ID   HFLX_SPITD              Reviewed;         408 AA.
AC   E0RQS7;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 62.
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};
GN   OrderedLocusNames=STHERM_c20490;
OS   Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX   NCBI_TaxID=665571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1;
RX   PubMed=20935097; DOI=10.1128/jb.01023-10;
RA   Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA   Daniel R., Liebl W.;
RT   "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT   Spirochaeta thermophila DSM 6192.";
RL   J. Bacteriol. 192:6492-6493(2010).
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; CP001698; ADN02983.1; -; Genomic_DNA.
DR   RefSeq; WP_013314822.1; NC_014484.1.
DR   AlphaFoldDB; E0RQS7; -.
DR   SMR; E0RQS7; -.
DR   STRING; 665571.STHERM_c20490; -.
DR   EnsemblBacteria; ADN02983; ADN02983; STHERM_c20490.
DR   KEGG; sta:STHERM_c20490; -.
DR   eggNOG; COG2262; Bacteria.
DR   HOGENOM; CLU_019597_0_1_12; -.
DR   OMA; AEMKTGR; -.
DR   Proteomes; UP000001296; 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.
FT   CHAIN           1..408
FT                   /note="GTPase HflX"
FT                   /id="PRO_0000412662"
FT   DOMAIN          198..361
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         204..211
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         229..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         251..254
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         317..320
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         339..341
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
SQ   SEQUENCE   408 AA;  46468 MW;  ECD1E0679B541B49 CRC64;
     MYDTGQEAPR CILVGRKTGR EETSSLPELS LLVEELGYIP ETILSFPLRT PERKFLFGPG
     QAEVVAREAR MRGIELVVFD EDLTPAQQRN WEHLVKSRVM DRTEVIIEIF SRHARTKQAQ
     LQTEKARLEY LLPRLRGAWS HLDRQRGGAR GTRGEGERQI ELDRRMILSR LARIRREMEA
     IERHQTTTRS RRLEAGIPRV SLVGYTNAGK SSLFTRLTGQ AVRIQDRPFV TLDTTTRTCL
     IPGWGRVVVS DTVGFIQHLP HTLVDAFHAT LEEVRDAHLL LEVVDLSSPN LLLHLSTTEE
     VLTEIGAHHI PRIRVYNKAD RSSPHPLLPP SDHPEILVSA KTGEGIEGLL SLIVREMERH
     YPIETLELPY HRLGESHEVL SRAVIIHQEY TDVGLFVRYA PSVPSVHE