AC   MF_01454;
DC   Protein; auto
TR   HAMAP; MF_01454; -; 1; level=0
XX
Names: GTPase_Obg
XX
ID   OBG
DE   RecName: Full=GTPase Obg;
DE            EC=3.6.5.-;
DE   AltName: Full=GTP-binding protein Obg;
GN   Name=obg;
XX
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family.
XX
DR   PROSITE; PS51710; G_OBG; 1; trigger=yes
DR   PROSITE; PS00905; GTP1_OBG; 1; trigger=no
DR   PROSITE; PS51881; OCT; 0-1; trigger=yes
DR   PROSITE; PS51883; OBG; 1; trigger=yes
DR   Pfam; PF01018; GTP1_OBG; 1; trigger=no
DR   Pfam; PF01926; MMR_HSR1; 1; trigger=yes
DR   PRINTS; PR00326; GTP1OBG; 4; trigger=no
DR   NCBIfam; TIGR02729; Obg_CgtA; 1; trigger=no
DR   NCBIfam; TIGR00231; Small_GTP; 1; trigger=no
DR   NCBIfam; TIGR03595; Obg_CgtA_exten; 1; trigger=no
DR   PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1; trigger=no
XX
KW   Cytoplasm
KW   GTP-binding
KW   Hydrolase
case <FT:6> or <FT:7>
KW   Magnesium
KW   Metal-binding
end case
KW   Nucleotide-binding
XX
GO   GO:0005525; F:GTP binding
GO   GO:0003924; F:GTPase activity
GO   GO:0005737; C:cytoplasm
GO   GO:0042254; P:ribosome biogenesis
XX
FT   From: OBG_ECOLI (P42641)
FT   BINDING         166..173
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-[FIKLMPRVY]-[PS]-[NS]-[ACSTV]-G-[KR]-S
FT   BINDING         191..195
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: F-[TS]-T-[LIKMR]-[VTHIESNYKAQFDR]
FT   BINDING         213..216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: [DE]-[ILMV]-P-[GS]
FT   BINDING         283..286
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: [NST]-[KQR]-x-[DE]
FT   BINDING         314..316
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: [ST]
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: [ST]
XX
Size: 326-534;
Related: None;
Template: P42641; P20964; B8GYI7; Q6E0U3; P95722;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: <Radical SAM domain>
Duplicate: in ANAMF, ANAMM
Plasmid: in CERS5
Comments: BRAHW is C-terminally fused to a radical SAM-type domain.
 It has been noted that "The C-terminal domains of these proteins, however,
 can vary in both length and sequence, which may result in functional
 differences between distantly related bacteria." PubMed:15554976
XX
# Revision 1.17 2023/06/01
//