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ATPE_BUCAP
ID   ATPE_BUCAP              Reviewed;         138 AA.
AC   O51871;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 131.
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=BUsg_009;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9216881; DOI=10.1007/s002849900217;
RA   Clark M.A., Baumann P.;
RT   "The (F1F0) ATP synthase of Buchnera aphidicola (endosymbiont of aphids):
RT   genetic analysis of the putative ATP operon.";
RL   Curr. Microbiol. 35:84-89(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9516544; DOI=10.1007/pl00006760;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT   aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT   gidA, and rho.";
RL   Curr. Microbiol. 36:158-163(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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; AF008210; AAC38109.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67581.1; -; Genomic_DNA.
DR   AlphaFoldDB; O51871; -.
DR   SMR; O51871; -.
DR   STRING; 198804.BUsg_009; -.
DR   EnsemblBacteria; AAM67581; AAM67581; BUsg_009.
DR   KEGG; bas:BUsg_009; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_2_0_6; -.
DR   OMA; MGGFAEI; -.
DR   Proteomes; UP000000416; 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; 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; 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; Transport.
FT   CHAIN           1..138
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188112"
SQ   SEQUENCE   138 AA;  15629 MW;  F340D9D75FCE0840 CRC64;
     MDFYLDIVSV EKRIFSGLVD RIQVSGSEGE MGIYPGHTQL LSIIKPGVIY IFHKNKTEEC
     LYISGGILEV QPSVVSILAD VAIRGIDLDR KRVVKAKKQA EEYFKKETTN VKKDDVLLEI
     SKAIAKLRVL EIMDKFKK
 
 
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