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Entry version 162 (26 Feb 2020)
Sequence version 2 (15 Dec 1998)
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Protein

Small ribosomal subunit biogenesis GTPase RsgA

Gene

rsgA

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

One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late maturation steps of the functional core of the 30S ribosomal subunit (PubMed:18223068, PubMed:21102555, PubMed:21303937, PubMed:25904134, PubMed:27382067). Binds the 30S subunit contacting the head, platform, and rRNA helix 44, which may assist the last maturation stages (PubMed:21788480, PubMed:21960487). Removes RbfA from mature, but not immature 30S ribosomes in a GTP-dependent manner; 95% removal in the presence of GTP, 90% removal in GMP-PNP and 65% removal in the presence of GDP (PubMed:21102555, PubMed:25904134). Circulary permuted GTPase that catalyzes rapid hydrolysis of GTP with a slow catalytic turnover (PubMed:12220175). Dispensible for viability, but important for overall fitness. The intrinsic GTPase activity is stimulated by the presence of 30S (160-fold increase in kcat) or 70S (96-fold increase in kcat) ribosomes (PubMed:14973029). Mature 30S ribosomes stimulate intrinsic GTPase more than do immature 30S ribosomes (PubMed:25904134). Ribosome-associated GTPase activity is stimulated by RbfA (PubMed:21102555). The GTPase is inhibited by aminoglycoside antibiotics such as neomycin and paromycin (PubMed:15466596) streptomycin and spectinomycin (PubMed:15828870). This inhibition is not due to competition for binding sites on the 30S or 70S ribosome (PubMed:15828870).2 Publications6 Publications

Caution

Was initially characterized with a propeptide of 20 residues; this is now thought to be the result of in vitro proteolysis when the protein is overexpressed (PubMed:12220175, PubMed:14973029).2 Publications

<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

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

<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

Measured in the absence of 30S ribosomes, kcat is 8.1 hour(-1) for GTP, 5.2 for dATP, 3.5 for ATP, 4.5 for ITP, 7.1 for dGTP, 2.1 for CTP.1 Publication
  1. KM=0.41 mM for GTP1 Publication
  2. KM=1.0 mM for dATP1 Publication
  3. KM=1.2 mM for ATP1 Publication
  4. KM=1.3 mM for ITP1 Publication
  5. KM=1.6 mM for dGTP1 Publication
  6. KM=2.4 mM for CTP1 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 bindingi297ZincUniRule annotation1
    Metal bindingi302ZincUniRule annotation1
    Metal bindingi304Zinc; via pros nitrogenUniRule annotation1
    Metal bindingi310ZincUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi160 – 163GTPUniRule annotation4
    Nucleotide bindingi214 – 222GTPUniRule annotation9

    <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

    • ribosomal small subunit biogenesis Source: EcoCyc

    <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 functionHydrolase, RNA-binding, rRNA-binding
    Biological processRibosome biogenesis
    LigandGTP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G7841-MONOMER
    ECOL316407:JW4122-MONOMER
    MetaCyc:G7841-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P39286

    <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:
    Small ribosomal subunit biogenesis GTPase RsgAUniRule annotation (EC:3.6.1.-UniRule 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:rsgA1 PublicationUniRule annotation
    Synonyms:engC, yjeQ
    Ordered Locus Names:b4161, JW4122
    <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

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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

    Reduced growth rate, reduced 70S ribosomes, accumulation of 17S rRNA (the precursor of 16S rRNA) (PubMed:15466596, PubMed:21303937, PubMed:25904134, PubMed:27382067). Ribosomal proteins S2 and S21 not found in 30S subunits, decreased S3 and RbfA in 30S subunits, distortion of rRNA helix 44 near the decoding center (PubMed:21303937, PubMed:27382067). The phenotype is partially suppressed by overexpression of a number of genes involved in ribosome function, including infB, era and ksgA (PubMed:15466596). Double rbfA-rsgA deletion mutants have the same phenotype as single mutants (PubMed:21102555). Single rgsA deletion is suppressed by a number of mutants in RbfA but not by wild-type RbfA; in all the RbfA mutants less RbfA is found bound to the 30S ribosome (PubMed:21102555).5 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>Mutagenesisi1 – 20Missing : Loss of GMP-PNP-dependent association with 30S ribosomal subunit, increased association with 50S and 70S ribosomes. 1 PublicationAdd BLAST20
    Mutagenesisi220K → A: Reduction in GTPase activity, 38% of wild-type kcat for GTP. Strong reduction, 5.2% of wild-type kcat for GTP; when associated with A-221. 1 Publication1
    Mutagenesisi221S → A: Reduction in GTPase activity, 22% of wild-type kcat for GTP. GTPase activity not stimulated by 30S ribosomes (PubMed:14973029). Strong reduction, 5.2% of wild-type kcat for GTP; when associated with A-220. 2 Publications1
    Mutagenesisi250T → A: Loss of GTPase activity, does not dissociate RbfA. 1 Publication1
    Mutagenesisi298 – 300KYR → AYA: About 2-fold decreased binding to mature and immature 30S ribosomes, GTPase activity stimulated by ribosomes. 1 Publication3
    Mutagenesisi320 – 350Missing : Slightly increased specific binding to mature and immature 30S ribosomes, GTPase activity not stimulated by ribosomes. No longer removes RbfA from mature 30S ribosomes, increases RbfA-binding about 5-fold. Does not complement a deletion mutant in vivo, fewer 70S ribosomes, slower growth than deletion mutant. 1 PublicationAdd BLAST31

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000081491 – 350Small ribosomal subunit biogenesis GTPase RsgAAdd BLAST350

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P39286

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P39286

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

    More...
    PaxDbi
    P39286

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P39286

    <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

    Monomer (Probable). All of the protein is associated with ribosomes; the ratio is substoichiometric at 1:200 RsgA/ribosome (PubMed:14973029). Association is tightest with the 30S subunit in the presence of the non-hydrolyzable GTP analog GMP-PNP (PubMed:14973029, PubMed:15466596). 2 cryoelectron microscopy (cryo-EM) structures in complex with 30S ribosomes have been resolved; the protein is determined to bind to different but partially overlapping regions of the 30S ribosomal subunit (PubMed:21788480, PubMed:21960487). One cryo-EM study suggests it contacts ribosomal proteins S3, S12 and S13 as well as 16S rRNA (PubMed:21788480). Another cryo-EM study shows it to bind 16S rRNA, no ribosomal proteins, and to cover the sites of intersubunit bridges B2a, B3 and B7a (PubMed:21960487). Has a significant preference for mature versus immature 30S ribosomes in the presence of GMP-PNP (PubMed:21102555, PubMed:27382067). Another study shows it binds equally well to mature and immature 30S ribosomal subunits in the presence of GMP-PNP (PubMed:25904134).

    1 Publication7 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4261080, 609 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-12581N

    Protein interaction database and analysis system

    More...
    IntActi
    P39286, 33 interactors

    Molecular INTeraction database

    More...
    MINTi
    P39286

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b4161

    <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
    P39286

    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
    P39286

    <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>Domaini104 – 273CP-type GAdd BLAST170

    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>Regioni1 – 113Necessary for association with the ribosome and for stimulation of GTPase activity by 30S ribosomes1 PublicationAdd BLAST113
    Regioni1 – 20Necessary for GMP-PNP-dependent association with the 30S ribosomal subunit2 Publications1 PublicationAdd BLAST20
    Regioni287 – 319Required for binding to mature and immature 30S ribosomes1 PublicationAdd BLAST33
    Regioni320 – 350Required to remove RbfA from mature 30S ribosomes1 PublicationAdd BLAST31

    <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

    Has 3 domains; an N-terminal OB-like domain (about residues 1-100), a central, circularly permutated GTPase module (residues 104-270) and the C-terminal zinc-finger domain (residues 280 to 350) (PubMed:25904134). The C-terminal domain has 2 regions; the zinc-binding domain (residues 287-319) is required for binding to 30S ribosomes while the extreme C-terminus (residues 320-350) helps remove RbfA from the mature 30S subunit.1 Publication

    <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 TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105E06 Bacteria
    COG1162 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_033617_2_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P39286

    KEGG Orthology (KO)

    More...
    KOi
    K06949

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P39286

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01854 YjeQ_EngC, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01820 GTPase_RsgA, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR030378 G_CP_dom
    IPR027417 P-loop_NTPase
    IPR004881 Ribosome_biogen_GTPase_RsgA
    IPR010914 RsgA_GTPase_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR32120 PTHR32120, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03193 RsgA_GTPase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540 SSF52540, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00157 TIGR00157, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50936 ENGC_GTPASE, 1 hit
    PS51721 G_CP, 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.

    P39286-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSKNKLSKGQ QRRVNANHQR RLKTSKEKPD YDDNLFGEPD EGIVISRFGM
    60 70 80 90 100
    HADVESADGD VHRCNIRRTI RSLVTGDRVV WRPGKPAAEG VNVKGIVEAV
    110 120 130 140 150
    HERTSVLTRP DFYDGVKPIA ANIDQIVIVS AILPELSLNI IDRYLVACET
    160 170 180 190 200
    LQIEPIIVLN KIDLLDDEGM AFVNEQMDIY RNIGYRVLMV SSHTQDGLKP
    210 220 230 240 250
    LEEALTGRIS IFAGQSGVGK SSLLNALLGL QKEILTNDIS DNSGLGQHTT
    260 270 280 290 300
    TAARLYHFPH GGDVIDSPGV REFGLWHLEP EQITQGFVEF HDYLGLCKYR
    310 320 330 340 350
    DCKHDTDPGC AIREAVEEGK IAETRFENYH RILESMAQVK TRKNFSDTDD
    Length:350
    Mass (Da):39,193
    Last modified:December 15, 1998 - 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:iDEB14E36D2F0F378
    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 AAA97060 differs from that shown. Reason: Erroneous initiation. Truncated 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
    U14003 Genomic DNA Translation: AAA97060.1 Different initiation.
    U00096 Genomic DNA Translation: AAC77121.2
    AP009048 Genomic DNA Translation: BAE78165.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S56389

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418585.4, NC_000913.3
    WP_000041964.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC77121; AAC77121; b4161
    BAE78165; BAE78165; BAE78165

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948674

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW4122
    eco:b4161

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2537

    <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
    U14003 Genomic DNA Translation: AAA97060.1 Different initiation.
    U00096 Genomic DNA Translation: AAC77121.2
    AP009048 Genomic DNA Translation: BAE78165.1
    PIRiS56389
    RefSeqiNP_418585.4, NC_000913.3
    WP_000041964.1, 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
    2YKRelectron microscopy9.80W1-350[»]
    4A2Ielectron microscopy16.50V35-337[»]
    5NO2electron microscopy5.16Z34-346[»]
    5NO3electron microscopy5.16Z34-346[»]
    5NO4electron microscopy5.16Z34-346[»]
    5UZ4electron microscopy5.80Z6-339[»]
    SMRiP39286
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4261080, 609 interactors
    DIPiDIP-12581N
    IntActiP39286, 33 interactors
    MINTiP39286
    STRINGi511145.b4161

    Proteomic databases

    EPDiP39286
    jPOSTiP39286
    PaxDbiP39286
    PRIDEiP39286

    Genome annotation databases

    EnsemblBacteriaiAAC77121; AAC77121; b4161
    BAE78165; BAE78165; BAE78165
    GeneIDi948674
    KEGGiecj:JW4122
    eco:b4161
    PATRICifig|1411691.4.peg.2537

    Organism-specific databases

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

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    EchoBASEi
    EB2372

    Phylogenomic databases

    eggNOGiENOG4105E06 Bacteria
    COG1162 LUCA
    HOGENOMiCLU_033617_2_0_6
    InParanoidiP39286
    KOiK06949
    PhylomeDBiP39286

    Enzyme and pathway databases

    BioCyciEcoCyc:G7841-MONOMER
    ECOL316407:JW4122-MONOMER
    MetaCyc:G7841-MONOMER
    SABIO-RKiP39286

    Miscellaneous databases

    EvolutionaryTraceiP39286

    Protein Ontology

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    PROi
    PR:P39286

    Family and domain databases

    CDDicd01854 YjeQ_EngC, 1 hit
    HAMAPiMF_01820 GTPase_RsgA, 1 hit
    InterProiView protein in InterPro
    IPR030378 G_CP_dom
    IPR027417 P-loop_NTPase
    IPR004881 Ribosome_biogen_GTPase_RsgA
    IPR010914 RsgA_GTPase_dom
    PANTHERiPTHR32120 PTHR32120, 1 hit
    PfamiView protein in Pfam
    PF03193 RsgA_GTPase, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    TIGRFAMsiTIGR00157 TIGR00157, 1 hit
    PROSITEiView protein in PROSITE
    PS50936 ENGC_GTPASE, 1 hit
    PS51721 G_CP, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    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 nameiRSGA_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: P39286
    Secondary accession number(s): Q2M6E1
    <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: February 1, 1995
    Last sequence update: December 15, 1998
    Last modified: February 26, 2020
    This is version 162 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, 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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