ID   OBG_BRUA2               Reviewed;         341 AA.
AC   Q2YLM2;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454};
DE   AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN   Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=BAB1_1853;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
CC   -!- FUNCTION: An essential GTPase which binds GTP, GDP and possibly
CC       (p)ppGpp with moderate affinity, with high nucleotide exchange rates
CC       and a fairly low GTP hydrolysis rate. Plays a role in control of the
CC       cell cycle, stress response, ribosome biogenesis and in those bacteria
CC       that undergo differentiation, in morphogenesis control.
CC       {ECO:0000255|HAMAP-Rule:MF_01454}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01454};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
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DR   EMBL; AM040264; CAJ11809.1; -; Genomic_DNA.
DR   RefSeq; WP_002964923.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YLM2; -.
DR   SMR; Q2YLM2; -.
DR   STRING; 359391.BAB1_1853; -.
DR   EnsemblBacteria; CAJ11809; CAJ11809; BAB1_1853.
DR   GeneID; 45125125; -.
DR   GeneID; 55591440; -.
DR   KEGG; bmf:BAB1_1853; -.
DR   PATRIC; fig|359391.11.peg.368; -.
DR   HOGENOM; CLU_011747_2_0_5; -.
DR   OMA; VVFDWEP; -.
DR   PhylomeDB; Q2YLM2; -.
DR   Proteomes; UP000002719; Chromosome I.
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:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd01898; Obg; 1.
DR   Gene3D; 2.70.210.12; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01454; GTPase_Obg; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR   InterPro; IPR006074; GTP1-OBG_CS.
DR   InterPro; IPR006169; GTP1_OBG_dom.
DR   InterPro; IPR036726; GTP1_OBG_dom_sf.
DR   InterPro; IPR045086; OBG_GTPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11702; PTHR11702; 1.
DR   Pfam; PF01018; GTP1_OBG; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF82051; SSF82051; 1.
DR   TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS00905; GTP1_OBG; 1.
DR   PROSITE; PS51883; OBG; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..341
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000385766"
FT   DOMAIN          1..159
FT                   /note="Obg"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT   DOMAIN          160..327
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         166..173
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         191..195
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         212..215
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         279..282
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         308..310
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ   SEQUENCE   341 AA;  36789 MW;  7C440746D70AB29B CRC64;
     MKFLDQAKIY IRSGNGGAGA VSFRREKFLE FGGPDGGDGG RGGDVWVEAV DGLNTLIDYR
     YQQHFKAKTG MHGMGRNMTG GKGDDVVLRV PVGTQIFEED NETLICDITE VGQRYRLAKG
     GNGGFGNLHF TTSTNRAPRR ANPGQEGIER TIWLRLKLIA DAGLVGLPNA GKSTFLASVT
     AAKPKIADYP FTTLHPNLGV ARIDGREFVI ADIPGLIEGA SEGVGLGDRF LGHVERTRVL
     LHLVSAQEED VAKAYQVIRG ELEAYEHGLA DKPEIVALSQ VDTLDPETRK AKVKALKKAC
     GCEPLLLSAV SHEGLNDTLR QLARIIDLSR AEEAGTAQAE E