Any feedback?
Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Escherichia coli and UniProt Accession P55798
for references in articles please use BRENDA:EC3.1.3.16Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.3.16 protein-serine/threonine phosphataseIUBMB Comments
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).
Specify your search results
Word Map
- 3.1.3.16
-
cyclosporine
- phosphatases
- tacrolimus
-
rejection
-
okadaic
- mycophenolate
-
allograft
- cardiac
- steroid
-
corticosteroid
- mofetil
- rapamycin
-
nephrotoxicity
- nfat
- sirolimus
- agonist
- t-cells
- creatinine
- hypertrophy
- mapks
- glycogen
- synaptic
- mtor
-
glomerular
- pkc
- platelet
-
ca2+-dependent
- hypertension
- episode
- erk
-
atopic
- cardiomyocytes
- nephropathy
-
everolimus
- dermatitis
- myocytes
-
trough
-
hyperphosphorylation
- azathioprine
-
posttransplant
-
prophylaxis
-
allogeneic
- proteinuria
- camkii
-
post-transplantation
- graft-versus-host
- rituximab
- cyclophilins
-
biopsy-proven
- prednisone
- diagnostics
- analysis
- drug development
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
calcineurin, protein phosphatase, pac-1, dusp1, dusp6, serine/threonine phosphatase, pp2ac, ppm1d, phosphoprotein phosphatase, laforin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy 3-methylglutaryl CoenzymeA reductase phosphatase
-
-
-
-
Aspergillus awamori acid protein phosphatase
-
-
-
-
BCKDH phosphatase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase phosphatase
-
-
-
-
calcineurin
-
-
-
-
Calcineurin A1
-
-
-
-
Calcineurin A2
-
-
-
-
CaM-kinase phosphatase
-
-
-
-
CaMKPase
-
-
-
-
casein phosphatase
-
-
-
-
DRES10
-
-
-
-
Fibroblast growth factor inducible protein 13
-
-
-
-
FIN13
-
-
-
-
Flap wing protein
-
-
-
-
HMG-CoA reductase phosphatase
-
-
-
-
Magnesium-dependent calcium inhibitable phosphatase
-
-
-
-
MCPP
-
-
-
-
Microtubule star protein
-
-
-
-
phosphatase 2A
-
-
-
-
phosphatase 2B
-
-
-
-
phosphatase C-II
-
-
-
-
Phosphatase esp1
-
-
-
-
phosphatase H-II
-
-
-
-
phosphatase I
-
-
-
-
phosphatase IB
-
-
-
-
phosphatase II
-
-
-
-
phosphatase III
-
-
-
-
phosphatase IV
-
-
-
-
phosphatase SP
-
-
-
-
phosphoprotein phosphatase
-
-
-
-
phosphopyruvate dehydrogenase phosphatase
-
-
-
-
phosphospectrin phosphatase
-
-
-
-
PK-Pase
-
-
-
-
polycation modulated (PCM-) phosphatase
-
-
-
-
PP-1A
-
-
-
-
PP-1B
-
-
-
-
PP-1G
-
-
-
-
PP2A-alpha
-
-
-
-
PP2A-beta
-
-
-
-
PP2C
-
-
-
-
PP2C-alpha
-
-
-
-
PP2C-beta
-
-
-
-
PP2C-delta
-
-
-
-
PP2C-gamma
-
-
-
-
Pp4
-
-
-
-
PP5
-
-
-
-
PP6
-
-
-
-
PPEF
-
-
-
-
PPN
-
-
-
-
PPT
-
-
-
-
protein D phosphatase
-
-
-
-
protein phosphatase
-
-
-
-
Protein phosphatase 1A
-
-
-
-
Protein phosphatase 1B
-
-
-
-
Protein phosphatase 1C
-
-
-
-
Protein phosphatase magnesium-dependent 1 delta
-
-
-
-
Protein phosphatase magnesium-dependent 1 gamma
-
-
-
-
Protein phosphatase with EF calcium-binding domain
-
-
-
-
PSPase
-
-
-
-
Retinal degeneration C protein
-
-
-
-
Suppressor protein SDS21
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-serine/threonine-phosphate phosphohydrolase
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).
CAS REGISTRY NUMBER
COMMENTARY
9025-75-6
-
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
[casein]-serine/threonine phosphate + H2O
[casein]-serine/threonine + phosphate
-
-
-
?
[myelin basic protein]-serine/threonine phosphate + H2O
[myelin basic protein]-serine/threonine + phosphate
-
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[YegI kinase]-serine/threonine phosphate + H2O
[YegI kinase]-serine/threonine + phosphate
dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC
-
-
?
additional information
?
-
the enzyme is a dual-specificity Ser/Thr/Tyr phosphatase also exhibiting the activity of EC 3.1.3.48
-
-
?
additional information
?
-
PphC displays low preference for pSer/pThr/pTyr peptides, the minimal activity against phosphopeptides is in contrast to the ability of PphC to dephosphorylate the pSer-containing protein substrate beta-casein. PphC may require additional residues for substrate recognition and/or binding that are not present in the phosphopeptides
-
-
?
additional information
?
-
-
PphC displays low preference for pSer/pThr/pTyr peptides, the minimal activity against phosphopeptides is in contrast to the ability of PphC to dephosphorylate the pSer-containing protein substrate beta-casein. PphC may require additional residues for substrate recognition and/or binding that are not present in the phosphopeptides
-
-
?
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
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
-
-
-
?
[YegI kinase]-serine/threonine phosphate + H2O
[YegI kinase]-serine/threonine + phosphate
dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
highly activating, PphC (YegK) is a Mn2+-dependent PP2C-like phosphatase, best at 1-2 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by sanguinarine chloride at 0.05 mM. Poor inhibition by orthovanadate at 0.005-0.05 mM
-
additional information
-
no inhibition by sanguinarine chloride at 0.05 mM. Poor inhibition by orthovanadate at 0.005-0.05 mM
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. Enzyme PrpA is a PPP phosphatase
evolution
enzyme PphC belongs to the eukaryote-like Ser/Thr phosphatases (eSTPs) in Escherichia coli, that have extensive sequence and structural homology to eukaryotic Ser/Thr protein phosphatase 2C (PP2C) phosphatases. But YegK is an atypical PP2C-like phosphatase. Unlike other bacterial PP2C homologues, YegK contains only six of the eight absolutely conserved residues that are involved in metal binding, coordination, and catalysis, instead of eleven. In particular, the amino acid sequence alignment clearly shows that YegK lacks the conserved glycine residue in motif VI and the aspartic acid residue in motif VIII
physiological function
the Escherichia coli eSTP acts to dephosphorylate another Ser/Thr kinase that is encoded in the same operon. Regulatory reversible protein phosphorylation is a conserved mechanism of signaling in all biological systems
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain C43 (DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pphC or yegK, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain C43 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Janczarek, M.; Vinardell, J.M.; Lipa, P.; Karas, M.
Hanks-type Serine/threonine protein kinases and phosphatases in bacteria roles in signaling and adaptation to various environments
Int. J. Mol. Sci.
19
2872-2901
2018
Streptococcus pneumoniae, Enterococcus faecium, Streptococcus mutans, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 (P37979), Pseudomonas aeruginosa (A0A072ZI21), Pseudomonas aeruginosa (Q9I757), Bacillus anthracis (A0A0F7RDQ4), Mycoplasma pneumoniae (A0A0H3DJW0), Bacillus subtilis (O34779), Bacillus subtilis (P37475), Mycoplasma genitalium (P47449), Escherichia coli (P55798), Mycobacterium tuberculosis (P9WHW5), Myxococcus xanthus (Q1D1H4), Rhizobium leguminosarum bv. viciae (Q1MCQ2), Mycoplasmopsis synoviae (Q4A6S8), Streptococcus pyogenes serotype M6 (Q5XAP6), Streptococcus agalactiae (Q8VQA1), Listeria monocytogenes serotype 1/2a (Q8Y678), Nostoc sp. PCC 7120 = FACHB-418 (Q8YW58), Staphylococcus aureus (Q9RL81), Pseudomonas aeruginosa ATCC 15692 (Q9I757), Bacillus subtilis 168 (O34779), Bacillus subtilis 168 (P37475), Mycoplasma pneumoniae FH (A0A0H3DJW0), Myxococcus xanthus DK 1622 (Q1D1H4), Mycoplasma genitalium NCTC 10195 (P47449), Mycoplasma pneumoniae NBRC 14401 (A0A0H3DJW0), Pseudomonas aeruginosa 1C (Q9I757), Synechocystis sp. PCC 6803 Kasuza (P37979), Mycoplasma genitalium ATCC 33530 (P47449), Mycoplasma pneumoniae ATCC 15531 (A0A0H3DJW0), Pseudomonas aeruginosa PRS 101 (Q9I757), Mycoplasma pneumoniae DSM 22911 (A0A0H3DJW0), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y678), Pseudomonas aeruginosa DSM 22644 (Q9I757), Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576 (Q8YW58), Pseudomonas aeruginosa CIP 104116 (Q9I757), Pseudomonas aeruginosa LMG 12228 (Q9I757), Mycobacterium tuberculosis H37Rv (P9WHW5), Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82 (Q8YW58), Streptococcus pyogenes serotype M6 ATCC BAA-946 (Q5XAP6), Mycoplasmopsis synoviae 53 (Q4A6S8), Mycoplasma genitalium G-37 (P47449), Listeria monocytogenes serotype 1/2a EGD-e (Q8Y678), Pseudomonas aeruginosa JCM 14847 (Q9I757), Mycoplasma pneumoniae NCTC 10119 (A0A0H3DJW0)
EXTERNAL LINKS (specific for EC-Number 3.1.3.16)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
