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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-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

Enzyme 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-HAMAP
    • helicase activity Source: UniProtKB-HAMAP
    • RNA binding Source: EcoCyc
    • RNA-dependent ATPase activity Source: InterPro

    GO - Biological processi

    • DNA-templated transcription, termination Source: EcoCyc
    • regulation of transcription, DNA-templated Source: UniProtKB-KW
    • transcription, DNA-templated Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Transcription, Transcription regulation, Transcription termination

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10845-MONOMER.
    ECOL316407:JW3756-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

    • cytosol Source: EcoCyc
    • membrane Source: UniProtKB
    Complete GO annotation...

    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

    WithEntry#Exp.IntActNotes
    itself3EBI-545468,EBI-545468
    gssP0AES04EBI-545468,EBI-557080
    hfqP0A6X34EBI-545468,EBI-547637
    nusGP0AFG06EBI-545468,EBI-369628
    rofP0AFW82EBI-545468,EBI-1114609

    Protein-protein interaction databases

    DIPiDIP-35363N.
    IntActiP0AG30. 64 interactors.
    MINTiMINT-1222551.
    STRINGi511145.b3783.

    Structurei

    Secondary structure

    1419
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 7Combined sources5
    Helixi11 – 19Combined sources9
    Turni20 – 22Combined sources3
    Helixi26 – 28Combined sources3
    Helixi31 – 44Combined sources14
    Beta strandi49 – 57Combined sources9
    Beta strandi59 – 61Combined sources3
    Beta strandi63 – 66Combined sources4
    Helixi68 – 70Combined sources3
    Helixi75 – 77Combined sources3
    Beta strandi79 – 81Combined sources3
    Helixi83 – 88Combined sources6
    Beta strandi96 – 102Combined sources7
    Beta strandi105 – 107Combined sources3
    Beta strandi110 – 119Combined sources10
    Helixi124 – 127Combined sources4
    Turni133 – 135Combined sources3
    Beta strandi138 – 140Combined sources3
    Beta strandi142 – 144Combined sources3
    Helixi156 – 165Combined sources10
    Beta strandi169 – 171Combined sources3
    Beta strandi173 – 177Combined sources5
    Beta strandi180 – 183Combined sources4
    Helixi184 – 198Combined sources15
    Beta strandi202 – 211Combined sources10
    Helixi213 – 220Combined sources8
    Beta strandi224 – 230Combined sources7
    Helixi236 – 255Combined sources20
    Beta strandi259 – 265Combined sources7
    Helixi267 – 277Combined sources11
    Beta strandi286 – 288Combined sources3
    Helixi291 – 301Combined sources11
    Beta strandi305 – 310Combined sources6
    Beta strandi312 – 319Combined sources8
    Beta strandi322 – 324Combined sources3
    Helixi326 – 338Combined sources13
    Beta strandi340 – 345Combined sources6
    Helixi347 – 351Combined sources5
    Turni360 – 362Combined sources3
    Beta strandi364 – 367Combined sources4
    Helixi368 – 370Combined sources3
    Helixi374 – 387Combined sources14
    Helixi392 – 401Combined sources10
    Turni402 – 405Combined sources4
    Helixi408 – 414Combined sources7

    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[»]
    ProteinModelPortaliP0AG30.
    SMRiP0AG30.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG30.

    Family & Domainsi

    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.
    OMAiFLRAPDY.
    PhylomeDBiP0AG30.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_01884. Rho. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR011129. Cold_shock_prot.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    IPR011112. Rho_N.
    IPR011113. Rho_RNA-bd.
    IPR004665. Term_rho.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF07498. Rho_N. 1 hit.
    PF07497. Rho_RNA_bind. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00357. CSP. 1 hit.
    SM00959. Rho_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF68912. SSF68912. 1 hit.
    TIGRFAMsiTIGR00767. rho. 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.
    PATRICi32123057. VBIEscCol129921_3898.

    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[»]
    ProteinModelPortaliP0AG30.
    SMRiP0AG30.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-35363N.
    IntActiP0AG30. 64 interactors.
    MINTiMINT-1222551.
    STRINGi511145.b3783.

    Proteomic databases

    EPDiP0AG30.
    PaxDbiP0AG30.
    PRIDEiP0AG30.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76788; AAC76788; b3783.
    BAE77515; BAE77515; BAE77515.
    GeneIDi948297.
    KEGGiecj:JW3756.
    eco:b3783.
    PATRICi32123057. VBIEscCol129921_3898.

    Organism-specific databases

    EchoBASEiEB0838.
    EcoGeneiEG10845. rho.

    Phylogenomic databases

    eggNOGiENOG4105C4P. Bacteria.
    COG1158. LUCA.
    HOGENOMiHOG000076952.
    InParanoidiP0AG30.
    KOiK03628.
    OMAiFLRAPDY.
    PhylomeDBiP0AG30.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10845-MONOMER.
    ECOL316407:JW3756-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0AG30.
    PROiP0AG30.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_01884. Rho. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR011129. Cold_shock_prot.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    IPR011112. Rho_N.
    IPR011113. Rho_RNA-bd.
    IPR004665. Term_rho.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF07498. Rho_N. 1 hit.
    PF07497. Rho_RNA_bind. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00357. CSP. 1 hit.
    SM00959. Rho_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF68912. SSF68912. 1 hit.
    TIGRFAMsiTIGR00767. rho. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiRHO_ECOLI
    AccessioniPrimary (citable) accession number: P0AG30
    Secondary accession number(s): P03002, Q2M891, Q48357
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: November 2, 2016
    This is version 110 of the entry and version 1 of the sequence. [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

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.