ID   ATPE_STRMU              Reviewed;         138 AA.
AC   P95790;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 142.
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; OrderedLocusNames=SMU_1527;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   PubMed=8996091; DOI=10.1016/s0378-1119(96)00502-1;
RA   Smith A.J., Quivey R.G., Faustoferri R.C.;
RT   "Cloning and nucleotide sequence analysis of the Streptococcus mutans
RT   membrane-bound, proton-translocating ATPase operon.";
RL   Gene 183:87-96(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000250}.
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; U31170; AAD13384.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59177.1; -; Genomic_DNA.
DR   PIR; JC5742; JC5742.
DR   RefSeq; NP_721871.1; NC_004350.2.
DR   RefSeq; WP_002262939.1; NC_004350.2.
DR   AlphaFoldDB; P95790; -.
DR   SMR; P95790; -.
DR   STRING; 210007.SMU_1527; -.
DR   PRIDE; P95790; -.
DR   EnsemblBacteria; AAN59177; AAN59177; SMU_1527.
DR   GeneID; 66819082; -.
DR   KEGG; smu:SMU_1527; -.
DR   PATRIC; fig|210007.7.peg.1359; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_1_0_9; -.
DR   OMA; MGGFAEI; -.
DR   PhylomeDB; P95790; -.
DR   SABIO-RK; P95790; -.
DR   Proteomes; UP000002512; 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   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 membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..138
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188216"
SQ   SEQUENCE   138 AA;  15588 MW;  2BF01999C2EA5D2F CRC64;
     MAEMTVQIVT PDGLKYDHHA KFILVKTPNG ELGVLANHEN LIAPLEVHEM KIKRIDDDSH
     VDWVAVNGGI IEIKDNLVTI VADSAERERD IDLSRAERAK KRAEKAIEEA KEQHRIDEVQ
     RAQVALRRAL NRINVGSK