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Information on EC 2.7.13.3 - histidine kinase and Organism(s) Bordetella pertussis and UniProt Accession P16575

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EC Tree
     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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This record set is specific for:
Bordetella pertussis
UNIPROT: P16575
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The taxonomic range for the selected organisms is: Bordetella pertussis
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
virulence sensor protein bvgS precursor
-
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
BvgA + ATP
?
show the reaction diagram
protein + ATP
?
show the reaction diagram
ATP + BctC
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
bvgS and bvgA control the expression of the virulence-associated genes in Bordetella species by a system similar to the two-component systems used by a variety of bacterial species to respond to environmental stimuli
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
bvgS and bvgA control the expression of the virulence-associated genes in Bordetella species by a system similar to the two-component systems used by a variety of bacterial species to respond to environmental stimuli
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
transmembrane protein
Manually annotated by BRENDA team
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
autophosphorylation
phosphoprotein
-
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H1172Q
mutation abolishes BvgS activity in vivo and eliminates detectable phosphorylation of BvgA in vitro. Activity of BvgS H1172Q can be restored by providing the wild-type C-terminal domain in trans
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytoplasmic portion of BvgS ('BvgS)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytoplasmic portion of BvgS ('BvgS) is overexpressed
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arico, B.; Miller, J.F.; Roy, C.; Stibitz, S.; Monack, D.; Falkow, S.; Gross, R.; Rappuoli, R.
Sequences required for expression of Bordetella pertussis virulence factors share homology with prokaryotic signal transduction proteins
Proc. Natl. Acad. Sci. USA
86
6671-6675
1989
Bordetella pertussis (P16575)
Manually annotated by BRENDA team
Arico, B.; Scarlato, V.; Monack, D.M.; Falkow, S.; Rappuoli, R.
Structural and genetic analysis of the bvg locus in Bordetella species
Mol. Microbiol.
5
2481-2491
1991
Bordetella pertussis (P16575), Bordetella bronchiseptica (P26762), Bordetella parapertussis (P40330)
Manually annotated by BRENDA team
Beier, D.; Schwarz, B.; Fuchs, T.M.; Gross, R.
In vivo characterization of the unorthodox BvgS two-component sensor protein of Bordetella pertussis
J. Mol. Biol.
248
596-610
1995
Bordetella pertussis (P16575), Bordetella pertussis
Manually annotated by BRENDA team
Perraud, A.L.; Kimmel, B.; Weiss, V.; Gross, R.
Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-terminal HPt domains of the sensor proteins
Mol. Microbiol.
27
875-887
1998
Bordetella pertussis (P16575), Escherichia coli (P30855)
Manually annotated by BRENDA team
Uhl, M.A.; Miller, J.F.
Autophosphorylation and phosphotransfer in the Bordetella pertussis BvgAS signal transduction cascade
Proc. Natl. Acad. Sci. USA
91
1163-1167
1994
Bordetella pertussis (P16575)
Manually annotated by BRENDA team
Uhl, M.A.; Miller, J.F.
Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay
EMBO J.
15
1028-1036
1996
Bordetella pertussis (P16575), Bordetella pertussis
Manually annotated by BRENDA team
Buelow, D.R.; Raivio, T.L.
Three (and more) component regulatory systems - auxiliary regulators of bacterial histidine kinases
Mol. Microbiol.
75
547-566
2010
Bacillus subtilis, Bordetella pertussis, Caulobacter vibrioides, Escherichia coli, Sinorhizobium meliloti, Vibrio harveyi (P54302)
Manually annotated by BRENDA team