YCHF_HAEIN
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 03-AUG-2022, entry version 153.
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; Proteobacteria; 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 RefSeq; WP_005693776.1; 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 OMA; VLRCFDN; -.
DR PhylomeDB; P44681; -.
DR BioCyc; HINF71421:G1GJ1-408-MON; -.
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 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 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