ID   VATE_NATPD              Reviewed;         192 AA.
AC   Q3ITD1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=V-type ATP synthase subunit E;
DE   AltName: Full=V-ATPase subunit E {ECO:0000255|HAMAP-Rule:MF_00311};
GN   Name=atpE {ECO:0000255|HAMAP-Rule:MF_00311}; OrderedLocusNames=NP_1024A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00311}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00311}.
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DR   EMBL; CR936257; CAI48603.1; -; Genomic_DNA.
DR   RefSeq; WP_011322238.1; NC_007426.1.
DR   AlphaFoldDB; Q3ITD1; -.
DR   SMR; Q3ITD1; -.
DR   STRING; 348780.NP_1024A; -.
DR   EnsemblBacteria; CAI48603; CAI48603; NP_1024A.
DR   GeneID; 3702542; -.
DR   KEGG; nph:NP_1024A; -.
DR   eggNOG; arCOG00869; Archaea.
DR   HOGENOM; CLU_120786_0_0_2; -.
DR   OMA; YAGNIDC; -.
DR   OrthoDB; 93762at2157; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.2320.30; -; 1.
DR   HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR   InterPro; IPR038495; ATPase_E_C.
DR   InterPro; IPR002842; ATPase_V1_Esu.
DR   Pfam; PF01991; vATP-synt_E; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..192
FT                   /note="V-type ATP synthase subunit E"
FT                   /id="PRO_1000059420"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..46
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   192 AA;  21656 MW;  A5AD40EC7DAEFF2A CRC64;
     MSLDTVVEDI RDEARARADE IRSEGEERAE EIIDEAEREA DDIVDEAERE AERKISQERD
     QKLSSAKLEA KQARLEARRE VLEEVHDDVE AQIADIDGDE REALTRSLLD AAAEEFDGDS
     VRVHGHEDDA DLLEGIVADY DGFEVGEPVD CLGGVVVESD ASRVRVNNTF DSILEDVWEE
     NLREISARLF EE