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Database: UniProt
Entry: A0A0J1JRZ1_9GAMM
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ID   A0A0J1JRZ1_9GAMM        Unreviewed;       140 AA.
AC   A0A0J1JRZ1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
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:KLV05027.1};
GN   ORFNames=ABT57_22415 {ECO:0000313|EMBL:KLV05027.1};
OS   Photobacterium ganghwense.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV05027.1, ECO:0000313|Proteomes:UP000035909};
RN   [1] {ECO:0000313|EMBL:KLV05027.1, ECO:0000313|Proteomes:UP000035909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV05027.1,
RC   ECO:0000313|Proteomes:UP000035909};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) 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}.
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:KLV05027.1}.
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DR   EMBL; LDOU01000028; KLV05027.1; -; Genomic_DNA.
DR   RefSeq; WP_047887491.1; NZ_PYMI01000013.1.
DR   AlphaFoldDB; A0A0J1JRZ1; -.
DR   STRING; 320778.ABT57_22415; -.
DR   PATRIC; fig|320778.3.peg.4806; -.
DR   OrthoDB; 9791445at2; -.
DR   Proteomes; UP000035909; 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; 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:KLV05027.1};
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:UP000035909};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00530}.
FT   DOMAIN          6..85
FT                   /note="ATP synthase F1 complex delta/epsilon subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02823"
FT   DOMAIN          89..134
FT                   /note="ATP synthase epsilon subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00401"
FT   COILED          86..113
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   140 AA;  15046 MW;  40D92C74A6E7338D CRC64;
     MAAITFHLDV VSAEKRLFSG RAENIQVTGS EGELGIHAGH TPLLTAITPG MVRITKQHGG
     EEVIYLSGGM LEVQPGAVTV LADTAIRGED LDRAKAEEAK RQAEERIHNQ HGDIDFAQAA
     SDLAKAIAQL RVIELTKKAR
//
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