P0A8R0 (RRAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 71.
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: Regulator of ribonuclease activity A | ||||||
| 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 | 161 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome. Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 |
| Subunit structure | Homotrimer. Forms a ring-like structure with a central cavity. Binds to both RNA-binding sites in the C-terminal region of Rne and to RhlB. Ref.5 Ref.8 Ref.10 Ref.11 |
| Subcellular location | Cytoplasm Potential HAMAP-Rule MF_00471. |
| Induction | Induced upon entry into stationary phase, in a RpoS-dependent manner. Stability of the rraA transcript is Rne dependent, suggesting the existence of a feedback mechanism in the regulation of RraA level. Ref.7 |
| Miscellaneous | RraA and RraB interact with Rne at separate sites within the Rne and exert distinct effects on the composition of the degradosome, affecting distinct sets of RNA transcripts. HAMAP-Rule MF_00471 |
| Sequence similarities | Belongs to the RraA family. |
| Caution | Although it was initially thought to be a methyltransferase of the menaquinone pathway, Ref.5 showed that it has no SAM-dependent methyltransferase activity and is not involved in the menaquinone pathway. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | RNA catabolic process Inferred from direct assay Ref.5. Source: EcoCyc negative regulation of endoribonuclease activityInferred from direct assay Ref.5. Source: EcoCyc regulation of RNA metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | endoribonuclease inhibitor activity Inferred from electronic annotation. Source: HAMAP ribonuclease inhibitor activityInferred from direct assay Ref.5. Source: EcoCyc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 161 | 161 | Regulator of ribonuclease activity A HAMAP-Rule MF_00471 | PRO_0000209611 | |||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 5 – 12 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 13 – 15 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 16 – 18 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 30 – 40 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 42 – 44 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 46 – 52 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 64 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 69 – 74 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 76 – 84 | 9 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 89 – 96 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 99 – 102 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 105 – 114 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 116 – 118 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 125 – 128 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 131 – 133 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 136 – 138 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 143 – 146 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 151 – 156 | 6 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Hudspeth M.E.S., Suvarna K., Meganathan R. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli." Lee K., Zhan X., Gao J., Qiu J., Feng Y., Meganathan R., Cohen S.N., Georgiou G. Cell 114:623-634(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RNE. |
| [6] | "RraA rescues Escherichia coli cells over-producing RNase E from growth arrest by modulating the ribonucleolytic activity." Yeom J.H., Lee K. Biochem. Biophys. Res. Commun. 345:1372-1376(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [7] | "Regulation of RraA, a protein inhibitor of RNase E-mediated RNA decay." Zhao M., Zhou L., Kawarasaki Y., Georgiou G. J. Bacteriol. 188:3257-3263(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. Strain: K12. |
| [8] | "Differential modulation of E. coli mRNA abundance by inhibitory proteins that alter the composition of the degradosome." Gao J., Lee K., Zhao M., Qiu J., Zhan X., Saxena A., Moore C.J., Cohen S.N., Georgiou G. Mol. Microbiol. 61:394-406(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RNE. Strain: K12. |
| [9] | "Inhibitory effects of RraA and RraB on RNAse E-related enzymes imply conserved functions in the regulated enzymatic cleavage of RNA." Yeom J.H., Go H., Shin E., Kim H.L., Han S.H., Moore C.J., Bae J., Lee K. FEMS Microbiol. Lett. 285:10-15(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [10] | "The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome." Gorna M.W., Pietras Z., Tsai Y.C., Callaghan A.J., Hernandez H., Robinson C.V., Luisi B.F. RNA 16:553-562(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RNE AND RHLB. |
| [11] | "The X-ray structure of Escherichia coli RraA (MenG), A protein inhibitor of RNA processing." Monzingo A.F., Gao J., Qiu J., Georgiou G., Robertus J.D. J. Mol. Biol. 332:1015-1024(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U56082 Genomic DNA. Translation: AAB01208.1. L19201 Genomic DNA. Translation: AAB03061.1. U00096 Genomic DNA. Translation: AAC76911.1. AP009048 Genomic DNA. Translation: BAE77381.1. | ||||||||||||||||||||||||
| PIR | S40872. | ||||||||||||||||||||||||
| RefSeq | NP_418364.1. NC_000913.2. YP_491522.1. NC_007779.1. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P0A8R0. | ||||||||||||||||||||||||
| SMR | P0A8R0. Positions 2-161. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| DIP | DIP-35864N. | ||||||||||||||||||||||||
| IntAct | P0A8R0. 9 interactions. | ||||||||||||||||||||||||
| STRING | 511145.b3929. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PaxDb | P0A8R0. | ||||||||||||||||||||||||
| PRIDE | P0A8R0. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| EnsemblBacteria | AAC76911; AAC76911; b3929. BAE77381; BAE77381; BAE77381. | ||||||||||||||||||||||||
| GeneID | 12932791. 948419. | ||||||||||||||||||||||||
| KEGG | ecj:Y75_p3258. eco:b3929. | ||||||||||||||||||||||||
| PATRIC | 32123373. VBIEscCol129921_4047. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| EchoBASE | EB1825. | ||||||||||||||||||||||||
| EcoGene | EG11879. rraA. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| eggNOG | COG0684. | ||||||||||||||||||||||||
| HOGENOM | HOG000252803. | ||||||||||||||||||||||||
| KO | K02553. | ||||||||||||||||||||||||
| OMA | ELCDIYH. | ||||||||||||||||||||||||
| ProtClustDB | PRK09372. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BioCyc | EcoCyc:EG11879-MONOMER. ECOL316407:JW3900-MONOMER. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| Genevestigator | P0A8R0. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| Gene3D | 3.50.30.40. 1 hit. | ||||||||||||||||||||||||
| HAMAP | MF_00471. RraA. | ||||||||||||||||||||||||
| InterPro | IPR005493. RNase_E_inh/diMeMenaQ_MeTrfase. IPR010203. RraA. IPR014339. RraA_gpbac. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF03737. Methyltransf_6. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| SUPFAM | SSF89562. RNaseE_inh/diMeMenaQ_MeTrfase. 1 hit. | ||||||||||||||||||||||||
| TIGRFAMs | TIGR01935. NOT-MenG. 1 hit. TIGR02998. RraA_entero. 1 hit. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| EvolutionaryTrace | P0A8R0. | ||||||||||||||||||||||||
Entry information
| Entry name | RRAA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A8R0 Secondary accession number(s): P32165, Q2M8M5 | ||||||||
| Entry history |
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| 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 |

Clusters with
