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Database: UniProt
Entry: A0A1G5LBS5_9ACTN
LinkDB: A0A1G5LBS5_9ACTN
Original site: A0A1G5LBS5_9ACTN 
ID   A0A1G5LBS5_9ACTN        Unreviewed;       502 AA.
AC   A0A1G5LBS5;
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=SAMN02745898_109206 {ECO:0000313|EMBL:SCZ09710.1};
OS   Streptomyces sp. 136MFCol5.1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCZ09710.1, ECO:0000313|Proteomes:UP000199326};
RN   [1] {ECO:0000313|EMBL:SCZ09710.1, ECO:0000313|Proteomes:UP000199326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCZ09710.1,
RC   ECO:0000313|Proteomes:UP000199326};
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; FMVI01000009; SCZ09710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5LBS5; -.
DR   OrthoDB; 9812272at2; -.
DR   Proteomes; UP000199326; 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:UP000199326}.
FT   DOMAIN          281..446
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  54399 MW;  CC23D4689BB1FD7D CRC64;
     MTSSSSLPQD AQNAQSATES LTESLRADAL MEEDVAWSHE IDGERDGEQL DRSERAALRR
     VAGLSTELED VTEVEYRQLR LERVVLVGVW TSGTVQDAEN SLAELAALAE TAGAQVLDAV
     FQRRDKPDPA TYIGSGKALE LRDIVLESGA DTVVCDGELS PGQLIHLEDV VKVKVVDRTA
     LILDIFAQHA KSREGKAQVS LAQMQYMLPR LRGWGQSLSR QMGGGGSSGG GGMATRGPGE
     TKIETDRRRI REKMAKMRRE IAEMKTGREI KRQERKRNKV PSVAIAGYTN AGKSSLLNRL
     TGAGVLVENA LFATLDPTVR RAETPTGRTY TLADTVGFVR HLPHHLVEAF RSTMEEVGES
     DLILHVVDGS HPVPEEQLAA VREVIRDVGA LDVPEIVVIN KADAADPLVL QRLLRIEKHA
     IAVSARTGAG MAELLALIDS ELPRPSVEIE ALVPYTQGGL VSRVHADGEV ISEEHTSEGT
     LLKARVHEQL AADLASFALA AH
//
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