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Entry version 202 (07 Apr 2021)
Sequence version 6 (29 Aug 2003)
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Protein

Ribonuclease E

Gene

rne

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Required to initiate rRNA degradation during both starvation and quality control; acts after RNase PH (rph) exonucleolytically digests the 3'-end of the 16S rRNA (PubMed:27298395). Degradation of 16S rRNA leads to 23S rRNA degradation (PubMed:27298395). Processes the 3 tRNA(Pro) precursors immediately after the 3'-CCA to generate the mature ends (PubMed:27288443).UniRule annotation12 Publications
Prefers 5'-monophosphorylated substrates over 5'-triphosphorylated substrates (PubMed:10762247). 5'-monophosphate-assisted cleavage requires at least 2 and preferably 3 or more unpaired 5'-terminal nucleotides. The optimal spacing between the 5' end and the scissile phosphate appears to be 8 nucleotides. Any sequence of unpaired nucleotides at the 5'-end is tolerated (PubMed:26694614).2 Publications

Miscellaneous

In K12 strains that are derived from W1485 (including MG1655 and W3110) the rph gene has a frameshift that leads to loss of its ribonuclease PH activity. In strain K12 / MG1655(Seq)* the wild-type Rph protein has been restored (PubMed:27298395).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The presence of a 5'-monophosphate on substrate RNA accelerates its cleavage by catalytically activating the enzyme (PubMed:15197283). Binding to the membrane stabilizes protein structure and increases affinity for the substrate.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.83 min(-1) for 5'-PO4 substrate and 0.088 min(-1) for 5-OH substrate.1 Publication
  1. KM=0.60 µM for 5'-phosphorylated fluorogenic substrate1 Publication
  2. KM=0.57 µM for 5'-OH fluorogenic substrate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi303Magnesium; catalytic1 Publication1
    Metal bindingi346Magnesium; catalytic1 Publication1
    Metal bindingi404Zinc; shared with dimeric partner2 Publications1
    Metal bindingi407Zinc; shared with dimeric partner2 Publications1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionEndonuclease, Hydrolase, Nuclease, RNA-binding, rRNA-binding, tRNA-binding
    Biological processrRNA processing, tRNA processing
    LigandMagnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG10859-MONOMER
    MetaCyc:EG10859-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.26.12, 2026

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Ribonuclease EUniRule annotation (EC:3.1.26.12UniRule annotation)
    Short name:
    RNase EUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:rne1 PublicationUniRule annotation
    Synonyms:ams1 Publication, hmp1
    Ordered Locus Names:b1084, JW1071
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cytoplasm, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Essential, it cannot be deleted. In a temperature sensitive mutant at non-permissive temperature, slow processing of the 17S rRNA precursor to 16S rRNA; a double rne-rng mutated strain no longer processes the 17S rRNA precursor.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi57F → A: Reduces RNA cleavage by over 98%. 1 Publication1
    Mutagenesisi66G → S: Disrupts folding of the S1 motif. 1 Publication1
    Mutagenesisi67F → A: Reduces RNA cleavage by over 98%. 1 Publication1
    Mutagenesisi112K → A: Reduces RNA cleavage by 98%. 1 Publication1
    Mutagenesisi170T → V: Abolishes enzyme activity toward RNA substrates with a 5' monophosphate (PubMed:16237448). Strongly reduces enzyme activity toward cspA mRNA (PubMed:19889093). 2 Publications1
    Mutagenesisi303D → N: Reduces RNA cleavage by over 96%. 1 Publication1
    Mutagenesisi305N → D or L: Reduces RNA cleavage by over 96%. 1 Publication1
    Mutagenesisi346D → N: Reduces RNA cleavage by over 96%. 1 Publication1
    Mutagenesisi373R → A or D: Reduces RNA cleavage by 89%. 1 Publication1
    Mutagenesisi404C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. 1 Publication1
    Mutagenesisi407C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000973731 – 1061Ribonuclease EAdd BLAST1061

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P21513

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P21513

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P21513

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

    UniRule annotation11 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4261023, 251 interactors
    850013, 1 interactor

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-403, RNA degradosome

    Database of interacting proteins

    More...
    DIPi
    DIP-10727N

    Protein interaction database and analysis system

    More...
    IntActi
    P21513, 63 interactors

    Molecular INTeraction database

    More...
    MINTi
    P21513

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b1084

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    11061
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Biological Magnetic Resonance Data Bank

    More...
    BMRBi
    P21513

    Small Angle Scattering Biological Data Bank

    More...
    SASBDBi
    P21513

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P21513

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P21513

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini39 – 119S1 motifUniRule annotationAdd BLAST81

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni57 – 112Interaction with RNAAdd BLAST56
    Regioni169 – 170Interaction with RNA 5'-terminal monophosphate2
    Regioni404 – 407Required for zinc-mediated homotetramerization and catalytic activity4
    Regioni833 – 850Interaction with enolaseAdd BLAST18
    Regioni1021 – 1061Interaction with PNPaseAdd BLAST41

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the RNase E/G family. RNase E subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG1530, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_003468_1_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P21513

    Family and domain databases

    Database of protein disorder

    More...
    DisProti
    DP00207

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00970, RNase_E, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR012340, NA-bd_OB-fold
    IPR021968, PNPase_C
    IPR019307, RNA-bd_AU-1/RNase_E/G
    IPR028878, RNase_E
    IPR004659, RNase_E/G
    IPR022967, S1_dom
    IPR003029, S1_domain

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF12111, PNPase_C, 1 hit
    PF10150, RNase_E_G, 1 hit
    PF00575, S1, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00316, S1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50249, SSF50249, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00757, RNaseEG, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50126, S1, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P21513-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE
    60 70 80 90 100
    PSLEAAFVDY GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV
    110 120 130 140 150
    IVQIDKEERG NKGAALTTFI SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE
    160 170 180 190 200
    LKEALASLEL PEGMGLIVRT AGVGKSAEAL QWDLSFRLKH WEAIKKAAES
    210 220 230 240 250
    RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA RQHIAALGRP
    260 270 280 290 300
    DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT
    310 320 330 340 350
    AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM
    360 370 380 390 400
    TPVRHQRAVE NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS
    410 420 430 440 450
    HHVCPRCSGT GTVRDNESLS LSILRLIEEE ALKENTQEVH AIVPVPIASY
    460 470 480 490 500
    LLNEKRSAVN AIETRQDGVR CVIVPNDQME TPHYHVLRVR KGEETPTLSY
    510 520 530 540 550
    MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA PTPAEPAAPV
    560 570 580 590 600
    VAPAPKAAPA TPAAPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA
    610 620 630 640 650
    KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT
    660 670 680 690 700
    AETRESRQQA EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE
    710 720 730 740 750
    EQSVQETEQE ERVRPVQPRR KQRQLNQKVR YEQSVAEEAV VAPVVEETVA
    760 770 780 790 800
    AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ QEENNADNRD NGGMPRRSRR
    810 820 830 840 850
    SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG KVWIRYPIVR
    860 870 880 890 900
    PQDVQVEEQR EQEEVHVQPM VTEVPVAAAI EPVVSAPVVE EVAGVVEAPV
    910 920 930 940 950
    QVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEQAEPVVEP
    960 970 980 990 1000
    QEETADIEEV VETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVAAVEPEVT
    1010 1020 1030 1040 1050
    VEHNHATAPM TRAPAPEYVP EAPRHSDWQR PTFAFEGKGA AGGHTATHHA
    1060
    SAAPARPQPV E
    Length:1,061
    Mass (Da):118,197
    Last modified:August 29, 2003 - v6
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD4066D80E1DE7D37
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA23443 differs from that shown. Reason: Frameshift.Curated
    The sequence CAA38206 differs from that shown. Reason: Frameshift.Curated
    The sequence CAA47818 differs from that shown. Reason: Frameshift.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti390Q → H in AAA23443 (PubMed:1704367).Curated1
    Sequence conflicti487L → V in CAA47818 (PubMed:1447789).Curated1
    Sequence conflicti487L → V in AAA23443 (PubMed:1704367).Curated1
    Sequence conflicti564A → R in CAA47818 (PubMed:1447789).Curated1
    Sequence conflicti784N → K in CAA47818 (PubMed:1447789).Curated1
    Sequence conflicti838A → R in AAA23443 (PubMed:1704367).Curated1
    Sequence conflicti905P → R in CAA47818 (PubMed:1447789).Curated1
    Sequence conflicti1048H → R in AAA03347 (PubMed:8415644).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    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

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A64852, S27311

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415602.1, NC_000913.3
    WP_000827360.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74168; AAC74168; b1084
    BAA35893; BAA35893; BAA35893

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    57731871
    945641

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1071
    eco:b1084

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1184

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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
    WP_000827360.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB 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[»]
    5F6CX-ray3.00A1-510[»]
    B1-511[»]
    6G63X-ray3.95A/G/L/N1-510[»]
    BMRBiP21513
    SASBDBiP21513
    SMRiP21513
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4261023, 251 interactors
    850013, 1 interactor
    ComplexPortaliCPX-403, RNA degradosome
    DIPiDIP-10727N
    IntActiP21513, 63 interactors
    MINTiP21513
    STRINGi511145.b1084

    Proteomic databases

    jPOSTiP21513
    PaxDbiP21513
    PRIDEiP21513

    Genome annotation databases

    EnsemblBacteriaiAAC74168; AAC74168; b1084
    BAA35893; BAA35893; BAA35893
    GeneIDi57731871
    945641
    KEGGiecj:JW1071
    eco:b1084
    PATRICifig|1411691.4.peg.1184

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0852

    Phylogenomic databases

    eggNOGiCOG1530, Bacteria
    HOGENOMiCLU_003468_1_2_6
    InParanoidiP21513

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10859-MONOMER
    MetaCyc:EG10859-MONOMER
    BRENDAi3.1.26.12, 2026

    Miscellaneous databases

    EvolutionaryTraceiP21513

    Protein Ontology

    More...
    PROi
    PR:P21513

    Family and domain databases

    DisProtiDP00207
    HAMAPiMF_00970, RNase_E, 1 hit
    InterProiView protein in InterPro
    IPR012340, NA-bd_OB-fold
    IPR021968, PNPase_C
    IPR019307, RNA-bd_AU-1/RNase_E/G
    IPR028878, RNase_E
    IPR004659, RNase_E/G
    IPR022967, S1_dom
    IPR003029, S1_domain
    PfamiView protein in Pfam
    PF12111, PNPase_C, 1 hit
    PF10150, RNase_E_G, 1 hit
    PF00575, S1, 1 hit
    SMARTiView protein in SMART
    SM00316, S1, 1 hit
    SUPFAMiSSF50249, SSF50249, 1 hit
    TIGRFAMsiTIGR00757, RNaseEG, 1 hit
    PROSITEiView protein in PROSITE
    PS50126, S1, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRNE_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P21513
    Secondary accession number(s): P77591
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: August 29, 2003
    Last modified: April 7, 2021
    This is version 202 of the entry and version 6 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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