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P0A7Y0

- RNC_ECOLI

UniProt

P0A7Y0 - RNC_ECOLI

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Protein

Ribonuclease 3

Gene

rnc

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

Functioni

Digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs; cleavage can occur in assembled 30S, 50S and even 70S subunits and is influenced by the presence of ribosomal proteins. The E.coli enzyme does not cleave R.capsulatus rRNA precursor, although R.capsulatus will complement an E.coli disruption, showing substrate recognition is different. Removes the intervening sequences from Salmonella typhimurium rRNA precursor. Complements the pre-crRNA processing defect in an rnc deletion in S.pyogenes strain 370, although this E.coli strain does not have the corresponding CRISPR locus (strain TOP10) (PubMed:23535272).11 Publications

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.1 Publication

Cofactori

Divalent cations, preferably Mg2+. While only 1 Mg2+ is detected by crystallography, other evidence indicates there may be more than 1 metal necessary for catalysis. Binding of the second metal my be promoted by substrate binding.3 Publications

Enzyme regulationi

Non-competitively inhibited by 2-hydroxy-4H-isoquinoline-1,3-dione. Activity is down-regulated during cold shock by direct interaction with YmdB. Also down-regulated during entry into stationary phase by an YmdB-independent mechanism.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411MagnesiumCurated
Active sitei45 – 451Sequence Analysis
Metal bindingi114 – 1141MagnesiumBy similarity
Active sitei117 – 1171Curated
Metal bindingi117 – 1171MagnesiumCurated

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. ribonuclease III activity Source: EcoCyc
  4. rRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. mRNA processing Source: UniProtKB-HAMAP
  2. RNA phosphodiester bond hydrolysis Source: GOC
  3. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  4. RNA processing Source: EcoCyc
  5. rRNA catabolic process Source: InterPro
  6. rRNA processing Source: UniProtKB-HAMAP
  7. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

mRNA processing, rRNA processing, tRNA processing

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10857-MONOMER.
ECOL316407:JW2551-MONOMER.
MetaCyc:EG10857-MONOMER.
BRENDAi3.1.26.3. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease 3 (EC:3.1.26.3)
Alternative name(s):
Ribonuclease III
Short name:
RNase III
Gene namesi
Name:rnc
Ordered Locus Names:b2567, JW2551
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10857. rnc.

Subcellular locationi

Cytoplasm 1 Publication
Note: Loosely associated with ribosomes.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Slower than wild-type growth. Transient accumulation of the 30S rRNA precursor occurs; 90% of 16S rRNA is correctly processed while an extended version of 23S rRNA accumulates in the ribosome. Half-life of a number of RNase III processed transcripts increases. In the absence of era and rnc there is a defect in chromosome partitioning. In strain HT115, loss of immunity against a plasmid with homology to CRISPR spacer sequences (PubMed:23535272).6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381E → A: Reduced affinity for Mg(2+), no catalytic defect at 10 mM Mg(2+). 1 Publication
Mutagenesisi40 – 401L → G, D or R: Loss of activity. 1 Publication
Mutagenesisi40 – 401L → M or W: No effect. 1 Publication
Mutagenesisi41 – 411E → A: Reduced affinity for Mg(2+), catalytic defect. 85-fold reduced affinity for Mg(2+); when associated with A-114. 1 Publication
Mutagenesisi44 – 441G → S in rnc-105; slower growth, loss of RNase activity. 2 Publications
Mutagenesisi45 – 451D → A, E or N: 30000-fold reduction in catalytic efficiency, binds RNA normally. Partially rescued by Mn(2+). 1 Publication
Mutagenesisi65 – 651E → A: Reduced affinity for Mg(2+), no catalytic defect at 10 mM Mg(2+). 1 Publication
Mutagenesisi100 – 1001E → A: Reduced affinity for Mg(2+) and RNA. 1 Publication
Mutagenesisi114 – 1141D → A: Reduced affinity for Mg(2+), no catalytic defect at 10 mM Mg(2+). 85-fold reduced affinity for Mg(2+); when associated with A-41. 1 Publication
Mutagenesisi117 – 1171E → D: Nearly complete loss of RNase activity, still binds RNA. Partially rescued by Mn(2+). 2 Publications
Mutagenesisi117 – 1171E → K in rnc70; slower growth, loss of RNase activity. Dominant over wild-type. Binds ds-RNA. 2 Publications
Mutagenesisi117 – 1171E → Q: Loss of RNase activity, still binds RNA. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226Ribonuclease 3PRO_0000180395Add
BLAST

Proteomic databases

PaxDbiP0A7Y0.
PRIDEiP0A7Y0.

PTM databases

PhosSiteiP010446.

Expressioni

Inductioni

Expression increases as the growth rate increases. Encoded in the rnc-era-recO operon. Processes the 5' end of its own transcript leading to mRNA instability.2 Publications

Gene expression databases

GenevestigatoriP0A7Y0.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-48223N.
IntActiP0A7Y0. 6 interactions.
MINTiMINT-1227120.
STRINGi511145.b2567.

Structurei

3D structure databases

ProteinModelPortaliP0A7Y0.
SMRiP0A7Y0. Positions 5-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 128123RNase IIIAdd
BLAST
Domaini155 – 22571DRBMAdd
BLAST

Sequence similaritiesi

Contains 1 RNase III domain.Curated

Phylogenomic databases

eggNOGiCOG0571.
HOGENOMiHOG000246809.
InParanoidiP0A7Y0.
KOiK03685.
OMAiAQKDPKT.
OrthoDBiEOG6T1WVS.
PhylomeDBiP0A7Y0.

Family and domain databases

Gene3Di1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPiMF_00104. RNase_III.
InterProiIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PANTHERiPTHR11207. PTHR11207. 1 hit.
PfamiPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
SUPFAMiSSF69065. SSF69065. 1 hit.
TIGRFAMsiTIGR02191. RNaseIII. 1 hit.
PROSITEiPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7Y0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPIVINRLQ RKLGYTFNHQ ELLQQALTHR SASSKHNERL EFLGDSILSY
60 70 80 90 100
VIANALYHRF PRVDEGDMSR MRATLVRGNT LAELAREFEL GECLRLGPGE
110 120 130 140 150
LKSGGFRRES ILADTVEALI GGVFLDSDIQ TVEKLILNWY QTRLDEISPG
160 170 180 190 200
DKQKDPKTRL QEYLQGRHLP LPTYLVVQVR GEAHDQEFTI HCQVSGLSEP
210 220
VVGTGSSRRK AEQAAAEQAL KKLELE
Length:226
Mass (Da):25,550
Last modified:January 1, 1988 - v1
Checksum:iD9E2858F2E0AA3A5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 19528HLPLP…HCQVS → PSAAADLSGSPGTWSKRTIR NLLSTARSV in CAA26504. (PubMed:3895158)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02946 Genomic DNA. Translation: CAA26692.1.
X02673 Genomic DNA. Translation: CAA26504.1.
D64044 Genomic DNA. Translation: BAA10914.1.
U36841 Genomic DNA. Translation: AAA79829.1.
U00096 Genomic DNA. Translation: AAC75620.1.
AP009048 Genomic DNA. Translation: BAE76743.1.
M26415 Genomic DNA. Translation: AAA21843.1.
M14658 Unassigned DNA. Translation: AAA03241.1.
PIRiF65034. NREC3.
RefSeqiNP_417062.1. NC_000913.3.
YP_490795.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75620; AAC75620; b2567.
BAE76743; BAE76743; BAE76743.
GeneIDi12931603.
947033.
KEGGiecj:Y75_p2520.
eco:b2567.
PATRICi32120533. VBIEscCol129921_2669.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02946 Genomic DNA. Translation: CAA26692.1 .
X02673 Genomic DNA. Translation: CAA26504.1 .
D64044 Genomic DNA. Translation: BAA10914.1 .
U36841 Genomic DNA. Translation: AAA79829.1 .
U00096 Genomic DNA. Translation: AAC75620.1 .
AP009048 Genomic DNA. Translation: BAE76743.1 .
M26415 Genomic DNA. Translation: AAA21843.1 .
M14658 Unassigned DNA. Translation: AAA03241.1 .
PIRi F65034. NREC3.
RefSeqi NP_417062.1. NC_000913.3.
YP_490795.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0A7Y0.
SMRi P0A7Y0. Positions 5-224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48223N.
IntActi P0A7Y0. 6 interactions.
MINTi MINT-1227120.
STRINGi 511145.b2567.

PTM databases

PhosSitei P010446.

Proteomic databases

PaxDbi P0A7Y0.
PRIDEi P0A7Y0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75620 ; AAC75620 ; b2567 .
BAE76743 ; BAE76743 ; BAE76743 .
GeneIDi 12931603.
947033.
KEGGi ecj:Y75_p2520.
eco:b2567.
PATRICi 32120533. VBIEscCol129921_2669.

Organism-specific databases

EchoBASEi EB0850.
EcoGenei EG10857. rnc.

Phylogenomic databases

eggNOGi COG0571.
HOGENOMi HOG000246809.
InParanoidi P0A7Y0.
KOi K03685.
OMAi AQKDPKT.
OrthoDBi EOG6T1WVS.
PhylomeDBi P0A7Y0.

Enzyme and pathway databases

BioCyci EcoCyc:EG10857-MONOMER.
ECOL316407:JW2551-MONOMER.
MetaCyc:EG10857-MONOMER.
BRENDAi 3.1.26.3. 2026.

Miscellaneous databases

PROi P0A7Y0.

Gene expression databases

Genevestigatori P0A7Y0.

Family and domain databases

Gene3Di 1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPi MF_00104. RNase_III.
InterProi IPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view ]
PANTHERi PTHR11207. PTHR11207. 1 hit.
Pfami PF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
[Graphical view ]
SMARTi SM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view ]
SUPFAMi SSF69065. SSF69065. 1 hit.
TIGRFAMsi TIGR02191. RNaseIII. 1 hit.
PROSITEi PS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations."
    Nashimoto H., Uchida H.
    Mol. Gen. Genet. 201:25-29(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ENDORIBONUCLEASE, MUTAGENESIS OF GLY-44.
    Strain: K12.
  2. "The DNA sequence of the gene (rnc) encoding ribonuclease III of Escherichia coli."
    March P.E., Ahnn J., Inouye M.
    Nucleic Acids Res. 13:4677-4685(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / CS520.
  3. Nashimoto H., Saito N.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Genetic analysis of the rnc operon of Escherichia coli."
    Takiff H.E., Chen S.M., Court D.L.
    J. Bacteriol. 171:2581-2590(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45, DISRUPTION PHENOTYPE, OPERON STRUCTURE.
    Strain: K12 / W3110.
  7. "Expression and characterization of RNase III and Era proteins. Products of the rnc operon of Escherichia coli."
    Chen S.M., Takiff H.E., Barber A.M., Dubois G.C., Bardwell J.C., Court D.L.
    J. Biol. Chem. 265:2888-2895(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-30, MRNA PROCESSING, ATP-BINDING.
    Strain: K12 / W3110.
  8. "A GTP-binding protein of Escherichia coli has homology to yeast RAS proteins."
    Ahnn J., March P.E., Takiff H.E., Inouye M.
    Proc. Natl. Acad. Sci. U.S.A. 83:8849-8853(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 211-226.
  9. "Purification and properties of ribonuclease III from Escherichia coli."
    Robertson H.D., Webster R.E., Zinder N.D.
    J. Biol. Chem. 243:82-91(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A DS-RNA SPECIFIC ENDORIBONUCLEASE, SUBCELLULAR LOCATION, ASSOCIATION WITH RIBOSOMES.
    Strain: K12 / K38 / S26.
  10. "T7 early RNAs and Escherichia coli ribosomal RNAs are cut from large precursor RNAs in vivo by ribonuclease 3."
    Dunn J.J., Studier F.W.
    Proc. Natl. Acad. Sci. U.S.A. 70:3296-3300(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENTEROBACTERIA PHAGE T7 RNA PROCESSING, FUNCTION IN PROCESSING OF RRNA, DISRUPTION PHENOTYPE.
    Strain: K12 / A19.
  11. "Ribonuclease 3 does not degrade deoxyribonucleic acid-ribonucleic acid hybrids."
    Crouch R.J.
    J. Biol. Chem. 249:1314-1316(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A DS-RNA SPECIFIC ENDORIBONUCLEASE, CATALYTIC ACTIVITY.
    Strain: K12 / D10.
  12. "30 S pre-ribosomal RNA of Escherichia coli and products of cleavage by ribonuclease III: length and molecular weight."
    Nikolaev N., Schlessinger D., Wellauer P.K.
    J. Mol. Biol. 86:741-747(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROCESSING OF RRNA.
  13. "RNase III cleavage of single-stranded RNA. Effect of ionic strength on the fideltiy of cleavage."
    Dunn J.J.
    J. Biol. Chem. 251:3807-3814(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROCESSING OF RRNA, COFACTOR, SUBUNIT.
  14. "The synthesis of some proteins is affected in RNA processing mutants of Escherichia coli."
    Gitelman D.R., Apirion D.
    Biochem. Biophys. Res. Commun. 96:1063-1070(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN PROTEIN SYNTHESIS.
  15. "RNase III cleavage is obligate for maturation but not for function of Escherichia coli pre-23S rRNA."
    King T.C., Sirdeshmukh R., Schlessinger D.
    Proc. Natl. Acad. Sci. U.S.A. 81:185-188(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  16. "Cleavage by RNase III in the transcripts of the met Y-nus-A-infB operon of Escherichia coli releases the tRNA and initiates the decay of the downstream mRNA."
    Regnier P., Grunberg-Manago M.
    J. Mol. Biol. 210:293-302(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROCESSING OF TRNA.
  17. "RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression."
    Regnier P., Grunberg-Manago M.
    Biochimie 72:825-834(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROCESSING OF MRNA, INDUCTION.
  18. "The excision of intervening sequences from Salmonella 23S ribosomal RNA."
    Burgin A.B., Parodos K., Lane D.J., Pace N.R.
    Cell 60:405-414(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN EXCISION OF INTERVENING SEQUENCES.
    Strain: N2076.
  19. "Genetic uncoupling of the dsRNA-binding and RNA cleavage activities of the Escherichia coli endoribonuclease RNase III--the effect of dsRNA binding on gene expression."
    Dasgupta S., Fernandez L., Kameyama L., Inada T., Nakamura Y., Pappas A., Court D.L.
    Mol. Microbiol. 28:629-640(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-44 AND GLU-117, DISRUPTION PHENOTYPE.
    Strain: K12 / W3110.
  20. "Cell cycle arrest in Era GTPase mutants: a potential growth rate-regulated checkpoint in Escherichia coli."
    Britton R.A., Powell B.S., Dasgupta S., Sun Q., Margolin W., Lupski J.R., Court D.L.
    Mol. Microbiol. 27:739-750(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / W3110.
  21. "Different cleavage specificities of RNases III from Rhodobacter capsulatus and Escherichia coli."
    Conrad C., Rauhut R., Klug G.
    Nucleic Acids Res. 26:4446-4453(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  22. "Mechanism of action of Escherichia coli ribonuclease III. Stringent chemical requirement for the glutamic acid 117 side chain and Mn2+ rescue of the Glu117Asp mutant."
    Sun W., Nicholson A.W.
    Biochemistry 40:5102-5110(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, MUTAGENESIS OF GLU-117, CATALYTIC MODEL.
  23. "Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage."
    Blaszczyk J., Tropea J.E., Bubunenko M., Routzahn K.M., Waugh D.S., Court D.L., Ji X.
    Structure 9:1225-1236(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-40.
  24. "Functional interaction between RNase III and the Escherichia coli ribosome."
    Allas U., Liiv A., Remme J.
    BMC Mol. Biol. 4:8-8(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH RIBOSOMES.
  25. "Mutational analysis of the nuclease domain of Escherichia coli ribonuclease III. Identification of conserved acidic residues that are important for catalytic function in vitro."
    Sun W., Li G., Nicholson A.W.
    Biochemistry 43:13054-13062(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-38; GLU-41; ASP-45; GLU-65; GLU-100 AND ASP-114.
  26. "Catalytic mechanism of Escherichia coli ribonuclease III: kinetic and inhibitor evidence for the involvement of two magnesium ions in RNA phosphodiester hydrolysis."
    Sun W., Pertzev A., Nicholson A.W.
    Nucleic Acids Res. 33:807-815(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, COFACTOR, CATALYTIC MODEL.
  27. "YmdB: a stress-responsive ribonuclease-binding regulator of E. coli RNase III activity."
    Kim K.S., Manasherob R., Cohen S.N.
    Genes Dev. 22:3497-3508(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  28. "crRNA and tracrRNA guide Cas9-mediated DNA interference in Streptococcus thermophilus."
    Karvelis T., Gasiunas G., Miksys A., Barrangou R., Horvath P., Siksnys V.
    RNA Biol. 10:841-851(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENTYPE.
    Strain: HT115 and TOP10.
  29. "Structure of the dsRNA binding domain of E. coli RNase III."
    Kharrat A., Macias M.J., Gibson T.J., Nilges M., Pastore A.
    EMBO J. 14:3572-3584(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 153-226, RNA-BINDING.

Entry informationi

Entry nameiRNC_ECOLI
AccessioniPrimary (citable) accession number: P0A7Y0
Secondary accession number(s): P05797, P06141, Q2MAG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: October 29, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The original rnc-105 mutation is described as G44->D but the nucleotide sequence given indicates G44->S (PubMed:3903434). A later paper calls the same mutation G45->K (PubMed:9632264), which alters the residue and mutation.2 Publications

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3