ID   OBG_PAUCH               Reviewed;         329 AA.
AC   B1X580;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Putative GTPase Obg {ECO:0000305};
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:P42641};
DE   AltName: Full=GTP-binding protein Obg {ECO:0000250|UniProtKB:P42641};
GN   Name=obg {ECO:0000250|UniProtKB:P42641}; OrderedLocusNames=PCC_0681;
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore.
OC   Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(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. {ECO:0000250|UniProtKB:P42641}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P42641};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P42641}.
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. {ECO:0000250|UniProtKB:P42641}.
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DR   EMBL; CP000815; ACB43099.1; -; Genomic_DNA.
DR   RefSeq; YP_002049309.1; NC_011087.1.
DR   AlphaFoldDB; B1X580; -.
DR   SMR; B1X580; -.
DR   GeneID; 6481995; -.
DR   GO; GO:0070111; C:organellar chromatophore; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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   GTP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Organellar chromatophore; Plastid.
FT   CHAIN           1..329
FT                   /note="Putative GTPase Obg"
FT                   /id="PRO_0000386417"
FT   DOMAIN          1..159
FT                   /note="Obg"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT   DOMAIN          160..328
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   BINDING         166..173
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   BINDING         191..195
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   BINDING         213..216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   BINDING         280..283
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   BINDING         309..311
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
SQ   SEQUENCE   329 AA;  35359 MW;  FC18C9B80704BACC CRC64;
     MQFIDQARIM VYAGRGGDGI VAFRREKYVP AGGPSGGDGG RGGNVIFEAD SNLQTLLDFK
     YKRIFYAEDG NRGGPNRCSG VSGSNLVIKV PCGTEVRHLG SGILLGDLTE PSQQLMIAFG
     GRGGLGNAHY LSNRNRVPEK FTLGREGEEW PLQLELKLLA EVGIIGLPNA GKSTLIGNLS
     AAKPKIADYP FTTLIPNLGA VYRPNGDSII FADIPGLILG AANGAGLGYD FLRHIERTRL
     LVHLIDSSAK DLVHDLIVVE GELIAYGHGL ADRPRIVVLS KIELLSGEEL HQFSQALRMV
     SGCKILVISS AILSSIEFLK TQIWQQLGT