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Database: UniProt
Entry: R6U424_9FIRM
LinkDB: R6U424_9FIRM
Original site: R6U424_9FIRM 
ID   R6U424_9FIRM            Unreviewed;       134 AA.
AC   R6U424;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=ATP synthase epsilon chain {ECO:0000256|HAMAP-Rule:MF_00530};
DE   AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000256|HAMAP-Rule:MF_00530};
DE   AltName: Full=F-ATPase epsilon subunit {ECO:0000256|HAMAP-Rule:MF_00530};
GN   Name=atpC {ECO:0000256|HAMAP-Rule:MF_00530};
GN   ORFNames=BN580_01654 {ECO:0000313|EMBL:CDC74866.1};
OS   Firmicutes bacterium CAG:272.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263015 {ECO:0000313|EMBL:CDC74866.1, ECO:0000313|Proteomes:UP000017938};
RN   [1] {ECO:0000313|EMBL:CDC74866.1, ECO:0000313|Proteomes:UP000017938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:272 {ECO:0000313|Proteomes:UP000017938};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00530,
CC       ECO:0000256|RuleBase:RU003656}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00530};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00530}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000256|ARBA:ARBA00005712, ECO:0000256|HAMAP-Rule:MF_00530,
CC       ECO:0000256|RuleBase:RU003656}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDC74866.1}.
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DR   EMBL; CBFW010000256; CDC74866.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6U424; -.
DR   STRING; 1263015.BN580_01654; -.
DR   Proteomes; UP000017938; Unassembled WGS sequence.
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; 1.20.5.440; ATP synthase delta/epsilon subunit, C-terminal domain; 1.
DR   Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 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; IPR020547; ATP_synth_F1_esu_C.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   NCBIfam; TIGR01216; ATP_synt_epsi; 1.
DR   PANTHER; PTHR13822; ATP SYNTHASE DELTA/EPSILON CHAIN; 1.
DR   PANTHER; PTHR13822:SF7; ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL; 1.
DR   Pfam; PF00401; ATP-synt_DE; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF46604; Epsilon subunit of F1F0-ATP synthase C-terminal domain; 1.
DR   SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_00530,
KW   ECO:0000256|RuleBase:RU003656};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00530};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_00530};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00530};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00530};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00530};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017938};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00530}.
FT   DOMAIN          5..80
FT                   /note="ATP synthase F1 complex delta/epsilon subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02823"
FT   DOMAIN          86..131
FT                   /note="ATP synthase epsilon subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00401"
SQ   SEQUENCE   134 AA;  15517 MW;  EAB9CBF14F09D7BA CRC64;
     MSVFMLEILT PKRQFFKGEV EALTCTLPDG ELTVLRAHRP MLAALEIGSL KIKSDGEWRN
     AFSSEGFIEV RPDEVLVFTQ DCEWPEEIDA VRAEEARERE LEKLRQKQSL IEYHQTQIAL
     NRAMARLRVK KTVN
//
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