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Database: UniProt
Entry: A0A2D8R7T6_9GAMM
LinkDB: A0A2D8R7T6_9GAMM
Original site: A0A2D8R7T6_9GAMM 
ID   A0A2D8R7T6_9GAMM        Unreviewed;       461 AA.
AC   A0A2D8R7T6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900};
DE   AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900};
GN   Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900};
GN   ORFNames=CME36_01785 {ECO:0000313|EMBL:MAM86024.1};
OS   Hahellaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae.
OX   NCBI_TaxID=2048971 {ECO:0000313|EMBL:MAM86024.1, ECO:0000313|Proteomes:UP000225829};
RN   [1] {ECO:0000313|Proteomes:UP000225829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC       have a role during protein synthesis or ribosome biogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006809-2};
CC   -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}.
CC       Note=May associate with membranes. {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. HflX GTPase family. {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MAM86024.1}.
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DR   EMBL; NZNF01000005; MAM86024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D8R7T6; -.
DR   Proteomes; UP000225829; Unassembled WGS sequence.
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; 6.10.250.2860; -; 1.
DR   Gene3D; 3.40.50.11060; GTPase HflX, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03156; GTP_HflX; 1.
DR   PANTHER; PTHR10229:SF0; GTP-BINDING PROTEIN 6-RELATED; 1.
DR   PANTHER; PTHR10229; GTP-BINDING PROTEIN HFLX; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51705; G_HFLX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00900};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR006809-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR006809-2};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00900}.
FT   DOMAIN          198..372
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
FT   BINDING         204..211
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT   BINDING         229..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT   BINDING         251..254
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         317..320
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ   SEQUENCE   461 AA;  51889 MW;  B319B32623C34A01 CRC64;
     MFDRPDTGER ALLVHLELDK ENDCEDPQEF VDLALSAGAE VLEVVSVNRH FATPKFFIGS
     GKVEELADIV RLHKADVVLF NHALSPSQER NLEKAMQVRV LDRVGLILDI FAQRARTHEG
     KLQVELAQLE YMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR IKSIHKRLEK
     VRKQREQGRR ARLRNEVPVV ALVGYTNAGK STLFNRLTAS DVFAANQLFA TLDPTLRRIE
     VEGFGPIIFA DTVGFIRHLP HKLVDAFRAT LEETRDADLL LHLVDASDPR REDNQKQVAE
     VLKEIGADTV PAIKVMNKID ALDQAQWPLD ATGGRVDRDA EGLPERVWVS AIDGQGVDTL
     LGAIAELLGT NVRLLTVRCD MQMHSKLRSR FFERNVVENE TVDEAGRPLL TIRVEQHILD
     QLLSHAGVKL SEILVEDRAP PRVRYDENGF VADDNDDTLP A
//
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