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Database: UniProt
Entry: W0E7W9_9FIRM
LinkDB: W0E7W9_9FIRM
Original site: W0E7W9_9FIRM 
ID   W0E7W9_9FIRM            Unreviewed;       534 AA.
AC   W0E7W9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=DESME_07650 {ECO:0000313|EMBL:AHF06960.1};
OS   Desulfitobacterium metallireducens DSM 15288.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF06960.1, ECO:0000313|Proteomes:UP000010847};
RN   [1] {ECO:0000313|EMBL:AHF06960.1, ECO:0000313|Proteomes:UP000010847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG   DOE Joint Genome Institute;
RA   Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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   -!- 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}.
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DR   EMBL; CP007032; AHF06960.1; -; Genomic_DNA.
DR   RefSeq; WP_006715354.1; NZ_CP007032.1.
DR   AlphaFoldDB; W0E7W9; -.
DR   STRING; 871968.DESME_07650; -.
DR   KEGG; dmt:DESME_07650; -.
DR   eggNOG; COG2262; Bacteria.
DR   HOGENOM; CLU_019597_7_1_9; -.
DR   OrthoDB; 9812272at2; -.
DR   Proteomes; UP000010847; 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; 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   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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00900}; Reference proteome {ECO:0000313|Proteomes:UP000010847}.
FT   DOMAIN          363..534
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
SQ   SEQUENCE   534 AA;  59611 MW;  958D8C1773904415 CRC64;
     MDIFGDLSGI RLTQLEELKT LSSLRTERPE LIHVDLLDGL SILTDKWNKE IALYINRTGR
     VNGIAVGHHA SVKLPSVRVR EATHTRCIHT HPGGNFQLSS VDLSALESLS LESMTSIGIL
     NGKITGAELA CLTEDGTILT SNFSPQELER LDYDEFLSEN RTRQTPITRA LPEEERAYLV
     SVENEELAQE ILTELAELAR TAGVKVVGQL LQPKRYGSSV SYLGKGKLET LNQQLQNTHA
     NVLICDDELT PAQLRNLEEY TGIKVLDRTG LILDIFAQRA KSREGKLQVE LAQLQYLLPR
     LTGQGRSLSR LGGGIGTRGP GESKLEMDKR RVRQRIYILE QDLKEIRKHR LTQRQQRIRS
     GLQLVALVGY TNAGKTTFLQ KAMEQTRAKG ESLSGENKLF ATLDPTVRSL QIGTYRQILM
     SDTVGFIQKL PPKLLNAFLA TLEEVQNADL LVHVLDASHA RALEQADTVH EILKELDCAD
     KPTITVLNKT DQVEQISDLN RLAQQLPHPV SLSLKQGDSL VPVWKMIEEL LPEN
//
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