Difference between revisions of "Obg"
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− | <pubmed>15325267,18689482,7961487,7961486,15583165,2537815,10781545,10419966, 12427945,12429099 2537815 20830302 </pubmed> | + | <pubmed>15325267,18689482,7961487,7961486,15583165,2537815,10781545,10419966, 12427945,12429099 2537815 20830302</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 02:48, 4 September 2011
- 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 |
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 |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
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