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Q8KY51

- PHPP_STRPN

UniProt

Q8KY51 - PHPP_STRPN

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Protein

Protein phosphatase PhpP

Gene
phpP
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - 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

Binds 2 manganese ions per subunit. Other divalent cations, such as Mg2+ or Ca2+, can not 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 1 By similarity
Metal bindingi36 – 361Manganese 2 By similarity
Metal bindingi37 – 371Manganese 1; via carbonyl oxygen By similarity
Metal bindingi192 – 1921Manganese 2 By similarity
Metal bindingi231 – 2311Manganese 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB-KW
  3. protein binding Source: IntAct
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

PptaseDBiP3D0706178.

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

Cytoplasm
Note: Mainly localizes to the midcell division sites. PhpP and StkP interact within a membrane-associated protein complex facing the cytoplasm.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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.1 Publication

Interactioni

Subunit structurei

Interacts with the kinase domain of StkP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SP_0376Q97SI52EBI-6405646,EBI-6507368
stkPQ8KY502EBI-6405646,EBI-6405629

Protein-protein interaction databases

IntActiQ8KY51. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8KY51.
SMRiQ8KY51. Positions 1-238.

Family & Domainsi

Sequence similaritiesi

Belongs to the PP2C family.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8KY51-1 [UniParc]FASTAAdd to Basket

« Hide

MEISLLTDVG QKRTNNQDYV NHYVNRAGRT MIILADGMGG HRAGNIASEM    50
AVTDLGVAWV DTQIDTVNEV REWFAHYLEI ENQKIHQLGQ DEAYRGMGTT 100
LEVLAIIDNQ AIYAHIGDSR IGLIRGEEYH QLTSDHSLVN ELLKAGQLTP 150
EEAEAHPQKN IITQSIGQKD EIQPDFGTVI LESGDYLLLD SDGLTNMISG 200
SEIRDIVTSD IPLADKTETL VRFANNAGGL DNITVALVSM NEEDAE 246
Length:246
Mass (Da):27,104
Last modified:October 1, 2002 - v1
Checksum:iCDD968CCE6E86E94
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF285441 Genomic DNA. Translation: AAM47529.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF285441 Genomic DNA. Translation: AAM47529.1 .

3D structure databases

ProteinModelPortali Q8KY51.
SMRi Q8KY51. Positions 1-238.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8KY51. 2 interactions.

Protein family/group databases

PptaseDBi P3D0706178.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.60.40.10. 1 hit.
InterProi IPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81606. SSF81606. 1 hit.
ProtoNeti Search...

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: June 11, 2014
This is version 41 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

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