Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2012 Jan;40(Database issue):D321-4.
doi: 10.1093/nar/gkr915. Epub 2011 Nov 12.

BYKdb: The Bacterial Protein tYrosine Kinase Database

Free PMC article

BYKdb: The Bacterial Protein tYrosine Kinase Database

Fanny Jadeau et al. Nucleic Acids Res. .
Free PMC article


Bacterial tyrosine-kinases share no resemblance with their eukaryotic counterparts and they have been unified in a new protein family named BY-kinases. These enzymes have been shown to control several biological functions in the bacterial cells. In recent years biochemical studies, sequence analyses and structure resolutions allowed the deciphering of a common signature. However, BY-kinase sequence annotations in primary databases remain incomplete. This prompted us to develop a specialized database of computer-annotated BY-kinase sequences: the Bacterial protein tyrosine-kinase database (BYKdb). BY-kinase sequences are first identified, thanks to a workflow developed in a previous work. A second workflow annotates the UniProtKB entries in order to provide the BYKdb entries. The database can be accessed through a web interface that allows static and dynamic queries and offers integrated sequence analysis tools. BYKdb can be found at


Figure 1.
Figure 1.
Snapshot of the BYKdb web interface. (A) The BYKdb home page, with the resources accessible as clickable buttons (B) A pre-computed dataset of BY-kinase and TAD sequences and alignments, ordered by phylum and by cluster. (C) The multiple sequence alignment of firmicutes CD viewed in the ‘EditAlignment’ applet. (D) Dynamic queries against the BYKdb. (E) The ‘Annotate’ tool detailed results page for one input sequence.

Similar articles

See all similar articles

Cited by 12 articles

See all "Cited by" articles


    1. Bourret RB, Hess JF, Borkovich KA, Pakula AA, Simon MI. Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria. J. Biol. Chem. 1989;264:7085–7088. - PubMed
    1. Reizer J, Saier MH, Jr, Deutscher J, Grenier F, Thompson J, Hengstenberg W. The phosphoenolpyruvate: sugar phosphotransferase system in gram-positive bacteria: properties, mechanism, and regulation. Crit. Rev. Microbiol. 1988;15:297–338. - PubMed
    1. Bakal CJ, Davies JE. No longer an exclusive club: eukaryotic signalling domains in bacteria. Trends Cell Biol. 2000;10:32–38. - PubMed
    1. Grangeasse C, Cozzone AJ, Deutscher J, Mijakovic I. Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology. Trends Biochem. Sci. 2007;32:86–94. - PubMed
    1. Walker JE, Saraste M, Runswick MJ, Gay NJ. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1:945–951. - PMC - PubMed

Publication types

MeSH terms