Difference between revisions of "EpsB"
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| − | * '''Description:''' extracellular polysaccharide synthesis, | + | * '''Description:''' extracellular polysaccharide synthesis, protein tyrosine kinase <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
| Line 10: | Line 10: | ||
|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || protein tyrosine kinase |
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || [[biofilm formation]] | |style="background:#ABCDEF;" align="center"|'''Function''' || [[biofilm formation]] | ||
| Line 43: | Line 43: | ||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[protein modification]]}}, | {{SubtiWiki category|[[protein modification]]}}, | ||
| − | {{SubtiWiki category|[[biofilm formation]]}} | + | {{SubtiWiki category|[[biofilm formation]]}}, |
| + | {{SubtiWiki category|[[phosphoproteins]]}} | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| Line 83: | Line 84: | ||
* '''[[Domains]]:''' | * '''[[Domains]]:''' | ||
| − | * '''Modification:''' | + | * '''Modification:''' autophosphorylated on Tyr-225 and Tyr-227 {{PubMed|25085422}} |
* '''[[Cofactors]]:''' | * '''[[Cofactors]]:''' | ||
Revision as of 09:30, 5 August 2014
- Description: extracellular polysaccharide synthesis, protein tyrosine kinase
| Gene name | epsB |
| Synonyms | yveL |
| Essential | no |
| Product | protein tyrosine kinase |
| Function | biofilm formation |
| Gene expression levels in SubtiExpress: epsB | |
| Interactions involving this protein in SubtInteract: EpsB | |
| Regulation of this protein in SubtiPathways: epsB | |
| MW, pI | 24 kDa, 9.918 |
| Gene length, protein length | 681 bp, 227 aa |
| Immediate neighbours | epsC, epsA |
| 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
protein modification, biofilm formation, phosphoproteins
This gene is a member of the following regulons
AbrB regulon, RemA regulon, SinR regulon
The gene
Basic information
- Locus tag: BSU34360
Phenotypes of a mutant
Database entries
- BsubCyc: BSU34360
- 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:
- Modification: autophosphorylated on Tyr-225 and Tyr-227 PubMed
- Effectors of protein activity:
Database entries
- BsubCyc: BSU34360
- UniProt: P71051
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
- induction by sequestration of SinR by SinI or SlrA PubMed
- 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
- the amount of the mRNA is substantially decreased upon depletion of RNase Y (this is likely due to the increased stability of the sinR mRNA) PubMed
Biological materials
- Mutant:
- GP1518 (aphA3) PubMed, available in Jörg Stülke's lab
- GP1519 (epsA-epsB, aphA3) PubMed, available in Jörg Stülke's lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH) PubMed, available in Jörg Stülke's lab
- Antibody:
- FLAG-tag construct: GP1541 epsB-FLAG 3x spc (based on pGP1331) available in Jörg Stülke's lab
Labs working on this gene/protein
Richard Losick, Harvard Univ., Cambridge, USA homepage
Your additional remarks
References
Reviews
Joseph D Chao, Dennis Wong, Yossef Av-Gay
Microbial protein-tyrosine kinases.
J Biol Chem: 2014, 289(14);9463-72
[PubMed:24554699]
[WorldCat.org]
[DOI]
(I p)
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
Alexander K W Elsholz, Sarah A Wacker, Richard Losick
Self-regulation of exopolysaccharide production in Bacillus subtilis by a tyrosine kinase.
Genes Dev: 2014, 28(15);1710-20
[PubMed:25085422]
[WorldCat.org]
[DOI]
(I p)
Lei Shi, Boyang Ji, Lorena Kolar-Znika, Ana Boskovic, Fanny Jadeau, Christophe Combet, Christophe Grangeasse, Damjan Franjevic, Emmanuel Talla, Ivan Mijakovic
Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substrates.
Genome Biol Evol: 2014, 6(4);800-17
[PubMed:24728941]
[WorldCat.org]
[DOI]
(I p)
Jan Gerwig, Taryn B Kiley, Katrin Gunka, Nicola Stanley-Wall, Jörg Stülke
The protein tyrosine kinases EpsB and PtkA differentially affect biofilm formation in Bacillus subtilis.
Microbiology (Reading): 2014, 160(Pt 4);682-691
[PubMed:24493247]
[WorldCat.org]
[DOI]
(I p)
Jared T Winkelman, Anna C Bree, Ashley R Bate, Patrick Eichenberger, Richard L Gourse, Daniel B Kearns
RemA is a DNA-binding protein that activates biofilm matrix gene expression in Bacillus subtilis.
Mol Microbiol: 2013, 88(5);984-97
[PubMed:23646920]
[WorldCat.org]
[DOI]
(I p)
Christine Diethmaier, Nico Pietack, Katrin Gunka, Christoph Wrede, Martin Lehnik-Habrink, Christina Herzberg, Sebastian Hübner, Jörg Stülke
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]
[WorldCat.org]
[DOI]
(I p)
Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947]
[WorldCat.org]
[DOI]
(I p)
Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675]
[WorldCat.org]
[DOI]
(I p)
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)
