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 | Bacteria |
Templates | P42641 (OBG_ECOLI); P20964 (OBG_BACSU); B8GYI7 (OBG_CAUVN); Q6E0U3 (OBG_VIBHA); P95722 (OBG_STRCO): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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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 | Mg(2+) |
Subunit | Monomer. |
Subcellular location | Cytoplasm. |
Similarity | Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. |
Keywords
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case <FT:6> or <FT:7>
end case
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.
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; trigger=PRU01047; |
PS00905; GTP1_OBG; 1; | |
PS51881; OCT; 0-1; trigger=PRU01229; | |
PS51883; OBG; 1; trigger=PRU01231; | |
Pfam | PF01018; GTP1_OBG; 1; |
PF01926; MMR_HSR1; 1; trigger=Yes; | |
PRINTS | PR00326; GTP1OBG; 4; |
NCBIfam | TIGR02729; Obg_CgtA; 1; |
TIGR00231; Small_GTP; 1; | |
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 |