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Entry version 189 (18 Sep 2019)
Sequence version 2 (01 Feb 1994)
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Protein

GTPase Era

Gene

era

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 essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring on the order of seconds whereas hydrolysis occurs on the order of minutes. Plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing and 30S ribosomal subunit biogenesis. One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late assembly stage of the 30S ribosomal subunit. Its presence in the 30S subunit may prevent translation initiation. Seems to be critical for maintaining cell growth and cell divison rates; a dramatic reduction in Era protein levels temporarily arrests cell growth just before cytokinesis (at the predivisional two-cell stage) and delays cell division. Era mutant era1 suppresses some temperature-sensitive mutations that affect DNA replication and chromosome partitioning and segregation. The dominant-negative Era-de mutant which is missing residues in a putative effector region, is unable to complement the disruption mutant; upon overproduction it shows a significant decrease in cell viability and a synthetic lethal phenotype in the presence of acetate. Era function probably overlaps RbfA (PubMed:16825789). Binds to the pre-30S ribosomal subunit through several stages of protein assembly (PubMed:20188109).4 Publications

Miscellaneous

When overexpressed partially suppresses the slow growth and decreased 70S ribosome phenotype of an rsgA knockout; RsgA may be involved in 30S ribosomal subunit biogenesis (PubMed:18223068). When overexpressed partially suppresses the 30S ribosomal subunit assembly defects and cold-sensitivity of an rbfA knockout; an era mutant missing residues 39-49 fully suppresses these phenotypes (PubMed:12753192). Overexpression is not able to suppress a rimM disruption phenotype nor a C23U mutation in 16S rRNA. Also suppresses temperature-sensitive mutations in DNA primase (PubMed:9093842).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

GTPase is competitively inhibited by GDP but not by ADP, ATP, CTP or UTP.1 Publication

<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

  1. KM=15.4 µM for GTP (for His-tagged protein at pH 8.0, 5 mM MgCl2)2 Publications
  2. KM=9.0 µM for GTP (for overexpressed protein at pH 8.0, 5 mM MgCl2)2 Publications

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi15 – 22GTP8
    Nucleotide bindingi62 – 66GTP5
    Nucleotide bindingi124 – 127GTP4

    <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 functionRNA-binding, rRNA-binding
    Biological processRibosome biogenesis
    LigandGTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG10270-MONOMER
    ECOL316407:JW2550-MONOMER
    MetaCyc:EG10270-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P06616

    <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_and_taxonomy_section">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:
    GTPase Era
    Short name:
    ERA
    Alternative name(s):
    GTP-binding protein Era
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:era
    Synonyms:rbaA, sdgE
    Ordered Locus Names:b2566, JW2550
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10270 era

    <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

    GO - Cellular componenti

    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

    Lethality. In the presence of 1% protein cells grow extremely slowly and are blocked at the predivisional two-cell stage of the cell cycle. In the absence of Era and Rnc there is an additional defect in chromosome partitioning. In depletion experiments cells grow normally for 2 hours when protein levels fall. After 4 hours 16S rRNA levels decrease with a concomitant rise in the 17S precursor rRNA molecule (extra sequences at both the 5' and 3' end compared to mature 16S rRNA) and a loss of 70S ribosome assembly.3 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi8C → A in era770; 20-fold reduction in GTP-binding. Confers growth sensitivity at 42 degrees Celsius; when associated with an unpublished 22 residue replacement in the C-terminus. 1 Publication1
    Mutagenesisi17P → R in era1; suppresses a number of temperature-sensitive mutations affecting cell cycle. 2 Publications1
    Mutagenesisi17P → V: Confers sensitivity to cold. 2 Publications1
    Mutagenesisi26N → S: Confers sensitivity to cold; overexpression does not suppress an rbfA disruption. 1 Publication1
    Mutagenesisi39 – 49KAQTTRHRIVG → R in Era-de; does not complement a disruption mutant, overexpression in a wt cells inhibits growth. Binds GTP poorly, Km for GTP increases 5-fold, Vmax for GTPase is 55% that of wt. Does not autophosphorylate. Complements cold-sensitivity and 16S rRNA processing in an rbfA disruption mutant. 1 PublicationAdd BLAST11
    Mutagenesisi42 – 43TT → AA: Does not complement a disruption mutant, Km for GTP increases 12-fold, Vmax for GTPase is 49% that of wt. Overexpression partially suppresses an rbfA disruption. 2 Publications2
    Mutagenesisi156A → D: Confers sensitivity to cold; overexpression partially suppresses an rbfA disruption. 1 Publication1
    Mutagenesisi200E → K: Confers sensitivity to cold, cells do not divide properly but do replicate DNA and segregate nucleoids normally. 16S rRNA processing is decreased, ribosome assembly is defective. Suppressed by overexpression of RsmA. Overexpression does not suppress an rbfA disruption, while at 37 degrees Celsius the rbfA/era E220K mutant grows very poorly, a dominant-negative effect. This mutant still binds 30S ribosomes. 2 Publications1

    <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_processing_section">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 methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001800122 – 301GTPase EraAdd BLAST300

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei36Phosphothreonine; by autocatalysis1 Publication1
    Modified residuei37Phosphoserine; by autocatalysis1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P06616

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

    More...
    PaxDbi
    P06616

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P06616

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P06616

    <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

    Expression increases as the growth rate increases. Encoded in the rnc-era-recO operon.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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer. Binds both 16S rRNA and 30S ribosomal subunits; binding is inhibited by GDP and GTP (PubMed:10094501). Bind preferentially to mature 30S ribosomal subunits over immature subunits in the presence of GMP-PNP (PubMed:27382067). Binds to MazG; GDP-bound Era binds more tightly to MazG than GTP-bound Era (PubMed:19706445).

    2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263220, 465 interactors
    851375, 7 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-9521N

    Protein interaction database and analysis system

    More...
    IntActi
    P06616, 29 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2566

    <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

    1301
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    P06616

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P06616

    <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_and_domains_section">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>Domaini7 – 175Era-type GAdd BLAST169
    Domaini206 – 283KH type-2Add BLAST78

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CWT Bacteria
    COG1159 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000245597

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P06616

    KEGG Orthology (KO)

    More...
    KOi
    K03595

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P06616

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd04163 Era, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.300.20, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00367 GTPase_Era, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR030388 G_ERA_dom
    IPR005662 GTP-bd_Era
    IPR006073 GTP_binding_domain
    IPR015946 KH_dom-like_a/b
    IPR004044 KH_dom_type_2
    IPR009019 KH_sf_prok-type
    IPR027417 P-loop_NTPase
    IPR005225 Small_GTP-bd_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07650 KH_2, 1 hit
    PF01926 MMR_HSR1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540 SSF52540, 1 hit
    SSF54814 SSF54814, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00436 era, 1 hit
    TIGR00231 small_GTP, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51713 G_ERA, 1 hit
    PS50823 KH_TYPE_2, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P06616-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSIDKSYCGF IAIVGRPNVG KSTLLNKLLG QKISITSRKA QTTRHRIVGI
    60 70 80 90 100
    HTEGAYQAIY VDTPGLHMEE KRAINRLMNK AASSSIGDVE LVIFVVEGTR
    110 120 130 140 150
    WTPDDEMVLN KLREGKAPVI LAVNKVDNVQ EKADLLPHLQ FLASQMNFLD
    160 170 180 190 200
    IVPISAETGL NVDTIAAIVR KHLPEATHHF PEDYITDRSQ RFMASEIIRE
    210 220 230 240 250
    KLMRFLGAEL PYSVTVEIER FVSNERGGYD INGLILVERE GQKKMVIGNK
    260 270 280 290 300
    GAKIKTIGIE ARKDMQEMFE APVHLELWVK VKSGWADDER ALRSLGYVDD

    L
    Length:301
    Mass (Da):33,810
    Last modified:February 1, 1994 - 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:i53F275F07BDAE593
    GO

    <p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 33682±5 Da from positions 2 - 301. Determined by ESI. 1 Publication

    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
    M14658 Unassigned DNA Translation: AAA03242.1
    D64044 Genomic DNA Translation: BAA10913.1
    U36841 Genomic DNA Translation: AAA79828.1
    U00096 Genomic DNA Translation: AAC75619.1
    AP009048 Genomic DNA Translation: BAE76742.1
    X02673 Genomic DNA Translation: CAA26505.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S44713 RGECGT

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417061.1, NC_000913.3
    WP_000020749.1, NZ_STEB01000011.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75619; AAC75619; b2566
    BAE76742; BAE76742; BAE76742

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947036

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2550
    eco:b2566

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4168

    <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
    M14658 Unassigned DNA Translation: AAA03242.1
    D64044 Genomic DNA Translation: BAA10913.1
    U36841 Genomic DNA Translation: AAA79828.1
    U00096 Genomic DNA Translation: AAC75619.1
    AP009048 Genomic DNA Translation: BAE76742.1
    X02673 Genomic DNA Translation: CAA26505.1
    PIRiS44713 RGECGT
    RefSeqiNP_417061.1, NC_000913.3
    WP_000020749.1, NZ_STEB01000011.1

    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
    1EGAX-ray2.40A/B1-301[»]
    3IEUX-ray2.80A/B1-301[»]
    SMRiP06616
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4263220, 465 interactors
    851375, 7 interactors
    DIPiDIP-9521N
    IntActiP06616, 29 interactors
    STRINGi511145.b2566

    PTM databases

    iPTMnetiP06616

    Proteomic databases

    jPOSTiP06616
    PaxDbiP06616
    PRIDEiP06616

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75619; AAC75619; b2566
    BAE76742; BAE76742; BAE76742
    GeneIDi947036
    KEGGiecj:JW2550
    eco:b2566
    PATRICifig|1411691.4.peg.4168

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0266
    EcoGeneiEG10270 era

    Phylogenomic databases

    eggNOGiENOG4105CWT Bacteria
    COG1159 LUCA
    HOGENOMiHOG000245597
    InParanoidiP06616
    KOiK03595
    PhylomeDBiP06616

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10270-MONOMER
    ECOL316407:JW2550-MONOMER
    MetaCyc:EG10270-MONOMER
    SABIO-RKiP06616

    Miscellaneous databases

    EvolutionaryTraceiP06616

    Protein Ontology

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    PROi
    PR:P06616

    Family and domain databases

    CDDicd04163 Era, 1 hit
    Gene3Di3.30.300.20, 1 hit
    HAMAPiMF_00367 GTPase_Era, 1 hit
    InterProiView protein in InterPro
    IPR030388 G_ERA_dom
    IPR005662 GTP-bd_Era
    IPR006073 GTP_binding_domain
    IPR015946 KH_dom-like_a/b
    IPR004044 KH_dom_type_2
    IPR009019 KH_sf_prok-type
    IPR027417 P-loop_NTPase
    IPR005225 Small_GTP-bd_dom
    PfamiView protein in Pfam
    PF07650 KH_2, 1 hit
    PF01926 MMR_HSR1, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    SSF54814 SSF54814, 1 hit
    TIGRFAMsiTIGR00436 era, 1 hit
    TIGR00231 small_GTP, 1 hit
    PROSITEiView protein in PROSITE
    PS51713 G_ERA, 1 hit
    PS50823 KH_TYPE_2, 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 nameiERA_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: P06616
    Secondary accession number(s): Q2MAG4
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: February 1, 1994
    Last modified: September 18, 2019
    This is version 189 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

    3D-structure, Complete proteome, 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
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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