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Protein

ECF RNA polymerase sigma-E factor

Gene

rpoE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released (PubMed:7889935, PubMed:2691330, PubMed:9159522, PubMed:9159523). Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock (PubMed:7889935) and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS of the outer membrane (PubMed:7889934, PubMed:11274153, PubMed:16336047).7 Publications

Enzyme regulationi

ECF sigma-E is held in an inactive form by its cognate anti-sigma factor (RseA) until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal (periplasmic stress and excess LPS) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The anti-sigma factor RseA is an inner membrane protein, binding sigma-E in the cytoplasm and RseB in the periplasm. RseA is first cut extracytoplasmically (site-1 protease, S1P, by DegS), then within the membrane itself (site-2 protease, S2P, by RseP), while cytoplasmic proteases (predominantly ClpX-ClpP) finish degrading the regulatory protein, liberating sigma-E (PubMed:15371343). Degradation of RseA requires 2 signals to activate DegS; an outer membrane protein (OMP) signal activates DegS, while an LPS signal causes release of RseB from RseA, freeing RseA to be cleaved (PubMed:23687042). The rate-limiting step in this protease cascade is the first signal-sensing cleavage (half-life about 1 minute) (PubMed:17210793).4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi156 – 17520H-T-H motifBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • DNA-templated transcription, initiation Source: InterPro
  • regulation of transcription, DNA-templated Source: EcoCyc
  • response to osmotic stress Source: EcoCyc
  • response to temperature stimulus Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Sigma factor

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:RPOE-MONOMER.
ECOL316407:JW2557-MONOMER.
MetaCyc:RPOE-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ECF RNA polymerase sigma-E factor
Alternative name(s):
RNA polymerase sigma-E factor
Sigma-24
Gene namesi
Name:rpoE
Synonyms:sigE
Ordered Locus Names:b2573, JW2557
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11897. rpoE.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Reduced viability at 37 degrees Celsius, death at 42 degrees Celsius (PubMed:7889935). Loss of transcription from rpoE-dependent promoters (PubMed:7889935). Increased sensitivity to outer membrane disruption (PubMed:7889934).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251L → P in SR1576; loss of sigma factor activity. 1 Publication
Mutagenesisi165 – 1651C → A: Binds RNAP and RseA normally. 1 Publication
Mutagenesisi172 – 1721S → P in SR1723; loss of sigma factor activity. 1 Publication
Mutagenesisi178 – 1781R → G in SR1502; decreased sigma factor activity. Does not bind RseA, still binds RNAP. 2 Publications
Mutagenesisi181 – 1811I → A in SR1503; decreased sigma factor activity. Does not bind RseA, still binds RNAP. 1 Publication
Mutagenesisi185 – 1851V → A in SR1504; decreased sigma factor activity. Does not bind RseA, still binds RNAP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191ECF RNA polymerase sigma-E factorPRO_0000093997Add
BLAST

Proteomic databases

EPDiP0AGB6.
PaxDbiP0AGB6.
PRIDEiP0AGB6.

Expressioni

Inductioni

Induced after shifting to 50 degrees Celsius (PubMed:2691330) (at protein level), when the level of outer membrane proteins (OMP) increases (PubMed:8276244) (at protein level, PubMed:10500101), as periplasmic levels of LPS levels increase (PubMed:23687042) and by some misfolded periplasmic proteins (PubMed:9351822). Positively autoregulated (via promoter P2) (PubMed:7889935), slightly induced by elevated temperatures (PubMed:7889934). Transiently induced by cold shock in a PNPase-dependent fashion (PubMed:14527658). Part of the rpoE-rseA-rseB-rseC operon (PubMed:9159522, PubMed:9159523).10 Publications

Interactioni

Subunit structurei

Interacts transiently with the RNAP catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNAP holoenzyme that can initiate transcription (PubMed:12016219, PubMed:12718891, PubMed:7889935, PubMed:2691330). Interacts 1:1 with anti-sigma-E factor RseA which prevents binding to RNAP catalytic core (PubMed:9159522, PubMed:9159523, PubMed:11777003, PubMed:12016219, PubMed:15371343, PubMed:12718891). An N-terminal (residues 1-108) RseA sigma-E complex also interacts with SspB.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mqsAQ468642EBI-1129580,EBI-1120353

Protein-protein interaction databases

BioGridi4263046. 221 interactions.
DIPiDIP-10774N.
IntActiP0AGB6. 30 interactions.
STRINGi511145.b2573.

Structurei

Secondary structure

1
191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1514Combined sources
Helixi19 – 3719Combined sources
Turni38 – 403Combined sources
Helixi43 – 453Combined sources
Helixi46 – 6015Combined sources
Helixi61 – 633Combined sources
Beta strandi66 – 683Combined sources
Helixi70 – 8920Combined sources
Helixi95 – 10410Combined sources
Beta strandi121 – 1233Combined sources
Helixi124 – 13714Combined sources
Helixi140 – 15011Combined sources
Helixi156 – 1627Combined sources
Helixi167 – 18519Combined sources
Helixi186 – 1883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OR7X-ray2.00A/B1-191[»]
2H27X-ray2.30A/D122-191[»]
ProteinModelPortaliP0AGB6.
SMRiP0AGB6. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGB6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 153153Binds RNAP core1 PublicationAdd
BLAST
Regioni25 – 9268Sigma-70 factor domain-2Add
BLAST
Regioni129 – 18052Sigma-70 factor domain-4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 6114Polymerase core bindingAdd
BLAST

Domaini

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.1 Publication
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.2 Publications

Sequence similaritiesi

Belongs to the sigma-70 factor family. ECF subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105EMN. Bacteria.
COG1595. LUCA.
HOGENOMiHOG000094755.
InParanoidiP0AGB6.
KOiK03088.
OMAiDAENYES.
OrthoDBiEOG6ZD6DW.
PhylomeDBiP0AGB6.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR014284. RNA_pol_sigma-70_dom.
IPR000838. RNA_pol_sigma70_ECF_CS.
IPR007627. RNA_pol_sigma70_r2.
IPR013249. RNA_pol_sigma70_r4_t2.
IPR014286. RNA_pol_sigma70_RpoE.
IPR013325. RNA_pol_sigma_r2.
IPR013324. RNA_pol_sigma_r3_r4.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04542. Sigma70_r2. 1 hit.
PF08281. Sigma70_r4_2. 1 hit.
[Graphical view]
SUPFAMiSSF88659. SSF88659. 1 hit.
SSF88946. SSF88946. 1 hit.
TIGRFAMsiTIGR02939. RpoE_Sigma70. 1 hit.
TIGR02937. sigma70-ECF. 1 hit.
PROSITEiPS01063. SIGMA70_ECF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AGB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQLTDQVL VERVQKGDQK AFNLLVVRYQ HKVASLVSRY VPSGDVPDVV
60 70 80 90 100
QEAFIKAYRA LDSFRGDSAF YTWLYRIAVN TAKNYLVAQG RRPPSSDVDA
110 120 130 140 150
IEAENFESGG ALKEISNPEN LMLSEELRQI VFRTIESLPE DLRMAITLRE
160 170 180 190
LDGLSYEEIA AIMDCPVGTV RSRIFRAREA IDNKVQPLIR R
Length:191
Mass (Da):21,696
Last modified:December 20, 2005 - v1
Checksum:iC71EEF5939C3611E
GO

Sequence cautioni

The sequence BAA10920.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13169 Genomic DNA. No translation available.
U37089 Genomic DNA. Translation: AAC45314.1.
D64044 Genomic DNA. Translation: BAA10920.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75626.1.
AP009048 Genomic DNA. Translation: BAE76749.1.
U10148 Genomic DNA. Translation: AAA83998.1.
PIRiI60227.
RefSeqiNP_417068.1. NC_000913.3.
WP_001295364.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75626; AAC75626; b2573.
BAE76749; BAE76749; BAE76749.
GeneIDi947050.
KEGGiecj:JW2557.
eco:b2573.
PATRICi32120545. VBIEscCol129921_2675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13169 Genomic DNA. No translation available.
U37089 Genomic DNA. Translation: AAC45314.1.
D64044 Genomic DNA. Translation: BAA10920.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75626.1.
AP009048 Genomic DNA. Translation: BAE76749.1.
U10148 Genomic DNA. Translation: AAA83998.1.
PIRiI60227.
RefSeqiNP_417068.1. NC_000913.3.
WP_001295364.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OR7X-ray2.00A/B1-191[»]
2H27X-ray2.30A/D122-191[»]
ProteinModelPortaliP0AGB6.
SMRiP0AGB6. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263046. 221 interactions.
DIPiDIP-10774N.
IntActiP0AGB6. 30 interactions.
STRINGi511145.b2573.

Proteomic databases

EPDiP0AGB6.
PaxDbiP0AGB6.
PRIDEiP0AGB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75626; AAC75626; b2573.
BAE76749; BAE76749; BAE76749.
GeneIDi947050.
KEGGiecj:JW2557.
eco:b2573.
PATRICi32120545. VBIEscCol129921_2675.

Organism-specific databases

EchoBASEiEB1843.
EcoGeneiEG11897. rpoE.

Phylogenomic databases

eggNOGiENOG4105EMN. Bacteria.
COG1595. LUCA.
HOGENOMiHOG000094755.
InParanoidiP0AGB6.
KOiK03088.
OMAiDAENYES.
OrthoDBiEOG6ZD6DW.
PhylomeDBiP0AGB6.

Enzyme and pathway databases

BioCyciEcoCyc:RPOE-MONOMER.
ECOL316407:JW2557-MONOMER.
MetaCyc:RPOE-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AGB6.
PROiP0AGB6.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR014284. RNA_pol_sigma-70_dom.
IPR000838. RNA_pol_sigma70_ECF_CS.
IPR007627. RNA_pol_sigma70_r2.
IPR013249. RNA_pol_sigma70_r4_t2.
IPR014286. RNA_pol_sigma70_RpoE.
IPR013325. RNA_pol_sigma_r2.
IPR013324. RNA_pol_sigma_r3_r4.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04542. Sigma70_r2. 1 hit.
PF08281. Sigma70_r4_2. 1 hit.
[Graphical view]
SUPFAMiSSF88659. SSF88659. 1 hit.
SSF88946. SSF88946. 1 hit.
TIGRFAMsiTIGR02939. RpoE_Sigma70. 1 hit.
TIGR02937. sigma70-ECF. 1 hit.
PROSITEiPS01063. SIGMA70_ECF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia coli."
    Nashimoto H.
    (In) Nierhaus K.H. (eds.); The translational apparatus, pp.185-195, Plenum Press, New York (1993)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli."
    Raina S., Missiakas D., Georgopoulos C.
    EMBO J. 14:1043-1055(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A SIGMA FACTOR, SUBUNIT, AUTOREGULATION, GENE IDENTIFICATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LEU-25; SER-172 AND ARG-178.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574 and K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Nashimoto H., Saito N.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Functional equivalence of Escherichia coli sigma E and Pseudomonas aeruginosa AlgU: E. coli rpoE restores mucoidy and reduces sensitivity to reactive oxygen intermediates in algU mutants of P. aeruginosa."
    Yu H., Schurr M.J., Deretic V.
    J. Bacteriol. 177:3259-3268(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 171-191.
    Strain: K12 / VD1870.
  7. "rpoE, the gene encoding the second heat-shock sigma factor, sigma E, in Escherichia coli."
    Rouviere P.E., de Las Penas A., Mecsas J., Lu C.Z., Rudd K.E., Gross C.A.
    EMBO J. 14:1032-1042(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-56, GENE IDENTIFICATION, FUNCTION AS A SIGMA FACTOR, INDUCTION, REGULON, DISRUPTION PHENOTYPE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Identification of the sigma E subunit of Escherichia coli RNA polymerase: a second alternate sigma factor involved in high-temperature gene expression."
    Erickson J.W., Gross C.A.
    Genes Dev. 3:1462-1471(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A SIGMA FACTOR, SUBUNIT, INDUCTION AT HIGH TEMPERATURE.
    Strain: SC122.
  9. "The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins."
    Mecsas J., Rouviere P.E., Erickson J.W., Donohue T.J., Gross C.A.
    Genes Dev. 7:2618-2628(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION IN RESPONSE TO OUTER MEMBRANE PROTEIN LEVELS.
  10. "Analysis of promoters controlled by the putative sigma factor AlgU regulating conversion to mucoidy in Pseudomonas aeruginosa: relationship to sigma E and stress response."
    Martin D.W., Schurr M.J., Yu H., Deretic V.
    J. Bacteriol. 176:6688-6696(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE IDENTIFICATION.
  11. "Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase sigma factors involved in the regulation of extracytoplasmic functions."
    Lonetto M.A., Brown K.L., Rudd K.E., Buttner M.J.
    Proc. Natl. Acad. Sci. U.S.A. 91:7573-7577(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE IDENTIFICATION.
  12. "Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins."
    Missiakas D., Mayer M.P., Lemaire M., Georgopoulos C., Raina S.
    Mol. Microbiol. 24:355-371(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A SIGMA FACTOR, ENZYME REGULATION, INTERACTION WITH RSEA, SUBUNIT, SUBCELLULAR LOCATION, OPERON.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  13. "The sigmaE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigmaE."
    De Las Penas A., Connolly L., Gross C.A.
    Mol. Microbiol. 24:373-385(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A SIGMA FACTOR, INTERACTION WITH RSEA, SUBUNIT, OPERON.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  14. "The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems."
    Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.
    EMBO J. 16:6394-6406(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  15. "The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor."
    Ades S.E., Connolly L.E., Alba B.M., Gross C.A.
    Genes Dev. 13:2449-2461(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  16. "RseB binding to the periplasmic domain of RseA modulates the RseA:sigmaE interaction in the cytoplasm and the availability of sigmaE.RNA polymerase."
    Collinet B., Yuzawa H., Chen T., Herrera C., Missiakas D.
    J. Biol. Chem. 275:33898-33904(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSEA, SUBCELLULAR LOCATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  17. "Characterization of the Escherichia coli sigma E regulon."
    Dartigalongue C., Missiakas D., Raina S.
    J. Biol. Chem. 276:20866-20875(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULON.
  18. "Interaction of the conserved region 4.2 of sigma(E) with the RseA anti-sigma factor."
    Tam C., Collinet B., Lau G., Raina S., Missiakas D.
    J. Biol. Chem. 277:27282-27287(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNA POLYMERASE AND RSEA, SUBUNIT, DOMAIN, MUTAGENESIS OF CYS-165; ARG-178; ILE-181 AND VAL-185.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  19. "Changes in Escherichia coli transcriptome during acclimatization at low temperature."
    Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G., Deho G.
    Res. Microbiol. 154:573-580(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY COLD SHOCK.
    Strain: K12 / MG1655 / ATCC 47076.
  20. "Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation."
    Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.
    Genes Dev. 18:2292-2301(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION BY CLPX-CLPP, INTERACTION WITH RSEA AND SSPB.
  21. "Conserved and variable functions of the sigmaE stress response in related genomes."
    Rhodius V.A., Suh W.C., Nonaka G., West J., Gross C.A.
    PLoS Biol. 4:E2-E2(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, REGULON.
    Strain: K12 / MG1655 / ATCC 47076.
  22. "Design principles of the proteolytic cascade governing the sigmaE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction."
    Chaba R., Grigorova I.L., Flynn J.M., Baker T.A., Gross C.A.
    Genes Dev. 21:124-136(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  23. "Dual molecular signals mediate the bacterial response to outer-membrane stress."
    Lima S., Guo M.S., Chaba R., Gross C.A., Sauer R.T.
    Science 340:837-841(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INDUCTION BY LIPOPOLYSACCHARIDE.
    Strain: K12.
  24. "Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA."
    Campbell E.A., Tupy J.L., Gruber T.M., Wang S., Sharp M.M., Gross C.A., Darst S.A.
    Mol. Cell 11:1067-1078(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RSEA, INTERACTION WITH RNA POLYMERASE, SUBUNIT.
  25. "The structural basis for promoter -35 element recognition by the group IV sigma factors."
    Lane W.J., Darst S.A.
    PLoS Biol. 4:1491-1500(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 122-191 IN COMPLEX WITH DNA, DOMAIN.

Entry informationi

Entry nameiRPOE_ECOLI
AccessioniPrimary (citable) accession number: P0AGB6
Secondary accession number(s): P34086, Q2MAF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 16, 2016
This is version 90 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.