Difference between revisions of "MraZ"
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* '''Operon:''' ''[[mraZ]]-[[mraW]]-[[ftsL]]-[[pbpB]]'' {{PubMed|8636036,8244929}} | * '''Operon:''' ''[[mraZ]]-[[mraW]]-[[ftsL]]-[[pbpB]]'' {{PubMed|8636036,8244929}} | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mraZ_1580121_1580552_1 mraZ] {{PubMed|22383849}} |
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+ | * '''Sigma factor:''' | ||
* '''Regulation:''' | * '''Regulation:''' |
Revision as of 08:24, 13 April 2012
- Description: Putative DNA-binding protein
Gene name | mraZ |
Synonyms | yllB |
Essential | no |
Product | unknown |
Function | unknown |
MW, pI | 16 kDa, 4.969 |
Gene length, protein length | 429 bp, 143 aa |
Immediate neighbours | bshC, mraW |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15130
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
the E.coli homolog: mraZ
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: mraZ family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- nucleoid (heterogeneous) PubMed
Database entries
- Structure:
- UniProt: P55343
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- 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
Melanie A Adams, Christian M Udell, Gour Pada Pal, Zongchao Jia
MraZ from Escherichia coli: cloning, purification, crystallization and preliminary X-ray analysis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2005, 61(Pt 4);378-80
[PubMed:16511046]
[WorldCat.org]
[DOI]
(I p)
Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537]
[WorldCat.org]
[DOI]
(P p)
R A Daniel, A M Williams, J Errington
A complex four-gene operon containing essential cell division gene pbpB in Bacillus subtilis.
J Bacteriol: 1996, 178(8);2343-50
[PubMed:8636036]
[WorldCat.org]
[DOI]
(P p)
A Yanouri, R A Daniel, J Errington, C E Buchanan
Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis.
J Bacteriol: 1993, 175(23);7604-16
[PubMed:8244929]
[WorldCat.org]
[DOI]
(P p)