ID A0A252BQ22_9PROT Unreviewed; 138 AA.
AC A0A252BQ22;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=HK24_02515 {ECO:0000313|EMBL:OUJ09120.1};
OS Gluconobacter sp. DsW_058.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1511210 {ECO:0000313|EMBL:OUJ09120.1, ECO:0000313|Proteomes:UP000194786};
RN [1] {ECO:0000313|Proteomes:UP000194786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Winans N.J., Newell P.D., Douglas A.E.;
RL Submitted (JUN-2014) 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|ARBA:ARBA00003543, ECO:0000256|HAMAP-
CC 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:OUJ09120.1}.
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DR EMBL; JOPH01000002; OUJ09120.1; -; Genomic_DNA.
DR RefSeq; WP_046900215.1; NZ_JOPH01000002.1.
DR AlphaFoldDB; A0A252BQ22; -.
DR GeneID; 66594916; -.
DR Proteomes; UP000194786; 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; 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; 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; 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 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:UP000194786};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00530}.
FT DOMAIN 3..82
FT /note="ATP synthase F1 complex delta/epsilon subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02823"
SQ SEQUENCE 138 AA; 15136 MW; 86D245C02FB52591 CRC64;
MPLRIEIVSP EKRLVDRQVD MAVVPGMEGD IAAMPDRAPL MLQLRGGVVA LYEGDKIVDR
YFVGGGFADM GAEHCTILAD SAQLMSELSA DDARDRLRDL ETTWAQIEPN DTDAHDRLSR
EIQSVRAELE AVEGPASV
//
