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Information on EC 2.7.11.1 - non-specific serine/threonine protein kinase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WI83
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2.7.11.1 non-specific serine/threonine protein kinaseIUBMB Comments
This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analysed to date.
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Word Map
- 2.7.11.1
- jnk
- mapks
-
signal-regulated
- rapamycin
- agonist
- necrosis
- endothelial
- cardiac
- mtor
- parkinsonism
- caspase-3
- metastasis
- bcl-2
- synaptic
- cyclin
- alzheimer
- cyclase
- hippocampal
- forskolin
- sirnas
- neurodegenerative
- autophosphorylation
-
neuroprotective
- creb
-
phorbol
- tumorigenesis
- cardiomyocytes
- wortmannin
- pten
-
cyclin-dependent
- ventricular
- gtpases
- myocytes
- cytoskeleton
-
adenylyl
- nf-kappab
- myocardial
- ischemia
-
dominant-negative
- nmda
-
hyperphosphorylation
-
postsynaptic
-
anti-apoptotic
- src
- phosphoprotein
- isoproterenol
- rhoa
- staurosporine
-
tensin
-
l-type
- medicine
- pharmacology
- molecular biology
- drug development
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
protein kinase a, 14-3-3, camkii, p-akt, lrrk2, c-jun n-terminal kinase, serine/threonine kinase, raf-1, protein kinase b, gsk-3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A-kinase
-
-
-
-
A-T, mutated
-
-
-
-
A-T, mutated homolog
-
-
-
-
AMH type II receptor
-
-
-
-
Anti-sigma B factor rsbT
-
-
-
-
AP50 kinase
-
-
-
-
Ataxia telangiectasia mutated
-
-
-
-
Ataxia telangiectasia mutated homolog
-
-
-
-
ATP-protein transphosphorylase
-
-
-
-
betaIIPKC
-
-
-
-
Breast-tumor-amplified kinase
-
-
-
-
Calcium-dependent protein kinase C
-
-
-
-
Calcium/phospholipid-dependent protein kinase
-
-
-
-
cAMP-dependent protein kinase A
-
-
-
-
casein kinase
-
-
-
-
casein kinase 2
-
-
-
-
casein kinase I
-
-
-
-
casein kinase II
-
-
-
-
casein kinase-2
-
-
-
-
CDC25 suppressing protein kinase
-
-
-
-
Cell division cycle 2-like
-
-
-
-
CK-2
-
-
-
-
CK2
-
-
-
-
CK2-alpha
-
-
-
-
CKI
-
-
-
-
CKII
-
-
-
-
CLP-36 interacting kinase
-
-
-
-
cyclic monophosphate-dependent protein kinase
-
-
-
-
cyclic nucleotide-dependent protein kinase
-
-
-
-
cyclin-dependent kinase
-
-
-
-
cytidine 3',5'-cyclic monophosphate-responsive protein kinase
-
-
-
-
DNA-PKcs
-
-
-
-
DNPK1
-
-
-
-
dSTPK61
-
-
-
-
G11 protein
-
-
-
-
hARK1
-
-
-
-
histone kinase
-
-
-
-
hPDK1
-
-
-
-
Hpr kinase
-
-
-
-
hPSK
-
-
-
-
HSPK 21
-
-
-
-
HSPK 36
-
-
-
-
hydroxyalkyl-protein kinase
-
-
-
-
Kinase interacting with stathmin
-
-
-
-
kinase, casein (phosphorylating)
-
-
-
-
kinase, protamine (phosphorylating)
-
-
-
-
kinase, protein (phosphorylating)
-
-
-
-
kinase, protein, A (phosphorylating)
-
-
-
-
kinase, protein, C (phosphorylating)
-
-
-
-
Lymphocyte-oriented kinase
-
-
-
-
M phase-specific cdc2 kinase
-
-
-
-
mitogen-activated S6 kinase
-
-
-
-
mPDK1
-
-
-
-
MPSK
-
-
-
-
Myristoylated and palmitoylated serine-threonine kinase
-
-
-
-
NY-REN-55 antigen
-
-
-
-
P-CIP2
-
-
-
-
P460
-
-
-
-
p46Eg265
-
-
-
-
p46XlEg22
-
-
-
-
p82 kinase
-
-
-
-
pEg2
-
-
-
-
phosphorylase b kinase kinase
-
-
-
-
Phototropin
-
-
-
-
Pim-2h
-
-
-
-
PKA
-
-
-
-
PkB kinase
-
-
-
-
PknE
PknH
PknI
pp39-mos
-
-
-
-
Pre-mRNA protein kinase
-
-
-
-
protamine kinase
-
-
-
-
protein glutamyl kinase
-
-
-
-
protein kinase (phosphorylating)
-
-
-
-
Protein kinase B kinase
-
-
-
-
protein kinase CK2
-
-
-
-
Protein kinase Krct
-
-
-
-
Protein kinase MST
-
-
-
-
protein kinase p58
-
-
-
-
Protein kinase PKL12
-
-
-
-
protein phosphokinase
-
-
-
-
protein serine kinase
-
-
-
-
protein serine-threonine kinase
-
-
-
-
protein-aspartyl kinase
-
-
-
-
protein-cysteine kinase
-
-
-
-
protein-serine kinase
-
-
-
-
protein-serine/threonine kinase
-
-
-
-
PRP4 kinase
-
-
-
-
PRP4 pre-mRNA processing factor 4 homolog
-
-
-
-
PSK-H1
-
-
-
-
Raf kinase
-
-
-
-
Raf-1
-
-
-
-
ratAurA
-
-
-
-
ribosomal protein S6 kinase II
-
-
-
-
ribosomal S6 protein kinase
-
-
-
-
RP1 protein
-
-
-
-
S-receptor kinase
-
-
-
-
serine kinase
-
-
-
-
serine protein kinase
-
-
-
-
serine(threonine) protein kinase
-
-
-
-
serine-specific protein kinase
-
-
-
-
serine-threonine kinase
serine/threonine kinase
Serine/threonine kinase 15
-
-
-
-
Serine/threonine kinase Ayk1
-
-
-
-
serine/threonine protein kinase
Serine/threonine-protein kinase NRK2
-
-
-
-
Serine/threonine-protein kinase NYD-SPK
-
-
-
-
SRK
-
-
-
-
Ste20-like kinase
-
-
-
-
STE20-like kinase MST1
-
-
-
-
STE20-like kinase MST2
-
-
-
-
STE20-like kinase MST3
-
-
-
-
StpK
Switch protein/serine kinase
-
-
-
-
T-antigen kinase
-
-
-
-
threonine-specific protein kinase
-
-
-
-
Twitchin kinase
-
-
-
-
type-2 casein kinase
-
-
-
-
serine/threonine kinase
-
-
-
-
serine/threonine protein kinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
active site structure
-
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
Lys45 is important for PknH catalytic and autophosphorylation activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (non-specific)
This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analysed to date.
CAS REGISTRY NUMBER
COMMENTARY
191808-15-8
phosphoinositide dependent protein kinase 1
340830-03-7
-
37278-10-7
-
377752-08-4
ribosomal protein S6 kinase 2
389133-24-8
ribosomal S6 kinase 3
52660-18-1
casein kinase, protein kinase CK2
9026-43-1
this CAS Reg. No. encompasses a great variety of protein kinases including the serine/threonine specific kinases
90698-26-3
ribosomal protein S6 kinase 1
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase
ADP + phosphorylated-UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase
evidence is provided that mycobacterial mMurD is a substrate of PknA
-
-
?
ATP + a protein
ADP + a phosphoprotein
autophosphorylation on Thr
-
-
?
ATP + EmbR
ADP + phosphorylated-EmbR
PknH phosphorylates the transcriptional regulator EmbR, but not its homologue EmbR2
-
-
?
ATP + FHA-domain containing protein GarA
ADP + phosphorylated FHA-domain containing protein GarA
-
-
-
?
ATP + glutamine synthetase
ADP + phosphorylated glutamine synthetase
-
-
-
?
ATP + myelic basic protein
ADP + myelic basic phosphoprotein
-
phosphorylation of serine and threonine residues by PknB
-
-
?
ATP + histone
ADP + phosphorylated histone
histones from calf thymus, phosphorylation on Ser
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
myelin basic proteins from bovine brain, phosphorylation on Ser
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
PknB, PknD, PknE, and PknF
-
-
?
additional information
?
-
-
enzyme is involved in stress response and adaptation to environmental changes in mycobacteria
-
-
?
additional information
?
-
-
PknB performs autophosphorylation
-
-
?
additional information
?
-
-
PknB, PknD, PknE, and PknF perform autophosphorylation
-
-
?
additional information
?
-
-
PknH performs autophosphorylation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + FHA-domain containing protein GarA
ADP + phosphorylated FHA-domain containing protein GarA
-
-
-
?
ATP + glutamine synthetase
ADP + phosphorylated glutamine synthetase
-
-
-
?
additional information
?
-
-
enzyme is involved in stress response and adaptation to environmental changes in mycobacteria
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
additional information
-
no activity with cations other than Mg2+ or Mn2+
additional information
-
no activity with Mg2+ alone, no activity with Cu2+ or Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP-PNP
-
ATP analogue adenosine 5'-(beta,gamma-imino)triphosphate
EmbR2
EmbR2, a homologue of EmbR, inhibits PknH by binding to at least two of the three threonine sites known to undergo autophosphorylation in PknH which leads to a dose-response inhibition of the autokinase activity. Moreover, EmbR2 inhibits PknH-dependent phosphorylation of EmbR in a dose-dependent manner
-
additional information
-
enzyme expression level is decreased under low pH and heat shock conditions
-
staurosporine
inhibits phosphorylation of myelin basic proteins
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
autophosphorylation patterns for activation of PknB, PknD, PknE, and PknF, e.g. PknB phosphorylation at Thr171 and Thr173 of the activation loop and at Thr294 of the juxtamembrane domain are necessary for activity
-
additional information
activation of PknI kinase from Mycobacteriumxa0tuberculosis via dimerization of the extracellular sensor domain
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
enzyme expression level under stress conditions, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
PknB, PknD, PknE, and PknF possess an N-terminal kinase domain, a juxtamembrane domain of varying length, and an activation loop
-
deduced amino acid sequence contains two transmembrane segments, which flank a highly repetitive region, suggesting a receptor-like anchoring
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the enzyme-deletion mutant DELTApknE shows in presence of stress (pH, surfactant and cell wall-damaging agents) and anti-tuberculosis drugs a defective growth in pH 7.0 and lysozyme (a cell wall-damaging agent) with better survival in pH 5.5, SDS, and kanamycin (a second-line anti-tuberculosis drug). DELTApknE is reduced in cell size during growth in liquid media and exhibits hypervirulence in a guinea pig model of infection
physiological function
physiological function
the enzyme is involved in the adaptive responses and contributes to the suppression of apoptosis
physiological function
the enzyme (PknG) regulates many physiological processes, such as nitrogen and energy metabolism, cell wall synthesis and protein translation
physiological function
the enzyme is required for regulating Mycobacterium tuberculosis growth within macrophage
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
-
x * 61805, amino acid sequence calculation, x * 55000, recombinant cytoplasmic domain, SDS-PAGE, x * 80000-85000, recombinant full-length PknI, migrates probably as a doublet, SDS-PAGE
61805
-
x * 61805, amino acid sequence calculation, x * 55000, recombinant cytoplasmic domain, SDS-PAGE, x * 80000-85000, recombinant full-length PknI, migrates probably as a doublet, SDS-PAGE
68000
-
x * 97000, recombinant GST-fusion PknH, SDS-PAGE, x * 68000, non-tagged PknH, SDS-PAGE
97000
-
x * 97000, recombinant GST-fusion PknH, SDS-PAGE, x * 68000, non-tagged PknH, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
PknI sensor domain (PknI_SD) adopts two conformations in solution: monomer and dimer
monomer
PknI sensor domain (PknI_SD) adopts two conformations in solution: monomer and dimer
additional information
?
-
x * 61805, amino acid sequence calculation, x * 55000, recombinant cytoplasmic domain, SDS-PAGE, x * 80000-85000, recombinant full-length PknI, migrates probably as a doublet, SDS-PAGE
?
-
x * 97000, recombinant GST-fusion PknH, SDS-PAGE, x * 68000, non-tagged PknH, SDS-PAGE
additional information
-
PknB, PknD, PknE, and PknF possess an N-terminal kinase domain, a juxtamembrane domain of varying length, and an activation loop
additional information
-
PknH contains 11 subdomains, schematic structure, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
PknB, PknD, PknE, and PknF are autophosphorylated at multiple sites, phosphorylation patterns, overview, the enzymes are dephosphorylated by the cognate mycobacterial phosphatase PstP
phosphoprotein
-
PknH performs autophosphorylation, mutant K45M is inactive
phosphoprotein
enzyme possesses autophosphorylation activity. The activation loop phosphorylated residues Thr173 and Thr175 are essential for the autophosphorylation activity of PknL. Phosphorylation of the activation loop Thr173 residue is also required for optimal PknL-mediated phosphorylation of Rv2175c
phosphoprotein
simulated PknI_KJD dimerization activates kinase autophosphorylation activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged N-terminal catalytic domain of PknB, residues 1-331, hanging drop vapour diffusion method, 0.001 ml protein solution containing 5 mg/ml protein mixed with equal volume of 0.1 M HEPES, pH 7.5, 30 mM MgCl2, 0.15 mM inhibitor AMP-PNP, 27% PEG 400, and 4% 1,3-butanediol, 19°C, versus 1 ml of a solution containing 0.1 M HEPES, pH 7.5, 30 mM MgCl2, and 27% PEG 400, 2-3 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
vapor diffusion method, crystal structures of PknI sensor domain (PknI_SD) monomer and dimer, as well as PknI kinase domain (PknI_KD)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA370-399/K48M
mutant protein shows no autophosphorylation activity, indicating that Lys48 is essential for catalysing the phosphorylation reaction
DELTA370-399/S171A
mutant protein shows similar autophosphorylation activity compared to wild-type, indicating that Ser171 is not an autophosphorylated residue
DELTA370-399/S174A
mutant protein shows similar autophosphorylation activity compared to wild-type, indicating that Ser171 is not an autophosphorylated residue
DELTA370-399/T173A
mutant protein shows an autophosphorylation activity of only 19% compared to wild-type
DELTA370-399/T173A/T175A
mutant protein shows an autophosphorylation activity of only 19% compared to wild-type
DELTA370-399/T175A
mutant protein shows an autophosphorylation activity of only 46% compared to wild-type
additional information
additional information
results of a solid-phase binding assays reveal a high affinity in vitro binding between PknA and mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase mMurD
additional information
-
results of a solid-phase binding assays reveal a high affinity in vitro binding between PknA and mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase mMurD
additional information
generation of the enzyme-deletion mutant DELTApknE. Mutant DELTApknE in presence of stress (pH, surfactant and cell wall-damaging agents) and anti-tuberculosis drugs shows defective growth in pH 7.0 and lysozyme with better survival in pH 5.5, SDS, and kanamycin. DELTApknE is resistant to kanamycin
additional information
-
generation of the enzyme-deletion mutant DELTApknE. Mutant DELTApknE in presence of stress (pH, surfactant and cell wall-damaging agents) and anti-tuberculosis drugs shows defective growth in pH 7.0 and lysozyme with better survival in pH 5.5, SDS, and kanamycin. DELTApknE is resistant to kanamycin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme is purified as a fusion protein with gluthatione S-transferase
recombinant His-tagged full-length and cytoplasmic domain of PknI from Escherichia coli strain BL21 by nickel affinity chromatography
-
recombinant His-tagged N-terminal catalytic domain of PknB and His-tagged residues 1-279 construct from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged PknB, PknD, PknE, and PknF rom Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant wild-type and mutant GST-fusion PknH from Escherichia coli by glutathione affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged PknB, PknD, PknE, and PknF in Escherichia coli strain BL21(DE3)
-
expression of N-terminal catalytic domain of PknB, comprising residues 1-331, and of a construct comprising residues 1-279 in Escherichia coli BL21(DE3) as His-tagged proteins
-
gene pknI, DNA and amino acid sequence determination and analysis, NaCl-inducible expression of N-terminally His-tagged full-length and cytoplasmic domain of PknI in Escherichia coli strain BL21 in inclusion bodies
-
gene Rv1266c or pknH, overexpression of wild-type and mutant GST-fusion PknH in Escherichia coli
-
the cytosolic domain of PknL (DELTA370-399) is expressed in Escherichia coli as a GST-fusion protein
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
EmbR2 is a regulator of PknH activation, thus directly participating in the control of the PknH/EmbR pair
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; et al.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Nature
393
537-544
1998
Mycobacterium tuberculosis (P9WI79)
Peirs, P.; De Wit, L.; Braibant, M.; Huygen, K.; Content, J.
A serine/threonine protein kinase from Mycobacterium tuberculosis
Eur. J. Biochem.
244
604-612
1997
Mycobacterium tuberculosis (P9WI79), Mycobacterium tuberculosis
Duran, R.; Villarino, A.; Bellinzoni, M.; Wehenkel, A.; Fernandez, P.; Boitel, B.; Cole, S.T.; Alzari, P.M.; Cervenansky, C.
Conserved autophosphorylation pattern in activation loops and juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein kinases
Biochem. Biophys. Res. Commun.
333
858-867
2005
Mycobacterium tuberculosis
Sharma, K.; Chandra, H.; Gupta, P.K.; Pathak, M.; Narayan, A.; Meena, L.S.; D'Souza, R.C.J.; Chopra, P.; Ramachandran, S.; Singh, Y.
PknH, a transmembrane Hank's type serine/threonine kinase from Mycobacterium tuberculosis is differentially expressed under stress conditions
FEMS Microbiol. Lett.
233
107-113
2004
Mycobacterium tuberculosis
Ortiz-Lombardia, M.; Pompeo, F.; Boitel, B.; Alzari, P.M.
Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis
J. Biol. Chem.
278
13094-13100
2003
Mycobacterium tuberculosis
Gopalaswamy, R.; Narayanan, P.R.; Narayanan, S.
Cloning, overexpression, and characterization of a serine/threonine protein kinase pknI from Mycobacterium tuberculosis H37Rv
Protein Expr. Purif.
36
82-89
2004
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Molle, V.; Reynolds, R.C.; Alderwick, L.J.; Besra, G.S.; Cozzone, A.J.; Fuetterer, K.; Kremer, L.
EmbR2, a structural homologue of EmbR, inhibits the Mycobacterium tuberculosis kinase/substrate pair PknH/EmbR
Biochem. J.
410
309-317
2008
Mycobacterium tuberculosis (P9WI71), Mycobacterium tuberculosis H37Rv (P9WI71)
Thakur, M.; Chakraborti, P.K.
Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis
Biochem. J.
415
27-33
2008
Mycobacterium tuberculosis (P9WI83), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WI83)
Canova, M.J.; Veyron-Churlet, R.; Zanella-Cleon, I.; Cohen-Gonsaud, M.; Cozzone, A.J.; Becchi, M.; Kremer, L.; Molle, V.
The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c
Proteomics
8
521-533
2008
Mycobacterium tuberculosis (P9WI63), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WI63)
Kumar, D.; Palaniyandi, K.; Challu, V.; Kumar, P.; Narayanan, S.
PknE, a serine/threonine protein kinase from Mycobacterium tuberculosis has a role in adaptive responses
Arch. Microbiol.
195
75-80
2013
Mycobacterium tuberculosis (P9WI77), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WI77)
Gil, M.; Lima, A.; Rivera, B.; Rossello, J.; Urdniz, E.; Cascioferro, A.; Carrin, F.; Wehenkel, A.; Bellinzoni, M.; Batthyny, C.; Pritsch, O.; Denicola, A.; Alvarez, M.; Carvalho, P.; Lisa, M.; Brosch, R.; Piuri, M.; Alzari, P.; Durn, R.
New substrates and interactors of the mycobacterial serine/threonine protein kinase PknG identified by a tailored interactomic approach
J. Proteomics
192
321-333
2019
Mycobacterium tuberculosis (P9WI73), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WI73)
Yan, Q.; Jiang, D.; Qian, L.; Zhang, Q.; Zhang, W.; Zhou, W.; Mi, K.; Guddat, L.; Yang, H.; Rao, Z.
Structural insight into the activation of PknI kinase from M.xa0tuberculosis via dimerization of the extracellular sensor domain
Structure
25
1286-1294.e4
2017
Mycobacterium tuberculosis (P9WI69), Mycobacterium tuberculosis H37Rv (P9WI69)
EXTERNAL LINKS (specific for EC-Number 2.7.11.1)
Transporter Classification Database (TCDB): 8.A.23.1.35, 9.B.321.1.1, 8.A.104.1.10, 1.A.87.2.4, 1.I.1.1.3, 1.A.87.2.9, 8.A.104.1.1, 1.A.87.2.6, 1.I.1.1.5, 9.A.15.1.1, 1.A.4.5.8, 1.A.4.5.1, 1.A.87.2.11, 8.A.104.1.9, 1.A.87.2.3, 8.A.104.1.5, 2.A.133.1.3
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