ID   M4KYG2_BACIU            Unreviewed;       460 AA.
AC   M4KYG2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 44.
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 Efficiency in
RT   the Suppression of Plasmodiophora brassicae.";
RL   Genome Announc. 1:E0006613-E0006613(2013).
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; CP004019; AGE63584.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGE63584; AGE63584; C663_1792.
DR   KEGG; bsx:C663_1792; -.
DR   PATRIC; fig|1233100.3.peg.1908; -.
DR   HOGENOM; CLU_019597_1_0_9; -.
DR   Proteomes; UP000011821; Chromosome.
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; 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   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          241..403
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
FT   BINDING         247..254
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT   BINDING         272..276
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT   BINDING         294..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         360..363
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         381..383
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
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
//