RRAB_ECOLI
ID RRAB_ECOLI Reviewed; 138 AA.
AC P0AF90; P37163; Q2M654;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Regulator of ribonuclease activity B {ECO:0000255|HAMAP-Rule:MF_01888};
GN Name=rraB {ECO:0000255|HAMAP-Rule:MF_01888}; Synonyms=yjgD;
GN OrderedLocusNames=b4255, JW4212;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RX PubMed=6329710; DOI=10.1002/j.1460-2075.1982.tb01259.x;
RA Piette J., Cunin R., van Vliet F., Charlier D.R.M., Crabeel M., Ota Y.,
RA Glansdorff N.;
RT "Homologous control sites and DNA transcription starts in the related argF
RT and argI genes of Escherichia coli K12.";
RL EMBO J. 1:853-857(1982).
RN [5]
RP IDENTIFICATION.
RX PubMed=8253666; DOI=10.1128/jb.175.24.7776-7785.1993;
RA Persson B.C., Bjoerk G.R.;
RT "Isolation of the gene (miaE) encoding the hydroxylase involved in the
RT synthesis of 2-methylthio-cis-ribozeatin in tRNA of Salmonella typhimurium
RT and characterization of mutants.";
RL J. Bacteriol. 175:7776-7785(1993).
RN [6]
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 [7]
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 [8]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=19717586; DOI=10.1128/jb.00344-09;
RA Zhou L., Zhao M., Wolf R.Z., Graham D.E., Georgiou G.;
RT "Transcriptional regulation of the Escherichia coli gene rraB, encoding a
RT protein inhibitor of RNase E.";
RL J. Bacteriol. 191:6665-6674(2009).
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. {ECO:0000255|HAMAP-Rule:MF_01888,
CC ECO:0000269|PubMed:16771842, ECO:0000269|PubMed:18510556}.
CC -!- SUBUNIT: Interacts with the C-terminal region of Rne.
CC {ECO:0000255|HAMAP-Rule:MF_01888, ECO:0000269|PubMed:16771842}.
CC -!- INTERACTION:
CC P0AF90; P0AEK4: fabI; NbExp=2; IntAct=EBI-544031, EBI-370029;
CC P0AF90; P0A9Z1: glnB; NbExp=3; IntAct=EBI-544031, EBI-551053;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01888}.
CC -!- INDUCTION: Constitutively expressed. Expression is increased by a
CC reduction in intracellular concentration of UDP-GlcNAc.
CC {ECO:0000269|PubMed:19717586}.
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 RraB family. {ECO:0000255|HAMAP-
CC Rule:MF_01888}.
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DR EMBL; U14003; AAA97151.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77212.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78252.1; -; Genomic_DNA.
DR EMBL; M24186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S56480; S56480.
DR RefSeq; NP_418676.1; NC_000913.3.
DR RefSeq; WP_000002953.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P0AF90; -.
DR SMR; P0AF90; -.
DR BioGRID; 4263244; 13.
DR BioGRID; 853060; 2.
DR DIP; DIP-47905N; -.
DR IntAct; P0AF90; 18.
DR STRING; 511145.b4255; -.
DR jPOST; P0AF90; -.
DR PaxDb; P0AF90; -.
DR PRIDE; P0AF90; -.
DR EnsemblBacteria; AAC77212; AAC77212; b4255.
DR EnsemblBacteria; BAE78252; BAE78252; BAE78252.
DR GeneID; 66671826; -.
DR GeneID; 948773; -.
DR KEGG; ecj:JW4212; -.
DR KEGG; eco:b4255; -.
DR PATRIC; fig|1411691.4.peg.2449; -.
DR EchoBASE; EB2347; -.
DR eggNOG; COG3076; Bacteria.
DR HOGENOM; CLU_128640_0_0_6; -.
DR OMA; FCFDAIA; -.
DR PhylomeDB; P0AF90; -.
DR BioCyc; EcoCyc:G7885-MON; -.
DR PRO; PR:P0AF90; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IDA:EcoCyc.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:EcoCyc.
DR GO; GO:0050790; P:regulation of catalytic activity; IDA:EcoCyc.
DR GO; GO:0060699; P:regulation of endoribonuclease activity; IDA:UniProtKB.
DR Gene3D; 3.30.70.970; -; 1.
DR HAMAP; MF_01888; RraB; 1.
DR InterPro; IPR016716; RraB.
DR InterPro; IPR036701; RraB-like_sf.
DR InterPro; IPR009671; RraB_dom.
DR Pfam; PF06877; RraB; 1.
DR PIRSF; PIRSF018193; UCP018193; 1.
DR SUPFAM; SSF89946; SSF89946; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..138
FT /note="Regulator of ribonuclease activity B"
FT /id="PRO_0000169759"
FT REGION 114..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 138 AA; 15603 MW; E23D6DBE6547FD0F CRC64;
MANPEQLEEQ REETRLIIEE LLEDGSDPDA LYTIEHHLSA DDLETLEKAA VEAFKLGYEV
TDPEELEVED GDIVICCDIL SECALNADLI DAQVEQLMTL AEKFDVEYDG WGTYFEDPNG
EDGDDEDFVD EDDDGVRH
