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Database: UniProt
Entry: A0A1H0M2F4_9ACTN
LinkDB: A0A1H0M2F4_9ACTN
Original site: A0A1H0M2F4_9ACTN 
ID   A0A1H0M2F4_9ACTN        Unreviewed;       499 AA.
AC   A0A1H0M2F4;
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=SAMN05216259_11235 {ECO:0000313|EMBL:SDO74350.1};
OS   Actinacidiphila guanduensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310781 {ECO:0000313|EMBL:SDO74350.1, ECO:0000313|Proteomes:UP000199341};
RN   [1] {ECO:0000313|EMBL:SDO74350.1, ECO:0000313|Proteomes:UP000199341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2022 {ECO:0000313|EMBL:SDO74350.1,
RC   ECO:0000313|Proteomes:UP000199341};
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; FNIE01000012; SDO74350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0M2F4; -.
DR   STRING; 310781.SAMN05216259_11235; -.
DR   OrthoDB; 9812272at2; -.
DR   Proteomes; UP000199341; 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   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:UP000199341}.
FT   DOMAIN          277..442
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
FT   REGION          214..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          243..270
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   499 AA;  54308 MW;  CA00675D959C2D4C CRC64;
     MTSNASSSSP HDRQRLPEHL RAEALMEEDA ALGLDTDGDW DGDQLDRSDR ASLRRVAGLS
     TELEDVTEVE YRQLRLERVV LVGVWTSGTV DDAEQSLAEL AALAETAGAL VLDGVIQRRD
     KPDPATYIGS GKAQELRDIV VETGADTVVC DGELSPGQLI HLEDVVKVKV VDRTALILDI
     FAQHAKSREG KAQVSLAQMQ YMLPRLRGWG QSLSRQMGGG GSGSSGGGMA TRGPGETKIE
     TDRRRIREKM AKMRREIAEM KTSRDLKRQE RKRHKVPSVA IAGYTNAGKS SLLNRLTGAG
     VLVENALFAT LDPTVRRAET PSGRVYTLAD TVGFVRHLPH HLVEAFRSTM EEVGEADLIL
     HVVDGSHPVP EEQLAAVREV FRDVGAHDVP EIVVVNKADA ADPLVLQRLL REEKHAIAVS
     ARSGLGIDKL LALIDDTLPR PDVEVEALVP YTHGALVSRV HASGEVLSEE HTGEGTLLRV
     RVHEELAAEL APFTLAARH
//
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