ID   M4KYG2_BACIU            Unreviewed;       460 AA.
AC   M4KYG2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   15-FEB-2017, entry version 29.
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   -!- 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}.
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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   CDD; cd01878; HflX; 1.
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   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}.
FT   DOMAIN      241    403       Hflx-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51705}.
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
//