ID A0A2H9LCE1_9ARCH Unreviewed; 100 AA.
AC A0A2H9LCE1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=V-type ATP synthase subunit F {ECO:0000256|ARBA:ARBA00020758, ECO:0000256|HAMAP-Rule:MF_00312};
DE AltName: Full=V-ATPase subunit F {ECO:0000256|HAMAP-Rule:MF_00312};
GN Name=atpF {ECO:0000256|HAMAP-Rule:MF_00312};
GN ORFNames=COT15_01075 {ECO:0000313|EMBL:PIU21676.1};
OS Candidatus Diapherotrites archaeon CG08_land_8_20_14_0_20_34_12.
OC Archaea; Candidatus Diapherotrites.
OX NCBI_TaxID=1974404 {ECO:0000313|EMBL:PIU21676.1, ECO:0000313|Proteomes:UP000229798};
RN [1] {ECO:0000313|EMBL:PIU21676.1, ECO:0000313|Proteomes:UP000229798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG08_land_8_20_14_0_20_34_12 {ECO:0000313|EMBL:PIU21676.1};
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|HAMAP-Rule:MF_00312}.
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit family.
CC {ECO:0000256|ARBA:ARBA00010148, ECO:0000256|HAMAP-Rule:MF_00312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIU21676.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PEXL01000015; PIU21676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9LCE1; -.
DR Proteomes; UP000229798; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; ATPase, V1 complex, subunit F; 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; AtpF-like; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_00312};
KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00312};
KW Hydrolase {ECO:0000313|EMBL:PIU21676.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00312};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00312}.
SQ SEQUENCE 100 AA; 11295 MW; 86B880105E279F37 CRC64;
MQIAIVGSDD FITGFRLAGI KALYETNGQD IDRKMQGMIE IEDIGIIVLR EEDYQKVGLA
TKRKLEKMVS PVIITLAGEE KSSLRELIKR SIGVDLWKEK
//