ID A0A6G9GVK8_9ACTN Unreviewed; 503 AA.
AC A0A6G9GVK8;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, 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 ECO:0000313|EMBL:QIQ02302.1};
GN ORFNames=HA039_08275 {ECO:0000313|EMBL:QIQ02302.1};
OS Streptomyces liangshanensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2717324 {ECO:0000313|EMBL:QIQ02302.1, ECO:0000313|Proteomes:UP000501179};
RN [1] {ECO:0000313|EMBL:QIQ02302.1, ECO:0000313|Proteomes:UP000501179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QMT-12 {ECO:0000313|EMBL:QIQ02302.1,
RC ECO:0000313|Proteomes:UP000501179};
RA Gao J.;
RT "A novel species.";
RL Submitted (MAR-2020) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP050177; QIQ02302.1; -; Genomic_DNA.
DR RefSeq; WP_167026039.1; NZ_CP050177.1.
DR AlphaFoldDB; A0A6G9GVK8; -.
DR KEGG; slia:HA039_08275; -.
DR Proteomes; UP000501179; Chromosome.
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 GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR CDD; cd01878; HflX; 1.
DR FunFam; 3.40.50.11060:FF:000001; GTPase HflX; 1.
DR FunFam; 3.40.50.300:FF:000690; GTPase 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 PIRSF; PIRSF006809; GTP-binding_hflX_prd; 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|ARBA:ARBA00022490, 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:UP000501179}.
FT DOMAIN 280..445
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 54540 MW; 3F3DA5E07C1BA9F2 CRC64;
MTSSSSPSQH AQTFADDSTA DTRTDSLRAD ALMEEDVAWS HEIDGARDGE QLDRSDRAAL
RRVAGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGTVRDS ENSLAELAAL AETAGALVLD
GVIQRRDKPD PATYIGSGKA QELRDIVLES GADTVVCDGE LSPGQLIHLE DVVKVKVVDR
TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGQSL SRQMGGGGGG GMATRGPGET
KIETDRRRIR EKMAKMRREI AEMKTGREIK RQERRRNRVP SVAIAGYTNA GKSSLLNRLT
GAGVLVENAL FATLDPTVRR AETPSGRTYT LADTVGFVRH LPHHLVEAFR STMEEVGDSD
LILHVVDGSH PSPEEQLAAV REVVRDVGAV DVREIVVINK ADAADPLVLQ RLLGAERYAI
AVSARTGQGI AELLALIDAE LPRPEVEVEV LVPYTLGGLV SRVHAEGEVL SEEHTPEGTL
LKARVHEELA AALSGYVPVP VAP
//
