ID YCHF_HAEIN Reviewed; 363 AA. AC P44681; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 159. 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=HI_0393; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C., RA Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DOMAIN. RX PubMed=12837776; DOI=10.1128/jb.185.14.4031-4037.2003; RA Teplyakov A., Obmolova G., Chu S.Y., Toedt J., Eisenstein E., Howard A.J., RA Gilliland G.L.; RT "Crystal structure of the YchF protein reveals binding sites for GTP and RT nucleic acid."; RL J. Bacteriol. 185:4031-4037(2003). RN [4] RP FUNCTION, AND ATPASE ACTIVITY. RX PubMed=17430889; DOI=10.1074/jbc.m700541200; RA Koller-Eichhorn R., Marquardt T., Gail R., Wittinghofer A., Kostrewa D., RA Kutay U., Kambach C.; RT "Human OLA1 defines an ATPase subfamily in the Obg family of GTP-binding RT proteins."; RL J. Biol. Chem. 282:19928-19937(2007). CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S CC ribosomal subunit in a nucleotide-independent manner (By similarity). CC Does not hydrolyze GTP. {ECO:0000255|HAMAP-Rule:MF_00944, CC ECO:0000269|PubMed:17430889}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- DOMAIN: Composed of 3 distinct structural domains: the N-terminal CC domain, which has a mononucleotide binding fold typical for the P-loop CC NTPases, followed by a pronounced alpha-helical coiled coil domain and CC the C-terminal domain, which may be involved in RNA binding. CC {ECO:0000269|PubMed:12837776}. CC -!- MASS SPECTROMETRY: Mass=40011; Method=MALDI; CC Evidence={ECO:0000269|PubMed:10675023}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC22052.1; -; Genomic_DNA. DR PIR; I64150; I64150. DR RefSeq; NP_438555.1; NC_000907.1. DR PDB; 1JAL; X-ray; 2.40 A; A/B=1-363. DR PDBsum; 1JAL; -. DR AlphaFoldDB; P44681; -. DR SMR; P44681; -. DR STRING; 71421.HI_0393; -. DR EnsemblBacteria; AAC22052; AAC22052; HI_0393. DR KEGG; hin:HI_0393; -. DR PATRIC; fig|71421.8.peg.412; -. DR eggNOG; COG0012; Bacteria. DR HOGENOM; CLU_018395_0_1_6; -. DR OrthoDB; 9810373at2; -. DR PhylomeDB; P44681; -. DR BioCyc; HINF71421:G1GJ1-408-MONOMER; -. DR EvolutionaryTrace; P44681; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central. 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 CDD; cd04867; TGS_YchF_OLA1; 1. DR CDD; cd01900; YchF; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.10.150.300; TGS-like domain; 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 NCBIfam; TIGR00092; redox-regulated ATPase YchF; 1. DR PANTHER; PTHR23305; OBG GTPASE FAMILY; 1. DR PANTHER; PTHR23305:SF18; OBG-TYPE G DOMAIN-CONTAINING PROTEIN; 1. 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; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF81271; TGS-like; 1. DR PROSITE; PS51710; G_OBG; 1. DR PROSITE; PS51880; TGS; 1. PE 1: Evidence at protein level; KW 3D-structure; 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_0000201678" 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" FT STRAND 4..8 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 15..24 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 41..45 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 49..58 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 67..72 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 80..83 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 90..95 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 98..105 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 121..151 FT /evidence="ECO:0007829|PDB:1JAL" FT TURN 152..154 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 156..173 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 185..191 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 202..207 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 217..228 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 238..243 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 253..256 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 267..276 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 279..285 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 287..296 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 301..306 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 312..315 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 318..322 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 324..329 FT /evidence="ECO:0007829|PDB:1JAL" FT HELIX 333..338 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:1JAL" FT STRAND 356..361 FT /evidence="ECO:0007829|PDB:1JAL" SQ SEQUENCE 363 AA; 39751 MW; 08E00CBEF7D0F65E CRC64; MGFKCGIVGL PNVGKSTLFN ALTKAGIEAA NYPFCTIEPN TGVVPMPDPR LDALAEIVKP ERILPTTMEF VDIAGLVAGA SKGEGLGNKF LANIRETDAI GHVVRCFEND DIVHVAGKID PLDDIDTINT ELALADLDSC ERAIQRLQKR AKGGDKEAKF ELSVMEKILP VLENAGMIRS VGLDKEELQA IKSYNFLTLK PTMYIANVNE DGFENNPYLD RVREIAAKEG AVVVPVCAAI ESEIAELDDE EKVEFLQDLG IEEPGLNRVI RAGYALLNLQ TYFTAGVKEV RAWTVSVGAT APKAAAVIHT DFEKGFIRAE VIAYEDFIQF NGENGAKEAG KWRLEGKDYI VQDGDVMHFR FNV //