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Database: UniProt
Entry: A0A0A2TL47_9FIRM
LinkDB: A0A0A2TL47_9FIRM
Original site: A0A0A2TL47_9FIRM 
ID   A0A0A2TL47_9FIRM        Unreviewed;       366 AA.
AC   A0A0A2TL47;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN   Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944};
GN   ORFNames=JT05_05160 {ECO:0000313|EMBL:KGP76394.1};
OS   Desulfosporosinus sp. Tol-M.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP76394.1, ECO:0000313|Proteomes:UP000030439};
RN   [1] {ECO:0000313|EMBL:KGP76394.1, ECO:0000313|Proteomes:UP000030439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Abu Laban N., Tan B., Dao A., Foght J.;
RT   "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT   probing of toluene- degrading methanogenic culture enriched from oil sands
RT   tailing of Alberta, Canada.";
RL   Submitted (OCT-2014) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KGP76394.1}.
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DR   EMBL; JQID01000071; KGP76394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2TL47; -.
DR   STRING; 1536651.JT05_05160; -.
DR   Proteomes; UP000030439; 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; IPR004095; TGS.
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.
DR   PROSITE; PS51880; TGS; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030439}.
FT   DOMAIN          3..259
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   DOMAIN          281..364
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00944"
SQ   SEQUENCE   366 AA;  40138 MW;  C01C8E787D94B74E CRC64;
     MTLHAGIVGL PNVGKSTLFN AITQAGAEAA NYPFCTIEPN VGMVEVPDFR LQKLAEMVHP
     KKIVPATVEF VDIAGLVQGA SQGEGLGNKF LSHIREVDAI VHVVRCFEDE NVVHVEGNVN
     PKRDIETIDL ELVLADMESV EKRIERSSKL LKTGGKKAQG ELALLERLKE VFNQGKGARF
     LTYTDEERVI LKGFSLLTLK PVLYVANVGE KSLSTAADNP YVQQVMAIAA EEGAEAIVVC
     AQIEAEIAEL EEGEKEVFLQ DLGLEESGLD HLIRVAFHLL GLMTFFTAGP MEVKAWTIHQ
     ATKAPQAAGV IHTDFEHGFI RAEVVAYKHF VGNNGLIGAR DKGLVRLEGK EYIMRDGDIV
     HFRFNV
//
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