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Q04J42 (PHPP_STRP2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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·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
Ordered Locus Names:SPD_1543
OrganismStreptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) [Complete proteome] [HAMAP]
Taxonomic identifier373153 [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 other phosphorylated protein substrates. 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 By similarity. Also dephosphorylates DivIVA in vivo. Ref.2

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.2

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subcellular location

Cytoplasm. Note: Mainly localizes to the midcell division sites in a StkP-dependent manner, since PhpP is present at midcell only when StkP is active. Ref.2

Sequence similarities

Belongs to the PP2C family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Protein phosphatase PhpP
PRO_0000418149

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

Sequences

Sequence LengthMass (Da)Tools
Q04J42 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: C7D368C6ECE86E94

FASTA24627,103
        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 
LESGDYLLLN SDGLTNMISG SEIRDIVTSD IPLADKTETL VRFANNAGGL DNITVALVSM 


NEEDAE 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6."
Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.
J. Bacteriol. 189:38-51(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D39 / NCTC 7466.
[2]"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: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Strain: D39 / NCTC 7466.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000410 Genomic DNA. Translation: ABJ54228.1.
RefSeqYP_816996.1. NC_008533.1.

3D structure databases

ProteinModelPortalQ04J42.
SMRQ04J42. Positions 1-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING373153.SPD_1543.

Protein family/group databases

PptaseDBP3D1211217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ54228; ABJ54228; SPD_1543.
GeneID4441334.
KEGGspd:SPD_1543.
PATRIC19684355. VBIStrPne27904_1711.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000235782.
KOK01090.
OMAFFIVADG.
OrthoDBEOG65N17S.
ProtClustDBCLSK877236.

Enzyme and pathway databases

BioCycSPNE373153:GIX6-1543-MONOMER.

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_STRP2
AccessionPrimary (citable) accession number: Q04J42
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: November 14, 2006
Last modified: April 16, 2014
This is version 50 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