ID A0A0M2U475_9FIRM Unreviewed; 587 AA.
AC A0A0M2U475;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SY88_22040 {ECO:0000313|EMBL:KKM08885.1};
OS Clostridiales bacterium PH28_bin88.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM08885.1, ECO:0000313|Proteomes:UP000034222};
RN [1] {ECO:0000313|EMBL:KKM08885.1, ECO:0000313|Proteomes:UP000034222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Robbins S., Tyson G.;
RT "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL Submitted (MAR-2015) 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}.
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:KKM08885.1}.
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DR EMBL; LAKY01000072; KKM08885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2U475; -.
DR STRING; 1605376.SY88_22040; -.
DR PATRIC; fig|1605376.3.peg.454; -.
DR Proteomes; UP000034222; 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 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:UP000034222}.
FT DOMAIN 358..533
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT COILED 318..345
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 587 AA; 63947 MW; C036DC4FC7BF15EC CRC64;
MEVERTSLVS VDLAQRMAVI SGLLQREVAV YLNRRGRVVG VALGEHDRVS LPDFQGRRGA
NRLSGIRCVH THPGGSGMLS GVDCTALSSL RLDCMAALGL QNGLVTDIYA GFLRPATGSP
DPEYLVKGPM TLHDLEGFDL MALVEAIEEE LRGEEVLYTG DDRAERAVVV GLDMPSRGSA
GYSAGESLAE LAQLVEAAGA TVVDAVLQRK GHVDRAYFIG KGLAEQLSLR LRQLRANLVV
LDHEVSGTQA RNLEALMGVK VIDRTAVILD IFAQRAKTRE GKLQVELAQL QYMLPRLVGS
GAQMSRLAGG IGTRGPGETK LETDRRHIRR RIEEIEKQLA EVQKHRRVQR AGRRGGTPTV
ALVGYTNAGK STLRYCLVKR AASSRTNWED EDAGTNRVFA TLDPTLRGIT LPGGKEVLVG
DTVGFIQKLP HQLVSAFRAT LEEVVEADLL LHVIDASSPR WEAQMAAVEQ VLEELGVANK
PRINVFNKMD LVEPGAVALP PADGNPCVTV SAVMGTGLDL LLEEMARVLR VETRQVRLSI
LYRYSGLLSE LYAAVRVVSV NYQEDGIAVE AVVRDDQMHR YSDYLAP
//