ID   YCHF_ECO57              Reviewed;         363 AA.
AC   P0ABU3; P31216; P76018;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 108.
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=Z1974, ECs1708;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG56061.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35131.1; -; Genomic_DNA.
DR   PIR; D90842; D90842.
DR   RefSeq; NP_309735.1; NC_002695.1.
DR   RefSeq; WP_000505866.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0ABU3; -.
DR   SMR; P0ABU3; -.
DR   STRING; 155864.EDL933_1907; -.
DR   EnsemblBacteria; AAG56061; AAG56061; Z1974.
DR   EnsemblBacteria; BAB35131; BAB35131; ECs_1708.
DR   GeneID; 66674977; -.
DR   GeneID; 913155; -.
DR   KEGG; ece:Z1974; -.
DR   KEGG; ecs:ECs_1708; -.
DR   PATRIC; fig|386585.9.peg.1806; -.
DR   eggNOG; COG0012; Bacteria.
DR   HOGENOM; CLU_018395_0_1_6; -.
DR   OMA; VLRCFDN; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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_0000201676"
FT   DOMAIN          3..256
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;  39667 MW;  9C2DAFFAC7586F53 CRC64;
     MGFKCGIVGL PNVGKSTLFN ALTKAGIEAA NFPFCTIEPN TGVVPMPDPR LDQLAEIVKP
     QRTLPTTMEF VDIAGLVKGA SKGEGLGNQF LTNIRETEAI GHVVRCFEND NIIHVSGKVN
     PADDIEVINT ELALADLDTC ERAIHRVQKK AKGGDKDAKA ELAVLEKCLP QLENAGMLRA
     LDLSAEEKAA IRYLSFLTLK PTMYIANVNE DGFENNPYLD QVREIAAKEG SVVVPVCAAV
     EADIAELDDE ERDEFMQELG LEEPGLNRVI RAGYKLLNLQ TYFTAGVKEV RAWTIPVGAT
     APQAAGKIHT DFEKGFIRAQ TISFEDFITY KGEQGAKEAG KMRAEGKDYI VKDGDVMNFL
     FNV