HAMAP rule MF_01454
General rule information
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| Accession | MF_01454 |
| Dates | 3-SEP-2009 (Created)
1-JUN-2023 (Last updated, Version 17) |
| Name | GTPase_Obg |
| Scope(s) |
Bacteria |
| Template(s) | P42641 (OBG_ECOLI); P20964 (OBG_BACSU); B8GYI7 (OBG_CAUVN); Q6E0U3 (OBG_VIBHA); P95722 (OBG_STRCO); [ Recover all ] |
| Triggered by |
HAMAP; MF_01454 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | OBG |
| Protein name | RecName: Full=GTPase Obg; EC=3.6.5.-; AltName: Full=GTP-binding protein Obg; |
| Gene name | Name=obg; |
Comments
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| FUNCTION | An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; |
| SUBUNIT | Monomer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. |
Keywords
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| Cytoplasm | |
| GTP-binding | |
| Hydrolase | |
| case <FT:6> or <FT:7> | |
| Magnesium | |
| Metal-binding | |
| end case | |
| Nucleotide-binding | |
Gene Ontology
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| GO:0005525; Molecular function:GTP binding |
| GO:0003924; Molecular function:GTPase activity |
| GO:0005737; Cellular component:cytoplasm |
| GO:0042254; Biological process:ribosome biogenesis |
Cross-references
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| PROSITE | PS51710; G_OBG; 1; |
| PROSITE | PS00905; GTP1_OBG; 1; |
| PROSITE | PS51881; OCT; 0-1; |
| PROSITE | PS51883; OBG; 1; |
| Pfam | PF01018; GTP1_OBG; 1; |
| Pfam | PF01926; MMR_HSR1; 1; |
| PRINTS | PR00326; GTP1OBG; 4; |
| NCBIfam | TIGR02729; Obg_CgtA; 1; |
| NCBIfam | TIGR00231; Small_GTP; 1; |
| NCBIfam | TIGR03595; Obg_CgtA_exten; 1; |
| PIRSF | PIRSF002401; GTP_bd_Obg/CgtA; 1; |
Features
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| From: OBG_ECOLI (P42641) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 166 | 173 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
G-[FIKLMPRVY]-[PS]-[NS]-[ACSTV]-G-[KR]-S | ||||||||
| BINDING | 191 | 195 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
F-[TS]-T-[LIKMR]-[VTHIESNYKAQFDR] | ||||||||
| BINDING | 213 | 216 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
[DE]-[ILMV]-P-[GS] | ||||||||
| BINDING | 283 | 286 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
[NST]-[KQR]-x-[DE] | ||||||||
| BINDING | 314 | 316 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
|||||||||
| BINDING | 173 | 173 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
[ST] | ||||||||
| BINDING | 193 | 193 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
[ST] | ||||||||
Additional information
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| Size range | 326-534 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: <Radical SAM domain> |
| 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 |