ID   OBG_WOLPP               Reviewed;         337 AA.
AC   B3CNP2;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=WP0204;
OS   Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=570417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wPip;
RX   PubMed=18550617; DOI=10.1093/molbev/msn133;
RA   Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA   Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT   "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL   Mol. Biol. Evol. 25:1877-1887(2008).
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; AM999887; CAQ54312.1; -; Genomic_DNA.
DR   RefSeq; WP_007302664.1; NC_010981.1.
DR   AlphaFoldDB; B3CNP2; -.
DR   SMR; B3CNP2; -.
DR   STRING; 570417.WP0204; -.
DR   PRIDE; B3CNP2; -.
DR   EnsemblBacteria; CAQ54312; CAQ54312; WP0204.
DR   KEGG; wpi:WP0204; -.
DR   eggNOG; COG0536; Bacteria.
DR   HOGENOM; CLU_011747_2_0_5; -.
DR   OMA; VVFDWEP; -.
DR   OrthoDB; 603226at2; -.
DR   Proteomes; UP000008814; 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: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; 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; PS51883; OBG; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..337
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000386387"
FT   DOMAIN          1..159
FT                   /note="Obg"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT   DOMAIN          160..329
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         310..312
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ   SEQUENCE   337 AA;  37332 MW;  679CF4BDB6F55C39 CRC64;
     MDFIDEVKLY LKAGDGGDGC ASFRREKFVE FGGPNGGNGG KGGDIIFISD ANLNTLLNFR
     CRRHIKASSG KSGTSRDRSG TAGKDIILKV PVGTQIIDEE SEEVIVDLDK PDMEFQVVQG
     GKGGLGNTNF KSSTNRAPRH FTHGQPGEER NIVLKLKVLS DVGIIGMPNV GKSKFLTRCS
     NSDTKVGDYE FTTIRPHLGV AKVDYSEIVI ADIPGIIADA HLGVGLGHKF LKHIERCKIL
     LHLIDVTHDE IISAYNCTHN ELKLYNSDLV EKEEIVVLNK CDLLEETEIL EKKNHLANYL
     DREVLCLSID DDLQPILRLL NEKVKTKEIN VYDPFKM