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Database: UniProt
Entry: A0A1I4UAI1_9FLAO
LinkDB: A0A1I4UAI1_9FLAO
Original site: A0A1I4UAI1_9FLAO 
ID   A0A1I4UAI1_9FLAO        Unreviewed;       412 AA.
AC   A0A1I4UAI1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-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=SAMN05421738_103157 {ECO:0000313|EMBL:SFM85972.1};
OS   Algoriella xinjiangensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Algoriella.
OX   NCBI_TaxID=684065 {ECO:0000313|EMBL:SFM85972.1, ECO:0000313|Proteomes:UP000199149};
RN   [1] {ECO:0000313|EMBL:SFM85972.1, ECO:0000313|Proteomes:UP000199149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XJ109 {ECO:0000313|EMBL:SFM85972.1,
RC   ECO:0000313|Proteomes:UP000199149};
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   -!- 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; FOUZ01000003; SFM85972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4UAI1; -.
DR   STRING; 684065.SAMN05421738_103157; -.
DR   OrthoDB; 9812272at2; -.
DR   Proteomes; UP000199149; 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   412 AA;  48146 MW;  7426195DD3607E73 CRC64;
     MLEKKETQYE KVVLIGLVTQ KQSEEKLTEY MDELEFLTYT AGAEVATRFT QKVDKPDPKF
     FVGSGKLNEI LEYVVANNID TLIFDDELSP SQLKNIEKVV ERKVIDRTQL ILDIFAQRAQ
     TSYARTQVEL AQYQYLLPRL TRMWTHLERQ RGGIGMRGPG ETEIETDRRI IRDRITLLKD
     KLKTVDRQMA TQRKNRGALV RVALVGYTNV GKSTLMNVLS KSDVFAEDKL FATLDTTVRK
     VVIGNLPFLL TDTVGFIRKL PTQLIESFKS TLDEVREADL LIHVVDISHE SFEDHVNSVN
     EILAEIDSKD KPTIMVFNKI DNFSYIEKAE DDLSEMKFEN YSLEDWKRTW MSKNEYETLF
     ISATENDNLE ELRKALYEKV KEIHMKRFPY NNFLFQYYEE EVEEEDDSQD EE
//
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