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Database: UniProt
Entry: A0A430FR32_9BIFI
LinkDB: A0A430FR32_9BIFI
Original site: A0A430FR32_9BIFI 
ID   A0A430FR32_9BIFI        Unreviewed;       103 AA.
AC   A0A430FR32;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=ATP synthase F0F1 subunit epsilon {ECO:0000313|EMBL:RSX55281.1};
GN   ORFNames=D2E24_1416 {ECO:0000313|EMBL:RSX55281.1};
OS   Bifidobacterium samirii.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=2306974 {ECO:0000313|EMBL:RSX55281.1, ECO:0000313|Proteomes:UP000287470};
RN   [1] {ECO:0000313|EMBL:RSX55281.1, ECO:0000313|Proteomes:UP000287470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2033B {ECO:0000313|EMBL:RSX55281.1,
RC   ECO:0000313|Proteomes:UP000287470};
RA   Lugli G.A., Duranti S., Milani C.;
RT   "Characterization of the phylogenetic diversity of five novel species
RT   belonging to the genus Bifidobacterium.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU003656}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. 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|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:RSX55281.1}.
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DR   EMBL; QXGK01000014; RSX55281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A430FR32; -.
DR   OrthoDB; 9791445at2; -.
DR   Proteomes; UP000287470; 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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 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,
KW   ECO:0000256|RuleBase:RU003656};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003656};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU003656}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287470};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003656}.
FT   DOMAIN          9..87
FT                   /note="ATP synthase F1 complex delta/epsilon subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02823"
SQ   SEQUENCE   103 AA;  10960 MW;  4D57235CA4BB134D CRC64;
     MADSSRTLLQ VNIVAADHPV WHGEAQSVTI PASSGGMGIL PNHEPVLTVI RNGLVTLVDA
     EGGRHTFEVT DGFISFDSNK LTVAVERGHD VVRTSDEEPA DAE
//
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