ID M4KYG2_BACIU Unreviewed; 460 AA. AC M4KYG2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 13-NOV-2013, entry version 6. DE RecName: Full=GTPase HflX; DE AltName: Full=GTP-binding protein HflX; GN Name=ynbA; Synonyms=hflX; ORFNames=C663_1792; OS Bacillus subtilis XF-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1233100; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=XF-1; RX PubMed=23558530; RA Guo S., Mao Z., Wu Y., Hao K., He P., He Y.; RT "Genome Sequencing of Bacillus subtilis Strain XF-1 with High RT Efficiency in the Suppression of Plasmodiophora brassicae."; RL Genome Announc. 1:E0006613-E0006613(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis (By similarity). CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=May associate with membranes CC (By similarity). CC -!- SIMILARITY: Belongs to the HflX GTPase family. CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain. 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; CP004019; AGE63584.1; -; Genomic_DNA. DR RefSeq; YP_007426921.1; NC_020244.1. DR ProteinModelPortal; M4KYG2; -. DR EnsemblBacteria; AGE63584; AGE63584; C663_1792. DR GeneID; 14561883; -. DR KEGG; bsx:C663_1792; -. DR KO; K03665; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC. DR HAMAP; MF_00900; GTPase_HflX; 1; -. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 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; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 3: Inferred from homology; KW Cytoplasm; GTP-binding; Nucleotide-binding. FT DOMAIN 242 361 G (By similarity). FT NP_BIND 247 255 GTP (By similarity). FT NP_BIND 360 363 GTP (By similarity). SQ SEQUENCE 460 AA; 52450 MW; B9C8A9195B8E0ADC CRC64; MRGLFFARIS AFQSNRFVVY TCRVWYDNTT AQYAKERNIH LNEQETIQEK AILVGCQLPH ITDEHFENSM EELASLTKTA DGKVLTSVTQ KRNRADAATY IGKGKVEELK ALVEELEADL LIFNDELSPS QLKSLATAIE VKMIDRTQLI LDIFAKRART REGKLQIELA QLQYALPRLT GQGINLSRQG GGIGARGPGE TKLETDRRHI RNRIHEINTQ LSTVIRHRSR YRERRKKNGV LQIALVGYTN AGKSTWFNRL TSADSYEEDL LFATLDPMTR KMVLPSGYSV LLSDTVGFIQ DLPTTLIAAF RSTLEEVKEA DLILHLIDSS NEDYAGHEKT VLRLLEELEA DDIPMLTAYN KRDQKLPDFI PSAGRDHIMV SAKFEDDAAA FKEAIQRYLR QELLTSFEAH VPASEGKLLS RIKSETMVDR FYFNEENEQY DISGYVQEEQ SIIGELKKYM //