ID A0A0C4Y7P1_9BURK Unreviewed; 138 AA.
AC A0A0C4Y7P1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=F7R26_019985 {ECO:0000313|EMBL:QOT76371.1}, RR42_m4104
GN {ECO:0000313|EMBL:AJG21452.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG21452.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG21452.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG21452.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0000313|EMBL:QOT76371.1, ECO:0000313|Proteomes:UP000397656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 49340 {ECO:0000313|Proteomes:UP000397656}, and DSM 11853
RC {ECO:0000313|EMBL:QOT76371.1};
RA Salva-Serra F., Donoso R.A., Cho K.H., Yoo J.A., Lee K., Yoon S.-H.,
RA Perez-Pantoja D., Moore E.R.B.;
RT "Complete genome sequence of Cupriavidus basilensis CCUG 49340T.";
RL Submitted (OCT-2020) 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|ARBA:ARBA00011648,
CC ECO:0000256|HAMAP-Rule:MF_00530, 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}.
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DR EMBL; CP010536; AJG21452.1; -; Genomic_DNA.
DR EMBL; CP062803; QOT76371.1; -; Genomic_DNA.
DR RefSeq; WP_043350759.1; NZ_SUQM01000042.1.
DR AlphaFoldDB; A0A0C4Y7P1; -.
DR STRING; 68895.RR42_m4104; -.
DR KEGG; cbw:RR42_m4104; -.
DR OrthoDB; 9791445at2; -.
DR Proteomes; UP000031843; Chromosome main.
DR Proteomes; UP000397656; Chromosome 1.
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; 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: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}; Cell membrane {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_00530};
KW Hydrolase {ECO:0000313|EMBL:AJG21452.1};
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:UP000031843};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00530}.
FT DOMAIN 6..83
FT /note="ATP synthase F1 complex delta/epsilon subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02823"
FT DOMAIN 88..131
FT /note="ATP synthase epsilon subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00401"
FT COILED 87..118
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 138 AA; 14631 MW; DCE490BDEFBE182F CRC64;
MATILVDVVS AESSIFSGQA KFVALPGESG ELGILPGHTP LITRIQPGAV RIEKEDGSEE
FVFVAGGILE VQPKHVTVLA DTAIRGSDLD EAKAQEAKRA AEELMQNQSS DLDLARAQSE
LAVAAAQLAA IARLRRKR
//
