ID V7PVL7_9BACT Unreviewed; 369 AA.
AC V7PVL7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944};
GN ORFNames=O210_OD1C00001G0112 {ECO:0000313|EMBL:ETB63654.1};
OS Parcubacteria bacterium RAAC4_OD1_1.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1394712 {ECO:0000313|EMBL:ETB63654.1, ECO:0000313|Proteomes:UP000018547};
RN [1] {ECO:0000313|EMBL:ETB63654.1, ECO:0000313|Proteomes:UP000018547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA Castelle C.J., Thomas B.C., Banfield J.F.;
RT "Small genomes and sparse metabolisms of sediment-associated bacteria from
RT four candidate phyla.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S
CC ribosomal subunit in a nucleotide-independent manner.
CC {ECO:0000256|HAMAP-Rule:MF_00944}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00944}.
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:ETB63654.1}.
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DR EMBL; AWSN01000001; ETB63654.1; -; Genomic_DNA.
DR AlphaFoldDB; V7PVL7; -.
DR STRING; 1394712.O210_OD1C00001G0112; -.
DR PATRIC; fig|1394712.3.peg.108; -.
DR Proteomes; UP000018547; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR CDD; cd04867; TGS_YchF_OLA1; 1.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.150.300; TGS-like domain; 1.
DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom_sf.
DR InterPro; IPR013029; YchF_C.
DR InterPro; IPR041706; YchF_N.
DR NCBIfam; TIGR00092; redox-regulated ATPase YchF; 1.
DR PANTHER; PTHR23305; OBG GTPASE FAMILY; 1.
DR PANTHER; PTHR23305:SF18; OBG-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51710; G_OBG; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00944}; Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00944}; Reference proteome {ECO:0000313|Proteomes:UP000018547}.
FT DOMAIN 2..264
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT COILED 134..161
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00944"
SQ SEQUENCE 369 AA; 41246 MW; A4A4B776E4A1A545 CRC64;
MLSLGIVGLP NVGKSTLFNA LTKKGVPCEN YPFCTIDPSV GVVAVPDDRL WKLSEFSKSA
KTIPAAIEFV DIAGLVKGAS VGEGLGNKFL ANIREVDAIF EMVRIFPLKM DKEEEILHVM
GDIDPLRDIE IINLELILAD LETATKRKNN IQKEVKRIDK EAILEDEALS KLILTLESGK
LANTINFNEK EIEKIKQLSL LTMKPFIYGF NKRAGSANLD ESNPEIFKEL TDYIESMGSR
YVVIDAKIEH ELKDFEGEEK EMFRKELGGE DDGINNLITE GYKLLGLDTY FTTGEDETRA
WTIKKGSTAP VAGMAIHTDF KDKFIRAEVI NWQDLLNAGS YAEARAKGKV RIEGKEYIVK
DGDVVEFKI
//