ID   VATF_PYRFU              Reviewed;         103 AA.
AC   Q8U4A7;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=V-type ATP synthase subunit F {ECO:0000255|HAMAP-Rule:MF_00312};
DE   AltName: Full=V-ATPase subunit F {ECO:0000255|HAMAP-Rule:MF_00312};
GN   Name=atpF {ECO:0000255|HAMAP-Rule:MF_00312}; OrderedLocusNames=PF0181;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00312}.
CC   -!- SIMILARITY: Belongs to the V-ATPase F subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00312}.
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DR   EMBL; AE009950; AAL80305.1; -; Genomic_DNA.
DR   RefSeq; WP_011011294.1; NZ_CP023154.1.
DR   PDB; 2QAI; X-ray; 2.40 A; A/B=1-103.
DR   PDBsum; 2QAI; -.
DR   AlphaFoldDB; Q8U4A7; -.
DR   SMR; Q8U4A7; -.
DR   STRING; 186497.PF0181; -.
DR   EnsemblBacteria; AAL80305; AAL80305; PF0181.
DR   GeneID; 41711972; -.
DR   KEGG; pfu:PF0181; -.
DR   PATRIC; fig|186497.12.peg.188; -.
DR   eggNOG; arCOG04102; Archaea.
DR   HOGENOM; CLU_135754_2_0_2; -.
DR   OMA; QIPDKFG; -.
DR   OrthoDB; 113093at2157; -.
DR   PhylomeDB; Q8U4A7; -.
DR   EvolutionaryTrace; Q8U4A7; -.
DR   Proteomes; UP000001013; Chromosome.
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; 3.40.50.10580; -; 1.
DR   HAMAP; MF_00312; ATP_synth_F_arch; 1.
DR   InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR   InterPro; IPR022944; ATPase_V1-cplx_fsu_bac/arc.
DR   InterPro; IPR036906; ATPase_V1_fsu_sf.
DR   Pfam; PF01990; ATP-synt_F; 1.
DR   SUPFAM; SSF159468; SSF159468; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; Hydrogen ion transport; Ion transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..103
FT                   /note="V-type ATP synthase subunit F"
FT                   /id="PRO_0000144822"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:2QAI"
FT   HELIX           9..18
FT                   /evidence="ECO:0007829|PDB:2QAI"
FT   STRAND          21..25
FT                   /evidence="ECO:0007829|PDB:2QAI"
FT   HELIX           30..44
FT                   /evidence="ECO:0007829|PDB:2QAI"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:2QAI"
FT   HELIX           56..62
FT                   /evidence="ECO:0007829|PDB:2QAI"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:2QAI"
FT   HELIX           89..96
FT                   /evidence="ECO:0007829|PDB:2QAI"
SQ   SEQUENCE   103 AA;  11740 MW;  2BCA7C129AF1E02F CRC64;
     MKIVVMGDSD TVVGFRLAGV HEAYEYDESL ESVERARNKL RELLERDDVG IILITERLAQ
     RIGSLPEVKF PIILQIPDKF GSIYGEDILR DVVRRAIGVE LKR