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Database: UniProt
Entry: A0A1Q6A1C8_9SPHI
LinkDB: A0A1Q6A1C8_9SPHI
Original site: A0A1Q6A1C8_9SPHI 
ID   A0A1Q6A1C8_9SPHI        Unreviewed;        84 AA.
AC   A0A1Q6A1C8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=ATP synthase epsilon chain {ECO:0000313|EMBL:OKS87813.1};
GN   ORFNames=RG47T_3276 {ECO:0000313|EMBL:OKS87813.1};
OS   Mucilaginibacter polytrichastri.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1302689 {ECO:0000313|EMBL:OKS87813.1, ECO:0000313|Proteomes:UP000186720};
RN   [1] {ECO:0000313|EMBL:OKS87813.1, ECO:0000313|Proteomes:UP000186720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RG4-7 {ECO:0000313|EMBL:OKS87813.1,
RC   ECO:0000313|Proteomes:UP000186720};
RA   Li Y.;
RT   "Whole Genome Sequencing of Mucilaginibacter polytrichastri RG4-7(T)
RT   isolated from the moss sample.";
RL   Submitted (NOV-2016) 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: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {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:OKS87813.1}.
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DR   EMBL; MPPL01000001; OKS87813.1; -; Genomic_DNA.
DR   RefSeq; WP_074490363.1; NZ_MPPL01000001.1.
DR   AlphaFoldDB; A0A1Q6A1C8; -.
DR   STRING; 1302689.RG47T_3276; -.
DR   OrthoDB; 5294255at2; -.
DR   Proteomes; UP000186720; Unassembled WGS sequence.
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:UP000186720};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003656}.
FT   DOMAIN          2..79
FT                   /note="ATP synthase F1 complex delta/epsilon subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02823"
SQ   SEQUENCE   84 AA;  9048 MW;  5ABA0B2EE1F4DD3B CRC64;
     MILEILTPDK KVFEGEVASV TVPGTLGSFE ILNNHAPIIS TLEDGKLIVR AGNNAKQEVF
     LIHGGVVEVL DNKVMVLAEG ITHR
//
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