The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: bacterial tyrosine kinase
Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Other name(s): BY-kinase; bacterial protein tyrosine kinase
Systematic name: ATP:[protein]-L-tyrosine O-phosphotransferase (bacterial-type)
Comments: This family of enzymes includes most of the bacterial tyrosine kinases. These enzymes do not share sequence or structural homology with eukaryotic tyrosine kinases, and exploit ATP/GTP-binding Walker motifs to catalyse autophosphorylation and substrate phosphorylation on tyrosine. Two subfamilies have been defined: P-type enzymes contain an N-terminal transmembrane portion and an extracellular hairpin loop domain. The intracellular portion comprises the catalytic domain and a tyrosine-rich C-terminal domain that contains the site for autophosphorylation. In F-type enzymes the extracellular transmembrane domain and the intracellular catalytic domain are two independent proteins encoded by two separate genes. The majority of characterized bacterial tyrosine kinases regulate the production and export of capsular and extracellular polysaccharides, but other members are involved in many other functions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Grangeasse, C., Doublet, P., Vaganay, E., Vincent, C., Deleage, G., Duclos, B. and Cozzone, A.J. Characterization of a bacterial gene encoding an autophosphorylating protein tyrosine kinase. Gene 204 (1997) 259–265. [DOI] [PMID: 9434192]
2.  Wugeditsch, T., Paiment, A., Hocking, J., Drummelsmith, J., Forrester, C. and Whitfield, C. Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli. J. Biol. Chem. 276 (2001) 2361–2371. [DOI] [PMID: 11053445]
3.  Soulat, D., Jault, J.M., Duclos, B., Geourjon, C., Cozzone, A.J. and Grangeasse, C. Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism. J. Biol. Chem. 281 (2006) 14048–14056. [DOI] [PMID: 16565080]
4.  Lee, D.C., Zheng, J., She, Y.M. and Jia, Z. Structure of Escherichia coli tyrosine kinase Etk reveals a novel activation mechanism. EMBO J. 27 (2008) 1758–1766. [DOI] [PMID: 18497741]
5.  Chao, J.D., Wong, D. and Av-Gay, Y. Microbial protein-tyrosine kinases. J. Biol. Chem. 289 (2014) 9463–9472. [DOI] [PMID: 24554699]
[EC created 2021]

Data © 2001–2023 IUBMB
Web site © 2005–2023 Andrew McDonald