PMID:16487973

Citation	Jin, H and Pancholi, V (2006) Identification and biochemical characterization of a eukaryotic-type serine/threonine kinase and its cognate phosphatase in Streptococcus pyogenes: their biological functions and substrate identification. J. Mol. Biol. 357:1351-72
Abstract	A eukaryotic-type signaling system in group A Streptococcus (GAS) was identified and characterized. This system comprises primarily the products of two co-transcribed genes, a eukaryotic-type Ser/Thr kinase (SP-STK) and phosphatase (SP-STP) and their endogenous substrate histone-like protein (SP-HLP). Enzyme activities of SP-STK and SP-STP primarily depended on Mn(2+). The site on the substrate for reversible phosphorylation by these enzymes was found to be only the threonine residue. Using specific antibodies generated against these proteins, SP-STK was found to be membrane-associated with its N-terminal kinase domain facing the cytoplasm and its C-terminal repeat domain outside the membrane and cell-wall associated. Further, SP-STP, primarily a cytoplasmic protein, was found to be a major secretory protein of GAS and essential for bacterial survival. Three isogenic mutants, lacking either the entire SP-STK, or one of its two domains, were found displaying distinct pleiotropic effects on growth, colony morphology, cell division/septation, surface protein/virulence factor expression, bacterial ability to adhere to and invade human pharyngeal cells, and resist phagocytosis by human neutrophils. In addition to these properties, the ability of these three proteins to modulate the expression of the major virulence factors, the M protein and the capsule, indicates that these proteins are structurally and functionally distinct from the kinases and phosphatases described in other microorganisms and play a key role in GAS pathogenesis.
Links	PubMed Online version:10.1016/j.jmb.2006.01.020
Keywords	Amino Acid Sequence; Bacterial Adhesion; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Line; Cell Shape; Humans; Molecular Sequence Data; Phagocytosis; Pharynx/cytology; Pharynx/microbiology; Phosphoprotein Phosphatases/chemistry; Phosphoprotein Phosphatases/genetics; Phosphoprotein Phosphatases/metabolism; Phosphoprotein Phosphatases/ultrastructure; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases/chemistry; Protein-Serine-Threonine Kinases/genetics; Protein-Serine-Threonine Kinases/metabolism; Protein-Serine-Threonine Kinases/ultrastructure; Sequence Alignment; Signal Transduction/physiology; Streptococcus pyogenes/cytology; Streptococcus pyogenes/enzymology; Streptococcus pyogenes/genetics; Substrate Specificity; Transcription, Genetic
edit table

Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
STRPY:A0A2W5AMW9		GO:0062085: positive regulation of capsule polysaccharide biosynthetic process	ECO:0000315:		P		Figure 8c STK (Stk1 family PASTA domain-containing Ser/Thr kinase) Streptococcus pyogenes “the expression of intracellular and extracellular domains of SP-STK play a crucial role in the expression of certain surface proteins including...hyaluronic acid capsular polysaccharide”	complete CACAO 13386
STRP1:Q99YM9		GO:0004721: phosphoprotein phosphatase activity	ECO:0000314:		F		Figure 2a and 2b STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “SP-STP was also found to dephosphorylate 32P-labeled SP-STK, SP-STKK, and myelin basic protein (MBP) (Figure 2(a) and (b)).”	complete CACAO 13381

References

See Help:References for how to manage references in GONUTS.