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ATPE_ELUMP
ID   ATPE_ELUMP              Reviewed;         135 AA.
AC   B2KEX4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=ATP synthase epsilon chain {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=F-ATPase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
GN   Name=atpC {ECO:0000255|HAMAP-Rule:MF_00530}; OrderedLocusNames=Emin_1523;
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191;
RX   PubMed=19270133; DOI=10.1128/aem.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(2009).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00530}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00530};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR   EMBL; CP001055; ACC99070.1; -; Genomic_DNA.
DR   RefSeq; WP_012415684.1; NC_010644.1.
DR   AlphaFoldDB; B2KEX4; -.
DR   SMR; B2KEX4; -.
DR   STRING; 445932.Emin_1523; -.
DR   EnsemblBacteria; ACC99070; ACC99070; Emin_1523.
DR   KEGG; emi:Emin_1523; -.
DR   HOGENOM; CLU_084338_2_1_0; -.
DR   OrthoDB; 1696893at2; -.
DR   Proteomes; UP000001029; 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: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; -; 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   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..135
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_1000146330"
FT   REGION          83..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   135 AA;  15359 MW;  258C9AF3440B4761 CRC64;
     MKKLTFSFIS PERPIVQNQE ADFVALPAFE GEMGVLPGHV NSVVILMPGF VRFKNNGEEK
     EFAIIDGFAE VFKDHIDVFA SEASLSEEKQ SEEQKQRLER AKKALSSQDA DIDIELAEIQ
     LKTQILKMKM KKRKM
 
 
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