RRAA_ECOLI
ID RRAA_ECOLI Reviewed; 161 AA.
AC P0A8R0; P32165; Q2M8M5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Regulator of ribonuclease activity A;
GN Name=rraA; Synonyms=menG, yiiV; OrderedLocusNames=b3929, JW3900;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Hudspeth M.E.S., Suvarna K., Meganathan R.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH RNE.
RX PubMed=13678585; DOI=10.1016/j.cell.2003.08.003;
RA Lee K., Zhan X., Gao J., Qiu J., Feng Y., Meganathan R., Cohen S.N.,
RA Georgiou G.;
RT "RraA. a protein inhibitor of RNase E activity that globally modulates RNA
RT abundance in E. coli.";
RL Cell 114:623-634(2003).
RN [6]
RP FUNCTION.
RX PubMed=16725107; DOI=10.1016/j.bbrc.2006.05.018;
RA Yeom J.H., Lee K.;
RT "RraA rescues Escherichia coli cells over-producing RNase E from growth
RT arrest by modulating the ribonucleolytic activity.";
RL Biochem. Biophys. Res. Commun. 345:1372-1376(2006).
RN [7]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=16621818; DOI=10.1128/jb.188.9.3257-3263.2006;
RA Zhao M., Zhou L., Kawarasaki Y., Georgiou G.;
RT "Regulation of RraA, a protein inhibitor of RNase E-mediated RNA decay.";
RL J. Bacteriol. 188:3257-3263(2006).
RN [8]
RP FUNCTION, AND INTERACTION WITH RNE.
RC STRAIN=K12;
RX PubMed=16771842; DOI=10.1111/j.1365-2958.2006.05246.x;
RA Gao J., Lee K., Zhao M., Qiu J., Zhan X., Saxena A., Moore C.J.,
RA Cohen S.N., Georgiou G.;
RT "Differential modulation of E. coli mRNA abundance by inhibitory proteins
RT that alter the composition of the degradosome.";
RL Mol. Microbiol. 61:394-406(2006).
RN [9]
RP FUNCTION.
RX PubMed=18510556; DOI=10.1111/j.1574-6968.2008.01205.x;
RA Yeom J.H., Go H., Shin E., Kim H.L., Han S.H., Moore C.J., Bae J., Lee K.;
RT "Inhibitory effects of RraA and RraB on RNAse E-related enzymes imply
RT conserved functions in the regulated enzymatic cleavage of RNA.";
RL FEMS Microbiol. Lett. 285:10-15(2008).
RN [10]
RP FUNCTION, AND INTERACTION WITH RNE AND RHLB.
RX PubMed=20106955; DOI=10.1261/rna.1858010;
RA Gorna M.W., Pietras Z., Tsai Y.C., Callaghan A.J., Hernandez H.,
RA Robinson C.V., Luisi B.F.;
RT "The regulatory protein RraA modulates RNA-binding and helicase activities
RT of the E. coli RNA degradosome.";
RL RNA 16:553-562(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=14499605; DOI=10.1016/s0022-2836(03)00970-7;
RA Monzingo A.F., Gao J., Qiu J., Georgiou G., Robertus J.D.;
RT "The X-ray structure of Escherichia coli RraA (MenG), A protein inhibitor
RT of RNA processing.";
RL J. Mol. Biol. 332:1015-1024(2003).
CC -!- FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne)
CC and regulating its endonucleolytic activity. Can modulate Rne action in
CC a substrate-dependent manner by altering the composition of the
CC degradosome. Modulates RNA-binding and helicase activities of the
CC degradosome. {ECO:0000269|PubMed:13678585, ECO:0000269|PubMed:16725107,
CC ECO:0000269|PubMed:16771842, ECO:0000269|PubMed:18510556,
CC ECO:0000269|PubMed:20106955}.
CC -!- SUBUNIT: Homotrimer. Forms a ring-like structure with a central cavity.
CC Binds to both RNA-binding sites in the C-terminal region of Rne and to
CC RhlB. {ECO:0000269|PubMed:14499605}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced upon entry into stationary phase, in a RpoS-
CC dependent manner. Stability of the rraA transcript is Rne dependent,
CC suggesting the existence of a feedback mechanism in the regulation of
CC RraA level. {ECO:0000269|PubMed:16621818}.
CC -!- MISCELLANEOUS: RraA and RraB interact with Rne at separate sites within
CC the Rne and exert distinct effects on the composition of the
CC degradosome, affecting distinct sets of RNA transcripts.
CC -!- SIMILARITY: Belongs to the RraA family. {ECO:0000305}.
CC -!- CAUTION: Although it was initially thought to be a methyltransferase of
CC the menaquinone pathway, PubMed:13678585 showed that it has no SAM-
CC dependent methyltransferase activity and is not involved in the
CC menaquinone pathway. {ECO:0000305}.
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DR EMBL; U56082; AAB01208.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03061.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76911.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77381.1; -; Genomic_DNA.
DR PIR; S40872; S40872.
DR RefSeq; NP_418364.1; NC_000913.3.
DR RefSeq; WP_000872908.1; NZ_STEB01000017.1.
DR PDB; 1Q5X; X-ray; 2.00 A; A/B/C=1-161.
DR PDB; 2YJT; X-ray; 2.90 A; A/B/C=1-161.
DR PDB; 2YJV; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-161.
DR PDBsum; 1Q5X; -.
DR PDBsum; 2YJT; -.
DR PDBsum; 2YJV; -.
DR AlphaFoldDB; P0A8R0; -.
DR SMR; P0A8R0; -.
DR BioGRID; 4261785; 27.
DR BioGRID; 852716; 3.
DR DIP; DIP-35864N; -.
DR IntAct; P0A8R0; 12.
DR STRING; 511145.b3929; -.
DR jPOST; P0A8R0; -.
DR PaxDb; P0A8R0; -.
DR PRIDE; P0A8R0; -.
DR EnsemblBacteria; AAC76911; AAC76911; b3929.
DR EnsemblBacteria; BAE77381; BAE77381; BAE77381.
DR GeneID; 67417558; -.
DR GeneID; 948419; -.
DR KEGG; ecj:JW3900; -.
DR KEGG; eco:b3929; -.
DR PATRIC; fig|1411691.4.peg.2776; -.
DR EchoBASE; EB1825; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_4_0_6; -.
DR InParanoid; P0A8R0; -.
DR OMA; RSCDTQF; -.
DR PhylomeDB; P0A8R0; -.
DR BioCyc; EcoCyc:EG11879-MON; -.
DR EvolutionaryTrace; P0A8R0; -.
DR PRO; PR:P0A8R0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IDA:EcoCyc.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IDA:EcoCyc.
DR GO; GO:1902369; P:negative regulation of RNA catabolic process; IDA:EcoCyc.
DR CDD; cd16841; RraA_family; 1.
DR HAMAP; MF_00471; RraA; 1.
DR InterPro; IPR010203; RraA.
DR InterPro; IPR005493; RraA/RraA-like.
DR InterPro; IPR036704; RraA/RraA-like_sf.
DR InterPro; IPR014339; RraA_gpbac.
DR Pfam; PF03737; RraA-like; 1.
DR SUPFAM; SSF89562; SSF89562; 1.
DR TIGRFAMs; TIGR01935; NOT-MenG; 1.
DR TIGRFAMs; TIGR02998; RraA_entero; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..161
FT /note="Regulator of ribonuclease activity A"
FT /id="PRO_0000209611"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:1Q5X"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1Q5X"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1Q5X"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1Q5X"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1Q5X"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1Q5X"
SQ SEQUENCE 161 AA; 17360 MW; B30371B838DE21F8 CRC64;
MKYDTSELCD IYQEDVNVVE PLFSNFGGRA SFGGQIITVK CFEDNGLLYD LLEQNGRGRV
LVVDGGGSVR RALVDAELAR LAVQNEWEGL VIYGAVRQVD DLEELDIGIQ AMAAIPVGAA
GEGIGESDVR VNFGGVTFFS GDHLYADNTG IILSEDPLDI E
