Difference between revisions of "PtkA"
(→Original publications) |
|||
| Line 57: | Line 57: | ||
* Defect in [[biofilm formation]], this involves the kinase activity, but the target protein is unknown {{PubMed|20815827}} | * Defect in [[biofilm formation]], this involves the kinase activity, but the target protein is unknown {{PubMed|20815827}} | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU36250&redirect=T BSU36250] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ywqCD.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ywqCD.html] | ||
| Line 93: | Line 94: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU36250&redirect=T BSU36250] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2VED 2VED] (CapB, the homolog in ''Staphylococcus aureus'') | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2VED 2VED] (CapB, the homolog in ''Staphylococcus aureus'') | ||
Revision as of 14:59, 2 April 2014
- Description: protein tyrosine kinase
| Gene name | ptkA |
| Synonyms | ywqD |
| Essential | no |
| Product | protein tyrosine kinase |
| Function | protein phosphorylation |
| Gene expression levels in SubtiExpress: ptkA | |
| Interactions involving this protein in SubtInteract: PtkA | |
| MW, pI | 25 kDa, 9.628 |
| Gene length, protein length | 711 bp, 237 aa |
| Immediate neighbours | ptpZ, tkmA |
| 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
The gene
Basic information
- Locus tag: BSU36250
Phenotypes of a mutant
- Accumulation of extra chromosome equivalents PubMed
- Defect in biofilm formation, this involves the kinase activity, but the target protein is unknown PubMed
Database entries
- BsubCyc: BSU36250
- 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), autophosphorylation, phosphorylation of Ugd, TuaD, Ssb, SsbB
- Protein family: BY-kinase, see the Bacterial Protein Tyrosine Kinase Database)
- Paralogous protein(s): EpsB
Extended information on the protein
- Kinetic information:
- Domains: single BY-kinase domain
- Modification: autophosphorylation at residues Y225, Y227 and Y228 (primary site) PubMed, dephosphorylated by PtpZ PubMed
- Cofactors: ATP
- Effectors of protein activity: TkmA - transmembrane modulator, activates PtkA autophosphorylation and substrate phosphorylation PubMed
Database entries
- BsubCyc: BSU36250
- Structure: 2VED (CapB, the homolog in Staphylococcus aureus)
- UniProt: P96716
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- KO strain created with pMUTIN-2, available from Ivan Mijakovic
- GP1520 (spc), available in Jörg Stülke's lab
- GP1544 (ermC), available in Jörg Stülke's lab
- GP1587 (cat) , available in Jörg Stülke's lab
- GP1521 epsB (aphA3) ptkA (spc) double mutant available in Jörg Stülke's lab
- GP1529 tkmA-ptkA::spc available in Jörg Stülke's lab
- GP1610 (ptkA-ptpZ, spc), available in Jörg Stülke's lab
- Expression vector: pQE-30, N-terminally 6xHis-tagged, available from Ivan Mijakovic
- lacZ fusion: in a KO strain created with pMUTIN-2, available from Ivan Mijakovic
- GFP fusion: CFP-fusion, available from Ivan Mijakovic
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
- Antibody:
Labs working on this gene/protein
Ivan Mijakovic, Thiverval-Grignon, France
Your additional remarks
References
Reviews
Jörg Stülke
More than just activity control: phosphorylation may control all aspects of a protein's properties.
Mol Microbiol: 2010, 77(2);273-5
[PubMed:20497498]
[WorldCat.org]
[DOI]
(I p)
Original publications
