Literature summary for 2.7.11.1 extracted from

Canova, M.J.; Veyron-Churlet, R.; Zanella-Cleon, I.; Cohen-Gonsaud, M.; Cozzone, A.J.; Becchi, M.; Kremer, L.; Molle, V.
The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c (2008), Proteomics, 8, 521-533.

Search for more literature for 2.7.11.1

Cloned(Commentary)

Cloned (Comment)	Organism
the cytosolic domain of PknL (DELTA370-399) is expressed in Escherichia coli as a GST-fusion protein	Mycobacterium tuberculosis

Protein Variants

Protein Variants	Comment	Organism
DELTA370-399/K48M	mutant protein shows no autophosphorylation activity, indicating that Lys48 is essential for catalysing the phosphorylation reaction	Mycobacterium tuberculosis
DELTA370-399/S171A	mutant protein shows similar autophosphorylation activity compared to wild-type, indicating that Ser171 is not an autophosphorylated residue	Mycobacterium tuberculosis
DELTA370-399/S174A	mutant protein shows similar autophosphorylation activity compared to wild-type, indicating that Ser171 is not an autophosphorylated residue	Mycobacterium tuberculosis
DELTA370-399/T173A	mutant protein shows an autophosphorylation activity of only 19% compared to wild-type	Mycobacterium tuberculosis
DELTA370-399/T173A/T175A	mutant protein shows an autophosphorylation activity of only 19% compared to wild-type	Mycobacterium tuberculosis
DELTA370-399/T175A	mutant protein shows an autophosphorylation activity of only 46% compared to wild-type	Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
43000	-	deduced from cDNA	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WI63	-	-
Mycobacterium tuberculosis H37Rv	P9WI63	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	enzyme possesses autophosphorylation activity. The activation loop phosphorylated residues Thr173 and Thr175 are essential for the autophosphorylation activity of PknL. Phosphorylation of the activation loop Thr173 residue is also required for optimal PknL-mediated phosphorylation of Rv2175c	Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + Rv2175	-	Mycobacterium tuberculosis	ADP + phosphorylated-Rv2175	-	?
ATP + Rv2175	-	Mycobacterium tuberculosis H37Rv	ADP + phosphorylated-Rv2175	-	?

Synonyms

Synonyms	Comment	Organism
PknL	-	Mycobacterium tuberculosis
serine-threonine kinase	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)