VATE_SULTO
ID VATE_SULTO Reviewed; 191 AA.
AC Q971B8; F9VNC5; P22722;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=V-type ATP synthase subunit E;
DE AltName: Full=Sul-ATPase delta chain;
DE AltName: Full=V-ATPase subunit E;
GN Name=atpE; Synonyms=atpD; OrderedLocusNames=STK_14350;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2147683; DOI=10.1016/s0021-9258(18)45768-7;
RA Denda K., Konishi J., Hajiro K., Oshima T., Date T., Yoshida M.;
RT "Structure of an ATPase operon of an acidothermophilic archaebacterium,
RT Sulfolobus acidocaldarius.";
RL J. Biol. Chem. 265:21509-21513(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane.
CC -!- SUBUNIT: Sul-ATPase is composed of six (or maybe five) subunits: alpha,
CC beta, delta, gamma, C (proteolipid), and possibly epsilon.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
CC -!- CAUTION: Was originally reported as originating from S.acidocaldarius.
CC {ECO:0000305|PubMed:2147683}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA72940.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M57236; AAA72940.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BA000023; BAK54571.1; -; Genomic_DNA.
DR RefSeq; WP_069168198.1; NC_003106.2.
DR AlphaFoldDB; Q971B8; -.
DR SMR; Q971B8; -.
DR STRING; 273063.STK_14350; -.
DR PRIDE; Q971B8; -.
DR EnsemblBacteria; BAK54571; BAK54571; STK_14350.
DR GeneID; 1459466; -.
DR KEGG; sto:STK_14350; -.
DR PATRIC; fig|273063.9.peg.1635; -.
DR eggNOG; arCOG00869; Archaea.
DR OMA; GGIKIYY; -.
DR Proteomes; UP000001015; 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..191
FT /note="V-type ATP synthase subunit E"
FT /id="PRO_0000117326"
SQ SEQUENCE 191 AA; 22280 MW; 7C16251FF2AF08C3 CRC64;
MVSFEDLLNY SLNEEKNKIT EEFKKILSEM NQIIDEAYAE VYREYSAKIT DLVNKNNDRI
RGEIAKMEIE NKRLISKEMD YWIENVKENA KKSLYEFVKT DNYKKGLESI ISREVSDGSI
IYCSPSDQKS ISDIIKKKKI SCKIVVDEKI VGGIKIYYPD KSLSKDFTLE TILNQVFDDI
RDKIAQILFG E