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Literature summary extracted from

  • Wang, C.; Sang, J.; Wang, J.; Su, M.; Downey, J.S.; Wu, Q.; Wang, S.; Cai, Y.; Xu, X.; Wu, J.; Senadheera, D.B.; Cvitkovitch, D.G.; Chen, L.; Goodman, S.D.; Han, A.
    Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains (2013), PLoS Biol., 11, e1001493.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.13.3 additional information a sequential kinase activation model may involve helical bending of the DHp domain and repositioning of the CA domains. Model of VicK autokinase activation, overview Streptococcus mutans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.13.3 complete cytoplasmic region of enzyme VicK, X-ray diffraction structure determination and analysis Streptococcus mutans
2.7.13.3 purified full-length enzyme, X-ray diffraction structure determination and analysis at 3 A resolution, modeling Streptococcus mutans serotype c

Protein Variants

EC Number Protein Variants Comment Organism
2.7.13.3 D326A/N337A site-directed mutagenesis, the mutant is inactive in autophosphorylation Streptococcus mutans
2.7.13.3 D326A/N337A site-directed mutagenesis, the mutation abolishes VicK autokinase activity Streptococcus mutans serotype c
2.7.13.3 D326A/Q330A site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme Streptococcus mutans
2.7.13.3 D326A/Q330A site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity Streptococcus mutans serotype c
2.7.13.3 F383A/R385A site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme Streptococcus mutans
2.7.13.3 F383A/R385A site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity Streptococcus mutans serotype c
2.7.13.3 I403S site-directed mutagenesis, the mutation does not significantly affect VicK autokinase activity Streptococcus mutans serotype c
2.7.13.3 I403W site-directed mutagenesis, the mutation does not significantly affect VicK autokinase activity but dramatically increases autokinase activity in HK853 Streptococcus mutans serotype c
2.7.13.3 K341A/Y342A site-directed mutagenesis, the mutation negatively affects autokinase activity Streptococcus mutans serotype c
2.7.13.3 additional information deletion of the first G loop (del392-395, RAQG) negatively affects autokinase activity Streptococcus mutans serotype c
2.7.13.3 N334A/N337A site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation Streptococcus mutans
2.7.13.3 N334A/N337A site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type Streptococcus mutans serotype c
2.7.13.3 P222A site-directed mutagenesis, the mutant abolishes enzyme VicK's phosphatase activity Streptococcus mutans serotype c
2.7.13.3 P222A site-directed mutagenesis, the mutation eliminates the phosphatase activity of the enzyme Streptococcus mutans
2.7.13.3 P222G site-directed mutagenesis, the mutant retains full autokinase activity when compared to wild-type, but the mutation abolishes the VicK phosphatase activity Streptococcus mutans serotype c
2.7.13.3 P222G site-directed mutagenesis, the mutant shows phosphatase activity similar to the wild-type enzyme Streptococcus mutans
2.7.13.3 Q297A/I298A site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation Streptococcus mutans
2.7.13.3 Q297A/I298A site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type Streptococcus mutans serotype c
2.7.13.3 R294A site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation Streptococcus mutans
2.7.13.3 R294A site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type Streptococcus mutans serotype c
2.7.13.3 R382A/R385A site-directed mutagenesis, the mutant is inactive in autophosphorylation Streptococcus mutans
2.7.13.3 R382A/R385A site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme Streptococcus mutans
2.7.13.3 R382A/R385A site-directed mutagenesis, the mutation abolishes VicK autokinase activity Streptococcus mutans serotype c
2.7.13.3 R382A/R385A site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity Streptococcus mutans serotype c
2.7.13.3 T221A site-directed mutagenesis, the mutant retains full autokinase activity but the enzyme VicK's phosphatase activity is abolished Streptococcus mutans serotype c
2.7.13.3 T221A site-directed mutagenesis, the mutation eliminates the phosphatase activity but does not affect the autokinase activity of the enzyme Streptococcus mutans
2.7.13.3 T221A/P222A/P222G/V212A/V215A/S213A/S216A site-directed mutagenesis, the mutation only slightly reduces autokinase activity, while it abolishes the VicK phosphatase activity Streptococcus mutans serotype c
2.7.13.3 V212A/V215A/S213A/S216A site-directed mutagenesis, the mutation only slightly reduces autokinase activity, while it abolishes the VicK phosphatase activity Streptococcus mutans serotype c

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.13.3 plasma membrane VicK has one transmembrane domain, amino acids 9-30, that anchors itself to the cytoplasmic membrane Streptococcus mutans serotype c 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.13.3 Mg2+ required Streptococcus mutans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.13.3 103200
-
 holoenzyme, static light scattering Streptococcus mutans serotype c

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.13.3 ATP + protein L-histidine Streptococcus mutans
-
 ADP + protein N-phospho-L-histidine
-
 ?
2.7.13.3 ATP + protein L-histidine Streptococcus mutans ATCC 700610
-
 ADP + protein N-phospho-L-histidine
-
 ?
2.7.13.3 ATP + VicR L-histidine Streptococcus mutans
-
 ADP + VicR N-phospho-L-histidine
-
 ?
2.7.13.3 ATP + VicR L-histidine Streptococcus mutans ATCC 700610
-
 ADP + VicR N-phospho-L-histidine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.13.3 Streptococcus mutans Q8DT64
-
-
2.7.13.3 Streptococcus mutans ATCC 700610 Q8DT64
-
-
2.7.13.3 Streptococcus mutans serotype c Q8DT64
-
-
2.7.13.3 Streptococcus mutans serotype c ATCC 700610 Q8DT64
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.13.3 phosphoprotein model of VicK autokinase activation, overview Streptococcus mutans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.13.3 ATP + protein L-histidine
-
 Streptococcus mutans ADP + protein N-phospho-L-histidine
-
 ?
2.7.13.3 ATP + protein L-histidine
-
 Streptococcus mutans ATCC 700610 ADP + protein N-phospho-L-histidine
-
 ?
2.7.13.3 ATP + VicR L-histidine
-
 Streptococcus mutans ADP + VicR N-phospho-L-histidine
-
 ?
2.7.13.3 ATP + VicR L-histidine
-
 Streptococcus mutans ATCC 700610 ADP + VicR N-phospho-L-histidine
-
 ?
2.7.13.3 additional information VicK performs autophosphorylation for self-activation. VicK can also act as a phosphatase dephosphorylating phosphorylated VicR Streptococcus mutans ?
-
 ?
2.7.13.3 additional information VicK performs autophosphorylation for self-activation. VicK can also act as a phosphatase dephosphorylating phosphorylated VicR Streptococcus mutans ATCC 700610 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.13.3 dimer the dimeric VicK protein has a rod-shaped structure with the domains linearly connected like beads on a string Streptococcus mutans
2.7.13.3 dimer the holoenzyme exists as a stable dimer in solution. The overall structure of VicK is a long-rod dimer that anchors four connected domains: HAMP, Per-ARNT-SIM (PAS), DHp, and catalytic and ATP binding domain (CA). The HAMP, a signal transducer, and the PAS domain, major sensor, adopt canonical folds with dyad symmetry. In contrast, the dimer of the DHp and CA domains is asymmetric because of different helical bends in the DHp domain and spatial positions of the CA domains. A conserved proline, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. Following the transmembrane domain, the HAMP signal transducer domain and PAS sensor domain are directly connected to the catalytic domain through a DHp domain, a dimerization and histidine phosphorylation domain. Structure of the HAMP domain (aa 36-86), located at the uppermost position within the N-terminal region of the VicK structure, overview Streptococcus mutans serotype c
2.7.13.3 More enzyme VicK is composed of several domains (HAMP, PAS, DHp, and catalytic and ATP binding domain [CA]) in addition to a short transmembrane domain. Domain structure-function relationship and analysis, overview. The overall structure of VicK comprises a dimer in the shape of a long slim rod Streptococcus mutans

Synonyms

EC Number Synonyms Comment Organism
2.7.13.3 CovS UniProt Streptococcus mutans serotype c
2.7.13.3 sensor histidine kinase
-
 Streptococcus mutans
2.7.13.3 VicK
-
 Streptococcus mutans
2.7.13.3 VicK
-
 Streptococcus mutans serotype c
2.7.13.3 VicK-like protein UniProt Streptococcus mutans serotype c

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.13.3 37
-
 assay at Streptococcus mutans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.13.3 7.4
-
 assay at Streptococcus mutans

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.13.3 ATP
-
 Streptococcus mutans

General Information

EC Number General Information Comment Organism
2.7.13.3 malfunction mutations in the DHp domain affect kinase activity Streptococcus mutans
2.7.13.3 additional information conserved proline-222, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. The proline is essential for phosphatase activity. The C-terminal ends of the VicK dimer harbor two monomeric catalytic domains. The enzyme architecture with a signal transducer and sensor domain suggests a model where DHp helical bending and a CA swing movement are likely coordinated for autokinase activation, structure-function analysis, overview Streptococcus mutans serotype c
2.7.13.3 additional information the VicK kinase activates itself by helical bending of the DHp domain and coordinated swinging around of the catalytic and ATP binding domain to engage with the target histidine. Modelling of the active state structure of the catalytic ATP-binding domain and positioning of inactive domain. Structure-function analysis of the enzyme domains, detailed overview. Transient formation of the active site Streptococcus mutans
2.7.13.3 physiological function one of the main components of two-component systems, TCSs, is a sensor histidine kinase, which relays extracellular signals to intracellular pathways. VicK is an important sensor histidine kinase in the tooth decay pathogen Streptomyces mutans Streptococcus mutans