Difference between revisions of "EpsB"
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* '''Additional information:''' | * '''Additional information:''' | ||
** induction by sequestration of [[SinR]] by [[SinI]] or [[SlrA]] {{PubMed|15661000,19788541}} | ** induction by sequestration of [[SinR]] by [[SinI]] or [[SlrA]] {{PubMed|15661000,19788541}} | ||
| + | ** the ''[[epsA]]-[[epsB]]-[[epsC]]-[[epsD]]-[[epsE]]-[[epsF]]-[[epsG]]-[[epsH]]-[[epsI]]-[[epsJ]]-[[epsK]]-[[epsL]]-[[epsM]]-[[epsN]]-[[epsO]]'' operon is not expressed in a ''[[ymdB]]'' mutant {{PubMed|21856853}} | ||
| + | ** the amount of the mRNA is substantially decreased upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ||
=Biological materials = | =Biological materials = | ||
| Line 142: | Line 144: | ||
==Original publications== | ==Original publications== | ||
'''Additional publications:''' {{PubMed|20817675}} | '''Additional publications:''' {{PubMed|20817675}} | ||
| + | <big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | ||
| + | <big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big> | ||
| + | <big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | ||
| + | [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | ||
| + | |||
| + | <big>''Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J'' </big> | ||
| + | <big>'''A Novel Factor Controlling Bistability in ''Bacillus subtilis'': The YmdB Protein Affects</big> | ||
| + | <big>Flagellin Expression and Biofilm Formation.''' </big> | ||
| + | <big>J Bacteriol.: 2011, 193(21):5997-6007. </big> | ||
| + | [http://www.ncbi.nlm.nih.gov/pubmed/21856853 PubMed:21856853] | ||
| + | |||
<pubmed>15661000,16430695,18047568,18647168 18547145 </pubmed> | <pubmed>15661000,16430695,18047568,18647168 18547145 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 20:06, 19 November 2011
- Description: extracellular polysaccharide synthesis, putative protein tyrosine kinase
| Gene name | epsB |
| Synonyms | yveL |
| Essential | no |
| Product | unknown |
| Function | biofilm formation |
| Interactions involving this protein in SubtInteract: EpsB | |
| Regulation of this protein in SubtiPathways: Biofilm | |
| MW, pI | 24 kDa, 9.918 |
| Gene length, protein length | 681 bp, 227 aa |
| Immediate neighbours | epsC, epsA |
| 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
protein modification, biofilm formation
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU34360
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate (according to Swiss-Prot)
- Protein family: BY kinase, see the Bacterial Protein Tyrosine Kinase Database)
- Paralogous protein(s): PtkA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: P71051
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Richard Losick, Harvard Univ., Cambridge, USA homepage
Your additional remarks
References
Reviews
Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481]
[WorldCat.org]
[DOI]
(I p)
Original publications
Additional publications: PubMed
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947
Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J A Novel Factor Controlling Bistability in Bacillus subtilis: The YmdB Protein Affects Flagellin Expression and Biofilm Formation. J Bacteriol.: 2011, 193(21):5997-6007. PubMed:21856853
Kazuo Kobayashi
SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 69(6);1399-410
[PubMed:18647168]
[WorldCat.org]
[DOI]
(I p)
Vanesa Olivares-Illana, Philippe Meyer, Emmanuelle Bechet, Virginie Gueguen-Chaignon, Didier Soulat, Sylvie Lazereg-Riquier, Ivan Mijakovic, Josef Deutscher, Alain J Cozzone, Olivier Laprévote, Solange Morera, Christophe Grangeasse, Sylvie Nessler
Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus.
PLoS Biol: 2008, 6(6);e143
[PubMed:18547145]
[WorldCat.org]
[DOI]
(I p)
Yunrong Chai, Frances Chu, Roberto Kolter, Richard Losick
Bistability and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 67(2);254-63
[PubMed:18047568]
[WorldCat.org]
[DOI]
(P p)
Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695]
[WorldCat.org]
[DOI]
(P p)
Daniel B Kearns, Frances Chu, Steven S Branda, Roberto Kolter, Richard Losick
A master regulator for biofilm formation by Bacillus subtilis.
Mol Microbiol: 2005, 55(3);739-49
[PubMed:15661000]
[WorldCat.org]
[DOI]
(P p)
