Difference between revisions of "MurR"
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|style="background:#ABCDEF;" align="center"|'''Gene name''' | |style="background:#ABCDEF;" align="center"|'''Gene name''' | ||
| − | |'' | + | |''murR'' |
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| − | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | + | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ybbH '' |
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
Revision as of 17:06, 20 April 2010
- Description: probably transcriptional regulator of genes required for the utilization of N-acetylmuramic acid, homolog to E. coli MurR
| Gene name | murR |
| Synonyms | ybbH |
| Essential | no |
| Product | transcriptional repressor |
| Function | probably regulation of muramic acid utilization |
| MW, pI | 30 kDa, 6.873 |
| Gene length, protein length | 849 bp, 283 aa |
| Immediate neighbours | murP, murQ |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU01690
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 2O3F (N-terminal domain)
- UniProt: Q45581
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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
Silke Litzinger, Amanda Duckworth, Katja Nitzsche, Christian Risinger, Valentin Wittmann, Christoph Mayer
Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase.
J Bacteriol: 2010, 192(12);3132-43
[PubMed:20400549]
[WorldCat.org]
[DOI]
(I p)
Ulrike Dahl, Tina Jaeger, Bao Trâm Nguyen, Julia M Sattler, Christoph Mayer
Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid.
J Bacteriol: 2004, 186(8);2385-92
[PubMed:15060041]
[WorldCat.org]
[DOI]
(P p)
Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040]
[WorldCat.org]
[DOI]
(P p)
