ID   YCHF_BUCAI              Reviewed;         362 AA.
AC   P57288;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 122.
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=BU191;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB12908.1; -; Genomic_DNA.
DR   RefSeq; NP_240022.1; NC_002528.1.
DR   RefSeq; WP_009874148.1; NC_002528.1.
DR   AlphaFoldDB; P57288; -.
DR   SMR; P57288; -.
DR   STRING; 107806.10038873; -.
DR   EnsemblBacteria; BAB12908; BAB12908; BAB12908.
DR   KEGG; buc:BU191; -.
DR   PATRIC; fig|107806.10.peg.202; -.
DR   eggNOG; COG0012; Bacteria.
DR   HOGENOM; CLU_018395_0_1_6; -.
DR   OMA; VLRCFDN; -.
DR   Proteomes; UP000001806; 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..362
FT                   /note="Ribosome-binding ATPase YchF"
FT                   /id="PRO_0000201672"
FT   DOMAIN          3..255
FT                   /note="OBG-type G"
FT   DOMAIN          277..360
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   362 AA;  41157 MW;  D567BB9541CF9277 CRC64;
     MGFKCGIIGL PNVGKSTLFN LLTKGNSAVA NFPFCTIKPN IGIVPVIDER INNLNQIVSP
     QKTVNAFIEF IDIAGLVKGA SQGEGLGNQF LGNIRDVHAI AHVVRCFKDD NITHIYNQVQ
     PIKDIDIINS ELILSDFDLC EKTILKLQKK TLLKNKETQE KINTLKKCLN HLKQFFMLKT
     LNLNKTEKQL ISYLRFLTLK PTMYIANINE EKESYYFLDK LNEIAKKEGS IVIPIHANLE
     LDLVKMSDEE KKSFMKLFNI KTLGLNSIIS SGYHLLNLIT FFTVGDKEIR AWAIPNGSTS
     IEAAHKIHSD FSKGFIRAQI IKYVDFITYK SEAKIKEMGK FRTEGKQYYI QDGDIIHFLF
     NV