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Protein

Transcription termination factor Rho

Gene

rho

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Activity regulationi

ATPase activity is inhibited by bicyclomycin and dihydrobicyclomycin.1 Publication

Kineticsi

  1. KM=11 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei212ATP1
    Sitei326RNA-binding 21

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi169 – 174ATPSequence analysis6
    Nucleotide bindingi181 – 186ATP6

    GO - Molecular functioni

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

    GO - Biological processi

    Keywordsi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10845-MONOMER

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription termination factor Rho (EC:3.6.4.-)
    Alternative name(s):
    ATP-dependent helicase Rho
    Gene namesi
    Name:rho
    Synonyms:nitA, psuA, rnsC, sbaA, tsu
    Ordered Locus Names:b3783, JW3756
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10845 rho

    Subcellular locationi

    GO - Cellular componenti

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001889621 – 419Transcription termination factor RhoAdd BLAST419

    Proteomic databases

    EPDiP0AG30
    PaxDbiP0AG30
    PRIDEiP0AG30

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

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

    3D structure databases

    ProteinModelPortaliP0AG30
    SMRiP0AG30
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG30

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini48 – 123Rho RNA-BDPROSITE-ProRule annotationAdd BLAST76

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni61 – 66RNA-binding 16
    Regioni78 – 80RNA-binding 13
    Regioni108 – 110RNA-binding 13
    Regioni284 – 288RNA-binding 25

    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.

    Sequence similaritiesi

    Belongs to the Rho family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C4P Bacteria
    COG1158 LUCA
    HOGENOMiHOG000076952
    InParanoidiP0AG30
    KOiK03628
    OMAiDYNYLPG
    PhylomeDBiP0AG30

    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

    Sequencei

    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
    Checksum:i5970A85334C43467
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti411 – 419DFFEMMKRS → EVMTPTY in AAA68985 (PubMed:7828920).Curated9

    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

    Genome annotation databases

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

    Similar proteinsi

    Entry informationi

    Entry nameiRHO_ECOLI
    AccessioniPrimary (citable) accession number: P0AG30
    Secondary accession number(s): P03002, Q2M891, Q48357
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: September 12, 2018
    This is version 123 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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