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P00579

- RPOD_ECOLI

UniProt

P00579 - RPOD_ECOLI

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Protein
RNA polymerase sigma factor RpoD
Gene
rpoD, alt, b3067, JW3039
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

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 Publications

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
DNA bindingi573 – 59220H-T-H motif3 Publications

GO - Molecular functioni

  1. DNA bindingInferred from electronic annotationi Source: UniProtKB-HAMAP
  2. protein bindingInferred from physical interactioni PubMed 10764785PubMed 11591686PubMed 15690043PubMed 16606699PubMed 18359804PubMed 18826409PubMed 24561554 Source: IntAct
  3. sequence-specific DNA binding transcription factor activityInferred from electronic annotationi Source: InterPro
  4. sigma factor activityInferred from direct assayi PubMed 4882047 Source: EcoliWiki
Complete GO annotation...

GO - Biological processi

  1. response to heatInferred from expression patterni PubMed 8349564 Source: EcoliWiki
  2. transcription initiation from bacterial-type RNA polymerase promoterInferred from electronic annotationi Source: UniProtKB-HAMAP
  1. sequence-specific DNA binding transcription factor activityInferred from electronic annotationi Source: InterPro
  2. sigma factor activityInferred from direct assayi PubMed 4882047 Source: EcoliWiki
Complete GO annotation...

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 RpoD
Alternative name(s):
Sigma-70
Gene namesi
Name:rpoD
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 Reviewed prediction UniRule annotation

GO - Cellular componenti

  1. cytoplasmInferred from electronic annotationi Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
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 identifier
Chaini1 – 613613RNA polymerase sigma factor RpoDUniRule annotation
PRO_0000093885

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.6 Publications

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

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
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.

Miscellaneous databases

EvolutionaryTraceiP00579.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Regioni2 – 8079Sigma-70 factor domain-1UniRule annotation
Regioni379 – 44971Sigma-70 factor domain-2UniRule annotation
Regioni458 – 53477Sigma-70 factor domain-3UniRule annotation
Regioni547 – 60054Sigma-70 factor domain-4UniRule annotation
Regioni584 – 59916Interaction with anti-sigma factorsUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Motifi403 – 4064Interaction with polymerase core subunit RpoCUniRule annotation

Domaini

Contains 4 domains, connected by flexible linkers. In the active conformation, the domains are in an extended conformation, each making extensive interactions with the RNA polymerase catalytic core.3 Publications
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 Inferred.3 Publications
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.3 Publications
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 (1 Publication and 1 Publication). This domain is probably also responsible for interaction with Crp (1 Publication).3 Publications

Sequence similaritiesi

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]FASTA

« 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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti149 – 1491D → N in AAA24601. 1 Publication

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.
PIRiRNECS. A65095.
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 RNECS. A65095.
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...

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

« Hide 'large scale' publicationsDownload
  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. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    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 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: July 9, 2014
This is version 154 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. 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

External Data

Dasty 3

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