Reviewed,
UniProtKB/Swiss-Prot Q5XAQ1 (BPPI_STRP6)
Last modified
November 3, 2009.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase Including the following 2 domains: 1- Recommended name: Phosphatase EC=3.1.3.- 2- Recommended name: Peptidyl-prolyl cis-trans isomerase Short name=PPIase Short name=Rotamase EC=5.2.1.8 | ||
| Gene names |
| ||
| Organism | Streptococcus pyogenes serotype M6 [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 301450 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 470 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. UniProtKB Q9H2H8 |
| Catalytic activity | Peptidylproline (omega=180) = peptidylproline (omega=0). UniProtKB Q9H2H8 |
| Cofactor | Magnesium By similarity. UniProtKB P0A8Y5 |
| Sequence similarities | In the N-terminal section; belongs to the HAD-like hydrolase superfamily. Cof family. In the C-terminal section; belongs to the cyclophilin-type PPIase family. PPIL1 subfamily. Contains 1 PPIase cyclophilin-type domain. |
| Mass spectrometry | Molecular mass is 52146.29 Da from positions 1 - 470. Determined by ESI. Ref.2 |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase Isomerase Rotamase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | protein folding Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase 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 – 470 | 470 | Putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase | PRO_0000308515 | |||||
Regions | |||||||||
| Domain | 286 – 468 | 183 | PPIase cyclophilin-type | ||||||
Sites | |||||||||
| Active site | 22 | 1 | Nucleophile By similarity UniProtKB P0A8Y5 | ||||||
| Metal binding | 22 | 1 | Magnesium By similarity UniProtKB P0A8Y5 | ||||||
| Metal binding | 24 | 1 | Magnesium By similarity UniProtKB P0A8Y5 | ||||||
| Metal binding | 221 | 1 | Magnesium By similarity UniProtKB P0A8Y5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain." Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M. J. Infect. Dis. 190:727-738(2004) [PubMed: 15272401] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-946 / MGAS10394 / Serotype M6. |
| [2] | "Two-dimensional gel electrophoresis map of Streptococcus pyogenes proteins." Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., VanBogelen R.A. Submitted (MAY-2000) to UniProtKB Cited for: PROTEIN SEQUENCE OF 294-331; 371-394 AND 428-458, MASS SPECTROMETRY. Strain: JRS4 / Serotype M6. |
Cross-references
Sequence databases | |
|---|---|
| CP000003 Genomic DNA. Translation: AAT87512.1. | |
| RefSeq | YP_060695.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2942090. |
| GenomeReviews | Gene locus M6_Spy1377 in contig CP000003_GR. |
| KEGG | spa:M6_Spy1377. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q5XAQ1. |
| OMA | VLFPDHA. |
Enzyme and pathway databases | |
| BioCyc | SPYO286636:M6_SPY1377-MON. |
| BRENDA | 5.2.1.8. 314561. |
Family and domain databases | |
| InterPro | IPR013200. HAD-SF_hydro-like_3. IPR006379. HAD-SF_hydro_IIB. IPR000150. Hypothet_cof. IPR002130. PPIase_cyclophilin. [Graphical view] |
| Gene3D | G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit. |
| Pfam | PF08282. Hydrolase_3. 1 hit. PF00160. Pro_isomerase. 1 hit. [Graphical view] |
| PRINTS | PR00153. CSAPPISMRASE. |
| TIGRFAMs | TIGR00099. Cof-subfamily. 1 hit. TIGR01484. HAD-SF-IIB. 1 hit. |
| PROSITE | PS01228. COF_1. False negative. PS01229. COF_2. False negative. PS00170. CSA_PPIASE_1. False negative. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BPPI_STRP6 | ||||||||
| Accession | Primary (citable) accession number: Q5XAQ1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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