ID   ATPE_WOLPP              Reviewed;         113 AA.
AC   B3CN18;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=WP1158;
OS   Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=570417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wPip;
RX   PubMed=18550617; DOI=10.1093/molbev/msn133;
RA   Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA   Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT   "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL   Mol. Biol. Evol. 25:1877-1887(2008).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00530};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR   EMBL; AM999887; CAQ55266.1; -; Genomic_DNA.
DR   RefSeq; WP_012482002.1; NC_010981.1.
DR   AlphaFoldDB; B3CN18; -.
DR   SMR; B3CN18; -.
DR   STRING; 570417.WP1158; -.
DR   EnsemblBacteria; CAQ55266; CAQ55266; WP1158.
DR   KEGG; wpi:WP1158; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_2157366_0_0_5; -.
DR   OMA; NNCSIIT; -.
DR   OrthoDB; 1696893at2; -.
DR   Proteomes; UP000008814; 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; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Transport.
FT   CHAIN           1..113
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_1000127906"
SQ   SEQUENCE   113 AA;  12778 MW;  9A6615BE11E70A85 CRC64;
     MNTFKVQFFS PDNRISFDEV VSLSVNGLEG ELVILAYHSP YLIYLLPGII TAQMSNQTKE
     KVVIDNGILE VANNNCSIIT NQIQVFDHLT HDEESLKDKR VGIYLSYLDV KSL