HFLX_THEKO
ID HFLX_THEKO Reviewed; 442 AA.
AC Q5JGB4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=TK1976;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD86165.1; -; Genomic_DNA.
DR RefSeq; WP_011250926.1; NC_006624.1.
DR AlphaFoldDB; Q5JGB4; -.
DR SMR; Q5JGB4; -.
DR STRING; 69014.TK1976; -.
DR EnsemblBacteria; BAD86165; BAD86165; TK1976.
DR GeneID; 3235683; -.
DR KEGG; tko:TK1976; -.
DR PATRIC; fig|69014.16.peg.1931; -.
DR eggNOG; arCOG00353; Archaea.
DR HOGENOM; CLU_019597_2_0_2; -.
DR InParanoid; Q5JGB4; -.
DR OMA; FNNHAHV; -.
DR OrthoDB; 33372at2157; -.
DR PhylomeDB; Q5JGB4; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
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 InterPro; IPR005225; Small_GTP-bd_dom.
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 TIGRFAMs; TIGR00231; small_GTP; 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..442
FT /note="GTPase HflX"
FT /id="PRO_0000412667"
FT DOMAIN 186..362
FT /note="Hflx-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 192..199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 217..221
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 238..241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 306..309
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 341..343
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
SQ SEQUENCE 442 AA; 50606 MW; EEC96347DDC0D6DC CRC64;
MRAIGVIRNS RRERLSRAEF EELLRSAGYE VLAIVEQNRE EHPRYNIGPG KLEELKELVK
ELKPDKVIFA NRLTPSQAYN LWKELRIEIM DRWQLVLEIF EKRAHSKEAK LQVELASLQY
EIPLVKEAIR RIRLGDRAGF KGMGEYQTQQ YLKHIRYRMG KIRDELERVK ADREVKRKKR
ENAGFVLVAL AGYTNAGKST LLNALADENV EAKNQMFTTL DTTTRRFRLG TKRILATDTV
GFIDGLPPFI VEAFHSTLEE IVKADIVLLV LDSSEPWGEI RRKFLASLQV LRELKALEKP
IIVALNKIDL IEEADAEEKV RLIWELARER GISLEDVVKI SAREGRLEEL MDALNRVVLK
LPKYGAFRII VKEPEKVPAV MALINSVGEV LSVEYGEKTR IDAYVQTGMV GEIKKMGAEI
ERLNHSGEGE ELEQDEGYSD GG
