ID U7UDD1_9FIRM Unreviewed; 102 AA.
AC U7UDD1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=V-type ATP synthase subunit F {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=HMPREF1253_1223 {ECO:0000313|EMBL:ERT57437.1};
OS Peptoniphilus sp. BV3C26.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1111134 {ECO:0000313|EMBL:ERT57437.1, ECO:0000313|Proteomes:UP000017105};
RN [1] {ECO:0000313|EMBL:ERT57437.1, ECO:0000313|Proteomes:UP000017105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3C26 {ECO:0000313|EMBL:ERT57437.1,
RC ECO:0000313|Proteomes:UP000017105};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-2013) 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:ERT57437.1}.
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; AWXB01000057; ERT57437.1; -; Genomic_DNA.
DR RefSeq; WP_023055895.1; NZ_AWXB01000057.1.
DR AlphaFoldDB; U7UDD1; -.
DR STRING; 1111134.HMPREF1253_1223; -.
DR PATRIC; fig|1111134.3.peg.1224; -.
DR eggNOG; COG1436; Bacteria.
DR OrthoDB; 5311at2; -.
DR Proteomes; UP000017105; Unassembled WGS sequence.
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; 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 Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00312}; Reference proteome {ECO:0000313|Proteomes:UP000017105};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00312}.
SQ SEQUENCE 102 AA; 11150 MW; 3851BDD4EF1C88F3 CRC64;
MYKIAVVGDK DSVLAFKALG VDVRVAYNKD DARHQVDSLA KDGYGVIFIT EQLASLIEET
IERYNSEVVP AVILIPSNKG TLNIGMDRIN KNVEKAVGSN IL
//
