Difference between revisions of "TkmA"
| Line 45: | Line 45: | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| − | {{SubtiWiki regulon|[[AbrB regulon]]}} | + | {{SubtiWiki regulon|[[AbrB regulon]]}}, |
| + | {{SubtiWiki regulon|[[DegU regulon]]}}, | ||
| + | {{SubtiWiki regulon|[[Spo0A regulon]]}} | ||
| + | |||
=The gene= | =The gene= | ||
| Line 116: | Line 119: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | |||
** [[AbrB]]: transcription repression {{PubMed|20817675}} | ** [[AbrB]]: transcription repression {{PubMed|20817675}} | ||
| + | ** [[Spo0A]]: transcription activation {{PubMed|26283769}} | ||
| + | ** [[DegU]]-P: transcription activation {{PubMed|26283769}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
Revision as of 17:04, 19 August 2015
- Description: transmembrane modulator of PtkA activity, activates PtkA autophosphorylation and substrate phosphorylation
| Gene name | tkmA |
| Synonyms | ywqC |
| Essential | no |
| Product | modulator of PtkA activity |
| Function | control of protein tyrosine phosphorylation |
| Gene expression levels in SubtiExpress: tkmA | |
| Interactions involving this protein in SubtInteract: TkmA | |
| MW, pI | 26 kDa, 4.61 |
| Gene length, protein length | 744 bp, 248 aa |
| Immediate neighbours | ptkA, ywzD |
| 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
biofilm formation, protein modification, membrane proteins
This gene is a member of the following regulons
AbrB regulon, DegU regulon, Spo0A regulon
The gene
Basic information
- Locus tag: BSU36260
Phenotypes of a mutant
- the mutant exhibits a defect in biofilm formation, pronounced on LBGM medium, weak of MSgg medium PubMed
Database entries
- BsubCyc: BSU36260
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: transmembrane activation of PtkA protein tyrosine kinase activity
- Protein family: cpsC/capA family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- BsubCyc: BSU36260
- Structure:
- UniProt: P96715
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- GP1566 (spc) PubMed, available in Jörg Stülke's lab
- GP1567 epsA::aphA3 tkmA::spc 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), available in Jörg Stülke's lab
- FLAG-tag construct: GP1620 tkmA-FLAG 3x spc (based on pGP1331) available in Jörg Stülke's lab
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Tantan Gao, Jennifer Greenwich, Yan Li, Qi Wang, Yunrong Chai
The Bacterial Tyrosine Kinase Activator TkmA Contributes to Biofilm Formation Largely Independently of the Cognate Kinase PtkA in Bacillus subtilis.
J Bacteriol: 2015, 197(21);3421-32
[PubMed:26283769]
[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)
Abderahmane Derouiche, Vladimir Bidnenko, Rosa Grenha, Nathalie Pigonneau, Magali Ventroux, Mirita Franz-Wachtel, Sylvie Nessler, Marie-Françoise Noirot-Gros, Ivan Mijakovic
Interaction of bacterial fatty-acid-displaced regulators with DNA is interrupted by tyrosine phosphorylation in the helix-turn-helix domain.
Nucleic Acids Res: 2013, 41(20);9371-81
[PubMed:23939619]
[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)
Taryn B Kiley, Nicola R Stanley-Wall
Post-translational control of Bacillus subtilis biofilm formation mediated by tyrosine phosphorylation.
Mol Microbiol: 2010, 78(4);947-63
[PubMed:20815827]
[WorldCat.org]
[DOI]
(I p)
Ivan Mijakovic, Sandrine Poncet, Grégory Boël, Alain Mazé, Sylvie Gillet, Emmanuel Jamet, Paulette Decottignies, Christophe Grangeasse, Patricia Doublet, Pierre Le Maréchal, Josef Deutscher
Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.
EMBO J: 2003, 22(18);4709-18
[PubMed:12970183]
[WorldCat.org]
[DOI]
(P p)
