ID A0A075WRJ8_9BACT Unreviewed; 591 AA.
AC A0A075WRJ8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 08-NOV-2023, 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=HL41_03625 {ECO:0000313|EMBL:AIH03939.1};
OS Thermodesulfobacterium commune DSM 2178.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=289377 {ECO:0000313|EMBL:AIH03939.1, ECO:0000313|Proteomes:UP000028481};
RN [1] {ECO:0000313|EMBL:AIH03939.1, ECO:0000313|Proteomes:UP000028481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2178 {ECO:0000313|EMBL:AIH03939.1,
RC ECO:0000313|Proteomes:UP000028481};
RX PubMed=25635017;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of a Sulfate-Reducing Thermophilic Bacterium,
RT Thermodesulfobacterium commune DSM 2178T (Phylum Thermodesulfobacteria).";
RL Genome Announc. 3:0-0(2015).
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; CP008796; AIH03939.1; -; Genomic_DNA.
DR RefSeq; WP_038060372.1; NZ_JQLF01000005.1.
DR AlphaFoldDB; A0A075WRJ8; -.
DR STRING; 289377.HL41_03625; -.
DR PaxDb; 289377-HL41_03625; -.
DR KEGG; tcm:HL41_03625; -.
DR eggNOG; COG2262; Bacteria.
DR HOGENOM; CLU_019597_7_1_0; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000028481; 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 InterPro; IPR005225; Small_GTP-bd_dom.
DR NCBIfam; TIGR03156; GTP_HflX; 1.
DR NCBIfam; TIGR00231; small_GTP; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000028481}.
FT DOMAIN 394..561
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT COILED 353..387
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 591 AA; 67871 MW; 58559607C6F4EDFF CRC64;
MGYNVFGHTV GLKPSELKNL ERFYRRRVPP ASIISHELAR ELAKVSADLN RQVGLLINRK
GEIDYVVVGT FNRIELPELR GYRDHIARLK GLRFIHTHLL TSKITHSELD QDDLIDLALL
RLDLVGALEV HPNGEPGKIH IAHIIPDPEF FAGGSLSDKE NQFFYFLRPC YVWELKENFL
ELIKNLEDEL ERVKPLKEVE EQKDRAILIF LREPNDPYLE ERIFELRELA RTAGVTVVGE
IVQKKPSPDP RYVIGKGKLL EVMVLALRNR ANLLIFDREL TPSQVRAITE STDLRVIDRT
QLILDIFAQR AKSKEGKIQV EIAQLKYTLP RLRAKDDAFS RLTGGIGGRG PGETKLEIDK
RRIKDRIAKL ERELEKISQE RDIKRKRRKK LAFKTVALIG YTNAGKTTLF NTLAKSQYLA
EDKLFATLDP VTKAIRTPNN QVFLITDTVG FIRNLPEDLK KAFRATLEEL YSADLLLHIV
DISNPDFESQ IETVNQILEE MELLHYPLLM VFNKIDLLPP SEFQLIKALS HRYKAIPVSA
KRGDNLDLLL TKIEEILFKT PLEYLTDKVL EPVSLEEENP SKDPLTHKLD V
//
