Difference between revisions of "ManR"
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=ManR ManR] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=ManR ManR] | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/ | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=manR manR]''' |
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 75 kDa, 8.04 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 75 kDa, 8.04 |
Revision as of 10:33, 7 January 2014
Gene name | manR |
Synonyms | yjdC |
Essential | no |
Product | transcriptional activator, PRD-type |
Function | regulation of mannose utilization |
Gene expression levels in SubtiExpress: manR | |
Interactions involving this protein in SubtInteract: ManR | |
Metabolic function and regulation of this protein in SubtiPathways: manR | |
MW, pI | 75 kDa, 8.04 |
Gene length, protein length | 1944 bp, 648 aa |
Immediate neighbours | yjdB, manP |
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
utilization of specific carbon sources, transcription factors and their control, phosphoproteins
This gene is a member of the following regulons
The ManR regulon:
The gene
Basic information
- Locus tag: BSU12000
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: phosphorylation by ManP inactivates ManR (in the absence of mannose), phosphorylation by HPr stimluates ManR PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: O31644
- KEGG entry: [2]
- 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
Marian Wenzel, Josef Altenbuchner
The Bacillus subtilis mannose regulator, ManR, a DNA-binding protein regulated by HPr and its cognate PTS transporter ManP.
Mol Microbiol: 2013, 88(3);562-76
[PubMed:23551403]
[WorldCat.org]
[DOI]
(I p)
Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538]
[WorldCat.org]
[DOI]
(I e)
Tianqi Sun, Josef Altenbuchner
Characterization of a mannose utilization system in Bacillus subtilis.
J Bacteriol: 2010, 192(8);2128-39
[PubMed:20139185]
[WorldCat.org]
[DOI]
(I 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)
J Stülke, M Arnaud, G Rapoport, I Martin-Verstraete
PRD--a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria.
Mol Microbiol: 1998, 28(5);865-74
[PubMed:9663674]
[WorldCat.org]
[DOI]
(P p)