ID K6DE63_9BACI Unreviewed; 135 AA.
AC K6DE63;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 18-JUN-2025, entry version 50.
DE RecName: Full=ATP synthase epsilon chain {ECO:0000256|ARBA:ARBA00014480, ECO:0000256|HAMAP-Rule:MF_00530};
DE AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000256|ARBA:ARBA00031795, ECO:0000256|HAMAP-Rule:MF_00530};
DE AltName: Full=F-ATPase epsilon subunit {ECO:0000256|ARBA:ARBA00030215, ECO:0000256|HAMAP-Rule:MF_00530};
GN Name=atpC {ECO:0000256|HAMAP-Rule:MF_00530,
GN ECO:0000313|EMBL:EKN66584.1};
GN ORFNames=BABA_15782 {ECO:0000313|EMBL:EKN66584.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN66584.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN66584.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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|ARBA:ARBA00004202,
CC ECO:0000256|HAMAP-Rule:MF_00530}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004202, ECO:0000256|HAMAP-Rule:MF_00530}.
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:EKN66584.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJLS01000115; EKN66584.1; -; Genomic_DNA.
DR RefSeq; WP_007086152.1; NZ_AJLS01000115.1.
DR AlphaFoldDB; K6DE63; -.
DR STRING; 1117379.BABA_15782; -.
DR PATRIC; fig|1117379.3.peg.3272; -.
DR eggNOG; COG0355; Bacteria.
DR OrthoDB; 9804110at2; -.
DR Proteomes; UP000006316; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; 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 FunFam; 1.20.5.440:FF:000001; ATP synthase epsilon chain; 1.
DR FunFam; 2.60.15.10:FF:000001; ATP synthase epsilon chain; 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 NCBIfam; NF001846; PRK00571.1-3; 1.
DR NCBIfam; NF009980; PRK13446.1; 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; 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|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_00530};
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_00530}; Hydrolase {ECO:0000313|EMBL:EKN66584.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000006316};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00530}.
FT DOMAIN 4..82
FT /note="ATP synthase F1 complex delta/epsilon subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02823"
FT DOMAIN 86..132
FT /note="ATP synthase epsilon subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00401"
FT COILED 90..117
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 135 AA; 15079 MW; 6A9F27D6799C5105 CRC64;
MKTIKVSVVT PDGPVYESDV EMVSTKAQSG ELGILPGHIP MVAPLEIGAV RLKKDGKTEF
IAVSGGFLEV RPDQVTILAQ AAETSEHIDV ERAQRAKERA EQRLKEQKLE HIDFRRAELA
MRRAINRLNV SEHRI
//
