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Protein

Regulator of ribonuclease activity A

Gene

rraA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  • endoribonuclease inhibitor activity Source: UniProtKB-HAMAP
  • ribonuclease inhibitor activity Source: EcoCyc

GO - Biological processi

  • negative regulation of endoribonuclease activity Source: EcoCyc
  • RNA catabolic process Source: EcoCyc
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:EG11879-MONOMER.
ECOL316407:JW3900-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of ribonuclease activity A
Gene namesi
Name:rraA
Synonyms:menG, yiiV
Ordered Locus Names:b3929, JW3900
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11879. rraA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Regulator of ribonuclease activity APRO_0000209611Add
BLAST

Proteomic databases

EPDiP0A8R0.
PaxDbiP0A8R0.
PRIDEiP0A8R0.

Expressioni

Inductioni

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.1 Publication

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi4261785. 6 interactions.
DIPiDIP-35864N.
IntActiP0A8R0. 12 interactions.
STRINGi511145.b3929.

Structurei

Secondary structure

1
161
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128Combined sources
Helixi13 – 153Combined sources
Beta strandi16 – 183Combined sources
Beta strandi30 – 4011Combined sources
Beta strandi42 – 443Combined sources
Helixi46 – 527Combined sources
Beta strandi59 – 646Combined sources
Beta strandi69 – 746Combined sources
Helixi76 – 849Combined sources
Beta strandi89 – 968Combined sources
Helixi99 – 1024Combined sources
Beta strandi105 – 11410Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi125 – 1284Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi151 – 1566Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A8R0.
SMRiP0A8R0. Positions 2-161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8R0.

Family & Domainsi

Sequence similaritiesi

Belongs to the RraA family.Curated

Phylogenomic databases

eggNOGiENOG4108YYX. Bacteria.
COG0684. LUCA.
HOGENOMiHOG000252803.
InParanoidiP0A8R0.
KOiK02553.
OMAiLQICRQS.
OrthoDBiEOG6Z3KKK.
PhylomeDBiP0A8R0.

Family and domain databases

Gene3Di3.50.30.40. 1 hit.
HAMAPiMF_00471. RraA.
InterProiIPR010203. RraA.
IPR005493. RraA/RraA-like.
IPR014339. RraA_gpbac.
[Graphical view]
PfamiPF03737. Methyltransf_6. 1 hit.
[Graphical view]
SUPFAMiSSF89562. SSF89562. 1 hit.
TIGRFAMsiTIGR01935. NOT-MenG. 1 hit.
TIGR02998. RraA_entero. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A8R0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYDTSELCD IYQEDVNVVE PLFSNFGGRA SFGGQIITVK CFEDNGLLYD
60 70 80 90 100
LLEQNGRGRV LVVDGGGSVR RALVDAELAR LAVQNEWEGL VIYGAVRQVD
110 120 130 140 150
DLEELDIGIQ AMAAIPVGAA GEGIGESDVR VNFGGVTFFS GDHLYADNTG
160
IILSEDPLDI E
Length:161
Mass (Da):17,360
Last modified:June 7, 2005 - v1
Checksum:iB30371B838DE21F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56082 Genomic DNA. Translation: AAB01208.1.
L19201 Genomic DNA. Translation: AAB03061.1.
U00096 Genomic DNA. Translation: AAC76911.1.
AP009048 Genomic DNA. Translation: BAE77381.1.
PIRiS40872.
RefSeqiNP_418364.1. NC_000913.3.
WP_000872908.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76911; AAC76911; b3929.
BAE77381; BAE77381; BAE77381.
GeneIDi948419.
KEGGiecj:JW3900.
eco:b3929.
PATRICi32123373. VBIEscCol129921_4047.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56082 Genomic DNA. Translation: AAB01208.1.
L19201 Genomic DNA. Translation: AAB03061.1.
U00096 Genomic DNA. Translation: AAC76911.1.
AP009048 Genomic DNA. Translation: BAE77381.1.
PIRiS40872.
RefSeqiNP_418364.1. NC_000913.3.
WP_000872908.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A8R0.
SMRiP0A8R0. Positions 2-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261785. 6 interactions.
DIPiDIP-35864N.
IntActiP0A8R0. 12 interactions.
STRINGi511145.b3929.

Proteomic databases

EPDiP0A8R0.
PaxDbiP0A8R0.
PRIDEiP0A8R0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76911; AAC76911; b3929.
BAE77381; BAE77381; BAE77381.
GeneIDi948419.
KEGGiecj:JW3900.
eco:b3929.
PATRICi32123373. VBIEscCol129921_4047.

Organism-specific databases

EchoBASEiEB1825.
EcoGeneiEG11879. rraA.

Phylogenomic databases

eggNOGiENOG4108YYX. Bacteria.
COG0684. LUCA.
HOGENOMiHOG000252803.
InParanoidiP0A8R0.
KOiK02553.
OMAiLQICRQS.
OrthoDBiEOG6Z3KKK.
PhylomeDBiP0A8R0.

Enzyme and pathway databases

BioCyciEcoCyc:EG11879-MONOMER.
ECOL316407:JW3900-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A8R0.
PROiP0A8R0.

Family and domain databases

Gene3Di3.50.30.40. 1 hit.
HAMAPiMF_00471. RraA.
InterProiIPR010203. RraA.
IPR005493. RraA/RraA-like.
IPR014339. RraA_gpbac.
[Graphical view]
PfamiPF03737. Methyltransf_6. 1 hit.
[Graphical view]
SUPFAMiSSF89562. SSF89562. 1 hit.
TIGRFAMsiTIGR01935. NOT-MenG. 1 hit.
TIGR02998. RraA_entero. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiRRAA_ECOLI
AccessioniPrimary (citable) accession number: P0A8R0
Secondary accession number(s): P32165, Q2M8M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 13, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Caution

Although it was initially thought to be a methyltransferase of the menaquinone pathway, PubMed:13678585 showed that it has no SAM-dependent methyltransferase activity and is not involved in the menaquinone pathway.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.