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Q8KY51 (PHPP_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifier170187 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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 componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Protein phosphatase PhpP
PRO_0000418147

Sites

Metal binding361Manganese 1 By similarity
Metal binding361Manganese 2 By similarity
Metal binding371Manganese 1; via carbonyl oxygen By similarity
Metal binding1921Manganese 2 By similarity
Metal binding2311Manganese 2 By similarity

Experimental info

Mutagenesis1921D → A: Loss of phosphatase activity. Ref.2
Mutagenesis2311D → A: Loss of phosphatase activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8KY51 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: CDD968CCE6E86E94

FASTA24627,104
        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 

« Hide

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

ProteinModelPortalQ8KY51.
SMRQ8KY51. Positions 1-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8KY51. 2 interactions.

Protein family/group databases

PptaseDBP3D0706178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
ProtoNetSearch...

Entry information

Entry namePHPP_STRPN
AccessionPrimary (citable) accession number: Q8KY51
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families