934:227-234(1988).
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 four main
CC       subunits: a, b, b' and c. {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC       {ECO:0000269|Ref.2}; Peripheral membrane protein {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; X99599; CAA67911.1; -; Genomic_DNA.
DR   RefSeq; WP_013068670.1; NZ_VIBE01000018.1.
DR   AlphaFoldDB; P72248; -.
DR   SMR; P72248; -.
DR   GeneID; 31491765; -.
DR   OMA; MTIHVDI; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042717; C:plasma membrane-derived chromatophore 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   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..132
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188189"
SQ   SEQUENCE   132 AA;  13504 MW;  599491D7CB8C3455 CRC64;
     MADTMQFDLV SPERRLASVA ASEVRLPGVE GDLTAMPGHA PVILSLRPGI LTVVSAAGTA
     EYAVTGGFAE VSGEKVTVLA ERGLTRAELT AAVHAEMLAE AKKVADAAHP SVADAAAKML
     ADMEALGSHI NL