GO_REF:0000104

Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:16487973

Identification and biochemical characterization of a eukaryotic-type serine/threonine kinase and its cognate phosphatase in Streptococcus pyogenes: their biological functions and substrate identification.

Purified SP-STK and SP-STP are Mn2+-dependent enzymes, and the reversibly modified residue on their endogenous histone-like substrate SP-HLP is threonine.

"Enzyme activities of SP-STK and SP-STP primarily depended on Mn(2+)."
SP-STP is primarily cytoplasmic but is also a major secreted protein of GAS; the accompanying claim that it is essential for survival was later corrected by non-polar stp mutants.

"SP-STP, primarily a cytoplasmic protein, was found to be a major secretory protein of GAS and essential for bacterial survival."
The isogenic mutants constructed in this study lacked SP-STK or one of its domains, so phenotypes reported for them are kinase-mutant phenotypes.

"Three isogenic mutants, lacking either the entire SP-STK, or one of its two domains"

PMID:21917918

Role of serine/threonine phosphatase (SP-STP) in Streptococcus pyogenes physiology and virulence.

SP-STP dephosphorylates SP-STK-phosphorylated WalR and CovR in vitro, and the kinase modifies both regulators specifically on threonine.

"The SP-STP was able to dephosphorylate the SP-STK-phosphorylated SP-WalR"
Non-polar stp mutants in two M1 backgrounds form long chains with multiple asymmetric and parallel septa and thickened walls, reverted by complementation.

"revealed unusual staining patterns with multiple asymmetric and parallel septa formation"
Capsule production falls 3-4-fold in both stp mutants, with 14-100-fold lower has transcript, placing SP-STP as a positive regulator of capsule synthesis via CovR.

"In both of the STP mutants, we observed a 3–4-fold decrease in the capsule production"
Total saturated and unsaturated fatty acid content rises 2-3-fold in the stp mutant, alongside down-regulation of the fabT repressor homolog.

"both saturated fatty acid (SFA) and unsaturated fatty acid (UFA) content in the mutant were 2–3-fold up-regulated"
Adherence to pharyngeal cells is reduced only in the M1SF370-derived stp mutant, while that mutant is 6-fold more invasive, so loss of stp increases rather than decreases entry into host cells.

"although the M1ΔSTP mutant lost the ability to adhere to pharyngeal cells, the adherent mutant strain was 6-fold more invasive"

PMID:22262847

Serine/threonine phosphatase (SP-STP), secreted from Streptococcus pyogenes, is a pro-apoptotic protein.

Wild-type GAS inhibits pharyngeal cell proliferation by over 90% while stp mutants inhibit 5-18%, with restoration on complementation, establishing SP-STP as the apoptotic determinant.

"significantly lower inhibition of proliferation of pharyngeal cells treated with GAS strains devoid of SP-STP (M1ΔSTP and M1T1ΔSTP, 5 and 18%, respectively) unlike the wild-type GAS strains (>90% inhibition)"
Exogenously added SP-STP enters pharyngeal cells and accumulates in the nucleus of most cells within 12-24 h.

"More than 70% of the total cells displayed the labeled SP-STP within the nucleus"
SP-STP dephosphorylates CDK1-phosphorylated histone H1 in vitro and reduces the H1 Thr146 phospho-epitope in nuclei of treated cells.

"the purified SP-STP was able to dephosphorylate the H1∼P histone"
SP-STP-induced death is caspase-dependent and requires host transcription and translation.

"The programmed cell death induced by SP-STP, which requires active transcription and de novo protein synthesis, is also caspase-dependent"

file:STRP1/pppL/pppL-uniprot.txt

UniProt entry Q99YM9 (Q99YM9_STRP1)

The entry is a PPM-type phosphatase over almost its entire length, with PP2C InterPro, Pfam and PROSITE signatures and EC 3.1.3.16.

"FT DOMAIN 2..240"