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Database: UniProt
Entry: A0A0R1JKC4_9LACO
LinkDB: A0A0R1JKC4_9LACO
Original site: A0A0R1JKC4_9LACO 
ID   A0A0R1JKC4_9LACO        Unreviewed;       134 AA.
AC   A0A0R1JKC4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   ORFNames=FD02_GL002003 {ECO:0000313|EMBL:KRK71758.1};
OS   Lacticaseibacillus nasuensis JCM 17158.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK71758.1, ECO:0000313|Proteomes:UP000051804};
RN   [1] {ECO:0000313|EMBL:KRK71758.1, ECO:0000313|Proteomes:UP000051804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK71758.1,
RC   ECO:0000313|Proteomes:UP000051804};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRK71758.1}.
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DR   EMBL; AZDJ01000026; KRK71758.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1JKC4; -.
DR   STRING; 1291734.FD02_GL002003; -.
DR   PATRIC; fig|1291734.4.peg.2054; -.
DR   Proteomes; UP000051804; 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; 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   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:UP000051804};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00530}.
FT   DOMAIN          2..80
FT                   /note="ATP synthase F1 complex delta/epsilon subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02823"
FT   DOMAIN          85..131
FT                   /note="ATP synthase epsilon subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00401"
SQ   SEQUENCE   134 AA;  14651 MW;  A75C9B5EBBF36554 CRC64;
     MNIVTPDGLV YNHHATLVVV KTTAGELGLM AKHEPVVAPL TIGEVRVRRV DNPGHEDAIA
     VNGGFMEMSD NVASIVADSA ERERDIDLSR AEAARTRAQR RIEAAKAHDD VDELQRAQVS
     LQRAINRIHV KTGK
//
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