ID   ATPE_PROMO              Reviewed;         137 AA.
AC   P29709;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=ATP synthase epsilon chain, sodium ion specific;
DE   AltName: Full=F-ATPase epsilon subunit, sodium ion specific;
DE   AltName: Full=Na(+)-translocating ATPase subunit epsilon;
GN   Name=atpC; Synonyms=uncC;
OS   Propionigenium modestum.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Propionigenium.
OX   NCBI_TaxID=2333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 2376 / Gra Succ2;
RX   PubMed=1533602; DOI=10.1016/0378-1097(92)90559-7;
RA   Krumholz L.R., Esser U., Simoni R.D.;
RT   "Characterization of the genes coding for the F1F0 subunits of the sodium
RT   dependent ATPase of Propionigenium modestum.";
RL   FEMS Microbiol. Lett. 70:37-41(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-8.
RX   PubMed=8422943; DOI=10.1016/0014-5793(93)81742-i;
RA   Gerike U., Dimroth P.;
RT   "N-terminal amino acid sequences of the subunits of the Na(+)-translocating
RT   F1F0 ATPase from Propionigenium modestum.";
RL   FEBS Lett. 316:89-92(1993).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a sodium 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   -!- MISCELLANEOUS: The ATPase of P.modestum is of special interest because
CC       it uses sodium ions instead of protons as the physiological coupling
CC       ion.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; X58461; CAA41375.1; -; Genomic_DNA.
DR   PIR; S29042; S29042.
DR   AlphaFoldDB; P29709; -.
DR   SMR; P29709; -.
DR   TCDB; 3.A.2.1.2; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
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   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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; Cell inner membrane; Cell membrane; CF(1);
KW   Direct protein sequencing; Ion transport; Membrane; Sodium;
KW   Sodium transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8422943"
FT   CHAIN           2..137
FT                   /note="ATP synthase epsilon chain, sodium ion specific"
FT                   /id="PRO_0000188178"
SQ   SEQUENCE   137 AA;  15351 MW;  A5E75684CF7AD928 CRC64;
     MATFKLEVVT PLKKVLDRDA EMVIMRTIEG DMGVMADHAP FVAELAVGEM KIKSANGEEA
     YFVSGGFLEI SKEKTMILAD EAIDVKEIDV ERAKREAEIA KETLVKLKED KDIAVTQKSL
     QEALTKVRIA EQYMHHL