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Literature summary for 2.7.11.1 extracted from

  • Lima, A.; Duran, R.; Schujman, G.; Marchissio, M.; Portela, M.; Obal, G.; Pritsch, O.; de Mendoza, D.; Cervenansky, C.
    Serine/threonine protein kinase PrkA of the human pathogen Listeria monocytogenes: Biochemical characterization and identification of interacting partners through proteomic approaches (2011), J. Proteomics, 74, 1720-1734.
    View publication on PubMed
Search for more literature for 2.7.11.1

Cloned(Commentary)

Cloned (Comment) Organism
gene lmo1820, encodes PrkA, expression of His6-tagged PrkA catalytic domain in Escherichia coli strain M15 Listeria monocytogenes

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane a pattern of basic residues is followed by a predicted transmembrane domain suggesting that the N-terminal region (residues 1-338) is orientated toward the cytoplasm Listeria monocytogenes 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Listeria monocytogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
72000
-
 x * 72000, about, sequence calculation of the full-length enzyme, x * 39000-43000, several forms of the isolated recombinant His6-tagged catalytic domain, SDS-PAGE Listeria monocytogenes

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
-
 two eukaryotic-type Ser/Thr-kinases encoded by lmo1820 and lmo0618
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein PrkA is able to autophosphorylate specificly the residues Thr171, Thr174, and Thr176 within the sequence 160-183 of the PrkA activation loop, mass spectrometry analysis of tryptic peptides, overview Listeria monocytogenes

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged PrkA catalytic domain from Escherichia coli strain M15 by nickel affinity chromatography Listeria monocytogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + myelin basic protein
-
 Listeria monocytogenes ADP + phosphorylated myelin basic protein
-
 ?
additional information PrkA is able to autophosphorylate specific Thr residues within its activation loop sequence Listeria monocytogenes ?
-
 ?

Subunits

Subunits Comment Organism
? x * 72000, about, sequence calculation of the full-length enzyme, x * 39000-43000, several forms of the isolated recombinant His6-tagged catalytic domain, SDS-PAGE Listeria monocytogenes
More the C-terminal domain sequence of PrkA shows the presence of several copies of PASTA domains, i.e. penicillin-binding protein and Ser/Thr kinase associate Listeria monocytogenes

Synonyms

Synonyms Comment Organism
PrkA
-
 Listeria monocytogenes
serine/threonine protein kinase
-
 Listeria monocytogenes
StpK
-
 Listeria monocytogenes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Listeria monocytogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Listeria monocytogenes

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Listeria monocytogenes

pI Value

Organism Comment pI Value Maximum pI Value
Listeria monocytogenes PrkA, sequence calculation
-
 4.99

General Information

General Information Comment Organism
additional information the C-terminal domain sequence of PrkA shows the presence of several copies of extracellular PASTA domains, i.e. penicillin-binding protein and Ser/Thr kinase associate, a wel conserved intracellular kinase domain, and a N-terminal region (residues 1-338), which is orientated toward the cytoplasm Listeria monocytogenes
physiological function PrkA probably is involved in the regulation of a variety of fundamental biological processes, functional classification of the PrkAc putative interactors, overview Listeria monocytogenes