Q8DNR9 (PHPP_STRR6) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 60.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
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| Organism | Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 171101 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › ![]() |
Protein attributes
| Sequence length | 246 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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. |
| Catalytic activity | A phosphoprotein + H2O = a protein + phosphate. |
| Cofactor | Binds 2 manganese ions per subunit By similarity. |
| Subcellular location | Cytoplasm. Note: Mainly localizes to the midcell division sites. Delocalizes from the septum in the presence of antibiotics that target the latest stages of cell-wall biosynthesis and in cells that have stopped dividing. Ref.2 |
| Miscellaneous | Overexpression of PhpP leads to a phenotype comparable to cells lacking stkP, with an increased cell length. |
| Sequence similarities | Belongs to the PP2C family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Manganese Metal-binding |
| Molecular function | Hydrolase Protein phosphatase |
| Technical term | Complete proteome Reference proteome |
| 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 activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 246 | 246 | Protein phosphatase PhpP | PRO_0000418148 | |||||
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 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genome of the bacterium Streptococcus pneumoniae strain R6." Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N. Glass J.I.J. Bacteriol. 183:5709-5717(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-255 / R6. |
| [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: SUBCELLULAR LOCATION, OVEREXPRESSION. Strain: ATCC BAA-255 / R6. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE007317 Genomic DNA. Translation: AAL00381.1. |
| PIR | H95201. H98068. |
| RefSeq | NP_359170.1. NC_003098.1. |
3D structure databases | |
| ProteinModelPortal | Q8DNR9. |
| SMR | Q8DNR9. Positions 1-238. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 171101.spr1578. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAL00381; AAL00381; spr1578. |
| GeneID | 933328. |
| KEGG | spr:spr1578. |
| PATRIC | 19703179. VBIStrPne107296_1705. |
Phylogenomic databases | |
| eggNOG | COG0631. |
| HOGENOM | HOG000235782. |
| KO | K01090. |
| OMA | VSHLGHN. |
| ProtClustDB | CLSK877236. |
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_STRR6 | ||||||||
| Accession | Primary (citable) accession number: Q8DNR9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
