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Protein

Transcription termination factor Rho

Gene

rho

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

Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPase which utilizes all four ribonucleoside triphosphates as substrates.2 Publications

<p>This subsection of the ‘Function’ 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

ATPase activity is inhibited by bicyclomycin and dihydrobicyclomycin.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=11 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei212ATP1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei326RNA-binding 21

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi169 – 174ATPSequence analysis6
    Nucleotide bindingi181 – 186ATP6

    <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

    • ATP binding Source: UniProtKB-UniRule
    • helicase activity Source: UniProtKB-UniRule
    • identical protein binding Source: IntAct
    • RNA binding Source: EcoCyc
    • RNA-dependent ATPase activity Source: InterPro

    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 functionHelicase, Hydrolase, RNA-binding
    Biological processTranscription, Transcription regulation, Transcription termination
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG10845-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_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:
    Transcription termination factor Rho (EC:3.6.4.-)
    Alternative name(s):
    ATP-dependent helicase Rho
    <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:rho
    Synonyms:nitA, psuA, rnsC, sbaA, tsu
    Ordered Locus Names:b3783, JW3756
    <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
    EG10845 rho

    <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

    <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

    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>Mutagenesisi62F → L or A: Defective for RNA-binding. 1 Publication1
    Mutagenesisi64F → L or A: Defective for RNA-binding. 1 Publication1
    Mutagenesisi181K → Q: Partial loss of ATPase, helicase and termination activity. 1 Publication1
    Mutagenesisi184K → Q: Improves ATPase and helicase activity but reduced termination activity. 1 Publication1
    Mutagenesisi202C → G or S: Does not affect the kinetics of ATP hydrolysis and inhibition by bicyclomycin. 1 Publication1
    Mutagenesisi265D → N: Loss of ATPase activity, helicase and termination activity. 1 Publication1

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001889621 – 419Transcription termination factor RhoAdd BLAST419

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0AG30

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0AG30

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

    More...
    PaxDbi
    P0AG30

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0AG30

    <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

    Homohexamer. The homohexamer assembles into an open ring structure.5 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-35363N

    Protein interaction database and analysis system

    More...
    IntActi
    P0AG30, 67 interactors

    Molecular INTeraction database

    More...
    MINTi
    P0AG30

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_3972

    <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

    1419
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1A62X-ray1.55A1-130[»]
    1A63NMR-A1-130[»]
    1A8VX-ray2.00A/B1-118[»]
    1PV4X-ray3.00A/B/C/D/E/F1-419[»]
    1PVOX-ray3.00A/B/C/D/E/F1-419[»]
    1XPOX-ray3.15A/B/C/D/E/F1-419[»]
    1XPRX-ray3.15A/B/C/D/E/F1-419[»]
    1XPUX-ray3.05A/B/C/D/E/F1-419[»]
    2A8VX-ray2.40A/B/C1-118[»]
    2HT1X-ray3.51A/B1-411[»]
    3ICEX-ray2.80A/B/C/D/E/F1-419[»]
    5JJIX-ray2.60A/B/C/D/E/F2-417[»]
    5JJKX-ray3.15A/B/C/D/E/F2-417[»]
    5JJLX-ray3.20A/B/C/D/E/F2-417[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P0AG30

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

    More...
    SMRi
    P0AG30

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0AG30

    <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>Domaini48 – 123Rho RNA-BDPROSITE-ProRule annotationAdd BLAST76

    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>Regioni61 – 66RNA-binding 16
    Regioni78 – 80RNA-binding 13
    Regioni108 – 110RNA-binding 13
    Regioni284 – 288RNA-binding 25

    <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

    Each subunit has two RNA-binding sites, one at the surface of the hexameric ring, and one at the center of the open ring structure, where RNA helicase activity is thought to take place.

    <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 Rho family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C4P Bacteria
    COG1158 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000076952

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0AG30

    KEGG Orthology (KO)

    More...
    KOi
    K03628

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0AG30

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd04459 Rho_CSD, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01884 Rho, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003593 AAA+_ATPase
    IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
    IPR011129 CSD
    IPR012340 NA-bd_OB-fold
    IPR027417 P-loop_NTPase
    IPR011112 Rho_N
    IPR036269 Rho_N_sf
    IPR011113 Rho_RNA-bd
    IPR004665 Term_rho

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR15184:SF34 PTHR15184:SF34, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00006 ATP-synt_ab, 1 hit
    PF07498 Rho_N, 1 hit
    PF07497 Rho_RNA_bind, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00382 AAA, 1 hit
    SM00357 CSP, 1 hit
    SM00959 Rho_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50249 SSF50249, 1 hit
    SSF52540 SSF52540, 1 hit
    SSF68912 SSF68912, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00767 rho, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51856 RHO_RNA_BD, 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>.<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.

    P0AG30-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNLTELKNTP VSELITLGEN MGLENLARMR KQDIIFAILK QHAKSGEDIF
    60 70 80 90 100
    GDGVLEILQD GFGFLRSADS SYLAGPDDIY VSPSQIRRFN LRTGDTISGK
    110 120 130 140 150
    IRPPKEGERY FALLKVNEVN FDKPENARNK ILFENLTPLH ANSRLRMERG
    160 170 180 190 200
    NGSTEDLTAR VLDLASPIGR GQRGLIVAPP KAGKTMLLQN IAQSIAYNHP
    210 220 230 240 250
    DCVLMVLLID ERPEEVTEMQ RLVKGEVVAS TFDEPASRHV QVAEMVIEKA
    260 270 280 290 300
    KRLVEHKKDV IILLDSITRL ARAYNTVVPA SGKVLTGGVD ANALHRPKRF
    310 320 330 340 350
    FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELHLSRKIA
    360 370 380 390 400
    EKRVFPAIDY NRSGTRKEEL LTTQEELQKM WILRKIIHPM GEIDAMEFLI
    410
    NKLAMTKTND DFFEMMKRS
    Length:419
    Mass (Da):47,004
    Last modified:July 21, 1986 - 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:i5970A85334C43467
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti411 – 419DFFEMMKRS → EVMTPTY in AAA68985 (PubMed:7828920).Curated9

    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
    J01673 Genomic DNA Translation: AAA24532.1
    M87049 Genomic DNA Translation: AAA67583.1
    U00096 Genomic DNA Translation: AAC76788.1
    AP009048 Genomic DNA Translation: BAE77515.1
    M12779 Genomic DNA Translation: AAA24695.1
    S75640 Genomic DNA Translation: AAB20841.1
    L34404 Genomic DNA Translation: AAA68985.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A03530 TWECR

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418230.1, NC_000913.3
    WP_001054527.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76788; AAC76788; b3783
    BAE77515; BAE77515; BAE77515

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948297

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3756
    eco:b3783

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|511145.12.peg.3898

    <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
    J01673 Genomic DNA Translation: AAA24532.1
    M87049 Genomic DNA Translation: AAA67583.1
    U00096 Genomic DNA Translation: AAC76788.1
    AP009048 Genomic DNA Translation: BAE77515.1
    M12779 Genomic DNA Translation: AAA24695.1
    S75640 Genomic DNA Translation: AAB20841.1
    L34404 Genomic DNA Translation: AAA68985.1
    PIRiA03530 TWECR
    RefSeqiNP_418230.1, NC_000913.3
    WP_001054527.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A62X-ray1.55A1-130[»]
    1A63NMR-A1-130[»]
    1A8VX-ray2.00A/B1-118[»]
    1PV4X-ray3.00A/B/C/D/E/F1-419[»]
    1PVOX-ray3.00A/B/C/D/E/F1-419[»]
    1XPOX-ray3.15A/B/C/D/E/F1-419[»]
    1XPRX-ray3.15A/B/C/D/E/F1-419[»]
    1XPUX-ray3.05A/B/C/D/E/F1-419[»]
    2A8VX-ray2.40A/B/C1-118[»]
    2HT1X-ray3.51A/B1-411[»]
    3ICEX-ray2.80A/B/C/D/E/F1-419[»]
    5JJIX-ray2.60A/B/C/D/E/F2-417[»]
    5JJKX-ray3.15A/B/C/D/E/F2-417[»]
    5JJLX-ray3.20A/B/C/D/E/F2-417[»]
    ProteinModelPortaliP0AG30
    SMRiP0AG30
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-35363N
    IntActiP0AG30, 67 interactors
    MINTiP0AG30
    STRINGi316385.ECDH10B_3972

    Proteomic databases

    EPDiP0AG30
    jPOSTiP0AG30
    PaxDbiP0AG30
    PRIDEiP0AG30

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76788; AAC76788; b3783
    BAE77515; BAE77515; BAE77515
    GeneIDi948297
    KEGGiecj:JW3756
    eco:b3783
    PATRICifig|511145.12.peg.3898

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0838
    EcoGeneiEG10845 rho

    Phylogenomic databases

    eggNOGiENOG4105C4P Bacteria
    COG1158 LUCA
    HOGENOMiHOG000076952
    InParanoidiP0AG30
    KOiK03628
    PhylomeDBiP0AG30

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10845-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP0AG30

    Protein Ontology

    More...
    PROi
    PR:P0AG30

    Family and domain databases

    CDDicd04459 Rho_CSD, 1 hit
    HAMAPiMF_01884 Rho, 1 hit
    InterProiView protein in InterPro
    IPR003593 AAA+_ATPase
    IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
    IPR011129 CSD
    IPR012340 NA-bd_OB-fold
    IPR027417 P-loop_NTPase
    IPR011112 Rho_N
    IPR036269 Rho_N_sf
    IPR011113 Rho_RNA-bd
    IPR004665 Term_rho
    PANTHERiPTHR15184:SF34 PTHR15184:SF34, 1 hit
    PfamiView protein in Pfam
    PF00006 ATP-synt_ab, 1 hit
    PF07498 Rho_N, 1 hit
    PF07497 Rho_RNA_bind, 1 hit
    SMARTiView protein in SMART
    SM00382 AAA, 1 hit
    SM00357 CSP, 1 hit
    SM00959 Rho_N, 1 hit
    SUPFAMiSSF50249 SSF50249, 1 hit
    SSF52540 SSF52540, 1 hit
    SSF68912 SSF68912, 1 hit
    TIGRFAMsiTIGR00767 rho, 1 hit
    PROSITEiView protein in PROSITE
    PS51856 RHO_RNA_BD, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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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 nameiRHO_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: P0AG30
    Secondary accession number(s): P03002, Q2M891, Q48357
    <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: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: January 16, 2019
    This is version 126 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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