STRP1:Q99YM9

Species (Taxon ID)	Streptococcus pyogenes serotype M1. (301447)
Gene Name(s)	pppL (ECO:0000313 with EMBL:AAK34397.1)
Protein Name(s)	Putative phosphoprotein phosphatase (ECO:0000313 with EMBL:AAK34397.1)
External Links
UniProt	Q99YM9
EMBL	AE004092
RefSeq	NP_269676.1
ProteinModelPortal	Q99YM9
SMR	Q99YM9
STRING	160490.SPy_1626
PaxDb	Q99YM9
PRIDE	Q99YM9
EnsemblBacteria	AAK34397
GeneID	901879
KEGG	spy:SPy_1626
PATRIC	fig|160490.10.peg.1418
eggNOG	ENOG4108ZF3 COG0631
HOGENOM	HOG000235782
KO	K20074
OMA	EDHTWVA
SABIO-RK	Q99YM9
Proteomes	UP000000750
GO	GO:0004722
CDD	cd00143
Gene3D	3.60.40.10
InterPro	IPR015655 IPR036457 IPR001932
PANTHER	PTHR13832
SMART	SM00331 SM00332
SUPFAM	SSF81606
PROSITE	PS51746

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0035970	peptidyl-threonine dephosphorylation	PMID:21917918	ECO:0000314			P		Figure 3C STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “The SP-STP was able to dephosphorylate the SP-STK-phosphorylated SP-WalR (Fig. 3C), demonstrating that this couple functions as a cognate kinase-phosphatase pair.”	complete CACAO 13336
	GO:0045893	positive regulation of transcription, DNA-templated	PMID:21917918	ECO:0000315			P		Figure 3A and Figure 3B STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “In support of this, we also observed a simultaneous up-regulation of walR (2.7–3.2-fold) transcript at an early time point in both of the strains (Fig. 3, table below A and B).”	complete CACAO 13337
	GO:0019836	hemolysis by symbiont of host erythrocytes	PMID:21917918	ECO:0000315			P		Figure 4B STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “hemolysin production in the wild-type M1SF370 and M1T1 and their corresponding mutant and complemented strains. Complete lysis of shRBCs achieved upon the addition of 1% Triton X-100 was taken as control (100%).”	complete CACAO 13351
	GO:1905228	positive regulation of adhesion of symbiont to host epithelial cell	PMID:21917918	ECO:0000315			P		Figure 5A STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “The ability of the mutants and stp-complemented strains to adhere to...Detroit 562 human pharyngeal cells in comparison with that of the wild-type strains was determined by calculating adherence (percentage of initial inoculum)”	complete CACAO 13353
	GO:0000918	division septum site selection	PMID:21917918	ECO:0000315			P		Figure 2C and Figure 2D STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “Similar defects observed by transmission electron microscopy (Fig. 2, C and D) in conjunction with relatively thicker cell walls indicated that SP-STP plays a role in the regulation of septa formation and in turn cell division in GAS."	complete CACAO 13357
	GO:0045717	negative regulation of fatty acid biosynthetic process	PMID:21917918	ECO:0000315			P		Table 1 STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “The total lipid content analysis (fatty acid methyl ester) of the wild type and its corresponding STP mutant revealed that both saturated fatty acid (SFA) and unsaturated fatty acid (UFA) content in the mutant were 2–3-fold up-regulated”	complete CACAO 13379
	GO:0075294	positive regulation by symbiont of entry into host	PMID:21917918	ECO:0000315			P		Figure 5B STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “The ability of the mutants and stp-complemented strains to adhere to...Detroit 562 human pharyngeal cells in comparison with that of the wild-type strains was determined by calculating...invasion (percentage of adherence) (B)”	complete CACAO 13380
	GO:0004721	phosphoprotein phosphatase activity	PMID:16487973	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
	GO:0062085	positive regulation of capsule polysaccharide biosynthetic process	PMID:21917918	ECO:0000315			P		Figure 4a STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “the comparison of capsule content based on the biochemical estimation of the hyaluronic acid for the STP mutants and complemented GAS strains with respect to their corresponding wild-type strains.”	complete CACAO 13384
	GO:0052151	positive regulation by symbiont of host apoptotic process	PMID:22262847	ECO:0000315			P		Figure 2A STP (Putative phosphoprotein phosphatase) Streptococcus pyogenes “The results from the MTT assays revealed 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)... confirm[ing] that SP-STP plays a significant role in GAS-mediated apoptosis (Fig. 2A).”	complete CACAO 13401
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001932	F		Seeded From UniProt	complete
enables	GO:0004722	protein serine/threonine phosphatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015655	F		Seeded From UniProt	complete
involved_in	GO:0006470	protein dephosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015655	P		Seeded From UniProt	complete
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References

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