ID M4KYG2_BACIU Unreviewed; 460 AA. AC M4KYG2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 08-JUN-2016, entry version 26. 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=ynbA {ECO:0000313|EMBL:AGE63584.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C663_1792 {ECO:0000313|EMBL:AGE63584.1}; OS Bacillus subtilis XF-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1233100 {ECO:0000313|EMBL:AGE63584.1, ECO:0000313|Proteomes:UP000011821}; RN [1] {ECO:0000313|EMBL:AGE63584.1, ECO:0000313|Proteomes:UP000011821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XF-1 {ECO:0000313|EMBL:AGE63584.1}; 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. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00900}; 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- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Contains 1 Hflx-type G (guanine nucleotide-binding) CC domain. {ECO:0000256|HAMAP-Rule:MF_00900}. 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 ProteinModelPortal; M4KYG2; -. DR EnsemblBacteria; AGE63584; AGE63584; C663_1792. DR KEGG; bsx:C663_1792; -. DR KO; K03665; -. DR Proteomes; UP000011821; Chromosome. 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:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 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; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011821}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00900}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 241 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NP_BIND 247 254 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 272 276 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 294 297 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 360 363 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 381 383 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT METAL 254 254 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00900}. FT METAL 274 274 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00900}. 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 //