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Database: UniProt
Entry: A0A3M8FRD5_9BACT
LinkDB: A0A3M8FRD5_9BACT
Original site: A0A3M8FRD5_9BACT 
ID   A0A3M8FRD5_9BACT        Unreviewed;       367 AA.
AC   A0A3M8FRD5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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:RNC80531.1};
GN   ORFNames=ED559_01605 {ECO:0000313|EMBL:RNC80531.1};
OS   Phycisphaera sp.
OC   Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC   Phycisphaeraceae; Phycisphaera.
OX   NCBI_TaxID=2030824 {ECO:0000313|EMBL:RNC80531.1, ECO:0000313|Proteomes:UP000270436};
RN   [1] {ECO:0000313|EMBL:RNC80531.1, ECO:0000313|Proteomes:UP000270436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin4 {ECO:0000313|EMBL:RNC80531.1};
RA   Zheng Q., Wang Y., Jiao N.;
RT   "Metagenomics and metaproteomics analyze the interactions between
RT   Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT   Synechococcus culture.";
RL   Submitted (OCT-2018) 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:RNC80531.1}.
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DR   EMBL; RHLH01000001; RNC80531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8FRD5; -.
DR   Proteomes; UP000270436; 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:UP000270436}.
FT   DOMAIN          1..260
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         10..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00944"
SQ   SEQUENCE   367 AA;  39827 MW;  70FF22003B0E56D5 CRC64;
     MEAGIVGLPN VGKSTLFNAL TAAGALAANY PFATIEPNVG VVPIPDPRLK LINGHIETQK
     IVPAALRLVD IAGIVRGASE GEGLGNKFLS HIREVDAIVQ VVRCFEQQSG GDDVTHVDGS
     IDPIRDIETI QTELILADLQ TVENALPKAE RAVKARDPMD IARLSVLKKL LPILTEGKPA
     RVLELEDPAE VKALRMMTLI TSKKVLYVAN VDDTDPNGEG PLASKVRAHA EAEGMEMVPI
     CAKIESELSE LDEEDRAEML ADMGMDEPAL AKLARSAYRL LDQQSFYTAG PQEIRAWTVR
     VGSKAPQAAG VIHTDFEKGF IRAEVYSVSD LDELGSEKAI KEAGRLRVEG KDYVMRDADV
     CHFLFNV
//
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