YCHF_BUCAP
ID YCHF_BUCAP Reviewed; 362 AA.
AC Q8K9V2;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
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=BUsg_185;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM67750.1; -; Genomic_DNA.
DR RefSeq; WP_011053717.1; NC_004061.1.
DR AlphaFoldDB; Q8K9V2; -.
DR SMR; Q8K9V2; -.
DR STRING; 198804.BUsg_185; -.
DR EnsemblBacteria; AAM67750; AAM67750; BUsg_185.
DR KEGG; bas:BUsg_185; -.
DR eggNOG; COG0012; Bacteria.
DR HOGENOM; CLU_018395_0_1_6; -.
DR OMA; VLRCFDN; -.
DR OrthoDB; 603226at2; -.
DR Proteomes; UP000000416; 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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..362
FT /note="Ribosome-binding ATPase YchF"
FT /id="PRO_0000201673"
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; 41124 MW; 8D5C9E45B109F726 CRC64;
MGFKCGIIGL PNVGKSTLFN VLTKGNSAVA NFPFCTIKPN IGIVSVPDNR INNLSKIILP
KKITNAFIEF VDIAGLVKGA SKGEGLGNQF LSNIRDTHAI AHVVRCFKDD NVSHIYNQLQ
PKIDVDIINS ELILADFETC EKSILKLQKK LNFNKKEIEE KLVVLSKCLD HLKKFLMLKT
LELDENEKKI ISYLRFLTLK PTMYIANINE QKESCFFLNE LEKMAKKEGS SVIPINSNLE
LDLIKMNEDE QKYFMKSFNI TNLGLNNIIK SGYKILNLIT FFTAGIKEVR AWAIPNGSTS
LQAADKIHSD FRRGFIRAQI INYLDFIKYK SETKVKEAGK YRSEGKFYQI QDGDIINFLF
NV