Difference between revisions of "RacX"
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| − | * '''Description:''' amino acid racemase, production of D-amino acids | + | * '''Description:''' amino acid racemase, production of D-amino acids <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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|style="background:#ABCDEF;" align="center"| '''Product''' || amino acid racemase | |style="background:#ABCDEF;" align="center"| '''Product''' || amino acid racemase | ||
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| − | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || unknown |
|- | |- | ||
|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=BSU34430 racX] | |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=BSU34430 racX] | ||
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
| − | |||
{{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, V, W, X, Y)]]}} | {{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, V, W, X, Y)]]}} | ||
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=== Additional information=== | === Additional information=== | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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=References= | =References= | ||
| − | <pubmed>8491712,19063962,9987136 | + | <pubmed>8491712,19063962,9987136, 7592498, 20817675</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 20:07, 8 March 2014
- Description: amino acid racemase, production of D-amino acids
| Gene name | racX |
| Synonyms | |
| Essential | no |
| Product | amino acid racemase |
| Function | unknown |
| Gene expression levels in SubtiExpress: racX | |
| MW, pI | 25 kDa, 5.396 |
| Gene length, protein length | 681 bp, 227 aa |
| Immediate neighbours | yveF, pbpE |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
cell envelope stress proteins (controlled by SigM, V, W, X, Y)
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU34430
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: aspartate/glutamate racemases family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P32960
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675]
[WorldCat.org]
[DOI]
(I p)
María Mercedes Palomino, Carmen Sanchez-Rivas, Sandra M Ruzal
High salt stress in Bacillus subtilis: involvement of PBP4* as a peptidoglycan hydrolase.
Res Microbiol: 2009, 160(2);117-24
[PubMed:19063962]
[WorldCat.org]
[DOI]
(P p)
X Huang, A Gaballa, M Cao, J D Helmann
Identification of target promoters for the Bacillus subtilis extracytoplasmic function sigma factor, sigma W.
Mol Microbiol: 1999, 31(1);361-71
[PubMed:9987136]
[WorldCat.org]
[DOI]
(P p)
M A Strauch
Delineation of AbrB-binding sites on the Bacillus subtilis spo0H, kinB, ftsAZ, and pbpE promoters and use of a derived homology to identify a previously unsuspected binding site in the bsuB1 methylase promote.
J Bacteriol: 1995, 177(23);6999-7002
[PubMed:7592498]
[WorldCat.org]
[DOI]
(P p)
D L Popham, P Setlow
Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4* and an apparent amino acid racemase.
J Bacteriol: 1993, 175(10);2917-25
[PubMed:8491712]
[WorldCat.org]
[DOI]
(P p)
