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Database: UniProt
Entry: Q11GC4_CHESB
LinkDB: Q11GC4_CHESB
Original site: Q11GC4_CHESB 
ID   Q11GC4_CHESB            Unreviewed;       367 AA.
AC   Q11GC4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN   Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944};
GN   OrderedLocusNames=Meso_2159 {ECO:0000313|EMBL:ABG63551.1};
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG63551.1};
RN   [1] {ECO:0000313|EMBL:ABG63551.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BNC1 {ECO:0000313|EMBL:ABG63551.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL   Submitted (JUN-2006) 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}.
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DR   EMBL; CP000390; ABG63551.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11GC4; -.
DR   STRING; 266779.Meso_2159; -.
DR   KEGG; mes:Meso_2159; -.
DR   eggNOG; COG0012; Bacteria.
DR   HOGENOM; CLU_018395_0_1_5; -.
DR   OrthoDB; 9810373at2; -.
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00944}.
FT   DOMAIN          3..282
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   DOMAIN          282..365
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   367 AA;  39588 MW;  B26A149718538D55 CRC64;
     MGFKCGIVGL PNVGKSTLFN ALTKTAAAQA ANYPFCTIEP NTGEVAVPDP RLKKIAEIAA
     SKETVPTRIS FVDIAGLVRG ASKGEGLGNQ FLANIREVDA VVHVLRCFED DDITHVEGRI
     DPVADADTVE TELMLADLES LERRIVQVRK RATGKEKEAM SILPVMEEAL KLLQDGKPVR
     LVAAELDPEG MRILRSLNLL TSKPVLYVCN VAEGDAATGN AHTSAVEKMA EAQGARTVII
     SAAIEAEVAQ LPQEEAAEYL EAMGLHEPGL DRLIRAGYEL LDLITFFTAG PKEARAWTVQ
     KGAKAPQAAG VIHTDFERGF IRAQTIAYDD FVQLGGETAA REAGKARDEG KDYVVQDGDV
     MLFKFNV
//
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