VATE_PYRHO
ID VATE_PYRHO Reviewed; 198 AA.
AC O57724;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=V-type ATP synthase subunit E;
DE AltName: Full=V-ATPase subunit E;
GN Name=atpE; OrderedLocusNames=PH1978;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR EMBL; BA000001; BAA31105.1; -; Genomic_DNA.
DR PIR; B71214; B71214.
DR RefSeq; WP_010886042.1; NC_000961.1.
DR PDB; 2DM9; X-ray; 1.85 A; A/B=1-198.
DR PDB; 2DMA; X-ray; 2.05 A; A=1-198.
DR PDB; 4DT0; X-ray; 3.65 A; A=2-198.
DR PDBsum; 2DM9; -.
DR PDBsum; 2DMA; -.
DR PDBsum; 4DT0; -.
DR AlphaFoldDB; O57724; -.
DR SMR; O57724; -.
DR STRING; 70601.3258422; -.
DR EnsemblBacteria; BAA31105; BAA31105; BAA31105.
DR GeneID; 1442824; -.
DR KEGG; pho:PH1978; -.
DR eggNOG; arCOG00869; Archaea.
DR OMA; YAGNIDC; -.
DR OrthoDB; 93762at2157; -.
DR BRENDA; 7.1.2.2; 5244.
DR EvolutionaryTrace; O57724; -.
DR Proteomes; UP000000752; 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; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR038495; ATPase_E_C.
DR InterPro; IPR002842; ATPase_V1_Esu.
DR PANTHER; PTHR45715; PTHR45715; 1.
DR Pfam; PF01991; vATP-synt_E; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Hydrogen ion transport; Ion transport;
KW Transport.
FT CHAIN 1..198
FT /note="V-type ATP synthase subunit E"
FT /id="PRO_0000117322"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:2DM9"
FT HELIX 99..117
FT /evidence="ECO:0007829|PDB:2DM9"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:2DM9"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:2DM9"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:2DM9"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2DM9"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:2DM9"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2DM9"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:2DM9"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:2DM9"
SQ SEQUENCE 198 AA; 22888 MW; 4B12A0485F897CD2 CRC64;
MNGAELIIQE INKEAERKIE YILNEARQQA EKIKEEARRN AEAKAEWIIR RAKTQAELEK
QRIIANARLE VRRKRLAIQE EIISSVLEEV KRRLETMSED EYFESVKALL KEAIKELNEK
KVRVMSNEKT LGLIASRIEE IKSELGDVSI ELGETVDTMG GVIVETEDGR IRIDNTFEAR
MERFEGEIRS TIAKVLFG