ID A0A1M4X7E4_9FLAO Unreviewed; 408 AA.
AC A0A1M4X7E4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05444408_105223 {ECO:0000313|EMBL:SHE89313.1};
OS Chryseobacterium takakiae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1302685 {ECO:0000313|EMBL:SHE89313.1, ECO:0000313|Proteomes:UP000184236};
RN [1] {ECO:0000313|EMBL:SHE89313.1, ECO:0000313|Proteomes:UP000184236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26898 {ECO:0000313|EMBL:SHE89313.1,
RC ECO:0000313|Proteomes:UP000184236};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 -!- 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; FQVO01000005; SHE89313.1; -; Genomic_DNA.
DR RefSeq; WP_072884460.1; NZ_FQVO01000005.1.
DR AlphaFoldDB; A0A1M4X7E4; -.
DR STRING; 1302685.SAMN05444408_105223; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000184236; 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 InterPro; IPR005225; Small_GTP-bd_dom.
DR NCBIfam; TIGR03156; GTP_HflX; 1.
DR NCBIfam; TIGR00231; small_GTP; 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}.
FT DOMAIN 200..384
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT BINDING 206..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 231..235
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT BINDING 252..255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 318..321
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT BINDING 362..364
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ SEQUENCE 408 AA; 47530 MW; 9053E48084B16516 CRC64;
MLEKKEHNYE KAVLVGVVTQ HQDEDKLQEY MDELEFLAYT AGATVDKRFT QKLTQPDSKT
FIGSGKAQEI RDYVKEHEIG TVIFDDELSP SQLKNLEREM EVKILDRTNL ILDIFAQRAT
TSYARTQVEL AQYQYLLPRL TRMWTHLERQ KGGIGMRGPG ETEIETDRRI IRDRISLLKD
KLKTIDKQMA TQRNNRGKVV RVALVGYTNV GKSTLMNALS KSEVFAENKL FATLDTTVRK
VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHIDSVN
QILMEINAHQ KPMIMIFNKI DDFSYEKKDE DDLTPSTRKN ISLEEWKNTW MAKSKYPTVF
ISALTKENFP EMKKMIYDEV MKIHISRFPY NDFLFEYFDN DEEENNPD
//
