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P21513

- RNE_ECOLI

UniProt

P21513 - RNE_ECOLI

Protein

Ribonuclease E

Gene

rne

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 6 (29 Aug 2003)
      Previous versions | rss
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    Functioni

    Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs. Can also process other RNA species, such as RNAI, a molecule that controls the replication of ColE1 plasmid, and the cell division inhibitor DicF-RNA. It initiates the decay of RNAs by cutting them internally near their 5'-end. It is able to remove poly(A) tails by an endonucleolytic process.9 PublicationsUniRule annotation

    Catalytic activityi

    Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.3 PublicationsUniRule annotation

    Cofactori

    Binds 2 Zn2+ ions per homotetramer. Zinc ions are bound betweeen subunits and are essential for homotetramerization and catalytic activity, but not for RNA binding. In the absence of zinc, the protein dissociates into inactive dimers.
    Binds 1 Mg2+ ion per subunit.

    Enzyme regulationi

    Binding to the membrane stabilizes protein structure and increases affinity for the substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi303 – 3031Magnesium; catalytic
    Metal bindingi346 – 3461Magnesium; catalytic
    Metal bindingi404 – 4041Zinc; shared with dimeric partner
    Metal bindingi407 – 4071Zinc; shared with dimeric partner

    GO - Molecular functioni

    1. endoribonuclease activity Source: UniProtKB-HAMAP
    2. magnesium ion binding Source: UniProtKB-HAMAP
    3. protein binding Source: IntAct
    4. ribonuclease E activity Source: InterPro
    5. RNA binding Source: UniProtKB-HAMAP
    6. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. mRNA catabolic process Source: UniProtKB-HAMAP
    2. RNA catabolic process Source: EcoCyc
    3. rRNA 5'-end processing Source: EcoCyc
    4. rRNA processing Source: UniProtKB-HAMAP
    5. tRNA processing Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    rRNA processing, tRNA processing

    Keywords - Ligandi

    Magnesium, Metal-binding, RNA-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10859-MONOMER.
    ECOL316407:JW1071-MONOMER.
    MetaCyc:EG10859-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease EUniRule annotation (EC:3.1.26.12UniRule annotation)
    Short name:
    RNase EUniRule annotation
    Gene namesi
    Name:rneUniRule annotation
    Synonyms:ams, hmp1
    Ordered Locus Names:b1084, JW1071
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10859. rne.

    Subcellular locationi

    Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Associated with the cytoplasmic membrane via the N- and C-terminal regions.

    GO - Cellular componenti

    1. cytoplasm Source: EcoCyc
    2. cytoplasmic side of plasma membrane Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi57 – 571F → A: Reduces RNA cleavage by over 98%. 1 Publication
    Mutagenesisi66 – 661G → S: Disrupts folding of the S1 motif. 1 Publication
    Mutagenesisi67 – 671F → A: Reduces RNA cleavage by over 98%. Reduces affinity for RNA. 1 Publication
    Mutagenesisi112 – 1121K → A: Reduces RNA cleavage by 98%. Loss of RNA-binding. 1 Publication
    Mutagenesisi170 – 1701T → V: Abolishes enzyme activity toward RNA substrates with a 5' monophosphate (PubMed:16237448). Strongly reduces enzyme activity toward cspA mRNA (PubMed:19889093). 2 Publications
    Mutagenesisi303 – 3031D → N: Reduces RNA cleavage by over 96%. 1 Publication
    Mutagenesisi305 – 3051N → D or L: Reduces RNA cleavage by over 96%. 1 Publication
    Mutagenesisi346 – 3461D → N: Reduces RNA cleavage by over 96%. Reduces affinity for RNA. 1 Publication
    Mutagenesisi373 – 3731R → A or D: Reduces RNA cleavage by 89%. 1 Publication
    Mutagenesisi404 – 4041C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. 1 Publication
    Mutagenesisi407 – 4071C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10611061Ribonuclease EPRO_0000097373Add
    BLAST

    Proteomic databases

    PaxDbiP21513.
    PRIDEiP21513.

    Expressioni

    Gene expression databases

    GenevestigatoriP21513.

    Interactioni

    Subunit structurei

    Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, Rnase E assembles into a homotetramer formed by a dimer of dimers. Tetramerization is essential for catalytic activity, but not for RNA-binding. Interacts with RhlB, PNPase (pnp) and enolase (eno). Interacts with DeaD at reduced temperature.11 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dnaKP0A6Y89EBI-549958,EBI-542092
    enoP0A6P915EBI-549958,EBI-368855
    pnpP0505511EBI-549958,EBI-548080
    rhlBP0A8J816EBI-549958,EBI-555806

    Protein-protein interaction databases

    DIPiDIP-10727N.
    IntActiP21513. 61 interactions.
    MINTiMINT-1220086.
    STRINGi511145.b1084.

    Structurei

    Secondary structure

    1
    1061
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Beta strandi10 – 123
    Beta strandi14 – 207
    Beta strandi23 – 308
    Beta strandi32 – 343
    Beta strandi36 – 394
    Beta strandi42 – 509
    Helixi51 – 533
    Beta strandi55 – 6410
    Beta strandi66 – 694
    Helixi70 – 723
    Helixi75 – 773
    Beta strandi84 – 863
    Helixi90 – 923
    Beta strandi99 – 1068
    Beta strandi110 – 1123
    Beta strandi115 – 1184
    Beta strandi125 – 1306
    Beta strandi134 – 1363
    Turni145 – 1484
    Helixi151 – 1555
    Beta strandi165 – 1684
    Helixi170 – 1745
    Helixi177 – 19923
    Beta strandi205 – 2084
    Beta strandi210 – 2123
    Helixi213 – 2219
    Beta strandi226 – 2327
    Helixi234 – 24613
    Helixi250 – 2556
    Beta strandi256 – 2583
    Helixi265 – 2684
    Helixi272 – 2776
    Beta strandi281 – 2844
    Beta strandi290 – 2956
    Beta strandi300 – 3056
    Helixi315 – 33622
    Beta strandi341 – 3466
    Helixi353 – 36614
    Turni367 – 3693
    Beta strandi374 – 3796
    Beta strandi383 – 3897
    Helixi396 – 4005
    Beta strandi405 – 4117
    Helixi416 – 43217
    Beta strandi436 – 4438
    Helixi445 – 4517
    Turni452 – 4554
    Helixi456 – 46510
    Turni466 – 4683
    Beta strandi470 – 4756
    Beta strandi485 – 4906
    Turni491 – 4933
    Helixi499 – 5013
    Helixi502 – 5065
    Turni507 – 5093
    Helixi831 – 8333
    Helixi835 – 8384

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SLJNMR-A35-125[»]
    1SMXX-ray1.80A/B35-125[»]
    1SN8X-ray2.00A/B35-125[»]
    2BX2X-ray2.85L1-510[»]
    2C0BX-ray3.18L1-510[»]
    2C4RX-ray3.60L1-510[»]
    2FYMX-ray1.60B/E833-850[»]
    2VMKX-ray3.30A/B/C/D1-515[»]
    2VRTX-ray3.50A/B/C/D1-509[»]
    3GCMX-ray2.50D/E/F1021-1061[»]
    3GMEX-ray2.40D1021-1061[»]
    3H1CX-ray3.57D/E/F/H/J/L/N/P/S/U/W/Y1021-1061[»]
    3H8AX-ray1.90E/F823-850[»]
    DisProtiDP00207.
    ProteinModelPortaliP21513.
    SMRiP21513. Positions 1-510, 823-850.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21513.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 11981S1 motifUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni57 – 11256Interaction with RNAAdd
    BLAST
    Regioni169 – 1702Interaction with RNA 5'-terminal monophosphate
    Regioni404 – 4074Required for zinc-mediated homotetramerization and catalytic activity
    Regioni833 – 85018Interaction with enolaseAdd
    BLAST
    Regioni1021 – 106141Interaction with PNPaseAdd
    BLAST

    Domaini

    The N-terminal S1 motif binds RNA, and can also bind single-stranded DNA (in vitro). The C-terminal region interacts with the other degradosomal components.2 Publications

    Sequence similaritiesi

    Belongs to the RNase E/G family. RNase E subfamily.UniRule annotation
    Contains 1 S1 motif domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1530.
    HOGENOMiHOG000258027.
    KOiK08300.
    OMAiENTKEVH.
    OrthoDBiEOG6PCPTH.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    HAMAPiMF_00970. RNase_E.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR021968. PNPase_C.
    IPR003029. Rbsml_prot_S1_RNA-bd_dom.
    IPR019307. RNA-bd_AU-1/RNase_E/G.
    IPR022967. RNA-binding_domain_S1.
    IPR028878. RNase_E.
    IPR004659. RNase_E/G.
    [Graphical view]
    PfamiPF12111. PNPase_C. 1 hit.
    PF10150. RNase_E_G. 1 hit.
    PF00575. S1. 1 hit.
    [Graphical view]
    SMARTiSM00316. S1. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00757. RNaseEG. 1 hit.
    PROSITEiPS50126. S1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21513-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE     50
    PSLEAAFVDY GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV 100
    IVQIDKEERG NKGAALTTFI SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE 150
    LKEALASLEL PEGMGLIVRT AGVGKSAEAL QWDLSFRLKH WEAIKKAAES 200
    RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA RQHIAALGRP 250
    DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT 300
    AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM 350
    TPVRHQRAVE NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS 400
    HHVCPRCSGT GTVRDNESLS LSILRLIEEE ALKENTQEVH AIVPVPIASY 450
    LLNEKRSAVN AIETRQDGVR CVIVPNDQME TPHYHVLRVR KGEETPTLSY 500
    MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA PTPAEPAAPV 550
    VAPAPKAAPA TPAAPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA 600
    KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT 650
    AETRESRQQA EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE 700
    EQSVQETEQE ERVRPVQPRR KQRQLNQKVR YEQSVAEEAV VAPVVEETVA 750
    AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ QEENNADNRD NGGMPRRSRR 800
    SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG KVWIRYPIVR 850
    PQDVQVEEQR EQEEVHVQPM VTEVPVAAAI EPVVSAPVVE EVAGVVEAPV 900
    QVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEQAEPVVEP 950
    QEETADIEEV VETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVAAVEPEVT 1000
    VEHNHATAPM TRAPAPEYVP EAPRHSDWQR PTFAFEGKGA AGGHTATHHA 1050
    SAAPARPQPV E 1061
    Length:1,061
    Mass (Da):118,197
    Last modified:August 29, 2003 - v6
    Checksum:iD4066D80E1DE7D37
    GO

    Sequence cautioni

    The sequence AAA23443.1 differs from that shown. Reason: Frameshift at position 796.
    The sequence CAA38206.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence CAA47818.1 differs from that shown. Reason: Frameshift at position 1003.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti390 – 3901Q → H in AAA23443. (PubMed:1704367)Curated
    Sequence conflicti487 – 4871L → V in CAA47818. (PubMed:1447789)Curated
    Sequence conflicti487 – 4871L → V in AAA23443. (PubMed:1704367)Curated
    Sequence conflicti564 – 5641A → R in CAA47818. (PubMed:1447789)Curated
    Sequence conflicti784 – 7841N → K in CAA47818. (PubMed:1447789)Curated
    Sequence conflicti838 – 8381A → R in AAA23443. (PubMed:1704367)Curated
    Sequence conflicti905 – 9051P → R in CAA47818. (PubMed:1447789)Curated
    Sequence conflicti1048 – 10481H → R in AAA03347. (PubMed:8415644)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC74168.1.
    AP009048 Genomic DNA. Translation: BAA35893.1.
    X67470 Genomic DNA. Translation: CAA47818.1. Frameshift.
    M62747 Genomic DNA. Translation: AAA23443.1. Frameshift.
    X54309 Genomic DNA. Translation: CAA38206.1. Frameshift.
    L23942 Genomic DNA. Translation: AAA03347.1.
    PIRiA64852. S27311.
    RefSeqiNP_415602.1. NC_000913.3.
    YP_489352.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74168; AAC74168; b1084.
    BAA35893; BAA35893; BAA35893.
    GeneIDi12932029.
    945641.
    KEGGiecj:Y75_p1054.
    eco:b1084.
    PATRICi32117409. VBIEscCol129921_1127.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC74168.1 .
    AP009048 Genomic DNA. Translation: BAA35893.1 .
    X67470 Genomic DNA. Translation: CAA47818.1 . Frameshift.
    M62747 Genomic DNA. Translation: AAA23443.1 . Frameshift.
    X54309 Genomic DNA. Translation: CAA38206.1 . Frameshift.
    L23942 Genomic DNA. Translation: AAA03347.1 .
    PIRi A64852. S27311.
    RefSeqi NP_415602.1. NC_000913.3.
    YP_489352.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SLJ NMR - A 35-125 [» ]
    1SMX X-ray 1.80 A/B 35-125 [» ]
    1SN8 X-ray 2.00 A/B 35-125 [» ]
    2BX2 X-ray 2.85 L 1-510 [» ]
    2C0B X-ray 3.18 L 1-510 [» ]
    2C4R X-ray 3.60 L 1-510 [» ]
    2FYM X-ray 1.60 B/E 833-850 [» ]
    2VMK X-ray 3.30 A/B/C/D 1-515 [» ]
    2VRT X-ray 3.50 A/B/C/D 1-509 [» ]
    3GCM X-ray 2.50 D/E/F 1021-1061 [» ]
    3GME X-ray 2.40 D 1021-1061 [» ]
    3H1C X-ray 3.57 D/E/F/H/J/L/N/P/S/U/W/Y 1021-1061 [» ]
    3H8A X-ray 1.90 E/F 823-850 [» ]
    DisProti DP00207.
    ProteinModelPortali P21513.
    SMRi P21513. Positions 1-510, 823-850.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10727N.
    IntActi P21513. 61 interactions.
    MINTi MINT-1220086.
    STRINGi 511145.b1084.

    Proteomic databases

    PaxDbi P21513.
    PRIDEi P21513.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74168 ; AAC74168 ; b1084 .
    BAA35893 ; BAA35893 ; BAA35893 .
    GeneIDi 12932029.
    945641.
    KEGGi ecj:Y75_p1054.
    eco:b1084.
    PATRICi 32117409. VBIEscCol129921_1127.

    Organism-specific databases

    EchoBASEi EB0852.
    EcoGenei EG10859. rne.

    Phylogenomic databases

    eggNOGi COG1530.
    HOGENOMi HOG000258027.
    KOi K08300.
    OMAi ENTKEVH.
    OrthoDBi EOG6PCPTH.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10859-MONOMER.
    ECOL316407:JW1071-MONOMER.
    MetaCyc:EG10859-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P21513.
    PROi P21513.

    Gene expression databases

    Genevestigatori P21513.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    HAMAPi MF_00970. RNase_E.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR021968. PNPase_C.
    IPR003029. Rbsml_prot_S1_RNA-bd_dom.
    IPR019307. RNA-bd_AU-1/RNase_E/G.
    IPR022967. RNA-binding_domain_S1.
    IPR028878. RNase_E.
    IPR004659. RNase_E/G.
    [Graphical view ]
    Pfami PF12111. PNPase_C. 1 hit.
    PF10150. RNase_E_G. 1 hit.
    PF00575. S1. 1 hit.
    [Graphical view ]
    SMARTi SM00316. S1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00757. RNaseEG. 1 hit.
    PROSITEi PS50126. S1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Cloning and analysis of the entire Escherichia coli ams gene. ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein."
      Casaregola S., Jacq A., Laoudj D., McGurk G., Margarson S., Tempete M., Norris V., Holland I.B.
      J. Mol. Biol. 228:30-40(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1025.
      Strain: K12.
    5. "Analysis of the altered mRNA stability (ams) gene from Escherichia coli. Nucleotide sequence, transcriptional analysis, and homology of its product to MRP3, a mitochondrial ribosomal protein from Neurospora crassa."
      Claverie-Martin F., Diaz-Torres M., Yancey S.D., Kushner S.R.
      J. Biol. Chem. 266:2843-2851(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-844.
      Strain: K12.
    6. "Sequencing and expression of the rne gene of Escherichia coli."
      Chauhan A.K., Miczak A., Taraseviciene L., Apirion D.
      Nucleic Acids Res. 19:125-129(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-27.
      Strain: K12.
    7. "RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product."
      Cormack R.S., Genereaux J.L., Mackie G.A.
      Proc. Natl. Acad. Sci. U.S.A. 90:9006-9010(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 844-1061, CHARACTERIZATION.
      Strain: K12.
    8. "Maturation of 5-S rRNA: ribonuclease E cleavages and their dependence on precursor sequences."
      Roy M.K., Singh B., Ray B.K., Apirion D.
      Eur. J. Biochem. 131:119-127(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN 5S RRNA MATURATION.
    9. "Escherichia coli cell division inhibitor DicF-RNA of the dicB operon. Evidence for its generation in vivo by transcription termination and by RNase III and RNase E-dependent processing."
      Faubladier M., Cam K., Bouche J.P.
      J. Mol. Biol. 212:461-471(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROCESSING OF DICF-RNA.
    10. "RNase E, an endoribonuclease, has a general role in the chemical decay of Escherichia coli mRNA: evidence that rne and ams are the same genetic locus."
      Mudd E.A., Krisch H.M., Higgins C.F.
      Mol. Microbiol. 4:2127-2135(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome."
      Vanzo N.F., Li Y.S., Py B., Blum E., Higgins C.F., Raynal L.C., Krisch H.M., Carpousis A.J.
      Genes Dev. 12:2770-2781(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RHLB; PNPASE AND ENOLASE, DOMAIN.
    12. "RNase G (CafA protein) and RNase E are both required for the 5' maturation of 16S ribosomal RNA."
      Li Z., Pandit S., Deutscher M.P.
      EMBO J. 18:2878-2885(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN 16S RRNA MATURATION.
      Strain: K12.
    13. "RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E."
      Liou G.G., Jane W.N., Cohen S.N., Lin N.S., Lin-Chao S.
      Proc. Natl. Acad. Sci. U.S.A. 98:63-68(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    14. "Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli."
      Walsh A.P., Tock M.R., Mallen M.H., Kaberdin V.R., Gabain Av A., McDowall K.J.
      Nucleic Acids Res. 29:1864-1871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CLEAVAGE OF POLY(A).
    15. "RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors."
      Li Z., Deutscher M.P.
      RNA 8:97-109(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRNA MATURATION.
      Strain: K12.
    16. "Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'."
      Prud'homme-Genereux A., Beran R.K., Iost I., Ramey C.S., Mackie G.A., Simons R.W.
      Mol. Microbiol. 54:1409-1421(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DEAD.
      Strain: CF881.
    17. "'Zn-link': a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E."
      Callaghan A.J., Redko Y., Murphy L.M., Grossmann J.G., Yates D., Garman E., Ilag L.L., Robinson C.V., Symmons M.F., McDowall K.J., Luisi B.F.
      Biochemistry 44:4667-4675(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, RNA-BINDING, SUBUNIT, ZINC-BINDING, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-404 AND CYS-407.
    18. "RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome."
      Taghbalout A., Rothfield L.
      J. Biol. Chem. 283:13850-13855(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RHLB; PNPASE AND ENOLASE.
    19. "Rapid cleavage of RNA by RNase E in the absence of 5' monophosphate stimulation."
      Kime L., Jourdan S.S., Stead J.A., Hidalgo-Sastre A., McDowall K.J.
      Mol. Microbiol. 76:590-604(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF THR-170.
    20. "Membrane binding of Escherichia coli RNase E catalytic domain stabilizes protein structure and increases RNA substrate affinity."
      Murashko O.N., Kaberdin V.R., Lin-Chao S.
      Proc. Natl. Acad. Sci. U.S.A. 109:7019-7024(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
    21. "Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces."
      Schubert M., Edge R.E., Lario P., Cook M.A., Strynadka N.C., Mackie G.A., McIntosh L.P.
      J. Mol. Biol. 341:37-54(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 35-125, STRUCTURE BY NMR OF 35-125, SUBUNIT, RNA-BINDING, DOMAIN, MUTAGENESIS OF GLY-66.
    22. "Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover."
      Callaghan A.J., Marcaida M.J., Stead J.A., McDowall K.J., Scott W.G., Luisi B.F.
      Nature 437:1187-1191(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-510 IN COMPLEXES WITH RNA; ZINC AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF PHE-57; PHE-67; LYS-112; THR-170; ASP-303; ASN-305; ASP-346 AND ARG-373.
    23. "Recognition of enolase in the Escherichia coli RNA degradosome."
      Chandran V., Luisi B.F.
      J. Mol. Biol. 358:8-15(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 833-850 IN COMPLEX WITH ENO, SUBUNIT.
    24. "The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation."
      Koslover D.J., Callaghan A.J., Marcaida M.J., Garman E.F., Martick M., Scott W.G., Luisi B.F.
      Structure 16:1238-1244(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-515 IN COMPLEX WITH RNA AND ZINC IONS, SUBUNIT.
    25. "Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly."
      Nurmohamed S., Vaidialingam B., Callaghan A.J., Luisi B.F.
      J. Mol. Biol. 389:17-33(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1021-1061 IN COMPLEXES WITH PNP AND RNA, SUBUNIT.
    26. "Molecular recognition between Escherichia coli enolase and ribonuclease E."
      Nurmohamed S., McKay A.R., Robinson C.V., Luisi B.F.
      Acta Crystallogr. D 66:1036-1040(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 823-850 IN COMPLEX WITH ENO, INTERACTION WITH ENO, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.

    Entry informationi

    Entry nameiRNE_ECOLI
    AccessioniPrimary (citable) accession number: P21513
    Secondary accession number(s): P77591
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: August 29, 2003
    Last modified: October 1, 2014
    This is version 146 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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

    External Data

    Dasty 3