ID A0A1D9FL50_9CLOT Unreviewed; 364 AA.
AC A0A1D9FL50;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944};
GN ORFNames=BJL90_08410 {ECO:0000313|EMBL:AOY75914.1};
OS Clostridium formicaceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1497 {ECO:0000313|EMBL:AOY75914.1, ECO:0000313|Proteomes:UP000177894};
RN [1] {ECO:0000313|EMBL:AOY75914.1, ECO:0000313|Proteomes:UP000177894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27076 {ECO:0000313|EMBL:AOY75914.1,
RC ECO:0000313|Proteomes:UP000177894};
RA Bao T., Cheng C., Zhao J., Yang S.-T., Wang J., Wang M.;
RT "Complete Genome Sequence of Acetogen Clostridium formicoaceticum ATCC
RT 27076.";
RL Submitted (OCT-2016) 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; CP017603; AOY75914.1; -; Genomic_DNA.
DR RefSeq; WP_070966513.1; NZ_CP020559.1.
DR AlphaFoldDB; A0A1D9FL50; -.
DR STRING; 1497.BJL90_08410; -.
DR KEGG; cfm:BJL90_08410; -.
DR OrthoDB; 9807318at2; -.
DR Proteomes; UP000177894; 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}.
FT DOMAIN 1..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 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00944"
SQ SEQUENCE 364 AA; 40005 MW; DEABDD78E526273D CRC64;
MKLGIVGLPN VGKSTLFNAI TQAGAESANY PFCTIEPNVG VVAVPDDRLK FLTDLYQSEK
TIPAAIEFYD IAGLVRGASK GEGLGNKFLS HIREVASILQ VVRCFEDSNI THVEGSVNPL
RDIETINLEL IFSDLEMVEK RLQKSEKLAK GDKSLLAEVD LLKRIHSALE EGLSARSLEY
DEKELEILKT FNLLSMKPII YIANVAENEV ANEGADNPYV QQLKAFAKTE GAEVVVICAK
IEAEISELEE EEKAMFLEEL GLNQSGLDRL VQASYSLLGL ISYLTAGPKE VRAWTIKKGT
KAPQAAGKIH SDFERGFIRA EVVAFDALVS CGTYTAAKEK GLVRLEGKEY VVQDGDVILF
RFNV
//
