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Literature summary for 3.1.3.3 extracted from

  • 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 (2018), Int. J. Mol. Sci., 19, 2872-2901 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.3

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O-phospho-L(or D)-serine + H2O Bacillus subtilis
-
 L(or D)-serine + phosphate
-
 ?
O-phospho-L(or D)-serine + H2O Bacillus subtilis 168
-
 L(or D)-serine + phosphate
-
 ?
[RsbS]-serine/threonine phosphate + H2O Bacillus subtilis
-
 [RsbS]-serine/threonine + phosphate
-
 ?
[RsbS]-serine/threonine phosphate + H2O Bacillus subtilis 168
-
 [RsbS]-serine/threonine + phosphate
-
 ?
[RsbV]-serine/threonine phosphate + H2O Bacillus subtilis
-
 [RsbV]-serine/threonine + phosphate
-
 ?
[RsbV]-serine/threonine phosphate + H2O Bacillus subtilis 168
-
 [RsbV]-serine/threonine + phosphate
-
 ?
[TsbR]-serine/threonine phosphate + H2O Bacillus subtilis
-
 [TsbR]-serine/threonine + phosphate
-
 ?
[TsbR]-serine/threonine phosphate + H2O Bacillus subtilis 168
-
 [TsbR]-serine/threonine + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O07014
-
-
Bacillus subtilis P17906
-
-
Bacillus subtilis P40399
-
-
Bacillus subtilis 168 O07014
-
-
Bacillus subtilis 168 P17906
-
-
Bacillus subtilis 168 P40399
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-phospho-L(or D)-serine + H2O
-
 Bacillus subtilis L(or D)-serine + phosphate
-
 ?
O-phospho-L(or D)-serine + H2O
-
 Bacillus subtilis 168 L(or D)-serine + phosphate
-
 ?
[RsbS]-serine/threonine phosphate + H2O
-
 Bacillus subtilis [RsbS]-serine/threonine + phosphate
-
 ?
[RsbS]-serine/threonine phosphate + H2O
-
 Bacillus subtilis 168 [RsbS]-serine/threonine + phosphate
-
 ?
[RsbV]-serine/threonine phosphate + H2O
-
 Bacillus subtilis [RsbV]-serine/threonine + phosphate
-
 ?
[RsbV]-serine/threonine phosphate + H2O
-
 Bacillus subtilis 168 [RsbV]-serine/threonine + phosphate
-
 ?
[TsbR]-serine/threonine phosphate + H2O
-
 Bacillus subtilis [TsbR]-serine/threonine + phosphate
-
 ?
[TsbR]-serine/threonine phosphate + H2O
-
 Bacillus subtilis 168 [TsbR]-serine/threonine + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
BSU04700
-
 Bacillus subtilis
BSU04740
-
 Bacillus subtilis
BSU34110
-
 Bacillus subtilis
More cf. EC 3.1.3.16 Bacillus subtilis
phosphoserine phosphatase RsbP UniProt Bacillus subtilis
phosphoserine phosphatase RsbU UniProt Bacillus subtilis
phosphoserine phosphatase RsbX UniProt Bacillus subtilis
RsbP
-
 Bacillus subtilis
RsbU
-
 Bacillus subtilis
RsbX
-
 Bacillus subtilis
serine/threonine protein phosphatase
-
 Bacillus subtilis
sigma-B negative effector UniProt Bacillus subtilis
StP
-
 Bacillus subtilis
yvfP
-
 Bacillus subtilis

General Information

General Information Comment Organism
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 Bacillus subtilis
physiological function reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. The corresponding kinase to enzyme PrpC is kinase RsbB. Enzyme RsbX is a PPM phosphatase. The phosphoserine phosphatase is involved in sigma B regulation and stress response Bacillus subtilis
physiological function reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. The corresponding kinase to enzyme PrpC is kinase RsbV. Enzyme RsbU is a PPM phosphatase. The phosphoserine phosphatase is involved in energy stress response Bacillus subtilis
physiological function reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. The corresponding kinase to enzyme PrpC is kinase RsbV. Enzyme RsbU is a PPM phosphatase. The phosphoserine phosphatase is involved in sigma B regulation and stress response Bacillus subtilis