ID A0A1I1I3V4_9ACTN Unreviewed; 503 AA.
AC A0A1I1I3V4;
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=SAMN04487968_105105 {ECO:0000313|EMBL:SFC30482.1};
OS Nocardioides terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=574651 {ECO:0000313|EMBL:SFC30482.1, ECO:0000313|Proteomes:UP000198832};
RN [1] {ECO:0000313|EMBL:SFC30482.1, ECO:0000313|Proteomes:UP000198832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7056 {ECO:0000313|EMBL:SFC30482.1,
RC ECO:0000313|Proteomes:UP000198832};
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; FOLB01000005; SFC30482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1I3V4; -.
DR STRING; 574651.SAMN04487968_105105; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000198832; 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:UP000198832}.
FT DOMAIN 282..447
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..268
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..45
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 54397 MW; 6B7A0DE98C78688B CRC64;
MTNRPEPRPD ASPDFTLDDE LEVTADWDPD DEPVEIGVTG DDPEDDPTIG AMELAERHAL
RRVASLRTEL EDITEVEYRQ LRLERVVLVG VWTSGSSTDA DNSMAELALL AETAGSEVLE
AIYQRRQAPD PATYIGRGKV EALGEIVQVT GADTVICDGE LAPSQLRNLE DRLKVKVVDR
TALILDIFAQ HAKSKEGQAQ VELAQLNYMK QRLRGWGGNL SRQVGGRVAG GAGIGGRGPG
ETKIETDRRR INNRIAKLRR ELGEMKGTRD TKRASRQRHE IPAVAIAGYT NAGKSSLLNR
LTGAGVLVED ALFATLDPTT RRTTTSDGRV YTMSDTVGFV RHLPHQLVEA FRSTLEEVAD
ADLVVHVVDG SHPDPEGQLS AVREVFAEIG AADVPELVVI NKIDAADPLV VQRLLRTEPH
SVAVSARTGQ GIAEALAAVE ADLPRPAVAF EVLLPYSRGD LVNKIHQQGE IDTLEHTADG
TLVKGRATGA LAGELEPYSI AAV
//
