ID A0A179EVK0_ENTTH Unreviewed; 417 AA.
AC A0A179EVK0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:ASZ08096.1};
GN ORFNames=A6E74_00170 {ECO:0000313|EMBL:OAQ56823.1}, CK496_09295
GN {ECO:0000313|EMBL:ASZ08096.1}, ETH01_08860
GN {ECO:0000313|EMBL:GEK36599.1};
OS Enterococcus thailandicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=417368 {ECO:0000313|EMBL:OAQ56823.1, ECO:0000313|Proteomes:UP000078516};
RN [1] {ECO:0000313|EMBL:OAQ56823.1, ECO:0000313|Proteomes:UP000078516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0711D 46 {ECO:0000313|EMBL:OAQ56823.1,
RC ECO:0000313|Proteomes:UP000078516};
RA Beukers A.G., Zaheer R., Goji N., Cook S.R., Amoako K., Chaves A.V.,
RA Ward M.P., Mcallister T.A.;
RT "Draft genome of an Enterococcus thailandicus strain isolated from bovine
RT feces.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ASZ08096.1, ECO:0000313|Proteomes:UP000217197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A523 {ECO:0000313|EMBL:ASZ08096.1}, and a523
RC {ECO:0000313|Proteomes:UP000217197};
RA Ybazeta G., Douglas L., Graham J., Fraleigh N., Murad Y., Perez J.,
RA Diaz-Mitoma F., Nokhbeh R.;
RT "Whole genome sequencing and hybrid de novo assembly of Enterococcus
RT thailandicus a523.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEK36599.1, ECO:0000313|Proteomes:UP000321361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101867 {ECO:0000313|EMBL:GEK36599.1,
RC ECO:0000313|Proteomes:UP000321361};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Enterococcus thailandicus NBRC 101867.";
RL Submitted (JUL-2019) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR006809-2};
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; CP023074; ASZ08096.1; -; Genomic_DNA.
DR EMBL; BJUG01000003; GEK36599.1; -; Genomic_DNA.
DR EMBL; LWMN01000001; OAQ56823.1; -; Genomic_DNA.
DR RefSeq; WP_067480282.1; NZ_LWMN01000001.1.
DR AlphaFoldDB; A0A179EVK0; -.
DR GeneID; 77487835; -.
DR KEGG; eth:CK496_09295; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000078516; Unassembled WGS sequence.
DR Proteomes; UP000217197; Chromosome.
DR Proteomes; UP000321361; 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 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|HAMAP-Rule:MF_00900};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00900};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR006809-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR006809-2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00900}; Reference proteome {ECO:0000313|Proteomes:UP000078516}.
FT DOMAIN 197..359
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT BINDING 203..210
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 228..232
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 250..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 316..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 337..339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ SEQUENCE 417 AA; 47532 MW; B23D481F28FE29C6 CRC64;
MIEEKEKVVI VGVETEKNQS YFAESMKELI QLTKTAAGEV VFSLTQKRPQ VDRQTLIGKG
KLEELIQQAT AYEADLIIFN HELTPRQSQI ISDAVGLPVI DRVQLILDIF AMRARSREGK
LQVELAQLEY LLPRLVGQGK TLSRLGGGIG TRGPGETKLE TDRRHIRNKI YAVKRELKEV
EAHRERNRQQ RKNNEIFQIG LIGYTNAGKS TILNLLTQAD TYSKDQLFAT LDPLTKKWHF
PEGFEVTMTD TVGFIQDLPT QLIDAFHSTL EESQNMDLLL HVVDASAPER ILQEQTVLKL
MDELEMKDVP ILTVYNKADQ VNRGAFTPTL FPNRLISAKS ESGKQELTRA IKREIMELLT
PYTLFLPSEA GQQLSEIKRQ TLVLSEEFIE EKNSYEVRGF AKSTSKWIRR MTDELDS
//
