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Information on EC 2.7.13.3 - histidine kinase and Organism(s) Streptococcus mutans serotype c and UniProt Accession Q8DT64

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     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.13 Protein-histidine kinases
                2.7.13.3 histidine kinase
IUBMB Comments
This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). A number of histones can act as acceptor.
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Streptococcus mutans serotype c
UNIPROT: Q8DT64
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The taxonomic range for the selected organisms is: Streptococcus mutans serotype C
The enzyme appears in selected viruses and cellular organisms
Synonyms
histidine kinase, sensor kinase, sensor protein, phytochrome a, ethylene receptor, sensor histidine kinase, bacteriophytochrome, ornithine decarboxylase antizyme, chemotaxis protein, hybrid histidine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
VicK-like protein
UniProt
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:protein-L-histidine N-phosphotransferase
This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). A number of histones can act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
99283-67-7
protein-histidine kinases, EC 2.7.13.1, EC 2.7.13.2, and EC 2.7.13.3 are not distinguished in Chemical Abstracts
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
VicK has one transmembrane domain, amino acids 9-30, that anchors itself to the cytoplasmic membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103200
holoenzyme, static light scattering
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified full-length enzyme, X-ray diffraction structure determination and analysis at 3 A resolution, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D326A/N337A
site-directed mutagenesis, the mutation abolishes VicK autokinase activity
D326A/Q330A
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
F383A/R385A
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
I403S
site-directed mutagenesis, the mutation does not significantly affect VicK autokinase activity
I403W
site-directed mutagenesis, the mutation does not significantly affect VicK autokinase activity but dramatically increases autokinase activity in HK853
K341A/Y342A
site-directed mutagenesis, the mutation negatively affects autokinase activity
N334A/N337A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
P222A
site-directed mutagenesis, the mutant abolishes enzyme VicK's phosphatase activity
P222G
site-directed mutagenesis, the mutant retains full autokinase activity when compared to wild-type, but the mutation abolishes the VicK phosphatase activity
Q297A/I298A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
R294A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
R382A/R385A
T221A
site-directed mutagenesis, the mutant retains full autokinase activity but the enzyme VicK's phosphatase activity is abolished
T221A/P222A/P222G/V212A/V215A/S213A/S216A
site-directed mutagenesis, the mutation only slightly reduces autokinase activity, while it abolishes the VicK phosphatase activity
V212A/V215A/S213A/S216A
site-directed mutagenesis, the mutation only slightly reduces autokinase activity, while it abolishes the VicK phosphatase activity
additional information
deletion of the first G loop (del392-395, RAQG) negatively affects autokinase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
PLoS Biol.
11
e1001493
2013
Streptococcus mutans (Q8DT64), Streptococcus mutans serotype c (Q8DT64), Streptococcus mutans ATCC 700610 (Q8DT64), Streptococcus mutans serotype c ATCC 700610 (Q8DT64)
Manually annotated by BRENDA team