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Database: UniProt
Entry: E7N102_9FIRM
LinkDB: E7N102_9FIRM
Original site: E7N102_9FIRM 
ID   E7N102_9FIRM            Unreviewed;       145 AA.
AC   E7N102;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   ECO:0000313|EMBL:EFW30111.1};
GN   ORFNames=HMPREF9555_00653 {ECO:0000313|EMBL:EFW30111.1};
OS   Selenomonas artemidis F0399.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=749551 {ECO:0000313|EMBL:EFW30111.1, ECO:0000313|Proteomes:UP000004633};
RN   [1] {ECO:0000313|EMBL:EFW30111.1, ECO:0000313|Proteomes:UP000004633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0399 {ECO:0000313|EMBL:EFW30111.1,
RC   ECO:0000313|Proteomes:UP000004633};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) 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:EFW30111.1}.
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DR   EMBL; AECV01000008; EFW30111.1; -; Genomic_DNA.
DR   RefSeq; WP_009349331.1; NZ_GL638132.1.
DR   AlphaFoldDB; E7N102; -.
DR   STRING; 749551.HMPREF9555_00653; -.
DR   HOGENOM; CLU_084338_1_3_9; -.
DR   Proteomes; UP000004633; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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:SF10; ATP SYNTHASE EPSILON CHAIN, CHLOROPLASTIC; 1.
DR   Pfam; PF00401; ATP-synt_DE; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_00530}; Cell membrane {ECO:0000256|HAMAP-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   Hydrolase {ECO:0000313|EMBL:EFW30111.1};
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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00530}.
FT   DOMAIN          4..83
FT                   /note="ATP synthase F1 complex delta/epsilon subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02823"
FT   DOMAIN          87..139
FT                   /note="ATP synthase epsilon subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00401"
SQ   SEQUENCE   145 AA;  15539 MW;  00022D97D6ED5763 CRC64;
     MATIQLEIVS PDRVVYAADI DMLIARSTGG EIGILPKHIP LVTGLQPHAM KIHVDGGTEQ
     LFAVAGGFME VTPEKITVLA TAAEEPDEID INRAQRAYDR AQARLKRLRE GGVEDGGAAI
     DEHRAALALK RAVARLQATH TAVKA
//
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