ID   ATPE2_CERS4             Reviewed;         146 AA.
AC   Q3HKH5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=ATP synthase epsilon chain 2 {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=ATP synthase F1 sector epsilon subunit 2 {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=F-ATPase epsilon subunit 2 {ECO:0000255|HAMAP-Rule:MF_00530};
GN   Name=atpC2 {ECO:0000255|HAMAP-Rule:MF_00530}; ORFNames=RSP_3930;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OG   Plasmid pRS241a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Finished sequence of plasmid A of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (OCT-2005) 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.
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; DQ232586; ABA81769.1; -; Genomic_DNA.
DR   RefSeq; WP_011836235.1; NZ_CP030273.1.
DR   RefSeq; YP_001033874.1; NC_009007.1.
DR   AlphaFoldDB; Q3HKH5; -.
DR   SMR; Q3HKH5; -.
DR   EnsemblBacteria; ABA81769; ABA81769; RSP_3930.
DR   KEGG; rsp:RSP_3930; -.
DR   PATRIC; fig|272943.9.peg.4347; -.
DR   OMA; LPHRLDC; -.
DR   Proteomes; UP000002703; Plasmid A.
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; IPR024037; Alt_ATP_synth_F1_esu.
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.
DR   TIGRFAMs; TIGR03166; alt_F1F0_F1_eps; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Plasmid;
KW   Reference proteome; Transport.
FT   CHAIN           1..146
FT                   /note="ATP synthase epsilon chain 2"
FT                   /id="PRO_0000265873"
SQ   SEQUENCE   146 AA;  15596 MW;  FDD1B7D9A46F7C76 CRC64;
     MSLTLRVTTP LAAVLEEEGL ASIRAEDASG GFGLLPGHVD LLTVIEAGVL RFRRPEGPWH
     FCAIRGGVLR ATGGRLVTVA CREAVPGEDL ARLEAGLKRQ AEAADQAARR ARGEQVRLHA
     NAIRSLMRHL DRAPGADLSG IVEAFE