VATE_PYRAB
ID VATE_PYRAB Reviewed; 199 AA.
AC Q9UXU4; G8ZKU7;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=V-type ATP synthase subunit E;
DE AltName: Full=V-ATPase subunit E;
GN Name=atpE; OrderedLocusNames=PYRAB17640; ORFNames=PAB1182;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50669.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71238.1; -; Genomic_DNA.
DR PIR; G75028; G75028.
DR RefSeq; WP_010868883.1; NC_000868.1.
DR AlphaFoldDB; Q9UXU4; -.
DR SMR; Q9UXU4; -.
DR STRING; 272844.PAB1182; -.
DR EnsemblBacteria; CAB50669; CAB50669; PAB1182.
DR GeneID; 1496067; -.
DR KEGG; pab:PAB1182; -.
DR PATRIC; fig|272844.11.peg.1883; -.
DR eggNOG; arCOG00869; Archaea.
DR HOGENOM; CLU_105846_1_0_2; -.
DR OMA; YAGNIDC; -.
DR OrthoDB; 93762at2157; -.
DR PhylomeDB; Q9UXU4; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 PANTHER; PTHR45715; PTHR45715; 1.
DR Pfam; PF01991; vATP-synt_E; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Hydrogen ion transport; Ion transport; Transport.
FT CHAIN 1..199
FT /note="V-type ATP synthase subunit E"
FT /id="PRO_0000117320"
SQ SEQUENCE 199 AA; 23133 MW; F9230F07A89D5BD6 CRC64;
MSGAELIIQE INREAERKIE YILNEAREEA EKIKEEAKRR AESKAEWILR RAKTQAELEK
QRIIANARLE VRRKRLAVQE EIIRNVLDEV RKRLQEMPEE EYFESIKALL KEAVEELKEG
KVRVYSNERT LALISSRIEE IRDYLGSISI EIGSAISTMG GVIVETEDGR IRIDNTFEAR
MERFEGEIRA KIAKVLFGG