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Database: UniProt
Entry: Q1Q3G9_KUEST
LinkDB: Q1Q3G9_KUEST
Original site: Q1Q3G9_KUEST 
ID   Q1Q3G9_KUEST            Unreviewed;       134 AA.
AC   Q1Q3G9;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 79.
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   ECO:0000313|EMBL:CAJ74559.1};
GN   ORFNames=KsCSTR_22890 {ECO:0000313|EMBL:QII11668.1}, KSMBR1_0120
GN   {ECO:0000313|EMBL:SOH02640.1}, kuste3796
GN   {ECO:0000313|EMBL:CAJ74559.1};
OS   Kuenenia stuttgartiensis.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Kuenenia.
OX   NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ74559.1};
RN   [1] {ECO:0000313|EMBL:CAJ74559.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16598256; DOI=10.1038/nature04647;
RA   Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., Taylor M.W.,
RA   Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N.,
RA   Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A.,
RA   Snel B., Dutilh B.E., OpDenCamp H.J.M., vanDerDrift C., Cirpus I.,
RA   vanDePas-Schoonen K.T., Harhangi H.R., vanNiftrik L., Schmid M.,
RA   Keltjens J., vanDeVossenberg J., Kartal B., Meier H., Frishman D.,
RA   Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M.,
RA   LePaslier D.;
RT   "Deciphering the evolution and metabolism of an anammox bacterium from a
RT   community genome.";
RL   Nature 440:790-794(2006).
RN   [2] {ECO:0000313|EMBL:CAJ74559.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SOH02640.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH02640.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000221734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Frank J.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QII11668.1, ECO:0000313|Proteomes:UP000501926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSTR1 {ECO:0000313|EMBL:QII11668.1,
RC   ECO:0000313|Proteomes:UP000501926};
RA   Ding C., Adrian L.;
RT   "Newly sequenced genome of strain CSTR1 showed variability in Candidatus
RT   Kuenenia stuttgartiensis genomes.";
RL   Submitted (FEB-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|HAMAP-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|HAMAP-Rule:MF_00530,
CC       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; CT573071; CAJ74559.1; -; Genomic_DNA.
DR   EMBL; CP049055; QII11668.1; -; Genomic_DNA.
DR   EMBL; LT934425; SOH02640.1; -; Genomic_DNA.
DR   KEGG; kst:KSMBR1_0120; -.
DR   OrthoDB; 277064at2; -.
DR   Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
DR   Proteomes; UP000501926; Chromosome.
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; 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; 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, 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:CAJ74559.1};
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:UP000221734};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00530}.
FT   DOMAIN          5..83
FT                   /note="ATP synthase F1 complex delta/epsilon subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02823"
FT   COILED          85..112
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   134 AA;  14852 MW;  0469DC4A6242BD95 CRC64;
     MTKTFDLEII TPMKTVFKGL VKNITAMGTQ GSFGILIDHA PFITELQTSI LTIKDEKDST
     VSFAVDGGFF EMVANKAIVL ADSCVTKEEI DIVKVREEKR SAEEALSKEE ARGQKEHVMA
     TLKRAETWLS LANK
//
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