ID   ATPE_STRR6              Reviewed;         139 AA.
AC   P63668; Q7BDA6; Q97PT7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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}; OrderedLocusNames=spr1359;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=11580837; DOI=10.1046/j.1365-2958.2001.02597.x;
RA   Martin-Galiano A.J., Ferrandiz M.J., de la Campa A.G.;
RT   "The promoter of the operon encoding the F0F1 ATPase of Streptococcus
RT   pneumoniae is inducible by pH.";
RL   Mol. Microbiol. 41:1327-1338(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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 three main
CC       subunits: a, b and c. {ECO:0000255|HAMAP-Rule:MF_00530,
CC       ECO:0000269|PubMed:11580837}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11580837};
CC       Peripheral membrane protein {ECO:0000305|PubMed:11580837}.
CC   -!- INDUCTION: Induced by a decrease in external pH from 7.5 to 5.7.
CC       {ECO:0000269|PubMed:11580837}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR   EMBL; AF368465; AAL66417.1; -; Genomic_DNA.
DR   EMBL; AE007317; AAL00163.1; -; Genomic_DNA.
DR   PIR; F98041; F98041.
DR   RefSeq; NP_358952.1; NC_003098.1.
DR   RefSeq; WP_000068050.1; NC_003098.1.
DR   AlphaFoldDB; P63668; -.
DR   SMR; P63668; -.
DR   STRING; 171101.spr1359; -.
DR   EnsemblBacteria; AAL00163; AAL00163; spr1359.
DR   GeneID; 60233555; -.
DR   GeneID; 66806597; -.
DR   KEGG; spr:spr1359; -.
DR   PATRIC; fig|171101.6.peg.1473; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_1_0_9; -.
DR   OMA; MGGFAEI; -.
DR   Proteomes; UP000000586; 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); IBA:GO_Central.
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:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..139
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188218"
SQ   SEQUENCE   139 AA;  15638 MW;  972D40440D879172 CRC64;
     MAQLTVQIVT PDGLVYDHHA SYVSVRTLDG EMGILPRHEN MIAVLAVDEV KVKRIDDKDH
     VNWIAVNGGV IEIANDMITI VADSAERARD IDISRAERAK LRAERAIEEA QDKHLIDQER
     RAKIALQRAI NRINVGNRL