P0A6U5 (RSMG_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 65.
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 G EC=2.1.1.170 Alternative name(s): 16S rRNA 7-methylguanosine methyltransferase Short name=16S rRNA m7G methyltransferase Glucose-inhibited division protein B | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 207 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Specifically methylates the N7 position of guanosine in position 527 of 16S rRNA. Ref.6 |
| Catalytic activity | S-adenosyl-L-methionine + guanosine(527) in 16S rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanosine(527) in 16S rRNA. HAMAP MF_00074 |
| Subcellular location | Cytoplasm Potential HAMAP MF_00074. |
| Disruption phenotype | Low-level streptomycin resistance. Ref.6 |
| Sequence similarities | Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family. |
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) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | rRNA (guanine-N7-)-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 – 207 | 207 | Ribosomal RNA small subunit methyltransferase G HAMAP MF_00074 | PRO_0000184249 | |||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 2 – 10 | 9 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 11 – 13 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 18 – 34 | 17 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 49 – 60 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 61 – 63 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 66 – 72 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 75 – 79 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 80 – 86 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 90 – 97 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 99 – 111 | 13 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 115 – 121 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 124 – 126 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 133 – 137 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 141 – 143 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 144 – 151 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 154 – 167 | 14 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 170 – 174 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 180 – 189 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 196 – 204 | 9 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS." Walker J.E., Gay N.J., Saraste M., Eberle A.N. Biochem. J. 224:799-815(1984) [PubMed: 6395859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed: 7686882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "The promoters of the atp operon of Escherichia coli K12." Nielsen J., Joergensen B.B., von Meyenburg K., Hansen F.G. Mol. Gen. Genet. 193:64-71(1984) [PubMed: 6318052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-207. Strain: K12. |
| [6] | "Loss of a conserved 7-methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria." Okamoto S., Tamaru A., Nakajima C., Nishimura K., Tanaka Y., Tokuyama S., Suzuki Y., Ochi K. Mol. Microbiol. 63:1096-1106(2007) [PubMed: 17238915] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. Strain: K12. |
| [7] | "Crystal structure of the Escherichia coli glucose-inhibited division protein B (GidB) reveals a methyltransferase fold." Romanowski M.J., Bonanno J.B., Burley S.K. Proteins 47:563-567(2002) [PubMed: 12001236] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X01631 Genomic DNA. Translation: CAA25774.1. L10328 Genomic DNA. Translation: AAA62092.1. U00096 Genomic DNA. Translation: AAC76763.1. AP009048 Genomic DNA. Translation: BAE77548.1. X01383 Genomic DNA. Translation: CAA25639.1. | ||||||||||||
| PIR | BVECQB. C30389. | ||||||||||||
| RefSeq | NP_418196.1. NC_000913.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P0A6U5. | ||||||||||||
| SMR | P0A6U5. Positions 1-207. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-47992N. | ||||||||||||
| IntAct | P0A6U5. 9 interactions. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBESCT00000000419; EBESCP00000000419; EBESCG00000000346. EBESCT00000017232; EBESCP00000016523; EBESCG00000016291. | ||||||||||||
| GeneID | 948250. | ||||||||||||
| GenomeReviews | Gene locus JW3718 in contig AP009048_GR. Gene locus b3740 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW3718. eco:b3740. | ||||||||||||
| PATRIC | 32122979. VBIEscCol129921_3865. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB0371. | ||||||||||||
| EcoGene | EG10376. rsmG. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0357. | ||||||||||||
| GeneTree | EBGT00050000011126. | ||||||||||||
| HOGENOM | HBG686577. | ||||||||||||
| OMA | DSHFTLL. | ||||||||||||
| PhylomeDB | P0A6U5. | ||||||||||||
| ProtClustDB | PRK00107. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:EG10376-MONOMER. MetaCyc:EG10376-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P0A6U5. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00074. 16SrRNA_methyltr_G. [Tree] | ||||||||||||
| InterPro | IPR003682. rRNA_ssu_MeTfrase_G. [Graphical view] | ||||||||||||
| KO | K03501. | ||||||||||||
| Pfam | PF02527. GidB. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF003078. GidB. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00138. GidB. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | RSMG_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A6U5 Secondary accession number(s): P17113, Q2M858 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| 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 |

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