ID   HFLX_FLAPJ              Reviewed;         413 AA.
AC   A6H294;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=FP2414;
OS   Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS   JIP02/86).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=402612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX   PubMed=17592475; DOI=10.1038/nbt1313;
RA   Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA   Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA   Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT   "Complete genome sequence of the fish pathogen Flavobacterium
RT   psychrophilum.";
RL   Nat. Biotechnol. 25:763-769(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}.
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DR   EMBL; AM398681; CAL44468.1; -; Genomic_DNA.
DR   RefSeq; WP_011964502.1; NC_009613.3.
DR   RefSeq; YP_001297269.1; NC_009613.3.
DR   AlphaFoldDB; A6H294; -.
DR   SMR; A6H294; -.
DR   STRING; 402612.FP2414; -.
DR   EnsemblBacteria; CAL44468; CAL44468; FP2414.
DR   GeneID; 66553522; -.
DR   KEGG; fps:FP2414; -.
DR   PATRIC; fig|402612.5.peg.2470; -.
DR   eggNOG; COG2262; Bacteria.
DR   HOGENOM; CLU_019597_2_1_10; -.
DR   OMA; AEMKTGR; -.
DR   Proteomes; UP000006394; 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..413
FT                   /note="GTPase HflX"
FT                   /id="PRO_0000412657"
FT   DOMAIN          200..386
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         206..213
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         231..235
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         252..255
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         318..321
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT   BINDING         364..366
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
SQ   SEQUENCE   413 AA;  47692 MW;  1F43C3801251A3AC CRC64;
     MLEKETINFE KTIIVGIVTQ NQSEEKLKEY LDELEFLTFT AGGEVVKRFS QKMERPNPKT
     FLGTGKIEEI NLYVLENGIS TIVFDDELTP SQQKNISKII DCKILDRTHL ILDIFAQRAE
     TSYARTQVEL AQCIYLLPRL SGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRIALLKE
     KIKIIDKQQA TQRGNRGAMV RVALVGYTNV GKSTLMNAVG KSDVFVENKL FATLDTTVRK
     VVIKNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHQ DFEDHIDAVN
     KILLDIKSAD KPTIMVFNKI DAYKHLTIDA DDLMTERTSK HYTLQEWKNT WMNKVGEQNA
     LFISATNKEN FEEFRKKVYE TVREIHITRF PYNKFLYPDY EDAIDKEEEQ DQD