Difference between revisions of "Obg"
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+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[translation]]}}, | ||
+ | {{SubtiWiki category|[[phosphorelay]]}}, | ||
+ | {{SubtiWiki category|[[essential genes]]}}, | ||
+ | {{SubtiWiki category|[[GTP-binding proteins]]}} | ||
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+ | = This gene is a member of the following [[regulons]] = | ||
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=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 21:58, 8 December 2010
- 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 |
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.
- Localization:
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
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
Yuno Lee, Woo Young Bang, Songmi Kim, Prettina Lazar, Chul Wook Kim, Jeong Dong Bahk, Keun Woo Lee
Molecular modeling study for interaction between Bacillus subtilis Obg and Nucleotides.
PLoS One: 2010, 5(9);e12597
[PubMed:20830302]
[WorldCat.org]
[DOI]
(I e)
Shrin Kuo, Borries Demeler, W G Haldenwang
The growth-promoting and stress response activities of the Bacillus subtilis GTP binding protein Obg are separable by mutation.
J Bacteriol: 2008, 190(20);6625-35
[PubMed:18689482]
[WorldCat.org]
[DOI]
(I p)
Shrin Kuo, Shuyu Zhang, Robyn L Woodbury, W G Haldenwang
Associations between Bacillus subtilis sigmaB regulators in cell extracts.
Microbiology (Reading): 2004, 150(Pt 12);4125-36
[PubMed:15583165]
[WorldCat.org]
[DOI]
(P p)
Shuyu Zhang, W G Haldenwang
Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to ribosomes.
Biochem Biophys Res Commun: 2004, 322(2);565-9
[PubMed:15325267]
[WorldCat.org]
[DOI]
(P p)
John Buglino, Vincent Shen, Payam Hakimian, Christopher D Lima
Structural and biochemical analysis of the Obg GTP binding protein.
Structure: 2002, 10(11);1581-92
[PubMed:12429099]
[WorldCat.org]
[DOI]
(P p)
Takuya Morimoto, Pek Chin Loh, Tomohiro Hirai, Kei Asai, Kazuo Kobayashi, Shigeki Moriya, Naotake Ogasawara
Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis.
Microbiology (Reading): 2002, 148(Pt 11);3539-3552
[PubMed:12427945]
[WorldCat.org]
[DOI]
(P p)
J M Scott, J Ju, T Mitchell, W G Haldenwang
The Bacillus subtilis GTP binding protein obg and regulators of the sigma(B) stress response transcription factor cofractionate with ribosomes.
J Bacteriol: 2000, 182(10);2771-7
[PubMed:10781545]
[WorldCat.org]
[DOI]
(P p)
J M Scott, W G Haldenwang
Obg, an essential GTP binding protein of Bacillus subtilis, is necessary for stress activation of transcription factor sigma(B).
J Bacteriol: 1999, 181(15);4653-60
[PubMed:10419966]
[WorldCat.org]
[DOI]
(P p)
K M Welsh, K A Trach, C Folger, J A Hoch
Biochemical characterization of the essential GTP-binding protein Obg of Bacillus subtilis.
J Bacteriol: 1994, 176(23);7161-8
[PubMed:7961487]
[WorldCat.org]
[DOI]
(P p)
J Kok, K A Trach, J A Hoch
Effects on Bacillus subtilis of a conditional lethal mutation in the essential GTP-binding protein Obg.
J Bacteriol: 1994, 176(23);7155-60
[PubMed:7961486]
[WorldCat.org]
[DOI]
(P p)
K Trach, J A Hoch
The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein.
J Bacteriol: 1989, 171(3);1362-71
[PubMed:2537815]
[WorldCat.org]
[DOI]
(P p)