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Entry version 160 (02 Jun 2021)
Sequence version 1 (01 Nov 1995)
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Protein

GTPase ObgE/CgtA

Gene

obgE

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 abundant, essential GTPase which binds GTP, GDP and ppGpp with moderate affinity. Has high guanosine nucleotide exchange rate constants for GTP and GDP, and a relatively low GTP hydrolysis rate stimulated by the 50S ribosomal subunit. It is estimated there are 34000 molecules in log-phase cells and 5600 molecules in stationary-phase cells. Required for chromosome segregation. Plays a role in the stringent response, perhaps by sequestering 50S ribosomal subunits and decreasing protein synthesis (PubMed:19555460), and a non-essential role in the late steps of ribosome biogenesis, perhaps acting as a checkpoint for correct 50S subunit synthesis (Probable) (PubMed:24844575).

Overexpression increases bacterial persistence (in exponential and stationary phase) in response to antibiotics (PubMed:26051177).

Cells expressing high levels of Obg are more likely to form persister cells upon antibiotic exposure; this requires alarmone (p)ppGpp and acts via induced HokB, depolarizing cells, which probably reduces metabolic activity and induces persistence (PubMed:26051177).

The persister phenotype can be separated from the essential phenotype (PubMed:26051177).

1 Publication9 Publications

Required for correct chromosome partitioning; in temperature-sensitive (ts) mutant nucleoids do not partition but remain in the middle of cell, cells elongate but do not divide. Overexpression protects cells against UV damage. Ts mutants have impaired plasmid and lamdba phage replication, possibly via effects on DnaA (PubMed:12826057).

Regulates DnaA levels. Genetic interactions of Val-168 and a C-terminal insertion mutant with the double-strand break repair factors recA and recBCD, and with seqA suggests that ObgE, either directly or indirectly, promotes replication fork stability (PubMed:15721258).

May protect replication forks from stress induced by toxic levels of hydroxyl radicals (PubMed:22863262).

Initiation of DNA replication continues in ObgE-depleted cells.

8 Publications

Binds to pre-50S ribosomal subunits in a salt-dependent manner. Acts as a ribosome anti-association factor; guanosine nucleotides stimulate ObgE 50S subunit binding and also ObgE-mediated 70S ribosome dissociation (GDP<GTP<GMP-PNP<ppGpp) (PubMed:24844575).

Overexpression rescues an rrmJ deletion stabilizing the 70S ribosome. Even at permissive temperatures the ts mutant (Gln-80/Asn-85) shows disrupted 50S ribosomal subunit assembly, defects in 16 and 23S rRNA processing and altered association of some late-assembling ribosomal proteins (PubMed:11555285).

Dissociates from the pre-50S ribosome under conditions of amino acid starvation. The levels of (p)ppGpp rise in the ts mutant (Gln-80/Asn-85), possibly because ObgE controls SpoT. Binds GDP and ppGpp with the same affinity. During ribosome assembly ObgE acts later than the rRNA methyltransferase RrmJ and DEAD-box RNA helicases DeaD and SrmB.

8 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

Mg2+UniRule annotation1 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

Turnover number of 0.02/min.
  1. KM=18 µM for GTP (at 37 degrees Celsius2 Publications
  2. KM=7.9 µM for GTP (at 30 degrees Celsius2 Publications

    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 bindingi173MagnesiumUniRule annotation1
    Metal bindingi193MagnesiumUniRule 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 bindingi166 – 173GTPUniRule annotation8
    Nucleotide bindingi191 – 195GTPUniRule annotation5
    Nucleotide bindingi213 – 216GTPUniRule annotation4
    Nucleotide bindingi283 – 286GTPUniRule annotation4
    Nucleotide bindingi314 – 316GTPUniRule annotation3

    <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 functionDNA-binding, Hydrolase, RNA-binding, rRNA-binding
    LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G7656-MONOMER

    <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:
    GTPase ObgE/CgtAUniRule annotation (EC:3.6.5.-UniRule annotation1 Publication)
    Alternative name(s):
    GTP-binding protein ObgUniRule 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:obgE1 Publication
    Synonyms:cgtA1 Publication, obgUniRule annotation, yhbZ
    Ordered Locus Names:b3183, JW3150
    <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

    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

    Essential for growth, it cannot be disrupted.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi27 – 31KYIPK → EYIPE: Almost abolishes 50S subunit binding. 1 Publication5
    Mutagenesisi76 – 82RDCTGKR → GDCTGKG: Slight reduction in 50S subunit binding. 1 Publication7
    Mutagenesisi80G → E: Temperature-sensitive for growth at 42 degrees Celsius, defects in chromosome partitioning; when associated with N-85. 1 Publication1
    Mutagenesisi85D → N: Temperature-sensitive for growth at 42 degrees Celsius, defects in chromosome partitioning; when associated with E-80. 1 Publication1
    Mutagenesisi93G → D: No effect on persister cell formation upon overexpression. 1 Publication1
    Mutagenesisi136 – 139RTPR → GTPG: Almost abolishes 50S subunit binding. 1 Publication4
    Mutagenesisi159L → Q: Increased sensitivity to HU upon overexpression, supports normal growth, no effect in mazEF/relBE or tonB deletions. 1 Publication1
    Mutagenesisi163G → V: Increased sensitivity to HU upon overexpression, supports normal growth, no effect in mazEF/relBE or tonB deletions. 1 Publication1
    Mutagenesisi166G → V: No increase in persister cells upon overexpression, does not induce hokB expression, supports normal growth. 1 Publication1
    Mutagenesisi168P → V: Increased sensitivity to HU upon overexpression, supports normal growth, no effect in mazEF/relBE or tonB deletions. No effect on persister cell formation upon overexpression. 3 Publications1
    Mutagenesisi173S → N: No effect on persister cell formation upon overexpression. 1 Publication1
    Mutagenesisi193T → A: No effect on persister cell formation upon overexpression. 1 Publication1
    Mutagenesisi216G → A: Increased sensitivity to HU upon overexpression, supports normal growth, no effect in mazEF/relBE or tonB deletions. No effect on persister cell formation upon overexpression. 2 Publications1
    Mutagenesisi237R → C: Increased sensitivity to HU upon overexpression, supports normal growth, no effect in mazEF/relBE or tonB deletions. 1 Publication1
    Mutagenesisi314S → P: Severe growth defect at 42 degrees Celsius. Decreased levels of some ribosomal proteins, altered PTMs of others. 1 Publication1

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002054331 – 390GTPase ObgE/CgtAAdd BLAST390

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P42641

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

    More...
    PaxDbi
    P42641

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P42641

    <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

    Constitutively expressed, levels decrease toward stationary phase (at protein level). Induced in a dose-dependent manner by UV irradiation.2 Publications

    <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. Binds to the intersubunit face of the 50S ribosomal subunit where translation factors bind, protruding into the peptidyl-transfer center, leading to significant changes in both ObgE and 50S ribosome structure (PubMed:24844575). Associates with SpoT (PubMed:15292126, PubMed:17616600). Binding to 50S ribosomes does not require SpoT. 50S ribosomal subunit binding is enhanced by guanosine nucleotides (PubMed:24844575).

    5 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
    4261647, 163 interactors
    852007, 1 interactor

    Database of interacting proteins

    More...
    DIPi
    DIP-12273N

    Protein interaction database and analysis system

    More...
    IntActi
    P42641, 28 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b3183

    <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

    1390
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Small Angle Scattering Biological Data Bank

    More...
    SASBDBi
    P42641

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

    More...
    SMRi
    P42641

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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>Domaini1 – 159ObgPROSITE-ProRule annotationAdd BLAST159
    Domaini160 – 333OBG-type GUniRule annotationAdd BLAST174

    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>Regioni127 – 147DisorderedSequence analysisAdd BLAST21
    Regioni341 – 390Not required for 50S ribosome subunit association nor 70S dissociation1 PublicationAdd BLAST50
    Regioni360 – 390Not essential, but deletion increases sensitivity to DNA replication inhibitor hydroxyurea (HU)1 PublicationAdd BLAST31

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi128 – 142Polar residuesSequence analysisAdd BLAST15

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

    The C-terminus (residues 341-390) is not required for either 50S ribosome subunit association nor 70S ribosome dissociation.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 OBG-HflX-like GTPase superfamily. OBG GTPase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0536, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_011747_2_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P42641

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P42641

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01898, Obg, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.70.210.12, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01454, GTPase_Obg, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR031167, G_OBG
    IPR006073, GTP-bd
    IPR035101, GTP-bd_Obg
    IPR014100, GTP-bd_Obg/CgtA
    IPR006074, GTP1-OBG_CS
    IPR006169, GTP1_OBG_dom
    IPR036726, GTP1_OBG_dom_sf
    IPR027417, P-loop_NTPase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01018, GTP1_OBG, 1 hit
    PF01926, MMR_HSR1, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF002401, GTP_bd_Obg/CgtA, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00326, GTP1OBG

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540, SSF52540, 1 hit
    SSF82051, SSF82051, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02729, Obg_CgtA, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51710, G_OBG, 1 hit
    PS00905, GTP1_OBG, 1 hit
    PS51883, OBG, 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.

    P42641-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKFVDEASIL VVAGDGGNGC VSFRREKYIP KGGPDGGDGG DGGDVWMEAD
    60 70 80 90 100
    ENLNTLIDYR FEKSFRAERG QNGASRDCTG KRGKDVTIKV PVGTRVIDQG
    110 120 130 140 150
    TGETMGDMTK HGQRLLVAKG GWHGLGNTRF KSSVNRTPRQ KTNGTPGDKR
    160 170 180 190 200
    ELLLELMLLA DVGMLGMPNA GKSTFIRAVS AAKPKVADYP FTTLVPSLGV
    210 220 230 240 250
    VRMDNEKSFV VADIPGLIEG AAEGAGLGIR FLKHLERCRV LLHLIDIDPI
    260 270 280 290 300
    DGTDPVENAR IIISELEKYS QDLATKPRWL VFNKIDLLDK VEAEEKAKAI
    310 320 330 340 350
    AEALGWEDKY YLISAASGLG VKDLCWDVMT FIIENPVVQA EEAKQPEKVE
    360 370 380 390
    FMWDDYHRQQ LEEIAEEDDE DWDDDWDEDD EEGVEFIYKR
    Length:390
    Mass (Da):43,286
    Last modified:November 1, 1995 - v1
    <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:i3A6EBF56F24B7C47
    GO

    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
    U18997 Genomic DNA Translation: AAA57984.1
    U00096 Genomic DNA Translation: AAC76215.1
    AP009048 Genomic DNA Translation: BAE77227.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A65109

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417650.1, NC_000913.3
    WP_000673575.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76215; AAC76215; b3183
    BAE77227; BAE77227; BAE77227

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947694

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3150
    eco:b3183

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3548

    <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
    U18997 Genomic DNA Translation: AAA57984.1
    U00096 Genomic DNA Translation: AAC76215.1
    AP009048 Genomic DNA Translation: BAE77227.1
    PIRiA65109
    RefSeqiNP_417650.1, NC_000913.3
    WP_000673575.1, 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
    4CSUelectron microscopy5.5091-390[»]
    5M04X-ray1.85A1-340[»]
    SASBDBiP42641
    SMRiP42641
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4261647, 163 interactors
    852007, 1 interactor
    DIPiDIP-12273N
    IntActiP42641, 28 interactors
    STRINGi511145.b3183

    Proteomic databases

    jPOSTiP42641
    PaxDbiP42641
    PRIDEiP42641

    Genome annotation databases

    EnsemblBacteriaiAAC76215; AAC76215; b3183
    BAE77227; BAE77227; BAE77227
    GeneIDi947694
    KEGGiecj:JW3150
    eco:b3183
    PATRICifig|1411691.4.peg.3548

    Organism-specific databases

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

    More...
    EchoBASEi
    EB2647

    Phylogenomic databases

    eggNOGiCOG0536, Bacteria
    HOGENOMiCLU_011747_2_0_6
    InParanoidiP42641
    PhylomeDBiP42641

    Enzyme and pathway databases

    BioCyciEcoCyc:G7656-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P42641

    Family and domain databases

    CDDicd01898, Obg, 1 hit
    Gene3Di2.70.210.12, 1 hit
    HAMAPiMF_01454, GTPase_Obg, 1 hit
    InterProiView protein in InterPro
    IPR031167, G_OBG
    IPR006073, GTP-bd
    IPR035101, GTP-bd_Obg
    IPR014100, GTP-bd_Obg/CgtA
    IPR006074, GTP1-OBG_CS
    IPR006169, GTP1_OBG_dom
    IPR036726, GTP1_OBG_dom_sf
    IPR027417, P-loop_NTPase
    PfamiView protein in Pfam
    PF01018, GTP1_OBG, 1 hit
    PF01926, MMR_HSR1, 1 hit
    PIRSFiPIRSF002401, GTP_bd_Obg/CgtA, 1 hit
    PRINTSiPR00326, GTP1OBG
    SUPFAMiSSF52540, SSF52540, 1 hit
    SSF82051, SSF82051, 1 hit
    TIGRFAMsiTIGR02729, Obg_CgtA, 1 hit
    PROSITEiView protein in PROSITE
    PS51710, G_OBG, 1 hit
    PS00905, GTP1_OBG, 1 hit
    PS51883, OBG, 1 hit

    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 nameiOBG_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: P42641
    Secondary accession number(s): Q2M929
    <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: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: June 2, 2021
    This is version 160 of the entry and version 1 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, 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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