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Database: UniProt
Entry: Q39RR1_GEOMG
LinkDB: Q39RR1_GEOMG
Original site: Q39RR1_GEOMG 
ID   Q39RR1_GEOMG            Unreviewed;       364 AA.
AC   Q39RR1;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN   Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944,
GN   ECO:0000313|EMBL:ABB33063.1};
GN   OrderedLocusNames=Gmet_2845 {ECO:0000313|EMBL:ABB33063.1};
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB33063.1, ECO:0000313|Proteomes:UP000007073};
RN   [1] {ECO:0000313|EMBL:ABB33063.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB33063.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RX   PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA   Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT   "The genome sequence of Geobacter metallireducens: features of metabolism,
RT   physiology and regulation common and dissimilar to Geobacter
RT   sulfurreducens.";
RL   BMC Microbiol. 9:109-109(2009).
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; CP000148; ABB33063.1; -; Genomic_DNA.
DR   RefSeq; WP_004514571.1; NC_007517.1.
DR   AlphaFoldDB; Q39RR1; -.
DR   STRING; 269799.Gmet_2845; -.
DR   KEGG; gme:Gmet_2845; -.
DR   eggNOG; COG0012; Bacteria.
DR   HOGENOM; CLU_018395_0_1_7; -.
DR   Proteomes; UP000007073; Chromosome.
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:UP000007073}.
FT   DOMAIN          3..257
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   DOMAIN          279..362
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   364 AA;  39794 MW;  7DDE9A4A41A1BE1C CRC64;
     MGFNCGIVGL PNVGKSTIFN ALTSAGAESA NYPFCTIDPN VGIVQVPDER LERLAEIVNP
     ERILPTTIEF VDIAGLVKGA SQGEGLGNQF LGHIRSVDAI VHVVRCFDDE NVVHVSGSVD
     PIRDIEVIQT ELALADLDSV EKKFQRVEKQ AKGGDRKLKD ESEFYARVKG ALEKGTPGRH
     VEVGDDERLW MRDLHLLTDK PVLYVANVAE DDLEGAHPFV AKVRDLAESE GARVVVICGR
     IESEIAELDG DEKKVFLAEM GLAESGLDRL IRMGYDLLGL ITYFTAGKKE VRAWTIPAGT
     KAPQAAGVIH SDFEKGFIRA EVIAYRDFVA AGGETGAKEK GLMRLEGKEY VVQDGDVMHF
     RFNV
//
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