ID A0A4Q5YAP4_9BACT Unreviewed; 396 AA. AC A0A4Q5YAP4; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 14-DEC-2022, entry version 11. 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:RYZ18633.1}; GN ORFNames=EOO16_22000 {ECO:0000313|EMBL:RYZ18633.1}; OS Chitinophagaceae bacterium. OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; Chitinophagaceae. OX NCBI_TaxID=1869212 {ECO:0000313|EMBL:RYZ18633.1, ECO:0000313|Proteomes:UP000293837}; RN [1] {ECO:0000313|EMBL:RYZ18633.1, ECO:0000313|Proteomes:UP000293837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PMG_261 {ECO:0000313|EMBL:RYZ18633.1}; RX PubMed=30498029; DOI=.1073/pnas.1812668115; RA Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J., RA Murphy G.P., McGenity T.J., Murrell J.C.; RT "Poplar phyllosphere harbors disparate isoprene-degrading bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018). 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:RYZ18633.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; SEAK01000400; RYZ18633.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4Q5YAP4; -. DR Proteomes; UP000293837; 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; 3.40.50.11060; -; 1. DR Gene3D; 3.40.50.300; -; 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 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 TIGRFAMs; TIGR03156; GTP_HflX; 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 202..384 FT /note="Hflx-type G" FT /evidence="ECO:0000259|PROSITE:PS51705" FT BINDING 208..215 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1" FT BINDING 215 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2" FT BINDING 233..237 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1" FT BINDING 235 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR006809-2" FT BINDING 254..257 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|PIRSR:PIRSR006809-1" FT BINDING 320..323 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 396 AA; 45726 MW; A15E56855788067F CRC64; MIDNRNKIQE EEMAVLVGVV QKEQTETQVT EYLDELAFLA ETAGAVTVKR FVQKLARPEP KTFVGKGKLQ EIAAYVQSHG INLIIFDDEL TGAQIGNIEK ETKVKVIDRS DLILDIFARR AKTAQAKAQV ELAQYQYILP RLRGMWTHLE RLGGGIGTRG PGESEIETDR RIVREKISLL RKRLQEIDKQ AFTQRKERGE FIRVSLVGYT NVGKSTLMNL LSKSEVLAEN KLFATLDTTT RKIVYETTPF LLSDTVGFIR KLPHHLVESF KSTLDEVREA DILLHVVDLS HPQYEDQMGT VNKTLQELKS FEKPILIIFN KLDEYVAKTF DAWLDDATKA DLLRELEERW QRETNGNALF ISALQRTNID KLREVILEKV RELYRIRYPY KTEFFY //