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ATP + L-Tyr416-[Src]
ADP + H+ + O-phospho-L-Tyr416-[Src]
-
-
-
?
ATP + L-Tyr550-[DivL]
ADP + H+ + O-phospho-L-Tyr550-[DivL]
ATP + L-tyrosine in poly(Glu,Tyr)
ADP + H+ + O-phospho-L-tyrosyl-poly(Glu,Tyr)
ATP + L-tyrosyl-[AAVHEYLSA]
ADP + H+ + O-phospho-L-tyrosyl-[AAVHEYLSA]
AAVHEYLSA i.e. peptide derived from the tyrosine-rich BceF C-terminal region containing the third distal tyrosine only (733AAVHEYLSA741)
-
-
?
ATP + L-tyrosyl-[BtkB]
ADP + H+ + O-phospho-L-tyrosyl-[BtkB]
ATP + L-tyrosyl-[CapB2]
ADP + H+ + O-phospho-L-tyrosyl-[CapB2]
-
-
-
?
ATP + L-tyrosyl-[CpsD]
ADP + H+ + O-phospho-L-tyrosyl-[CpsD]
-
-
-
-
?
ATP + L-tyrosyl-[CtrA]
ADP + H+ + O-phospho-L-tyrosyl-[CtrA]
ATP + L-tyrosyl-[Etk]
ADP + H+ + O-phospho-L-tyrosyl-[Et]
-
-
-
?
ATP + L-tyrosyl-[ParB]
ADP + H+ + O-phospho-L-tyrosyl-[ParB]
-
substrate is chromosome segregation protein ParB. CpsD interacts with ParB and phosphorylation modulates the mobility of ParB
-
-
?
ATP + L-tyrosyl-[PGN_0224]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0224]
ATP + L-tyrosyl-[PGN_0613]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0613]
ATP + L-tyrosyl-[PTK1]
ADP + H+ + O-phospho-L-tyrosyl-[PTK1]
ATP + L-tyrosyl-[PTK]
ADP + H+ + O-phospho-L-tyrosyl-[PTK]
-
-
-
?
ATP + L-tyrosyl-[Wzc]
ADP + H+ + O-phospho-L-tyrosyl-[Wzc]
-
-
-
?
ATP + polyE4Y
ADP + H+ + polyE4-O-phospho-L-Tyr
-
-
-
?
ATP + [BtkA]-L-tyrosine
ADP + [BtkA]-L-tyrosine phosphate
ATP + [chain length determinant family protein Exo]-L-tyrosine
ADP + [chain length determinant family protein Exo]-L-tyrosine phosphate
ATP + [myelin]-L-tyrosine
ADP + [myelin]-L-tyrosine phosphate
additional information
?
-
ATP + L-Tyr550-[DivL]
ADP + H+ + O-phospho-L-Tyr550-[DivL]
-
-
-
?
ATP + L-Tyr550-[DivL]
ADP + H+ + O-phospho-L-Tyr550-[DivL]
-
-
-
?
ATP + L-tyrosine in poly(Glu,Tyr)
ADP + H+ + O-phospho-L-tyrosyl-poly(Glu,Tyr)
poly(Glu, Tyr; 4:1), used as universal substrate for protein tyrosine kinases
-
-
?
ATP + L-tyrosine in poly(Glu,Tyr)
ADP + H+ + O-phospho-L-tyrosyl-poly(Glu,Tyr)
poly(Glu, Tyr; 4:1), used as universal substrate for protein tyrosine kinases
-
-
?
ATP + L-tyrosyl-[BtkB]
ADP + H+ + O-phospho-L-tyrosyl-[BtkB]
-
-
-
?
ATP + L-tyrosyl-[BtkB]
ADP + H+ + O-phospho-L-tyrosyl-[BtkB]
-
-
-
-
?
ATP + L-tyrosyl-[BtkB]
ADP + H+ + O-phospho-L-tyrosyl-[BtkB]
-
-
-
?
ATP + L-tyrosyl-[CtrA]
ADP + H+ + O-phospho-L-tyrosyl-[CtrA]
-
-
-
?
ATP + L-tyrosyl-[CtrA]
ADP + H+ + O-phospho-L-tyrosyl-[CtrA]
-
-
-
?
ATP + L-tyrosyl-[PGN_0224]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0224]
substrate is UDP-acetyl-mannosamine dehydrogenase, a capsule related protein
-
-
?
ATP + L-tyrosyl-[PGN_0224]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0224]
substrate is UDP-acetyl-mannosamine dehydrogenase, a capsule related protein
-
-
?
ATP + L-tyrosyl-[PGN_0613]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0613]
substrate is UDP-glucose dehydrogenase, a capsule related protein
-
-
?
ATP + L-tyrosyl-[PGN_0613]
ADP + H+ + O-phospho-L-tyrosyl-[PGN_0613]
substrate is UDP-glucose dehydrogenase, a capsule related protein
-
-
?
ATP + L-tyrosyl-[PTK1]
ADP + H+ + O-phospho-L-tyrosyl-[PTK1]
-
-
-
?
ATP + L-tyrosyl-[PTK1]
ADP + H+ + O-phospho-L-tyrosyl-[PTK1]
-
-
-
?
ATP + [BtkA]-L-tyrosine
ADP + [BtkA]-L-tyrosine phosphate
-
-
-
?
ATP + [BtkA]-L-tyrosine
ADP + [BtkA]-L-tyrosine phosphate
-
-
-
?
ATP + [chain length determinant family protein Exo]-L-tyrosine
ADP + [chain length determinant family protein Exo]-L-tyrosine phosphate
-
-
-
?
ATP + [chain length determinant family protein Exo]-L-tyrosine
ADP + [chain length determinant family protein Exo]-L-tyrosine phosphate
-
-
-
?
ATP + [myelin]-L-tyrosine
ADP + [myelin]-L-tyrosine phosphate
-
-
-
?
ATP + [myelin]-L-tyrosine
ADP + [myelin]-L-tyrosine phosphate
-
-
-
?
additional information
?
-
no phosphorylation of synthetic substrates such as poly(Glu80 Tyr20) or angiotensin II is observed
-
-
-
additional information
?
-
no substrate: response regulator DivK
-
-
-
additional information
?
-
-
no substrate: response regulator DivK
-
-
-
additional information
?
-
no substrate: response regulator DivK
-
-
-
additional information
?
-
no substrate: synthetic peptide RRLIEDADYAARG
-
-
-
additional information
?
-
-
no substrate: synthetic peptide RRLIEDADYAARG
-
-
-
additional information
?
-
no substrate: synthetic peptide RRLIEDADYAARG
-
-
-
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0.123
L-tyrosyl-[AAVHEYLSA]
pH 7.5, 23°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
-
0.075
ATP
wild-type, pH 8, 30°C
0.253
ATP
mutant H384Y/Y527F, pH 8, 30°C
0.309
ATP
mutant H384Y, pH 8, 30°C
0.327
ATP
mutant H384Q, pH 8, 30°C
0.335
ATP
mutant H384Y/Y416F, pH 8, 30°C
0.34
ATP
mutant H384A, pH 8, 30°C
0.345
ATP
mutant H384Q/Y416F, pH 8, 30°C
additional information
L-tyrosine in poly(Glu,Tyr)
Km value 0.3 mg/ml, cytoplasmic fragment of BtkB (Ser444-Ser710), pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
-
Km value 0.3 mg/ml, cytoplasmic fragment of BtkB (Ser444-Ser710), pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
Km value 0.375 mg/ml, mutant Y686F/Y690F/Y693F/Y696F/Y699F, pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
-
Km value 0.375 mg/ml, mutant Y686F/Y690F/Y693F/Y696F/Y699F, pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
Km value 1.35 mg/ml, mutant R550Y, pH 7, 37°C
-
additional information
L-tyrosine in poly(Glu,Tyr)
-
Km value 1.35 mg/ml, mutant R550Y, pH 7, 37°C
-
additional information
polyE4Y
Km value 105 microg/ml, wild-type, pH 8, 30°C
-
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additional information
-
identification of BY-kinase sequences in UniProt Knowledgebase using a combination of similarity search with sequence-profile alignment, pattern matching and sliding window computation. The sequence is distinct from other protein families by the presence of three specific Walker-like motifs (one Walker-A-like followed by two Walker-B-like) and a YC. The BY-kinase family signature is summarized as a PROSITE pattern: G-K-[ST]-X(7,27)-[ILVFM](3)-D-X-D-X-RX(60,80)-[ILVFM](3)-D-X(2)-P-X(30,150)-Y-X(0,5)-Y, leading to identification of 640 sequences
metabolism
phosphorylating capacity of Cap5B2 is expressed only in the presence of a stimulatory protein, either Cap5A1 or Cap5A2, that enhances its affinity for the phosphoryl donor ATP. The last 27/29 amino acids of the C-terminal domain of either polypeptide are sufficient for stimulating Cap5B2 activity
metabolism
PTK1 can utilize ATP for autophosphorylation and is dephosphorylated by the tyrosine phosphatase, Ltp1
metabolism
regulatory interaction of tyrosine kinase Wzc, and its opposing tyrosine phosphatase, Wzb. The phosphatase Wzb utilizes a surface distal to the catalytic elements of the kinase, Wzc, to dock onto its catalytic domain WzcCD. WzcCD binds in a fashion largely independent of the C-terminal tyrosine cluster near the Wzb catalytic site, inducing allosteric changes therein. YC dephosphorylation is proximity-mediated and reliant on the elevated concentration of phosphorylated YC near the Wzb active site resulting from WzcCD docking
metabolism
the conformation of the Walker-A lysine is coupled to the global transitions of the cytoplasmic catalytic domain. Global closure drives ATP toward its reactive conformation, while active site ordering promotes the desolvation of ATP. The closed state is stabilized in the octameric ring with characteristic ATP conformations
metabolism
-
PTK1 can utilize ATP for autophosphorylation and is dephosphorylated by the tyrosine phosphatase, Ltp1
-
physiological function
a BtkA mutant is unable to complete maturation to heat- and sonication-resistant spores under both starvation- and glycerol-induced developmental conditions
physiological function
a BtkB mutant shows reduced maximum cell density as compared to the wild type when cultured in nutrient medium at 37°C. Under starvation conditions, BtkB mutant cells form fruiting bodies and spores about 24 h later than the wild-type strain. The BtkB mutant overproduces yellow pigment during development and shows a decrease in exopolysaccharide production when compared with the wild-type strain
physiological function
autophosphorylation of Wzc is essential for assembly of the serotype K30 group 1 capsule in Escherichia coli O9a:K30. It is not essential for either the synthesis of the K30 repeat units or for activity of the K30 polymerase enzyme. The tyrosine-rich domain at the C terminus of Wzc is the site of phosphorylation, and autophosphorylation of Wzc requires a functional Walker A motif. The N- and C-terminal domains of Wzc are both required for phosphorylation of the Wzc C terminus, and for capsule assembly
physiological function
-
BY-kinase CpsD and capsular polysaccharide biosynthesis protein CpsC are required for growth in Streptococcus pneumoniae. CpsD autokinase activity is dispensable for growth, but autophosphorylation modulates the length of the capsular polysaccharides. Cells lacking a functional CpsC or cpsD accumulate low molecular weight capsular polysaccharide and lyse because of the lethal sequestration of the lipid carrier undecaprenyl phosphate, resulting in inhibition of peptidoglycan synthesis. CpsC interacts with CpsD and the polymerase CpsH. CpsD phosphorylation reduces the length of capsular polysaccharide polymers presumably by controlling the activity of CpsC. The spatiotemporal coordination between capsular polysaccharide and peptidoglycan synthesis is dependent on CpsC and CpsD
physiological function
-
CpsD localizes at the cell division site and participates in the proper assembly of the capsule. The cytoplasmic C-terminal end of the transmembrane protein CpsC is required for CpsD autophosphorylation and localization at mid-cell. The CpsC/CpsD complex captures the polysaccharide polymerase CpsH at the division site and CPS production occurs exclusively at mid-cell and is tightly dependent on CpsD interaction with CpsC. Non-phosphorylated CpsD hinders capsule production and cell division, septal localization of non-phosphorylated CpsD impairs cell division
physiological function
DivL is autophosphorylated on residue Tyr550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle. DivL in vitro catalyzes phosphorylation of global response regulator CtrA and activates transcription in vitro of the cell cycle-regulated FliF promoter
physiological function
in a PTK1 mutant,community development with Streptococcus gordonii is severely abrogated. Ptk1 controls the levels of the transcriptional regulator CdhR and the fimbrial adhesin Mfa1 which mediates binding to Streptococcus gordonii. The PTK1 gene is in an operon with two genes involved in exopolysaccharide synthesis, and Ptk1 is necessary for exopolysaccharide production in Porphyromonas gingivalis. Knockout of PTK1 in an encapsulated strain of Porphyromonas gingivalis results in loss of capsule production
physiological function
protein tyrosine kinase Wzc participates in the production of capsular (CPS) and released (RPS) polysaccharides. The phosphorylation state of Wzc is dependent on the activity of phosphatase Wzb. The absence of phosphatase Wzb affects the phosphorylation/dephosphorylation cycles of Wzc, altering released polysaccharides production, and this effect is not replicated when the Y-rich region of Wzc is truncated
physiological function
-
DivL is autophosphorylated on residue Tyr550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle. DivL in vitro catalyzes phosphorylation of global response regulator CtrA and activates transcription in vitro of the cell cycle-regulated FliF promoter
-
physiological function
-
in a PTK1 mutant,community development with Streptococcus gordonii is severely abrogated. Ptk1 controls the levels of the transcriptional regulator CdhR and the fimbrial adhesin Mfa1 which mediates binding to Streptococcus gordonii. The PTK1 gene is in an operon with two genes involved in exopolysaccharide synthesis, and Ptk1 is necessary for exopolysaccharide production in Porphyromonas gingivalis. Knockout of PTK1 in an encapsulated strain of Porphyromonas gingivalis results in loss of capsule production
-
physiological function
-
a BtkA mutant is unable to complete maturation to heat- and sonication-resistant spores under both starvation- and glycerol-induced developmental conditions
-
physiological function
-
a BtkB mutant shows reduced maximum cell density as compared to the wild type when cultured in nutrient medium at 37°C. Under starvation conditions, BtkB mutant cells form fruiting bodies and spores about 24 h later than the wild-type strain. The BtkB mutant overproduces yellow pigment during development and shows a decrease in exopolysaccharide production when compared with the wild-type strain
-
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Y550F
mutant is not able to complement loss of DivL activity, mutant protein is autophosphorylated weakly at a level ca. 6fold lower than that of wild-type and 6fold less active in the phosphorylation of CtrA
Y550H
mutant is not able to complement loss of DivL activity, no autophosphorylation or phosphorylation of CtrA can be detected
Y550F
-
mutant is not able to complement loss of DivL activity, mutant protein is autophosphorylated weakly at a level ca. 6fold lower than that of wild-type and 6fold less active in the phosphorylation of CtrA
-
Y550H
-
mutant is not able to complement loss of DivL activity, no autophosphorylation or phosphorylation of CtrA can be detected
-
K540M
residues K540-D642 form a salt bridge. Mutant has a measurably higher affinity for ADP-g2+ over a range of Mg2+ concentrations. In presence of Mg2+, monomeric K540M protein forms oligomers
R614A
14.6% of wild-type activity
R614K
61.8% of wild-type activity
Y569F
mutant protein leads to production of exopolysaccharides with aberrant sizes. Mutation has little effect on the conformation of bound ATP
Y574A
98% of wild-type activity
Y574E
100% of wild-type activity
Y574F
12.1% of wild-type activity
Y574G
86.7% of wild-type activity
Y574N
26.9% of wild-type activity
H384A
upon recombinant expression, mutants accumulates to significant level in the insoluble fraction
H384Q
upon recombinant expression, mutants accumulates to significant level in the insoluble fraction
H384Q/Y416F
significant decrease in activity
H384Q/Y527F
significant decrease in activity
H384Y
mutation in a universally conserved residue among protein tyrosine kinases, residue is not essential for Src catalysis or its inactivation by C-terminal tail Tyr phosphorylation. His384 mutants undergo autophosphorylation on Tyr416 like wild-type Src but are not activated by autophosphorylation
H384Y/Y416F
significant decrease in activity
N391D
upon recombinant expression, mutant accumulates to a predominant level in the insoluble fraction and a significant level in the soluble fraction
R388A/A390R
upon recombinant expression, mutant does not accumulate to detectable levels
R550Y
mutation reduces autophosphorylation activity by about 95% and the poly(Glu, Tyr) activity by about 91%
Y686F/Y690F/Y693F/Y696F/Y699F
Y690F/Y693F
mutant is able to autophosphorylate
R550Y
-
mutation reduces autophosphorylation activity by about 95% and the poly(Glu, Tyr) activity by about 91%
-
Y686F/Y690F/Y693F/Y696F/Y699F
Y690F/Y693F
-
mutant is able to autophosphorylate
-
K55M
inactive P-loop mutant
Y686F/Y690F/Y693F/Y696F/Y699F
complete loss of autophosphorylation with only slightly reduced poly(Glu, Tyr) kinase activities
Y686F/Y690F/Y693F/Y696F/Y699F
mutant shows a great reduced level of autophosphorylation
Y686F/Y690F/Y693F/Y696F/Y699F
-
mutant shows a great reduced level of autophosphorylation
-
Y686F/Y690F/Y693F/Y696F/Y699F
-
complete loss of autophosphorylation with only slightly reduced poly(Glu, Tyr) kinase activities
-
additional information
a deletion mutant lacking the predicted activator domain (amino acids 444-464) loses autophosphorylation and poly(Glu, Tyr) kinase activities. A cytoplasmic fragment of BtkB (Ser444-Ser710) carrying replacments of all C-terminal tyrosine residues with phenylalanines, does not undergo autophosphorylation. This mutation does not significantly affect poly(Glu, Tyr) kinase activity. A cytoplasmic fragment of BtkB carrying mutations of the conserved motif ExxRxxR of BY kinases which is involved in the self-association of catalytic domains, leads to loss of autophosphorylation and poly(Glu, Tyr) kinase activities
additional information
-
a deletion mutant lacking the predicted activator domain (amino acids 444-464) loses autophosphorylation and poly(Glu, Tyr) kinase activities. A cytoplasmic fragment of BtkB (Ser444-Ser710) carrying replacments of all C-terminal tyrosine residues with phenylalanines, does not undergo autophosphorylation. This mutation does not significantly affect poly(Glu, Tyr) kinase activity. A cytoplasmic fragment of BtkB carrying mutations of the conserved motif ExxRxxR of BY kinases which is involved in the self-association of catalytic domains, leads to loss of autophosphorylation and poly(Glu, Tyr) kinase activities
additional information
a deletion mutant lacking the Y-cluster, amino acids 686-699, shows a great reduced level of autophosphorylation
additional information
-
a deletion mutant lacking the Y-cluster, amino acids 686-699, shows a great reduced level of autophosphorylation
additional information
-
a deletion mutant lacking the Y-cluster, amino acids 686-699, shows a great reduced level of autophosphorylation
-
additional information
-
a deletion mutant lacking the predicted activator domain (amino acids 444-464) loses autophosphorylation and poly(Glu, Tyr) kinase activities. A cytoplasmic fragment of BtkB (Ser444-Ser710) carrying replacments of all C-terminal tyrosine residues with phenylalanines, does not undergo autophosphorylation. This mutation does not significantly affect poly(Glu, Tyr) kinase activity. A cytoplasmic fragment of BtkB carrying mutations of the conserved motif ExxRxxR of BY kinases which is involved in the self-association of catalytic domains, leads to loss of autophosphorylation and poly(Glu, Tyr) kinase activities
-
additional information
expression of a chimeric protein CapAB protein comprides of the Cap5A1 C-terminal fragment fused to the N-terminal extremity of Cap5B2 and of its inactive P-loop mutant CapAB K55M
additional information
-
expression of a chimeric protein CapAB protein comprides of the Cap5A1 C-terminal fragment fused to the N-terminal extremity of Cap5B2 and of its inactive P-loop mutant CapAB K55M
additional information
-
mutants that change the phosphorylation status of CpsD are viable but with defective CPS production.When the C-terminal tyrosine residues of CpsD are changed to nonphosphorylable phenylalanine, cells synthesize very little low molecular weight capsular polysaccharide. When the C-terminal tyrosine residues of CpsD are changed phospho-mimicking glutamate, cells synthesize significantly more low molecular weight capsular polysaccharide
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Kemble, D.J.; Wang, Y.H.; Sun, G.
Bacterial expression and characterization of catalytic loop mutants of SRC protein tyrosine kinase
Biochemistry
45
14749-14754
2006
Gallus gallus (P00523)
brenda
Jadeau, F.; Bechet, E.; Cozzone, A.J.; Deleage, G.; Grangeasse, C.; Combet, C.
Identification of the idiosyncratic bacterial protein tyrosine kinase (BY-kinase) family signature
Bioinformatics
24
2427-2430
2008
Bacteria
brenda
Mayer, M.; Matiuhin, Y.; Nawatha, M.; Tabachnikov, O.; Fish, I.; Schutz, N.; Dvir, H.; Landau, M.
Structural and functional insights into the biofilm-associated BceF tyrosine kinase domain from Burkholderia cepacia
Biomolecules
11
1196
2021
Burkholderia cepacia (Q0GYW2), Burkholderia cepacia
brenda
Lee, D.; Zheng, J.; She, Y.; Jia, Z.
Structure of Escherichia coli tyrosine kinase Etk reveals a novel activation
EMBO J.
27
1758-1766
2008
Escherichia coli (P38134)
brenda
Kimura, Y.; Kato, T.; Mori, Y.
Function analysis of a bacterial tyrosine kinase, BtkB, in Myxococcus xanthus
FEMS Microbiol. Lett.
336
45-51
2012
Myxococcus xanthus (Q1DDI7), Myxococcus xanthus, Myxococcus xanthus DK1622 (Q1DDI7)
brenda
Grangeasse, C.; Doublet, P.; Vaganay, E.; Vincent, C.; Deleage, G.; Duclos, B.; Cozzone, A.J.
Characterization of a bacterial gene encoding an autophosphorylating protein tyrosine kinase
Gene
204
259-265
1997
Acinetobacter johnsonii (O52788)
brenda
Kimura, Y.; Yamashita, S.; Mori, Y.; Kitajima, Y.; Takegawa, K.
A Myxococcus xanthus bacterial tyrosine kinase, BtkA, is required for the formation of mature spores
J. Bacteriol.
193
5853-5857
2011
Myxococcus xanthus (Q1D7E6), Myxococcus xanthus, Myxococcus xanthus DK1622 (Q1D7E6)
brenda
Kato, T.; Shirakawa, Y.; Takegawa, K.; Kimura, Y.
Functional analysis of conserved motifs in a bacterial tyrosine kinase, BtkB, from Myxococcus xanthus
J. Biochem.
158
385-392
2015
Myxococcus xanthus (Q1DDI7), Myxococcus xanthus, Myxococcus xanthus DK1622 (Q1DDI7)
brenda
Wugeditsch,T.; Paiment, A.; Hocking,J.; Drummelsmith, J.; Forrester, C.; Whitfield, C.
Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli
J. Biol. Chem.
276
2361-2371
2001
Escherichia coli (Q9X4B9)
brenda
Soulat, D.; Jault, J.; Duclos, B.; Geourjon, C.; Cozzone, A.; Grangeasse, C.
Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism
J. Biol. Chem.
281
14048-14056
2006
Staphylococcus aureus (A8YPQ5), Staphylococcus aureus
brenda
Temel, D.B.; Dutta, K.; Alphonse, S.; Nourikyan, J.; Grangeasse, C.; Ghose, R.
Regulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase
J. Biol. Chem.
288
15212-15228
2013
Escherichia coli (P76387), Escherichia coli
brenda
Wright, C.J.; Xue, P.; Hirano, T.; Liu, C.; Whitmore, S.E.; Hackett, M.; Lamont, R.J.
Characterization of a bacterial tyrosine kinase in Porphyromonas gingivalis involved in polymicrobial synergy
MicrobiologyOpen
3
383-394
2014
Porphyromonas gingivalis (B2RKZ8), Porphyromonas gingivalis, Porphyromonas gingivalis DSM 20709 (B2RKZ8)
brenda
Pereira, S.; Santos, M.; Leite, J.; Flores, C.; Eisfeld, C.; Buettel, Z.; Mota, R.; Rossi, F.; De Philippis, R.; Gales, L.; Morais-Cabral, J.; Tamagnini, P.
The role of the tyrosine kinase Wzc (Sll0923) and the phosphatase Wzb (Slr0328) in the production of extracellular polymeric substances (EPS) by Synechocystis PCC 6803
MicrobiologyOpen
8
e00753
2019
Synechocystis sp. PCC 6803 (P72877)
brenda
Olivares-Illana, V.; Meyer, P.; Bechet, E.; Gueguen-Chaignon, V.; Soulat, D.; Lazereg-Riquier, S.; Mijakovic, I.; Deutscher, J.; Cozzone, A.; Laprevote, O.; Morera, S.; Grangeasse, C.; Nessler, S.
Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus
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6
1321-1331
2008
Staphylococcus aureus (A8YPQ5), Staphylococcus aureus
brenda
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Autophosphorylation of the bacterial tyrosine-kinase CpsD connects capsule synthesis with the cell cycle in Streptococcus pneumoniae
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11
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