P0AGL7 (RSME_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 61.
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: Ribosomal RNA small subunit methyltransferase E EC=2.1.1.193 Alternative name(s): 16S rRNA m3U1498 methyltransferase | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 243 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. Ref.6 Ref.7 |
| Catalytic activity | S-adenosyl-L-methionine + uracil(1498) in 16S rRNA = S-adenosyl-L-homocysteine + N(3)-methyluracil(1498) in 16S rRNA. Ref.6 |
| Subunit structure | Homodimer. Ref.7 |
| Subcellular location | Cytoplasm Probable. |
| Sequence similarities | Belongs to the RNA methyltransferase RsmE family. |
| Biophysicochemical properties | Kinetic parameters: KM=2.0 µM for 16S rRNA within 30S ribosomal subunits Ref.7 KM=26.7 µM for S-adenosyl-L-methionine pH dependence: Optimum pH is 7-9. |
| Sequence caution | The sequence AAA69113.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Biological process | rRNA processing |
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | rRNA base methylation Inferred from mutant phenotype Ref.6. Source: EcoCyc |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | rRNA (uridine-N3-)-methyltransferase activity Inferred from direct assay Ref.6. Source: EcoCyc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 243 | 243 | Ribosomal RNA small subunit methyltransferase E | PRO_0000176199 | |||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 5 – 7 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 17 – 19 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 22 – 29 | 8 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 39 – 43 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 45 – 57 | 13 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 62 – 71 | 10 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 77 – 85 | 9 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 88 – 90 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 91 – 101 | 11 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 106 – 111 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 121 – 142 | 22 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 156 – 161 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 165 – 171 | 7 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 176 – 178 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 179 – 181 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 188 – 193 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 201 – 209 | 9 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 213 – 216 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 224 – 238 | 15 | |||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [2] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "Location of the endA gene coding for endonuclease I on the physical map of the Escherichia coli K-12 chromosome." Jekel M., Wackernagel W. J. Bacteriol. 176:1550-1551(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128. Strain: K12. |
| [4] | "Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II." Gushima H., Yasuda S., Soeda E., Yokota M., Kondo M., Kimura A. Nucleic Acids Res. 12:9299-9307(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 127-243. Strain: B. |
| [5] | Rudd K.E., Baum B. Unpublished observations (AUG-1994) Cited for: IDENTIFICATION. |
| [6] | "Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family." Basturea G.N., Rudd K.E., Deutscher M.P. RNA 12:426-434(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS METHYLTRANSFERASE, CATALYTIC ACTIVITY. Strain: K12 / MG1655 / ATCC 47076. |
| [7] | "Substrate specificity and properties of the Escherichia coli 16S rRNA methyltransferase, RsmE." Basturea G.N., Deutscher M.P. RNA 13:1969-1976(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U28377 Genomic DNA. Translation: AAA69113.1. Different initiation. U00096 Genomic DNA. Translation: AAC75983.2. AP009048 Genomic DNA. Translation: BAE77009.1. X65169 Genomic DNA. No translation available. X01666 Genomic DNA. No translation available. | ||||||||||||
| RefSeq | NP_417421.4. NC_000913.2. YP_491145.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P0AGL7. | ||||||||||||
| SMR | P0AGL7. Positions 3-243. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P0AGL7. 5 interactions. | ||||||||||||
| STRING | 511145.b2946. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P0AGL7. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC75983; AAC75983; b2946. BAE77009; BAE77009; BAE77009. | ||||||||||||
| GeneID | 12930413. 945816. | ||||||||||||
| KEGG | ecj:Y75_p2876. eco:b2946. | ||||||||||||
| PATRIC | 32121302. VBIEscCol129921_3039. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB2269. | ||||||||||||
| EcoGene | EG12366. rsmE. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG1385. | ||||||||||||
| HOGENOM | HOG000015265. | ||||||||||||
| KO | K09761. | ||||||||||||
| OMA | MTQHVQG. | ||||||||||||
| ProtClustDB | PRK11713. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:EG12366-MONOMER. ECOL316407:JW2913-MONOMER. MetaCyc:EG12366-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P0AGL7. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR015947. PUA-like_domain. IPR006700. rRNA_ssu_MeTrfase-E. [Graphical view] | ||||||||||||
| Pfam | PF04452. Methyltrans_RNA. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF015601. MTase_slr0722. 1 hit. | ||||||||||||
| SUPFAM | SSF88697. PUA-like. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00046. TIGR00046. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | RSME_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0AGL7 Secondary accession number(s): P37912, P76647, Q2M9P7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Uncharacterized protein families (UPF) List of uncharacterized protein family (UPF) entries |
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
