Difference between revisions of "MtnA"
| Line 56: | Line 56: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13550&redirect=T BSU13550] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mtnKA.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mtnKA.html] | ||
| Line 91: | Line 92: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13550&redirect=T BSU13550] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2YVK 2YVK] | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2YVK 2YVK] | ||
Revision as of 13:32, 2 April 2014
- Description: 5-methylthioribose-1-phosphate isomerase
| Gene name | mtnA |
| Synonyms | ykrS, mtnS |
| Essential | no |
| Product | 5-methylthioribose-1-phosphate isomerase |
| Function | methionine salvage |
| Gene expression levels in SubtiExpress: mtnA | |
| Metabolic function and regulation of this protein in SubtiPathways: mtnA | |
| MW, pI | 38 kDa, 5.003 |
| Gene length, protein length | 1059 bp, 353 aa |
| Immediate neighbours | ogt, mtnK |
| 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
biosynthesis/ acquisition of amino acids, phosphoproteins, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13550
Phenotypes of a mutant
Database entries
- BsubCyc: BSU13550
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate (according to Swiss-Prot)
- Protein family: MtnA subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- phosphorylated on Arg-80 and Arg-298 PubMed
- Effectors of protein activity:
Database entries
- BsubCyc: BSU13550
- Structure: 2YVK
- UniProt: O31662
- KEGG entry: [3]
- E.C. number: 5.3.1.23
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Regulatory mechanism: S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed
- Additional information:
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P p)
Agnieszka Sekowska, Valérie Dénervaud, Hiroki Ashida, Karine Michoud, Dieter Haas, Akiho Yokota, Antoine Danchin
Bacterial variations on the methionine salvage pathway.
BMC Microbiol: 2004, 4;9
[PubMed:15102328]
[WorldCat.org]
[DOI]
(I e)
Maumita Mandal, Benjamin Boese, Jeffrey E Barrick, Wade C Winkler, Ronald R Breaker
Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria.
Cell: 2003, 113(5);577-86
[PubMed:12787499]
[WorldCat.org]
[DOI]
(P p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)
Brooke A Murphy, Frank J Grundy, Tina M Henkin
Prediction of gene function in methylthioadenosine recycling from regulatory signals.
J Bacteriol: 2002, 184(8);2314-8
[PubMed:11914366]
[WorldCat.org]
[DOI]
(P p)
A Sekowska, L Mulard, S Krogh, J K Tse, A Danchin
MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis.
BMC Microbiol: 2001, 1;15
[PubMed:11545674]
[WorldCat.org]
[DOI]
(I p)
