ID   HFLX_HYPBU              Reviewed;         375 AA.
AC   A2BLW4;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900};
DE   AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900};
GN   Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; OrderedLocusNames=Hbut_1138;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
CC   -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC       have a role during protein synthesis or ribosome biogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00900}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00900};
CC   -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00900}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}.
CC       Note=May associate with membranes. {ECO:0000255|HAMAP-Rule:MF_00900}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. HflX GTPase family. {ECO:0000255|HAMAP-Rule:MF_00900}.
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; CP000493; ABM80975.1; -; Genomic_DNA.
DR   RefSeq; WP_011822293.1; NC_008818.1.
DR   AlphaFoldDB; A2BLW4; -.
DR   SMR; A2BLW4; -.
DR   STRING; 415426.Hbut_1138; -.
DR   PRIDE; A2BLW4; -.
DR   EnsemblBacteria; ABM80975; ABM80975; Hbut_1138.
DR   GeneID; 4782129; -.
DR   KEGG; hbu:Hbut_1138; -.
DR   eggNOG; arCOG00353; Archaea.
DR   HOGENOM; CLU_019597_2_0_2; -.
DR   OMA; IRYAKIG; -.
DR   OrthoDB; 33372at2157; -.
DR   Proteomes; UP000002593; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01878; HflX; 1.
DR   Gene3D; 3.40.50.11060; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00900; GTPase_HflX; 1.
DR   InterPro; IPR030394; G_HFLX_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR032305; GTP-bd_M.
DR   InterPro; IPR016496; GTPase_HflX.
DR   InterPro; IPR025121; GTPase_HflX_N.
DR   InterPro; IPR042108; GTPase_HflX_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10229; PTHR10229; 1.
DR   Pfam; PF16360; GTP-bdg_M; 1.
DR   Pfam; PF13167; GTP-bdg_N; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03156; GTP_HflX; 1.
DR   PROSITE; PS51705; G_HFLX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..375
FT                   /note="GTPase HflX"
FT                   /id="PRO_0000412665"
FT   DOMAIN          194..371
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         200..207
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         225..229
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         246..249
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         314..317
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         349..351
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
SQ   SEQUENCE   375 AA;  41777 MW;  EC6F3E05E26A011D CRC64;
     MAKVAVWKPS ILVLPRGLAR WEVREAYVLA ETAGYRVVDV LYYRRVSSSK LLSDAKLEEL
     AEKAKSLVGN EYARIIVYDN LKPREYFRIV KATGVNTIDR TMLILEIFSL HAGSREAKLQ
     IELARLRHEL PLVREAIRLS KLKELPGFLG PGGYAIDAYY RYMVSRIAKI KRELRELRRR
     HEIERSKRRS AGLPHIAIVG YASAGKTSLF NAITGLQKPV GPEYFTTITP KRRAISFNGL
     RTVFIDTVGF IMRIPPEIIE AFHSTLEEAA TADVILYVVD VSEPDTVIAE KLDEGLQTLR
     RIGVIDKPLI IAANKIDLVP QEDIERLTRL LEGAASTLYP ALEAVIPVSA KTGAGVAKLL
     CRIATLLAGT KGSTC