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Entry version 124 (07 Apr 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Ribonuclease G

Gene

rng

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

An endonuclease that acts in the processing of the 5'-end of precursors of 16S rRNA (PubMed:10329633, PubMed:10362534, PubMed:10722715, PubMed:20176963, PubMed:24489121, PubMed:26694614). It prefers 5'-monophosphorylated over 5'-OH or 5'-triphosphorylated substrates and cleaves single-stranded sites rich in A and U residues; contributes to RNA turnover (PubMed:10722715, PubMed:11380618, PubMed:12450135, PubMed:18078441, PubMed:21717341, PubMed:10762247). 5'-monophosphate-assisted cleavage requires at least 2 and preferably 3 or more unpaired 5'-terminal nucleotides for cleavage. The optimal spacing between the 5' end and the scissile phosphate appears to be 6 nucleotides. Any sequence of unpaired nucleotides at the 5'-end is tolerated (PubMed:26694614). Processes the 5'-end precursors of 23S rRNA (PubMed:21717341). Participates in processing of tRNA(Pro) (proK and proM) (PubMed:27288443). Also involved in metabolism of some mRNAs (PubMed:11380618, PubMed:12450135, PubMed:18078441). Cells overproducing this protein form chains of cell with cytoplasmic axial filaments (PubMed:8300545). Could be involved in chromosome segregation and cell division. It may be one of the components of the cytoplasmic axial filaments bundles, or merely regulate the formation of this structure (Probable).1 Publication13 Publications
Confers adaptive resistance to aminoglycoside antibiotics through modulation of 16S rRNA processing.1 Publication

<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

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

<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). In contrast, another group has shown that the enzyme has a higher affinity for 5'-monophosphorylated substrate, which enhances substrate binding in vitro and the decay of RNA in vivo (PubMed:18078441).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 2.1 min(-1) for 14-base 5'-PO4 substrate and 0.096 min(-1) for 5-OH substrate (PubMed:15197283). kcat is 3.0 min(-1) for 13-base 5'-PO4 substrate and 1.2 min(-1) for 5-OH substrate (PubMed:18078441).2 Publications
  1. KM=0.23 µM for 5'-phosphorylated 14 base fluorogenic substrate1 Publication
  2. KM=0.33 µM for 5'-OH 14 base fluorogenic substrate1 Publication
  3. KM=0.12 µM for 5'-phosphorylated 13 base fluorogenic substrate1 Publication
  4. KM=21 µM for 5'-OH 13 base 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 bindingi304Magnesium; catalyticBy similarity1 Publication1
    Metal bindingi347Magnesium; catalyticBy similarity1 Publication1

    <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

    • cell cycle Source: UniProtKB-KW
    • cell division Source: UniProtKB-KW
    • rRNA processing Source: EcoliWiki
    • tRNA processing Source: UniProtKB-KW

    <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 processCell cycle, Cell division, rRNA processing, tRNA processing
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG11299-MONOMER
    MetaCyc:EG11299-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.26.3, 2165

    <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 G2 Publications (EC:3.1.26.-)
    Short name:
    RNase G2 Publications
    Alternative name(s):
    Cytoplasmic axial filament protein1 Publication
    <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:rng2 Publications
    Synonyms:cafA1 Publication, orfF1 Publication, yhdF
    Ordered Locus Names:b3247, JW3216
    <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, Cytoskeleton, 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

    Slow processing of the 17S rRNA precursor to 16S rRNA, with significant accumulation of a 16.3S rRNA precursor (PubMed:10329633, PubMed:10362534, PubMed:20176963). Ribosomes with the precursor 16S rRNA show decreased translational fidelity and an increased sensitivity to aminoglycoside antibiotics neomycin and paromomycin (PubMed:20176963). In contrast another group, using independently generated rng deletions in 2 different strains, showed decreased sensitivity to aminoglycoside antibiotics kanamycin, neomycin, paromomycin and streptomycin (PubMed:24489121). A double rne-rng mutated strain no longer processes the 17S rRNA precursor (PubMed:10329633, PubMed:10362534). Significant accumulation of AdhE and enolase, greatly increased stability of adhE and eno mRNA (PubMed:11380618, PubMed:12450135). Accumulation of a 23S rRNA precursor (PubMed:21717341).7 Publications

    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>Mutagenesisi131V → A: 3.9-fold reduced activity on 5'-PO(4) substrate, 1.9-fold reduced activity on 5'-OH substrate. Has wild-type 16S rRNA in vivo. 1 Publication1
    Mutagenesisi171R → A: Loss of activity. 1 Publication1
    Mutagenesisi171R → K: 34-fold reduced activity on 5'-PO(4) substrate, 2.4-fold reduced activity on 5'-OH substrate. Binds 5'-PO(4) substrate 65-fold less well than wild-type, kcat is nearly wild-type. Has wild-type 16S rRNA in vivo. 1 Publication1
    Mutagenesisi172T → V: 82-fold reduced activity on 5'-PO(4) substrate, 4.9-fold reduced activity on 5'-OH substrate. 1 Publication1
    Mutagenesisi304D → N: Loss of activity. Accumulates about 50% 16.3S rRNA, 50% wild-type 16SrRNA in vivo. 1 Publication1
    Mutagenesisi347D → N: Loss of 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
    <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_00000973832 – 489Ribonuclease GAdd BLAST488

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A9J0

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

    More...
    PaxDbi
    P0A9J0

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A9J0

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Its mRNA is degraded by RNase III (rnc); in the presence of aminoglycoside antibiotics levels of rng mRNA decrease, leading to longer precursor 16S rRNA in the ribosome, which prevents antibiotic-binding and thus increases resistance to aminoglycosides.1 Publication

    <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

    Homodimer, in equilibrium with possible higher multimers.

    3 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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4262071, 231 interactors
    852056, 1 interactor

    Database of interacting proteins

    More...
    DIPi
    DIP-48098N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A9J0, 20 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b3247

    <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

    3D structure databases

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

    More...
    SMRi
    P0A9J0

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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 – 128S1 motifPROSITE-ProRule annotationAdd BLAST90

    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>Regioni244 – 489Required for function, when replaced by GVHSRDDKQAGALHRTPADFRSL in mutant BUMMER, cells accumulate 16.3S rRNA precursor1 PublicationAdd BLAST246

    <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 G subfamily.Curated

    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_5_3_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A9J0

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A9J0

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

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

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A9J0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTAELLVNVT PSETRVAYID GGILQEIHIE REARRGIVGN IYKGRVSRVL
    60 70 80 90 100
    PGMQAAFVDI GLDKAAFLHA SDIMPHTECV AGEEQKQFTV RDISELVRQG
    110 120 130 140 150
    QDLMVQVVKD PLGTKGARLT TDITLPSRYL VFMPGASHVG VSQRIESESE
    160 170 180 190 200
    RERLKKVVAE YCDEQGGFII RTAAEGVGEA ELASDAAYLK RVWTKVMERK
    210 220 230 240 250
    KRPQTRYQLY GELALAQRVL RDFADAELDR IRVDSRLTYE ALLEFTSEYI
    260 270 280 290 300
    PEMTSKLEHY TGRQPIFDLF DVENEIQRAL ERKVELKSGG YLIIDQTEAM
    310 320 330 340 350
    TTVDINTGAF VGHRNLDDTI FNTNIEATQA IARQLRLRNL GGIIIIDFID
    360 370 380 390 400
    MNNEDHRRRV LHSLEQALSK DRVKTSVNGF SALGLVEMTR KRTRESIEHV
    410 420 430 440 450
    LCNECPTCHG RGTVKTVETV CYEIMREIVR VHHAYDSDRF LVYASPAVAE
    460 470 480
    ALKGEESHSL AEVEIFVGKQ VKVQIEPLYN QEQFDVVMM
    Length:489
    Mass (Da):55,364
    Last modified:January 23, 2007 - v2
    <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:i9517B3367C455C99
    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 AAA58050 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

    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
    X57166 Genomic DNA Translation: CAA40457.1
    U18997 Genomic DNA Translation: AAA58050.1 Different initiation.
    U00096 Genomic DNA Translation: AAC76279.2
    AP009048 Genomic DNA Translation: BAE77289.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A65117

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417713.2, NC_000913.3
    WP_000123197.1, NZ_STEB01000012.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76279; AAC76279; b3247
    BAE77289; BAE77289; BAE77289

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    58460270
    947744

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3216
    eco:b3247

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3482

    <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
    X57166 Genomic DNA Translation: CAA40457.1
    U18997 Genomic DNA Translation: AAA58050.1 Different initiation.
    U00096 Genomic DNA Translation: AAC76279.2
    AP009048 Genomic DNA Translation: BAE77289.1
    PIRiA65117
    RefSeqiNP_417713.2, NC_000913.3
    WP_000123197.1, NZ_STEB01000012.1

    3D structure databases

    SMRiP0A9J0
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi4262071, 231 interactors
    852056, 1 interactor
    DIPiDIP-48098N
    IntActiP0A9J0, 20 interactors
    STRINGi511145.b3247

    Proteomic databases

    jPOSTiP0A9J0
    PaxDbiP0A9J0
    PRIDEiP0A9J0

    Genome annotation databases

    EnsemblBacteriaiAAC76279; AAC76279; b3247
    BAE77289; BAE77289; BAE77289
    GeneIDi58460270
    947744
    KEGGiecj:JW3216
    eco:b3247
    PATRICifig|1411691.4.peg.3482

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1276

    Phylogenomic databases

    eggNOGiCOG1530, Bacteria
    HOGENOMiCLU_003468_5_3_6
    InParanoidiP0A9J0
    PhylomeDBiP0A9J0

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11299-MONOMER
    MetaCyc:EG11299-MONOMER
    BRENDAi3.1.26.3, 2165

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P0A9J0

    Family and domain databases

    InterProiView protein in InterPro
    IPR012340, NA-bd_OB-fold
    IPR019307, RNA-bd_AU-1/RNase_E/G
    IPR004659, RNase_E/G
    IPR022967, S1_dom
    IPR003029, S1_domain
    PfamiView protein in Pfam
    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

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    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiRNG_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: P0A9J0
    Secondary accession number(s): P25537, P76677, Q2M8W7
    <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: July 19, 2005
    Last sequence update: January 23, 2007
    Last modified: April 7, 2021
    This is version 124 of the entry and version 2 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

    Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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