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YCHF_BUCBP
ID   YCHF_BUCBP              Reviewed;         363 AA.
AC   Q89AR6;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Ribosome-binding ATPase YchF {ECO:0000255|HAMAP-Rule:MF_00944};
GN   Name=ychF {ECO:0000255|HAMAP-Rule:MF_00944}; Synonyms=engD;
GN   OrderedLocusNames=bbp_180;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S
CC       ribosomal subunit in a nucleotide-independent manner.
CC       {ECO:0000255|HAMAP-Rule:MF_00944}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00944}.
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DR   EMBL; AE016826; AAO26912.1; -; Genomic_DNA.
DR   RefSeq; WP_011091313.1; NC_004545.1.
DR   AlphaFoldDB; Q89AR6; -.
DR   SMR; Q89AR6; -.
DR   STRING; 224915.bbp_180; -.
DR   EnsemblBacteria; AAO26912; AAO26912; bbp_180.
DR   GeneID; 56470722; -.
DR   KEGG; bab:bbp_180; -.
DR   eggNOG; COG0012; Bacteria.
DR   HOGENOM; CLU_018395_0_1_6; -.
DR   OMA; VLRCFDN; -.
DR   OrthoDB; 603226at2; -.
DR   Proteomes; UP000000601; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   CDD; cd04867; TGS_YchF_OLA1; 1.
DR   CDD; cd01900; YchF; 1.
DR   Gene3D; 1.10.150.300; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF06071; YchF-GTPase_C; 1.
DR   PIRSF; PIRSF006641; CHP00092; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   TIGRFAMs; TIGR00092; TIGR00092; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..363
FT                   /note="Ribosome-binding ATPase YchF"
FT                   /id="PRO_0000201674"
FT   DOMAIN          3..257
FT                   /note="OBG-type G"
FT   DOMAIN          278..361
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00944"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  41674 MW;  ABD3986316D7A26C CRC64;
     MGFKCGFVGL PNVGKSTLFN YLTKLNIPAD NYPFCTIKSN VGIVPVLDNR LNKIAQVVCS
     NKIIPATIEL VDIAGLVKGA YKGEGLGNQF LDHIRDTNVI MHIVRCFENR YVTHIYGSVD
     PVRDVQIINL ELILSDIEVC KNRMCKLEIN KLSHNKQVNK ELLILKKCVY HLEKSKSLRS
     LNLTEEEIFV INYLRLITLK PVVYIFNISI DQSRNLYKRE IFDIIKNEHN AKTVNVCLDL
     MQSSKNDVSA YDHLSLKYKQ LFNKMLKNVI WAGFNALNLI TFFTAGKKEV HAWTTTNNLF
     IFQSVKCIHT DLSKGFIRAQ VISYDDFIKY KGEKRSKELG KIRIEGKRYV ICDGDIIHVL
     YNV
 
 
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