ID   OBG_CORML               Reviewed;         221 AA.
AC   P0C1E7; P46584;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=GTPase Obg {ECO:0000250|UniProtKB:P42641};
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:P42641};
DE   AltName: Full=GTP-binding protein Obg {ECO:0000250|UniProtKB:P42641};
DE   Flags: Fragment;
GN   Name=obg {ECO:0000250|UniProtKB:P42641};
OS   Corynebacterium melassecola.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=41643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17965 / AS B-4821;
RX   PubMed=8755867; DOI=10.1128/jb.178.15.4412-4419.1996;
RA   Ankri S., Serebrijski I., Reyes O., Leblon G.;
RT   "Mutations in the Corynebacterium glutamicum proline biosynthetic pathway:
RT   a natural bypass of the proA step.";
RL   J. Bacteriol. 178:4412-4419(1996).
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: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: Cytoplasm {ECO:0000250|UniProtKB:P42641}.
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; U31230; AAC44173.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C1E7; -.
DR   SMR; P0C1E7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.350; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR036346; GTP-bd_prot_GTP1/OBG_C_sf.
DR   InterPro; IPR015349; OCT_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF09269; DUF1967; 1.
DR   SUPFAM; SSF102741; SSF102741; 1.
DR   TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS51881; OCT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..221
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000236034"
FT   DOMAIN          1..61
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   DOMAIN          82..162
FT                   /note="OCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT   BINDING         10..13
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   BINDING         42..44
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P42641"
FT   NON_TER         1
SQ   SEQUENCE   221 AA;  24716 MW;  A0CA77DB6DF3DB02 CRC64;
     PSALRLVLLN KADAPEALKS FAEVLKVRLF EKQFGWPVFI ISAVARKALD PLKYKLLEIV
     QDARKKRPKE KAESVIIKPK AVVHRTKGQF QIKPDPEVQG GFIITGEKPE RWILQTDFEN
     DEAVGYLADR LSKLGIEDGL RKAGAHVGAN VTIGGISFEW EPMTTAGDDP ILTGRGTDVR
     LEQTSRISAA ERKRASQVRR GLIDELDYGE DQEASRERWE G