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P00579

- RPOD_ECOLI

UniProt

P00579 - RPOD_ECOLI

Protein

RNA polymerase sigma factor RpoD

Gene

rpoD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. Preferentially transcribes genes associated with fast growth, such as ribosomal operons, other protein-synthesis related genes, rRNA- and tRNA-encoding genes and prfB.6 PublicationsUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei562 – 5621Interaction with anti-sigma factors

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi573 – 59220H-T-H motifUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-HAMAP
    2. protein binding Source: IntAct
    3. sequence-specific DNA binding transcription factor activity Source: InterPro
    4. sigma factor activity Source: EcoliWiki

    GO - Biological processi

    1. response to heat Source: EcoliWiki
    2. transcription initiation from bacterial-type RNA polymerase promoter Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Sigma factor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:RPOD-MONOMER.
    ECOL316407:JW3039-MONOMER.
    MetaCyc:RPOD-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase sigma factor RpoDUniRule annotation
    Alternative name(s):
    Sigma-70UniRule annotation
    Gene namesi
    Name:rpoDUniRule annotation
    Synonyms:alt
    Ordered Locus Names:b3067, JW3039
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10896. rpoD.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi596 – 5961R → D or E: 2-fold reduction in activation of class II Crp-dependent promoters. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 613613RNA polymerase sigma factor RpoDPRO_0000093885Add
    BLAST

    Proteomic databases

    PaxDbiP00579.
    PRIDEiP00579.

    Expressioni

    Gene expression databases

    GenevestigatoriP00579.

    Interactioni

    Subunit structurei

    Interacts transiently with the RNA polymerase catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNA polymerase holoenzyme that can initiate transcription. Identified in a complex containing RpoD, the RNA polymerase subunits RpoA, RpoB and RpoZ, CRP and DNA. Interacts with Rsd; this prevents interaction with the RNA polymerase catalytic core and with promoter DNA, and as a consequence, promotes transcription from promoters that require alternative sigma factors. Interacts with phage T4 AsiA; this interferes with binding to DNA and to the RNA polymerase.5 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    asiAP322675EBI-545104,EBI-2124737From a different organism.
    rpoCP0A8T78EBI-545104,EBI-543604
    rsdP0AFX411EBI-545104,EBI-1134364

    Protein-protein interaction databases

    DIPiDIP-10773N.
    IntActiP00579. 56 interactions.
    MINTiMINT-1220595.
    STRINGi511145.b3067.

    Structurei

    Secondary structure

    1
    613
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi116 – 13419
    Helixi138 – 14811
    Turni149 – 1546
    Helixi158 – 1603
    Beta strandi162 – 1654
    Turni179 – 1824
    Turni187 – 1904
    Helixi214 – 23421
    Helixi243 – 25614
    Beta strandi259 – 2613
    Helixi263 – 29230
    Helixi299 – 3068
    Turni307 – 3093
    Helixi313 – 3153
    Helixi317 – 3204
    Helixi325 – 3295
    Helixi330 – 3323
    Helixi334 – 35118
    Helixi355 – 38228
    Helixi384 – 3918
    Beta strandi397 – 3993
    Helixi401 – 41818
    Helixi421 – 4233
    Helixi427 – 44519
    Turni547 – 5504
    Helixi553 – 56210
    Helixi573 – 59725

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SIGX-ray2.60A114-448[»]
    1TLHNMR-B533-613[»]
    2P7VX-ray2.60B546-613[»]
    3IYDelectron microscopy19.8F1-613[»]
    3T72X-ray4.33o/q533-609[»]
    4IGCX-ray3.70X/Y1-613[»]
    4JK1X-ray3.90X/Y1-613[»]
    4JK2X-ray4.20X/Y1-613[»]
    4JKRX-ray4.20F/L1-613[»]
    4KMUX-ray3.85X/Y1-613[»]
    4KN4X-ray3.96X/Y1-613[»]
    4KN7X-ray3.69X/Y1-613[»]
    4LJZX-ray3.59F/L92-613[»]
    4LK0X-ray3.91F/L92-613[»]
    4LK1X-ray3.84F/L1-613[»]
    4LLGX-ray3.79F/L1-613[»]
    4MEXX-ray3.90F/L1-613[»]
    4MEYX-ray3.95F/L1-613[»]
    ProteinModelPortaliP00579.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00579.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 8079Sigma-70 factor domain-1Add
    BLAST
    Regioni379 – 44971Sigma-70 factor domain-2Add
    BLAST
    Regioni458 – 53477Sigma-70 factor domain-3Add
    BLAST
    Regioni547 – 60054Sigma-70 factor domain-4Add
    BLAST
    Regioni584 – 59916Interaction with anti-sigma factorsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi403 – 4064Interaction with polymerase core subunit RpoC

    Domaini

    In the autoinhibited state, sigma-70 factor domain-1 packs closely together with sigma-70 factor domains-2 and -4, contrary to the extended conformation that is seen when the protein is part of the RNA polymerase holoenzyme.Curated
    The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC.
    The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-sigma factors prevents interaction of sigma factors with the RNA polymerase catalytic core (PubMed:19903881 and PubMed:21829166). This domain is probably also responsible for interaction with Crp (PubMed:10860740).1 Publication

    Sequence similaritiesi

    Belongs to the sigma-70 factor family. RpoD/SigA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0568.
    HOGENOMiHOG000270272.
    KOiK03086.
    OMAiFDFLVNS.
    OrthoDBiEOG6XHC70.
    PhylomeDBiP00579.

    Family and domain databases

    Gene3Di1.10.10.10. 2 hits.
    HAMAPiMF_00963. Sigma70_RpoD_SigA.
    InterProiIPR014284. RNA_pol_sigma-70_dom.
    IPR000943. RNA_pol_sigma70.
    IPR009042. RNA_pol_sigma70_r1_2.
    IPR007627. RNA_pol_sigma70_r2.
    IPR007624. RNA_pol_sigma70_r3.
    IPR007630. RNA_pol_sigma70_r4.
    IPR007631. RNA_pol_sigma_70_non-ess.
    IPR007127. RNA_pol_sigma_70_r1_1.
    IPR013325. RNA_pol_sigma_r2.
    IPR013324. RNA_pol_sigma_r3_r4.
    IPR012760. RNA_pol_sigma_RpoD_C.
    IPR028630. Sigma70_RpoD.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF04546. Sigma70_ner. 1 hit.
    PF03979. Sigma70_r1_1. 1 hit.
    PF00140. Sigma70_r1_2. 1 hit.
    PF04542. Sigma70_r2. 1 hit.
    PF04539. Sigma70_r3. 1 hit.
    PF04545. Sigma70_r4. 1 hit.
    [Graphical view]
    PRINTSiPR00046. SIGMA70FCT.
    SUPFAMiSSF88659. SSF88659. 2 hits.
    SSF88946. SSF88946. 1 hit.
    TIGRFAMsiTIGR02393. RpoD_Cterm. 1 hit.
    TIGR02937. sigma70-ECF. 1 hit.
    PROSITEiPS00715. SIGMA70_1. 1 hit.
    PS00716. SIGMA70_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00579-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEQNPQSQLK LLVTRGKEQG YLTYAEVNDH LPEDIVDSDQ IEDIIQMIND    50
    MGIQVMEEAP DADDLMLAEN TADEDAAEAA AQVLSSVESE IGRTTDPVRM 100
    YMREMGTVEL LTREGEIDIA KRIEDGINQV QCSVAEYPEA ITYLLEQYDR 150
    VEAEEARLSD LITGFVDPNA EEDLAPTATH VGSELSQEDL DDDEDEDEED 200
    GDDDSADDDN SIDPELAREK FAELRAQYVV TRDTIKAKGR SHATAQEEIL 250
    KLSEVFKQFR LVPKQFDYLV NSMRVMMDRV RTQERLIMKL CVEQCKMPKK 300
    NFITLFTGNE TSDTWFNAAI AMNKPWSEKL HDVSEEVHRA LQKLQQIEEE 350
    TGLTIEQVKD INRRMSIGEA KARRAKKEMV EANLRLVISI AKKYTNRGLQ 400
    FLDLIQEGNI GLMKAVDKFE YRRGYKFSTY ATWWIRQAIT RSIADQARTI 450
    RIPVHMIETI NKLNRISRQM LQEMGREPTP EELAERMLMP EDKIRKVLKI 500
    AKEPISMETP IGDDEDSHLG DFIEDTTLEL PLDSATTESL RAATHDVLAG 550
    LTAREAKVLR MRFGIDMNTD YTLEEVGKQF DVTRERIRQI EAKALRKLRH 600
    PSRSEVLRSF LDD 613
    Length:613
    Mass (Da):70,263
    Last modified:October 1, 1996 - v2
    Checksum:iCA4F0E30DEC1703D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491D → N in AAA24601. (PubMed:6269063)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01687 Genomic DNA. Translation: AAA24601.1.
    U28379 Genomic DNA. Translation: AAA89147.1.
    U00096 Genomic DNA. Translation: AAC76103.1.
    AP009048 Genomic DNA. Translation: BAE77118.1.
    PIRiA65095. RNECS.
    RefSeqiNP_417539.1. NC_000913.3.
    YP_491259.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76103; AAC76103; b3067.
    BAE77118; BAE77118; BAE77118.
    GeneIDi12932074.
    947567.
    KEGGiecj:Y75_p2993.
    eco:b3067.
    PATRICi32121550. VBIEscCol129921_3162.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01687 Genomic DNA. Translation: AAA24601.1 .
    U28379 Genomic DNA. Translation: AAA89147.1 .
    U00096 Genomic DNA. Translation: AAC76103.1 .
    AP009048 Genomic DNA. Translation: BAE77118.1 .
    PIRi A65095. RNECS.
    RefSeqi NP_417539.1. NC_000913.3.
    YP_491259.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SIG X-ray 2.60 A 114-448 [» ]
    1TLH NMR - B 533-613 [» ]
    2P7V X-ray 2.60 B 546-613 [» ]
    3IYD electron microscopy 19.8 F 1-613 [» ]
    3T72 X-ray 4.33 o/q 533-609 [» ]
    4IGC X-ray 3.70 X/Y 1-613 [» ]
    4JK1 X-ray 3.90 X/Y 1-613 [» ]
    4JK2 X-ray 4.20 X/Y 1-613 [» ]
    4JKR X-ray 4.20 F/L 1-613 [» ]
    4KMU X-ray 3.85 X/Y 1-613 [» ]
    4KN4 X-ray 3.96 X/Y 1-613 [» ]
    4KN7 X-ray 3.69 X/Y 1-613 [» ]
    4LJZ X-ray 3.59 F/L 92-613 [» ]
    4LK0 X-ray 3.91 F/L 92-613 [» ]
    4LK1 X-ray 3.84 F/L 1-613 [» ]
    4LLG X-ray 3.79 F/L 1-613 [» ]
    4MEX X-ray 3.90 F/L 1-613 [» ]
    4MEY X-ray 3.95 F/L 1-613 [» ]
    ProteinModelPortali P00579.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10773N.
    IntActi P00579. 56 interactions.
    MINTi MINT-1220595.
    STRINGi 511145.b3067.

    Chemistry

    BindingDBi P00579.

    Proteomic databases

    PaxDbi P00579.
    PRIDEi P00579.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76103 ; AAC76103 ; b3067 .
    BAE77118 ; BAE77118 ; BAE77118 .
    GeneIDi 12932074.
    947567.
    KEGGi ecj:Y75_p2993.
    eco:b3067.
    PATRICi 32121550. VBIEscCol129921_3162.

    Organism-specific databases

    EchoBASEi EB0889.
    EcoGenei EG10896. rpoD.

    Phylogenomic databases

    eggNOGi COG0568.
    HOGENOMi HOG000270272.
    KOi K03086.
    OMAi FDFLVNS.
    OrthoDBi EOG6XHC70.
    PhylomeDBi P00579.

    Enzyme and pathway databases

    BioCyci EcoCyc:RPOD-MONOMER.
    ECOL316407:JW3039-MONOMER.
    MetaCyc:RPOD-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00579.
    PROi P00579.

    Gene expression databases

    Genevestigatori P00579.

    Family and domain databases

    Gene3Di 1.10.10.10. 2 hits.
    HAMAPi MF_00963. Sigma70_RpoD_SigA.
    InterProi IPR014284. RNA_pol_sigma-70_dom.
    IPR000943. RNA_pol_sigma70.
    IPR009042. RNA_pol_sigma70_r1_2.
    IPR007627. RNA_pol_sigma70_r2.
    IPR007624. RNA_pol_sigma70_r3.
    IPR007630. RNA_pol_sigma70_r4.
    IPR007631. RNA_pol_sigma_70_non-ess.
    IPR007127. RNA_pol_sigma_70_r1_1.
    IPR013325. RNA_pol_sigma_r2.
    IPR013324. RNA_pol_sigma_r3_r4.
    IPR012760. RNA_pol_sigma_RpoD_C.
    IPR028630. Sigma70_RpoD.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF04546. Sigma70_ner. 1 hit.
    PF03979. Sigma70_r1_1. 1 hit.
    PF00140. Sigma70_r1_2. 1 hit.
    PF04542. Sigma70_r2. 1 hit.
    PF04539. Sigma70_r3. 1 hit.
    PF04545. Sigma70_r4. 1 hit.
    [Graphical view ]
    PRINTSi PR00046. SIGMA70FCT.
    SUPFAMi SSF88659. SSF88659. 2 hits.
    SSF88946. SSF88946. 1 hit.
    TIGRFAMsi TIGR02393. RpoD_Cterm. 1 hit.
    TIGR02937. sigma70-ECF. 1 hit.
    PROSITEi PS00715. SIGMA70_1. 1 hit.
    PS00716. SIGMA70_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12."
      Burton Z.F., Burgess R.R., Lin J., Moore D., Holder S., Gross C.A.
      Nucleic Acids Res. 9:2889-2903(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "The subunits of DNA-dependent RNA polymerase from E. coli: I. Amino acid analysis and primary structure of the N-terminal regions."
      Fujiki H., Zurek G.
      FEBS Lett. 55:242-244(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-4.
      Strain: K12.
    5. "Promoter selectivity of Escherichia coli RNA polymerase. Purification and properties of holoenzyme containing the heat-shock sigma subunit."
      Fujita N., Nomura T., Ishihama A.
      J. Biol. Chem. 262:1855-1859(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: K12 / W3350 / ATCC 27020.
    6. "Growth phase-dependent modification of RNA polymerase in Escherichia coli."
      Ozaki M., Wada A., Fujita N., Ishihama A.
      Mol. Gen. Genet. 230:17-23(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Polypeptides containing highly conserved regions of transcription initiation factor sigma 70 exhibit specificity of binding to promoter DNA."
      Dombroski A.J., Walter W.A., Record M.T. Jr., Siegele D.A., Gross C.A.
      Cell 70:501-512(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, DOMAIN.
    8. "Role of the sigma 70 subunit of Escherichia coli RNA polymerase in transcription activation."
      Kumar A., Grimes B., Fujita N., Makino K., Malloch R.A., Hayward R.S., Ishihama A.
      J. Mol. Biol. 235:405-413(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: intracellular levels of four species of sigma subunit under various growth conditions."
      Jishage M., Iwata A., Ueda S., Ishihama A.
      J. Bacteriol. 178:5447-5451(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: K12.
    10. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    11. "Interactions between activating region 3 of the Escherichia coli cyclic AMP receptor protein and region 4 of the RNA polymerase sigma(70) subunit: application of suppression genetics."
      Rhodius V.A., Busby S.J.
      J. Mol. Biol. 299:311-324(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROBABLE INTERACTION WITH CRP, MUTAGENESIS OF ARG-596.
    12. "In vitro transcription profiling of the sigmaS subunit of bacterial RNA polymerase: re-definition of the sigmaS regulon and identification of sigmaS-specific promoter sequence elements."
      Maciag A., Peano C., Pietrelli A., Egli T., De Bellis G., Landini P.
      Nucleic Acids Res. 39:5338-5355(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: K12 / MG1655 / ATCC 47076.
    13. "Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase."
      Malhotra A., Severinova E., Darst S.A.
      Cell 87:127-136(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 114-448.
    14. "T4 AsiA blocks DNA recognition by remodeling sigma70 region 4."
      Lambert L.J., Wei Y., Schirf V., Demeler B., Werner M.H.
      EMBO J. 23:2952-2962(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 533-613 IN COMPLEX WITH PHAGE T4 PROTEIN ASIA, SUBUNIT.
    15. "Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in complex with sigma70 domain 4."
      Patikoglou G.A., Westblade L.F., Campbell E.A., Lamour V., Lane W.J., Darst S.A.
      J. Mol. Biol. 372:649-659(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 546-613 IN COMPLEX WITH RSD, SUBUNIT.
    16. "Three-dimensional EM structure of an intact activator-dependent transcription initiation complex."
      Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E., Ebright R.H., Lawson C.L.
      Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOA; RPOB; RPOC; RPOZ; CRP AND DNA, DOMAIN, DNA-BINDING, SUBUNIT.
    17. "The structure of a transcription activation subcomplex reveals how sigma(70) is recruited to PhoB promoters."
      Blanco A.G., Canals A., Bernues J., Sola M., Coll M.
      EMBO J. 30:3776-3785(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.33 ANGSTROMS) OF 533-609 IN COMPLEX WITH RPOB; PHOB AND PHO BOX DNA, DNA-BINDING, SUBUNIT, DOMAIN.
    18. "X-ray crystal structure of Escherichia coli RNA polymerase sigma70 holoenzyme."
      Murakami K.S.
      J. Biol. Chem. 288:9126-9134(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) IN COMPLEX WITH RPOA; RPOB; RPOC AND RPOZ, SUBUNIT.

    Entry informationi

    Entry nameiRPOD_ECOLI
    AccessioniPrimary (citable) accession number: P00579
    Secondary accession number(s): Q2M9D8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 155 of the entry and version 2 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

    External Data

    Dasty 3