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Literature summary 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

Cloned(Commentary)

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.11.1 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

EC Number Metals/Ions Comment Organism Structure
2.7.11.1 Mn2+ required Listeria monocytogenes

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.11.1 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

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.1 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)

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.11.1 ? 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
2.7.11.1 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.1 37
-
 assay at Listeria monocytogenes

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.1 7
-
 assay at Listeria monocytogenes

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.1 ATP
-
 Listeria monocytogenes

pI Value

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

General Information

EC Number General Information Comment Organism
2.7.11.1 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
2.7.11.1 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