ID A0A0S6UT44_9BRAD Unreviewed; 460 AA.
AC A0A0S6UT44;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=BDOA9_0145340 {ECO:0000313|EMBL:GAJ35330.1};
OS Bradyrhizobium sp. DOA9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1126627 {ECO:0000313|EMBL:GAJ35330.1};
RN [1] {ECO:0000313|EMBL:GAJ35330.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOA9 {ECO:0000313|EMBL:GAJ35330.1};
RX PubMed=25710540; DOI=10.1371/journal.pone.0117392;
RA Okazaki S., Noisangiam R., Okubo T., Kaneko T., Oshima K., Hattori M.,
RA Teamtisong K., Songwattana P., Tittabutr P., Boonkerd N., Saeki K.,
RA Sato S., Uchiumi T., Minamisawa K., Teaumroong N.;
RT "Genome Analysis of a Novel Bradyrhizobium sp. DOA9 Carrying a Symbiotic
RT Plasmid.";
RL PLoS ONE 10:e0117392-e0117392(2015).
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; DF820425; GAJ35330.1; -; Genomic_DNA.
DR RefSeq; WP_025036296.1; NZ_DF820425.1.
DR AlphaFoldDB; A0A0S6UT44; -.
DR STRING; 1126627.BDOA9_0145340; -.
DR eggNOG; COG2262; Bacteria.
DR Proteomes; UP000066441; 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; IPR045498; HflX_C.
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; PF19275; HflX_C; 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 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};
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}.
FT DOMAIN 226..400
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT COILED 185..212
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 232..239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 257..261
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 279..282
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 348..351
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ SEQUENCE 460 AA; 50925 MW; 3CAD050EE40C0159 CRC64;
MEPRNFDGDA DRPRSAGATQ TGRVLVIGPY LRVRAGGADA QPETHALRDT EARLDEAAGL
ARAIDLVIAD AIVAPVSQIR PATYIGKGKV EEIAGLIKTL EVELVVMDCA LSPIQQRNLE
KEWHAKVLDR TGLILEIFGR RAKTREGSLQ VELAHLNYQR SRLVRSWTHL ERQRGGFGFM
GGPGETQIEA DRRLIQERIS KLESELKKVQ ATRRLHRAGR QRVPYRVVAL VGYTNAGKST
LFNRLTRAEV QAADMLFATL DPTLRALTLP HGGKAMLSDT VGFISNLPTQ LVAAFRATLE
EVLEADVILH VRDISHEDAE AQQSDVDAVL RQLGINPDDS GRIIEVWNKI DRFDPEQREE
LLNIAARRPE DHPAMLVSAV SGEGIDALLA AIEQRLAAKR TTLDLSIDAA DGAGISWLHR
NAEVLSKELH DGRFDMTVRV DETKRDIVVS RFDAVPHHAT
//
