ID   ATPE_ACEWD              Reviewed;         133 AA.
AC   P50009; H6LG97;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 127.
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; OrderedLocusNames=Awo_c02240;
OS   Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS   / WB1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=931626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX   PubMed=7748890; DOI=10.1016/0005-2728(95)00037-j;
RA   Forster A., Daniel R., Mueller V.;
RT   "The Na(+)-translocating ATPase of Acetobacterium woodii is a F1F0-type
RT   enzyme as deduced from the primary structure of its beta, gamma and epsilon
RT   subunits.";
RL   Biochim. Biophys. Acta 1229:393-397(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RA   Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA   Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT   "Complete genome sequence of Acetobacterium woodii.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-9.
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX   PubMed=8033902; DOI=10.1111/j.1432-1033.1994.tb18992.x;
RA   Reidlinger J., Mueller V.;
RT   "Purification of ATP synthase from Acetobacterium woodii and identification
RT   as a Na(+)-translocating F1F0-type enzyme.";
RL   Eur. J. Biochem. 223:275-283(1994).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a sodium gradient
CC       across the membrane.
CC   -!- ACTIVITY REGULATION: Inhibited by nitrate.
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}.
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DR   EMBL; U10505; AAA79909.1; -; Genomic_DNA.
DR   EMBL; CP002987; AFA47033.1; -; Genomic_DNA.
DR   PIR; I39749; I39749.
DR   RefSeq; WP_014354636.1; NC_016894.1.
DR   AlphaFoldDB; P50009; -.
DR   SMR; P50009; -.
DR   STRING; 931626.Awo_c02240; -.
DR   TCDB; 3.A.2.1.5; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   EnsemblBacteria; AFA47033; AFA47033; Awo_c02240.
DR   KEGG; awo:Awo_c02240; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_1_3_9; -.
DR   OMA; MGGFAEI; -.
DR   OrthoDB; 1696893at2; -.
DR   Proteomes; UP000007177; 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   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; 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   1: Evidence at protein level;
KW   ATP synthesis; Cell membrane; CF(1); Direct protein sequencing;
KW   Ion transport; Membrane; Reference proteome; Sodium; Sodium transport;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8033902"
FT   CHAIN           2..133
FT                   /note="ATP synthase epsilon chain, sodium ion specific"
FT                   /id="PRO_0000188084"
SQ   SEQUENCE   133 AA;  14837 MW;  99245EEC4B363E69 CRC64;
     MAETFRLKII APTGVFFDDD IERVVIRGIE GELAILAEHT PLTTNVAIGT FNIIFADKKK
     KNGTLLGGIA TINPRETIIL TDAAEWPEEI DIKRAQEAKE RALKRIHDDK FDTARARAAL
     ERAIARINSK ENV