ID K2G5N0_9BACT Unreviewed; 350 AA.
AC K2G5N0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944};
GN ORFNames=ACD_5C00166G0005 {ECO:0000313|EMBL:EKE25429.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE25429.1};
RN [1] {ECO:0000313|EMBL:EKE25429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKE25429.1}.
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DR EMBL; AMFJ01001174; EKE25429.1; -; Genomic_DNA.
DR AlphaFoldDB; K2G5N0; -.
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; 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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00944}.
FT DOMAIN 3..260
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00944"
SQ SEQUENCE 350 AA; 38915 MW; 1120090E3010209B CRC64;
MSLQIGIVGL PNVGKSTLFK ALTKNPVDIN NYPFCTIEPN VGVVKVPDIR LDKLSEMSQT
LKIVPAVIEF VDIAGIVKGA SEGEGLGNKF LANIREVDAI VQVVRVFENS NITHVHNKVD
PIGDIEVIET ELVLADLETV TKRIEKLQKD ARGNDKEAIA KLVVTERIKM TLEQGSLASM
TELDMSDQNT KLAVRELQLL TMKPFLYVYN VADVEAKIPD ELERRKHIKL DIKIEEELIE
MNEEEKAEMG LTSHIDDLIV AAYDLLGLQT YLTTGKQETR AWTIKKGATA PEAGAAIHTD
FQEKFIRADV IMWDKLIEIG SWGKAKEIGA VKTVGKDYIM SDGEVVEFKV
//
