ID A0A399G2X9_9ACTN Unreviewed; 490 AA.
AC A0A399G2X9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JAN-2026, entry version 32.
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 ECO:0000313|EMBL:UOE19915.1};
GN ORFNames=NI17_001210 {ECO:0000313|EMBL:UOE19915.1};
OS Thermobifida halotolerans.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsidaceae; Thermobifida.
OX NCBI_TaxID=483545 {ECO:0000313|EMBL:UOE19915.1, ECO:0000313|Proteomes:UP000265719};
RN [1] {ECO:0000313|EMBL:UOE19915.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE19915.1};
RA Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2020) 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; CP063196; UOE19915.1; -; Genomic_DNA.
DR RefSeq; WP_068687818.1; NZ_JBGBYW010000002.1.
DR AlphaFoldDB; A0A399G2X9; -.
DR KEGG; thao:NI17_001210; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000265719; 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 GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR CDD; cd01878; HflX; 1.
DR FunFam; 3.40.50.11060:FF:000001; GTPase 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|ARBA:ARBA00022490, 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:UP000265719}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..225
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 53259 MW; FA3153B412EB51BD CRC64;
MDMTRTSLNG HALNGASAAA AAPVDTRPGV DDELDRGQLE LQDRHALRRV QGLSTELHDI
TEVEYRSLRL ERVVLIGVWT TGTQQDADNS LLELKQLAET AGALVLEGLT QRRSRPDPAT
YVGSGKAAEL HDIVESTGAD TVICDGELAP GQLRQLEDIV KVKVIDRTAL ILDIFAQHAR
SKEGKAQVEL AQLTYLLPRL RGWGEALSRQ AGTSGGGNGG VGLRGPGETK LETDRRRINT
RMAKLRRQLS HMAVARDVKR DRRRTRQVPA VAIAGYTNAG KSSLLNRLTG AGVLVEDALF
ATLDPTVRRA RTPDGRGFTL SDTVGFVRHL PHQLVEAFRS TLEEVTDADL ILHVVDGAHP
DPEQQIASVR QVFAEIGASD IPELIVVNKV DAADPLLLRQ LRTRYPDAVE VSAHTGAGVD
ALLRAIAGAL PTFDREVSVL LPYDRGDLVS RVHQEGRILS EEHTGEGTAL HAWVPPLLAG
QLDRYVTAMR
//
