Q5PEA9 (SPTP_SALPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 59.
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: Secreted effector protein SptP Including the following 2 domains:
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| Gene names |
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| Organism | Salmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 295319 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › ![]() |
Protein attributes
| Sequence length | 543 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein includes tyrosine phosphatase and GTPase activating protein (GAP) activities. After bacterial internalization, GAP mediates the reversal of the cytoskeletal changes induced by SopE. This function is independent of its tyrosine phosphatase activity, which remains unclear By similarity. |
| Catalytic activity | Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. |
| Subunit structure | Forms a complex with SicP By similarity. |
| Subcellular location | Secreted By similarity. Host cytoplasm By similarity. Note: Secreted via type III secretion system 1 (SPI-1 TTSS), and delivered into the host cytoplasm By similarity. |
| Miscellaneous | Requires SicP as a chaperone for its stability and secretion By similarity. |
| Sequence similarities | In the N-terminal section; belongs to the YopE family. Contains 1 tyrosine-protein phosphatase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Virulence |
| Cellular component | Host cytoplasm Secreted |
| Molecular function | GTPase activation Hydrolase Protein phosphatase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine dephosphorylationInferred from electronic annotation. Source: GOC positive regulation of GTPase activityInferred from electronic annotation. Source: GOC |
| Cellular_component | extracellular space Inferred from electronic annotation. Source: InterPro host cell cytoplasmInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine phosphatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 543 | 543 | Secreted effector protein SptP | PRO_0000094864 | |||||
Regions | |||||||||
| Domain | 280 – 543 | 264 | Tyrosine-protein phosphatase | ||||||
| Region | 35 – 139 | 105 | Chaperone-binding By similarity | ||||||
| Region | 167 – 290 | 124 | GAP By similarity | ||||||
Sites | |||||||||
| Active site | 481 | 1 | Phosphocysteine intermediate By similarity | ||||||
Sequences
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References
| [1] | "Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. Wilson R.K.Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000026 Genomic DNA. Translation: AAV78593.1. |
| RefSeq | YP_151905.1. NC_006511.1. |
3D structure databases | |
| ProteinModelPortal | Q5PEA9. |
| SMR | Q5PEA9. Positions 36-139, 167-539. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 295319.SPA2736. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAV78593; AAV78593; SPA2736. |
| GeneID | 3177037. |
| KEGG | spt:SPA2736. |
| PATRIC | 32355024. VBISalEnt134188_2910. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | NOG74835. |
| HOGENOM | HOG000028733. |
| KO | K13740. |
| OMA | WIDKAST. |
| ProtClustDB | PRK15375. |
Enzyme and pathway databases | |
| BioCyc | SENT295319:GJBZ-2734-MONOMER. |
Family and domain databases | |
| Gene3D | 1.20.120.260. 1 hit. |
| InterPro | IPR011070. Globular_prot_asu/bsu. IPR015203. SicP-binding. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. IPR003546. Tyr_Pase_SptP/YopH. IPR014773. Uncharacterised_dom_YopE. [Graphical view] |
| Pfam | PF09119. SicP-binding. 1 hit. PF00102. Y_phosphatase. 1 hit. PF03545. YopE. 1 hit. [Graphical view] |
| PRINTS | PR01371. BACYPHPHTASE. |
| SMART | SM00194. PTPc. 1 hit. [Graphical view] |
| SUPFAM | SSF56568. AlphaBeta_subunt. 1 hit. SSF47233. Vir_YopE. 1 hit. |
| PROSITE | PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SPTP_SALPA | ||||||||
| Accession | Primary (citable) accession number: Q5PEA9 | ||||||||
| 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
