ID   ATPE_BRUMB              Reviewed;         135 AA.
AC   C0RF49;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=BMEA_A1847;
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=546272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457;
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00530}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       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; CP001488; ACO01521.1; -; Genomic_DNA.
DR   RefSeq; WP_002964875.1; NC_012441.1.
DR   AlphaFoldDB; C0RF49; -.
DR   SMR; C0RF49; -.
DR   EnsemblBacteria; ACO01521; ACO01521; BMEA_A1847.
DR   GeneID; 45052754; -.
DR   GeneID; 55591396; -.
DR   KEGG; bmi:BMEA_A1847; -.
DR   HOGENOM; CLU_084338_2_1_5; -.
DR   OMA; MGGFAEI; -.
DR   Proteomes; UP000001748; Chromosome I.
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   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Transport.
FT   CHAIN           1..135
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_1000146312"
SQ   SEQUENCE   135 AA;  14482 MW;  FF4512C4E9576C33 CRC64;
     MAQAFQFELV SPERLLLSAQ VTEVVIPGSE GYLTALAGHS PLMTTIMPGV VSVKLADGKT
     DSYVVFGGFA DITPQGCTVL AESATHVDDI DPADIQHRID HARKVLEDAS SNEHRTKAEI
     FLHQLMTLQG AILPA