Difference between revisions of "Obg"
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of the [[phosphorelay]] that activates [[Spo0A]] | of the [[phosphorelay]] that activates [[Spo0A]] | ||
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| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU27920 obg] |
of the [[phosphorelay]] that activates [[Spo0A]] | of the [[phosphorelay]] that activates [[Spo0A]] | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' ||'' [[pheB]]'', ''[[spo0B]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' ||'' [[pheB]]'', ''[[spo0B]]'' | ||
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| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU27920 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU27920 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU27920 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:obg_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:obg_context.gif]] | ||
Revision as of 13:28, 13 May 2013
- Description: GTP-binding protein involved in initiation of sporulation and assembly of the 50S ribosome subunit
| Gene name | obg |
| Synonyms | |
| Essential | Yes |
| Product | GTP-binding protein |
| Function | ribosome assembly, may be required to stimulate activity of the phosphorelay that activates Spo0A |
| Gene expression levels in SubtiExpress: obg
of the phosphorelay that activates Spo0A | |
| Interactions involving this protein in SubtInteract: Obg | |
| MW, pI | 47 kDa, 4.859 |
| Gene length, protein length | 1284 bp, 428 aa |
| Immediate neighbours | pheB, spo0B |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
translation, phosphorelay, essential genes, GTP-binding proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27920
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Binds and hydrolyzes GTP and readily exchanges GDP for GTP
- Protein family: GTP1/OBG family (according to Swiss-Prot) Era/Obg family
Extended information on the protein
- Kinetic information:
- Domains:
Obg possesses 3 domains: A N-terminal glycine-rich domain (1–158), a GTP binding domain (159–342) and a C-terminal TGS domain (343–428). The TGS domain has no known function, but it is named for three protein families in which it is found, ThrRS, GTPase, and SpoT.
- Modification:
- Cofactor(s):
GDP, GTP and probably ppGpp
- Effectors of protein activity:
Interaction with Rsb proteins.
Database entries
- UniProt: P20964
- KEGG entry: [3]
- E.C. number:
Additional information
The biochemical analysis of bacterial and human Obg proteins combined with the structural observation of the ppGpp nucleotide within the Obg active site suggest a potential role for ppGpp modulation of Obg function in B. subtilis.
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Bill Haldenwang, San Antonio, USA
- Naotake Ogasawara, Nara, Japan
Your additional remarks
References
Reviews
Natalie Verstraeten, Maarten Fauvart, Wim Versées, Jan Michiels
The universally conserved prokaryotic GTPases.
Microbiol Mol Biol Rev: 2011, 75(3);507-42, second and third pages of table of contents
[PubMed:21885683]
[WorldCat.org]
[DOI]
(I p)
Robert A Britton
Role of GTPases in bacterial ribosome assembly.
Annu Rev Microbiol: 2009, 63;155-76
[PubMed:19575570]
[WorldCat.org]
[DOI]
(I p)
Original publications
