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Literature summary for 2.7.13.3 extracted from

  • Kotajima, T.; Shiraiwa, Y.; Suzuki, I.
    Functional analysis of the N-terminal region of an essential histidine kinase, Hik2, in the cyanobacterium Synechocystis sp. PCC 6803 (2014), FEMS Microbiol. Lett., 351, 88-94.
    View publication on PubMed
Search for more literature for 2.7.13.3

Protein Variants

Protein Variants Comment Organism
D156A site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity Synechocystis sp.
G123A site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity Synechocystis sp.
additional information construction of a fused sensor, Hik2n-Hik7c, which has the signal input domain of Hik2 and the kinase domain of the phosphate-deficiency sensor Hik7. The coding region of the hik7 gene is replaced with the fused sensor to evaluate the signalling activity in vivo as the activity of alkaline phosphatase (AP), which is regulated by Hik7. Cells expressing Hik2n-Hik7c have weak AP activities under standard growth conditions. Saline stress by NaCl induces AP activity in a dose-dependent manner. Hik2n-Hik7c responds to Cl- concentration. Amino acid substitutions in the signal input domain of Hik2 all result in loss of this responsiveness, i.e. mutants Q22A, P114A, G123A, R129K, W134F, Q141A and D156A completely lose AP activity Synechocystis sp.
P114A site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity Synechocystis sp.
Q141A site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity Synechocystis sp.
Q22A site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2nHik7c construct is inactive in alkaline phosphatase activity Synechocystis sp.
R129K site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity Synechocystis sp.
W134F site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity Synechocystis sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the signal input domain of Hik2 does not contain any membrane-spanning regions except the GAF domain, so it is expected to be a cytosolic protein Synechocystis sp.
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Metals/Ions

Metals/Ions Comment Organism Structure
Cl- activates, the signal input domain of Hik2 responds to environmental Cl- concentration, key for induction of activity Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp. P73276
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Synonyms

Synonyms Comment Organism
Hik2
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 Synechocystis sp.
sensory transduction histidine kinase UniProt Synechocystis sp.
slr1147 locus name Synechocystis sp.

General Information

General Information Comment Organism
malfunction Hik2 mutants are not viable Synechocystis sp.
additional information Hik2 contains a GAF (cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA) domain in the signal input region Synechocystis sp.
physiological function Hik2 is one of three essential histidine kinases in the cyanobacterium Synechocystis sp. PCC 6803. The signal input domain of Hik2 responds to environmental Cl- concentration Synechocystis sp.