Reviewed,
UniProtKB/Swiss-Prot P0A841 (SURE_ECOL6)
Last modified
June 16, 2009.
Version 27.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Multifunctional protein surE Including the following 2 domains: 1- Recommended name: 5'/3'-nucleotidase EC=3.1.3.5 EC=3.1.3.6 Alternative name(s): Nucleoside monophosphate phosphohydrolase 2- Recommended name: Exopolyphosphatase EC=3.6.1.11 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 253 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs By similarity. |
| Catalytic activity | A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP MF_00060 A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP MF_00060 (Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate. HAMAP MF_00060 |
| Cofactor | Binds 1 divalent metal cation per subunit By similarity. |
| Subcellular location | Cytoplasm Potential. |
| Sequence similarities | Belongs to the surE nucleotidase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3'-nucleotidase activity Inferred from electronic annotation. Source: EC 5'-nucleotidase activityInferred from electronic annotation. Source: HAMAP exopolyphosphatase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: HAMAP nucleotide bindingInferred 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 – 253 | 253 | Multifunctional protein surE HAMAP MF_00060 | PRO_0000111811 | |||||
Sites | |||||||||
| Metal binding | 8 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 9 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 39 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 92 | 1 | Divalent metal cation By similarity | ||||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| AE014075 Genomic DNA. Translation: AAN81760.1. Different initiation. | |
| RefSeq | NP_755190.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1J9L based on UniProtKB P96112. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1039131. |
| GenomeReviews | Gene locus c3311 in contig AE014075_GR. |
| KEGG | ecc:c3311. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A841. |
| OMA | P0A841. SINIPIK. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.5. 292881. 3.1.3.6. 292881. 3.6.1.11. 292881. |
Family and domain databases | |
| HAMAP | MF_00060. [Tree] |
| InterPro | IPR002828. SurE-like_Pase/nucleotidase. [Graphical view] |
| Gene3D | G3DSA:3.40.1210.10. SurE-like_Pase/nucleotidase. 1 hit. |
| Pfam | PF01975. SurE. 1 hit. [Graphical view] |
| ProDom | PD005378. SurE. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00087. surE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | SURE_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P0A841 Secondary accession number(s): P36664 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


