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P0A8R0 (RRAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of ribonuclease activity A
Gene names
Name:rraA
Synonyms:menG, yiiV
Ordered Locus Names:b3929, JW3900
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Regulator of ribonuclease activity A HAMAP-Rule MF_00471
PRO_0000209611

Secondary structure

................................... 161
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A8R0 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: B30371B838DE21F8

FASTA16117,360
        10         20         30         40         50         60 
MKYDTSELCD IYQEDVNVVE PLFSNFGGRA SFGGQIITVK CFEDNGLLYD LLEQNGRGRV 

        70         80         90        100        110        120 
LVVDGGGSVR RALVDAELAR LAVQNEWEGL VIYGAVRQVD DLEELDIGIQ AMAAIPVGAA 

       130        140        150        160 
GEGIGESDVR VNFGGVTFFS GDHLYADNTG IILSEDPLDI E 

« Hide

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.
PIRS40872.
RefSeqNP_418364.1. NC_000913.2.
YP_491522.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q5XX-ray2.00A/B/C1-161[»]
2YJTX-ray2.90A/B/C1-161[»]
2YJVX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-161[»]
ProteinModelPortalP0A8R0.
SMRP0A8R0. Positions 2-161.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35864N.
IntActP0A8R0. 9 interactions.
STRING511145.b3929.

Proteomic databases

PaxDbP0A8R0.
PRIDEP0A8R0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76911; AAC76911; b3929.
BAE77381; BAE77381; BAE77381.
GeneID12932791.
948419.
KEGGecj:Y75_p3258.
eco:b3929.
PATRIC32123373. VBIEscCol129921_4047.

Organism-specific databases

EchoBASEEB1825.
EcoGeneEG11879. rraA.

Phylogenomic databases

eggNOGCOG0684.
HOGENOMHOG000252803.
KOK02553.
OMAELCDIYH.
ProtClustDBPRK09372.

Enzyme and pathway databases

BioCycEcoCyc:EG11879-MONOMER.
ECOL316407:JW3900-MONOMER.

Gene expression databases

GenevestigatorP0A8R0.

Family and domain databases

Gene3D3.50.30.40. 1 hit.
HAMAPMF_00471. RraA.
InterProIPR005493. RNase_E_inh/diMeMenaQ_MeTrfase.
IPR010203. RraA.
IPR014339. RraA_gpbac.
[Graphical view]
PfamPF03737. Methyltransf_6. 1 hit.
[Graphical view]
SUPFAMSSF89562. RNaseE_inh/diMeMenaQ_MeTrfase. 1 hit.
TIGRFAMsTIGR01935. NOT-MenG. 1 hit.
TIGR02998. RraA_entero. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A8R0.

Entry information

Entry nameRRAA_ECOLI
AccessionPrimary (citable) accession number: P0A8R0
Secondary accession number(s): P32165, Q2M8M5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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