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Protein

Protein phosphatase PhpP

Gene

phpP

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Cofactori

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit. Other divalent cations, such as Mg(2+) or Ca2+, cannot serve as cofactors.1 Publication

Enzyme regulationi

Phosphatase activity is inhibited by NaF but not by okadaic acid.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Manganese 1By similarity
Metal bindingi36 – 361Manganese 2By similarity
Metal bindingi37 – 371Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi192 – 1921Manganese 2By similarity
Metal bindingi231 – 2311Manganese 2By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase PhpP (EC:3.1.3.16)
Alternative name(s):
PP2C-type phosphatase
Ser/Thr phosphoprotein phosphatase
Short name:
STPP
Gene namesi
Name:phpP
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi192 – 1921D → A: Loss of phosphatase activity. 1 Publication
Mutagenesisi231 – 2311D → A: Loss of phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Protein phosphatase PhpPPRO_0000418147Add
BLAST

Expressioni

Inductioni

The phpP and stkP genes form an operon.

Interactioni

Subunit structurei

Interacts with the kinase domain of StkP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
stkPQ8KY502EBI-6405646,EBI-6405629

Protein-protein interaction databases

IntActiQ8KY51. 1 interaction.
STRINGi170187.SpneT_02001124.

Structurei

3D structure databases

ProteinModelPortaliQ8KY51.
SMRiQ8KY51. Positions 1-238.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 240239PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8KY51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEISLLTDVG QKRTNNQDYV NHYVNRAGRT MIILADGMGG HRAGNIASEM
60 70 80 90 100
AVTDLGVAWV DTQIDTVNEV REWFAHYLEI ENQKIHQLGQ DEAYRGMGTT
110 120 130 140 150
LEVLAIIDNQ AIYAHIGDSR IGLIRGEEYH QLTSDHSLVN ELLKAGQLTP
160 170 180 190 200
EEAEAHPQKN IITQSIGQKD EIQPDFGTVI LESGDYLLLD SDGLTNMISG
210 220 230 240
SEIRDIVTSD IPLADKTETL VRFANNAGGL DNITVALVSM NEEDAE
Length:246
Mass (Da):27,104
Last modified:October 1, 2002 - v1
Checksum:iCDD968CCE6E86E94
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285441 Genomic DNA. Translation: AAM47529.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285441 Genomic DNA. Translation: AAM47529.1.

3D structure databases

ProteinModelPortaliQ8KY51.
SMRiQ8KY51. Positions 1-238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8KY51. 1 interaction.
STRINGi170187.SpneT_02001124.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPHPP_STRPN
AccessioniPrimary (citable) accession number: Q8KY51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: October 1, 2002
Last modified: July 22, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.