ID   A0A1G9WFC3_9ACTO        Unreviewed;       539 AA.
AC   A0A1G9WFC3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN04487766_107118 {ECO:0000313|EMBL:SDM83254.1};
OS   Actinomyces ruminicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=332524 {ECO:0000313|EMBL:SDM83254.1, ECO:0000313|Proteomes:UP000199671};
RN   [1] {ECO:0000313|EMBL:SDM83254.1, ECO:0000313|Proteomes:UP000199671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPR-7B {ECO:0000313|EMBL:SDM83254.1,
RC   ECO:0000313|Proteomes:UP000199671};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNHU01000007; SDM83254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9WFC3; -.
DR   OrthoDB; 9812272at2; -.
DR   Proteomes; UP000199671; 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   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}; 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}.
FT   DOMAIN          319..485
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
FT   REGION          259..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  56790 MW;  730CD73E0B2FBE22 CRC64;
     MENTQHLSHS AVTDSTVTAD NDAARDDAPA VAADDPAAAL ASRVRSRAGT ALASTAGRAD
     YGDAADAGAL EREARAATRR VAGLSTELED VSEVEYRQVR LERVVLVGLE LPVSGAHPVP
     GRSGFVGPNG AAGSQDAETS LRELAALAET AGSEVLDALI QRRDHPDPAT YLGSGKAKEL
     AEMIADNGAD TVIVDGELAP SQRRALEDVV GVKVVDRTAL ILDIFAQHAK SREGKAQVEL
     AQLEYLLPRL RGWGESMSRQ AGGRVAGGQG IGSRGPGETK IELDRRRIRQ RMAKLRREIR
     AMAPSREVKR GSRRRGPIPS VAIAGYTNAG KSSLMNALTG AGIMVQDALF ATLDPTVRKA
     EAADGRIYTL TDTVGFVRNL PHELIEAFRS TLEEVAEADV LLHVVDAAHP DPLGQIVAVH
     AVLADIPGAM DVPELIVLNK ADLADAVTLA ALRTRLPDAA VVSARTGQGL PALRERVEAM
     LPRPEVAVDV VVPYSRGDLV SRVHADGDID TVEYVEDGTH VVARVDAALA AELAAVDAG
//