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OBG_WOLWR
ID   OBG_WOLWR               Reviewed;         340 AA.
AC   C0R5N5;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=WRi_002520;
OS   Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=66084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wRi;
RX   PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA   Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA   Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA   Andersson S.G.;
RT   "The mosaic genome structure of the Wolbachia wRi strain infecting
RT   Drosophila simulans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
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; CP001391; ACN95077.1; -; Genomic_DNA.
DR   RefSeq; WP_006280016.1; NZ_MKIF01000149.1.
DR   AlphaFoldDB; C0R5N5; -.
DR   SMR; C0R5N5; -.
DR   STRING; 66084.WRi_002520; -.
DR   PRIDE; C0R5N5; -.
DR   EnsemblBacteria; ACN95077; ACN95077; WRi_002520.
DR   KEGG; wri:WRi_002520; -.
DR   HOGENOM; CLU_011747_2_0_5; -.
DR   OMA; VVFDWEP; -.
DR   Proteomes; UP000001293; 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..340
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000386390"
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   340 AA;  37204 MW;  9FDDC64E370440AB CRC64;
     MGFIDEVKLC LKAGDGGDGC ASFRREKFVE FGGPNGGNGG KGGNIVFISD ANLNTLLHFR
     YRRHIKADSG KNGAGRDRSG TAGKDVILKV PVGAQIIDEE SEEIIVDLDK PGMEFQVAQG
     GKGGLGNTNF KSSTNKAPRH FTYGQPGEEK HVLLKLKVLS DVGIIGMPNA GKSKFLTRCS
     NSDTKVGDYP FTTVRPHLGM VKVDDSEVVI ADIPGIITDA HLGVGLGHKF LKHIERCQIL
     LHLIDVTHDD VVSAYSCIHN ELELYNSDLV EKEEIVVLNK CDLLREAEIL EKKNHLANYL
     NKEVLCLSIN GDLQPILRLL SEKLKKSNSK EIDVYDPFKA
 
 
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