ID A0A557ZVM7_9PSEU Unreviewed; 480 AA.
AC A0A557ZVM7;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 19.
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:TVT16069.1};
GN ORFNames=FNH05_36790 {ECO:0000313|EMBL:TVT16069.1};
OS Amycolatopsis rhizosphaerae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=2053003 {ECO:0000313|EMBL:TVT16069.1, ECO:0000313|Proteomes:UP000320011};
RN [1] {ECO:0000313|EMBL:TVT16069.1, ECO:0000313|Proteomes:UP000320011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBRC 6029 {ECO:0000313|EMBL:TVT16069.1,
RC ECO:0000313|Proteomes:UP000320011};
RA Duangmal K., Teo W.F.A.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TVT16069.1, ECO:0000313|Proteomes:UP000320011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBRC 6029 {ECO:0000313|EMBL:TVT16069.1,
RC ECO:0000313|Proteomes:UP000320011};
RA Srisuk N.;
RT "Amycolatopsis acidicola sp. nov., isolated from peat swamp forest soil.";
RL Submitted (AUG-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TVT16069.1}.
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DR EMBL; VJWX01000783; TVT16069.1; -; Genomic_DNA.
DR RefSeq; WP_144593441.1; NZ_VJWX01000783.1.
DR AlphaFoldDB; A0A557ZVM7; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000320011; 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 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 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};
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:UP000320011}.
FT DOMAIN 253..422
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..209
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 284..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 306..309
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 376..379
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 400..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ SEQUENCE 480 AA; 51970 MW; 6ADD5C63CBBD953B CRC64;
MTELTHTSAN TDFRDDPSVG ELELEDRVSL RRVAGLSTEL ADVTEVEYRQ LRLERVVLVG
VWTEGTAAQS EASLAELARL AETAGSEVLE GLVQRRDRPD PATYIGSGKV RELADIVIST
GADTVICDGE LSPGQLRQLE AKLKVKVIDR TALILDIFAQ HARSKEGKAQ VELAQLQYLI
PRLRGWGETL SRQAGGRAGG ANGGVGLRGP GETKLETDRR RINKRVAKLR REIAAMDTIR
DTKRGRRVAN EVPSVAIVGY TNAGKSSLLN AITGAGVLVE NALFATLDPT TRRASTPDGR
TYTLTDTVGF VRHLPHQLVD AFRSTLDEAA DADLLVHVVD GSDPAPEEQV NAVHEVLAEI
NRSRSQPLPP ELIVINKADA ADELSLVRLR YLLPDAVVVS ARTGEGVSAL LERIAERLPR
PEVTVEVLVP YTRGDLVART HADGEVLSEE HLPEGTRLCA RVRPDLASAL DAYVVHGSPA
//
