Difference between revisions of "YugI"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
| − | {{SubtiWiki category|[[proteins of unknown function]]}} | + | {{SubtiWiki category|[[proteins of unknown function]]}}, |
| + | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
| − | * '''Localization:''' cytoplasm (according to Swiss-Prot) | + | * '''[[Localization]]:''' |
| + | ** cytoplasm (according to Swiss-Prot) | ||
=== Database entries === | === Database entries === | ||
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** subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}} | ** subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}} | ||
** A [[ncRNA]] is predicted between ''[[yugI]]'' and ''[[alaT]]'' {{PubMed|20525796}} | ** A [[ncRNA]] is predicted between ''[[yugI]]'' and ''[[alaT]]'' {{PubMed|20525796}} | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
| − | <pubmed> 17981983, 19152054 19636895 9274030 11948165 20525796</pubmed> | + | <pubmed> 17981983, 19152054 19636895 9274030 11948165 20525796 15378759</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:41, 5 March 2014
- Description: similar to a domain of E. coli polyribonucleotide phosphorylase and to four repeated domains at the N-terminus of E. coli ribosomal protein S1, has an RNA-binding surface
| Gene name | yugI |
| Synonyms | |
| Essential | no |
| Product | unknown |
| Function | unknown |
| Gene expression levels in SubtiExpress: yugI | |
| MW, pI | 14 kDa, 5.918 |
| Gene length, protein length | 390 bp, 130 aa |
| Immediate neighbours | yuzA, alaT |
| 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
proteins of unknown function, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU31390
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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization:
- cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 2K4K
- UniProt: P80870
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Sigma factor:
- 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
Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796]
[WorldCat.org]
[DOI]
(I p)
Wenyu Yu, Bingke Yu, Jicheng Hu, Wei Xia, Changwen Jin, Bin Xia
1H, 13C, and 15N resonance assignments of a general stress protein GSP13 from Bacillus subtilis.
Biomol NMR Assign: 2008, 2(2);163-5
[PubMed:19636895]
[WorldCat.org]
[DOI]
(I p)
Wenyu Yu, Jicheng Hu, Bingke Yu, Wei Xia, Changwen Jin, Bin Xia
Solution structure of GSP13 from Bacillus subtilis exhibits an S1 domain related to cold shock proteins.
J Biomol NMR: 2009, 43(4);255-9
[PubMed:19152054]
[WorldCat.org]
[DOI]
(I p)
Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983]
[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)
Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165]
[WorldCat.org]
[DOI]
(P p)
Bauke Oudega, Gregory Koningstein, Luísa Rodrigues, Maria de Sales Ramon, Helmut Hilbert, Andreas Düsterhöft, Thomas M Pohl, Thomas Weitzenegger
Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).
Microbiology (Reading): 1997, 143 ( Pt 8);2769-2774
[PubMed:9274030]
[WorldCat.org]
[DOI]
(P p)
