ID   HFLX_CALS4              Reviewed;         428 AA.
AC   Q8RAS5;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=TTE1127;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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}.
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DR   EMBL; AE008691; AAM24362.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RAS5; -.
DR   SMR; Q8RAS5; -.
DR   STRING; 273068.TTE1127; -.
DR   PRIDE; Q8RAS5; -.
DR   EnsemblBacteria; AAM24362; AAM24362; TTE1127.
DR   KEGG; tte:TTE1127; -.
DR   eggNOG; COG2262; Bacteria.
DR   HOGENOM; CLU_019597_1_0_9; -.
DR   OMA; AEMKTGR; -.
DR   Proteomes; UP000000555; 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..428
FT                   /note="GTPase HflX"
FT                   /id="PRO_0000412663"
FT   DOMAIN          214..374
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         220..227
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         245..249
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         267..270
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         333..336
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         352..354
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
SQ   SEQUENCE   428 AA;  48467 MW;  9343788413CFDCA4 CRC64;
     MQKIEYIIIT KLWVGDCMEE LARDKERAIL VAIISSPEDE ETLNELKELA VTAGAEVIGI
     LTQKKKGINK AHYIGKGKLE ELKMFVENQQ ADLVIVNDEL TGTQIKNLED ALGVKIVDRT
     NLILDIFAKR ARSKEGMLQV ELAQLKYRLP RLVGLGGQLS RLGGGIGTRG PGETKLEVDR
     RHIRNRIKAI EEKLEELEKH RNLQRQRRKK NQIPVVAIVG YTNAGKSTLL NALTGADAYV
     EDKLFATLDP TARKLVLPSG REVILTDTVG FIRKLPHDLV EAFKSTLEEV KYADLLLHVI
     DVTSPDMDEK IKVVEKVLSD LGAIETPRIN VYNKIDLLEI VPSGNNRDIY ISAKNKIGLD
     RLLEAIEREL FKETEVVSFL FPYEKTREYN YLKERGKVIE EDFDEKGISV KAEVTCEIKE
     RLRNFIIS