Q8KY51 (PHPP_STRPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase PhpP
EC=3.1.3.16

Alternative name(s):
PP2C-type phosphatase
Ser/Thr phosphoprotein phosphatase
Short name=STPP

Gene names

Name:

phpP

Organism

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

Taxonomic identifier

170187 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pneumoniae

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase able to dephosphorylate StkP-P and a phosphothreonine residue in a phosphopeptide synthetic substrate. PhpP and its cognate protein kinase StkP appear to constitute a functional signaling couple in vivo, PhpP's primary role being probably to control phosphorylation levels of StkP and of its targets. PhpP thus performs an essential control of StkP activity. Ref.2 Ref.3
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. Ref.2
Cofactor	Binds 2 manganese ions per subunit. Other divalent cations, such as Mg2+ or Ca2+, can not serve as cofactors. Ref.2
Enzyme regulation	Phosphatase activity is inhibited by NaF but not by okadaic acid. Ref.2
Subunit structure	Interacts with the kinase domain of StkP. Ref.3
Subcellular location	Cytoplasm. Note: Mainly localizes to the midcell division sites. PhpP and StkP interact within a membrane-associated protein complex facing the cytoplasm. Ref.3 Ref.4
Induction	The phpP and stkP genes form an operon. Ref.2
Disruption phenotype	Attempts to construct an in-frame deletion of the phpP gene were unsuccessful and an allele encoding inactive D231A PhpP phosphatase is lethal in a wild-type genetic background. This suggests that PhpP is essential. Ref.3
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SP_0376	Q97SI5	2	EBI-6405646,EBI-6507368
stkP	Q8KY50	2	EBI-6405646,EBI-6405629

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 246	246	Protein phosphatase PhpP		PRO_0000418147
Sites
	Metal binding	36	1	Manganese 1 By similarity
	Metal binding	36	1	Manganese 2 By similarity
	Metal binding	37	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	192	1	Manganese 2 By similarity
	Metal binding	231	1	Manganese 2 By similarity
Experimental info
	Mutagenesis	192	1	D → A: Loss of phosphatase activity. Ref.2
	Mutagenesis	231	1	D → A: Loss of phosphatase activity. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8KY51 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: CDD968CCE6E86E94	FASTA	246	27,104
	10 20 30 40 50 60 MEISLLTDVG QKRTNNQDYV NHYVNRAGRT MIILADGMGG HRAGNIASEM AVTDLGVAWV 70 80 90 100 110 120 DTQIDTVNEV REWFAHYLEI ENQKIHQLGQ DEAYRGMGTT LEVLAIIDNQ AIYAHIGDSR 130 140 150 160 170 180 IGLIRGEEYH QLTSDHSLVN ELLKAGQLTP EEAEAHPQKN IITQSIGQKD EIQPDFGTVI 190 200 210 220 230 240 LESGDYLLLD SDGLTNMISG SEIRDIVTSD IPLADKTETL VRFANNAGGL DNITVALVSM NEEDAE

References

[1]	"A serine/threonine kinase involved in competence regulation." Echenique J.R., Trombe M.C. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Rx / Cp1015.
[2]	"Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates." Novakova L., Saskova L., Pallova P., Janecek J., Novotna J., Ulrych A., Echenique J., Trombe M.C., Branny P. FEBS J. 272:1243-1254(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, OPERON STRUCTURE, MUTAGENESIS OF ASP-192 AND ASP-231. Strain: Rx / Cp1015.
[3]	"The StkP/PhpP signaling couple in Streptococcus pneumoniae: cellular organization and physiological characterization." Osaki M., Arcondeguy T., Bastide A., Touriol C., Prats H., Trombe M.C. J. Bacteriol. 191:4943-4950(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH STKP, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. Strain: Rx / Cp1015.
[4]	"Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP." Beilharz K., Novakova L., Fadda D., Branny P., Massidda O., Veening J.W. Proc. Natl. Acad. Sci. U.S.A. 109:E905-E913(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: Rx1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF285441 Genomic DNA. Translation: AAM47529.1.
3D structure databases
ProteinModelPortal	Q8KY51.
SMR	Q8KY51. Positions 1-238.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8KY51. 2 interactions.
Protein family/group databases
PptaseDB	P3D0706178.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.60.40.10. 1 hit.
InterPro	IPR001932. PP2C-like. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PHPP_STRPN

Accession

Primary (citable) accession number: Q8KY51

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2012
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program