ID A0A1I5BIA0_9MICO Unreviewed; 511 AA.
AC A0A1I5BIA0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05216219_1898 {ECO:0000313|EMBL:SFN74376.1};
OS Mycetocola miduiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=995034 {ECO:0000313|EMBL:SFN74376.1, ECO:0000313|Proteomes:UP000198867};
RN [1] {ECO:0000313|Proteomes:UP000198867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11101 {ECO:0000313|Proteomes:UP000198867};
RA Varghese N., Submissions S.;
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; FOVM01000005; SFN74376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5BIA0; -.
DR STRING; 995034.SAMN05216219_1898; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000198867; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198867}.
FT DOMAIN 291..456
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 229..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 55516 MW; 08C1B05B7EB5288A CRC64;
MTQPSDTPDT PVDDDAVARV LKNAETRASG YSLFGTGKAT ALDAETGFET TDAGRDGEQF
DREDRQALRR VSGLSTELED VTEVEYRQLR IENVVLIGIY SQGSLQDAEN SIRELAALAE
TAGAVVLDGM LQRRPHPDPS TYLGKGKAEE LRGIVAALGA DTVIADTELA PSQRRALEDV
VKVKVIDRTA VILDIFSQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGQVGGAG
AGMGSRGPGE TKIELDRRRI HTRMARLRKQ IKGFGPAREA KRANRHRFEV PSVAIAGYTN
AGKSSLLNRI TKAGVLVENS LFATLDATVR RTQTEDGRLY TISDTVGFVR NLPHQLVEAF
RSTLEEVGEA DVIVHVVDGS HPDPAAQLTT VRDVIGDVGA RDIPELVVFN KSDLVDEDDR
LLLRGLEPNA IFASARTGEG IDEILAALGR LLPSPSVALD LLVPYDRGDV ISMLHRRGRV
DHLDYLEEGT HVRAMASEEL AAQVAEFARP A
//