YCHF_HAEDU
ID YCHF_HAEDU Reviewed; 363 AA.
AC Q7VMI2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
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=HD_0995;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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: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; AE017143; AAP95874.1; -; Genomic_DNA.
DR RefSeq; WP_010944924.1; NC_002940.2.
DR AlphaFoldDB; Q7VMI2; -.
DR SMR; Q7VMI2; -.
DR STRING; 233412.HD_0995; -.
DR PRIDE; Q7VMI2; -.
DR EnsemblBacteria; AAP95874; AAP95874; HD_0995.
DR KEGG; hdu:HD_0995; -.
DR eggNOG; COG0012; Bacteria.
DR HOGENOM; CLU_018395_0_1_6; -.
DR OMA; VLRCFDN; -.
DR Proteomes; UP000001022; 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_0000201677"
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; 39826 MW; A3F37CB817BE0406 CRC64;
MGFKCGIVGL PNVGKSTLFN ALTKAGIEAA NYPFCTIEPN TGVVPMPDPR LDALAEIVNP
ERVLPTTMEF VDIAGLVAGA SKGEGLGNKF LANIRETDAI GHVVRCFEND DIVHVAGKID
PADDIETINT ELALADLDSC ERAIQRLQKR AKSGDKDAKF ELSILEKILP VLENAGMIRS
VALDKDELHA IKGYNFLTLK PTMYIANVNE DSFENNPYLD RVRQLAEQEG AVVVPVCAAI
EAEIAELEDE EKVDFLQDLG IEEPGLNRVI RAGYRLLNLQ TYFTAGVKEV RAWTVAVGAT
APKAAAVIHT DFEKGFIRAE VIAYDDFIQF KGENGAKEAG KWRLEGKDYI VQDGDVMHFR
FNV