ID RPOE_ECOLI Reviewed; 191 AA.
AC P0AGB6; P34086; Q2MAF7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=ECF RNA polymerase sigma-E factor;
DE AltName: Full=RNA polymerase sigma-E factor;
DE AltName: Full=Sigma-24;
GN Name=rpoE; Synonyms=sigE; OrderedLocusNames=b2573, JW2557;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H.;
RT "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia
RT coli.";
RL (In) Nierhaus K.H. (eds.);
RL The translational apparatus, pp.185-195, Plenum Press, New York (1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A SIGMA FACTOR, SUBUNIT,
RP AUTOREGULATION, GENE IDENTIFICATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF LEU-25; SER-172 AND ARG-178.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and
RC K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7889935; DOI=10.1002/j.1460-2075.1995.tb07085.x;
RA Raina S., Missiakas D., Georgopoulos C.;
RT "The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of
RT Escherichia coli.";
RL EMBO J. 14:1043-1055(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 171-191.
RC STRAIN=K12 / VD1870;
RX PubMed=7768826; DOI=10.1128/jb.177.11.3259-3268.1995;
RA Yu H., Schurr M.J., Deretic V.;
RT "Functional equivalence of Escherichia coli sigma E and Pseudomonas
RT aeruginosa AlgU: E. coli rpoE restores mucoidy and reduces sensitivity to
RT reactive oxygen intermediates in algU mutants of P. aeruginosa.";
RL J. Bacteriol. 177:3259-3268(1995).
RN [7]
RP PROTEIN SEQUENCE OF 40-56, GENE IDENTIFICATION, FUNCTION AS A SIGMA FACTOR,
RP INDUCTION, REGULON, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7889934; DOI=10.1002/j.1460-2075.1995.tb07084.x;
RA Rouviere P.E., de Las Penas A., Mecsas J., Lu C.Z., Rudd K.E., Gross C.A.;
RT "rpoE, the gene encoding the second heat-shock sigma factor, sigma E, in
RT Escherichia coli.";
RL EMBO J. 14:1032-1042(1995).
RN [8]
RP FUNCTION AS A SIGMA FACTOR, SUBUNIT, AND INDUCTION AT HIGH TEMPERATURE.
RC STRAIN=SC122;
RX PubMed=2691330; DOI=10.1101/gad.3.9.1462;
RA Erickson J.W., Gross C.A.;
RT "Identification of the sigma E subunit of Escherichia coli RNA polymerase:
RT a second alternate sigma factor involved in high-temperature gene
RT expression.";
RL Genes Dev. 3:1462-1471(1989).
RN [9]
RP INDUCTION IN RESPONSE TO OUTER MEMBRANE PROTEIN LEVELS.
RX PubMed=8276244; DOI=10.1101/gad.7.12b.2618;
RA Mecsas J., Rouviere P.E., Erickson J.W., Donohue T.J., Gross C.A.;
RT "The activity of sigma E, an Escherichia coli heat-inducible sigma-factor,
RT is modulated by expression of outer membrane proteins.";
RL Genes Dev. 7:2618-2628(1993).
RN [10]
RP GENE IDENTIFICATION.
RX PubMed=7961422; DOI=10.1128/jb.176.21.6688-6696.1994;
RA Martin D.W., Schurr M.J., Yu H., Deretic V.;
RT "Analysis of promoters controlled by the putative sigma factor AlgU
RT regulating conversion to mucoidy in Pseudomonas aeruginosa: relationship to
RT sigma E and stress response.";
RL J. Bacteriol. 176:6688-6696(1994).
RN [11]
RP GENE IDENTIFICATION.
RX PubMed=8052622; DOI=10.1073/pnas.91.16.7573;
RA Lonetto M.A., Brown K.L., Rudd K.E., Buttner M.J.;
RT "Analysis of the Streptomyces coelicolor sigE gene reveals the existence of
RT a subfamily of eubacterial RNA polymerase sigma factors involved in the
RT regulation of extracytoplasmic functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7573-7577(1994).
RN [12]
RP FUNCTION AS A SIGMA FACTOR, ACTIVITY REGULATION, INTERACTION WITH RSEA,
RP SUBUNIT, SUBCELLULAR LOCATION, AND OPERON.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9159522; DOI=10.1046/j.1365-2958.1997.3601713.x;
RA Missiakas D., Mayer M.P., Lemaire M., Georgopoulos C., Raina S.;
RT "Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-
RT factor activity by the RseA, RseB and RseC proteins.";
RL Mol. Microbiol. 24:355-371(1997).
RN [13]
RP FUNCTION AS A SIGMA FACTOR, INTERACTION WITH RSEA, SUBUNIT, AND OPERON.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=9159523; DOI=10.1046/j.1365-2958.1997.3611718.x;
RA De Las Penas A., Connolly L., Gross C.A.;
RT "The sigmaE-mediated response to extracytoplasmic stress in Escherichia
RT coli is transduced by RseA and RseB, two negative regulators of sigmaE.";
RL Mol. Microbiol. 24:373-385(1997).
RN [14]
RP INDUCTION.
RX PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
RA Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
RT "The chaperone-assisted membrane release and folding pathway is sensed by
RT two signal transduction systems.";
RL EMBO J. 16:6394-6406(1997).
RN [15]
RP INDUCTION.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=10500101; DOI=10.1101/gad.13.18.2449;
RA Ades S.E., Connolly L.E., Alba B.M., Gross C.A.;
RT "The Escherichia coli sigma(E)-dependent extracytoplasmic stress response
RT is controlled by the regulated proteolysis of an anti-sigma factor.";
RL Genes Dev. 13:2449-2461(1999).
RN [16]
RP INTERACTION WITH RSEA, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11777003; DOI=10.1074/jbc.m006214200;
RA Collinet B., Yuzawa H., Chen T., Herrera C., Missiakas D.;
RT "RseB binding to the periplasmic domain of RseA modulates the RseA:sigmaE
RT interaction in the cytoplasm and the availability of sigmaE.RNA
RT polymerase.";
RL J. Biol. Chem. 275:33898-33904(2000).
RN [17]
RP REGULON.
RX PubMed=11274153; DOI=10.1074/jbc.m100464200;
RA Dartigalongue C., Missiakas D., Raina S.;
RT "Characterization of the Escherichia coli sigma E regulon.";
RL J. Biol. Chem. 276:20866-20875(2001).
RN [18]
RP INTERACTION WITH RNA POLYMERASE AND RSEA, SUBUNIT, DOMAIN, AND MUTAGENESIS
RP OF CYS-165; ARG-178; ILE-181 AND VAL-185.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12016219; DOI=10.1074/jbc.m202881200;
RA Tam C., Collinet B., Lau G., Raina S., Missiakas D.;
RT "Interaction of the conserved region 4.2 of sigma(E) with the RseA anti-
RT sigma factor.";
RL J. Biol. Chem. 277:27282-27287(2002).
RN [19]
RP INDUCTION BY COLD SHOCK.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14527658; DOI=10.1016/s0923-2508(03)00167-0;
RA Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G.,
RA Deho G.;
RT "Changes in Escherichia coli transcriptome during acclimatization at low
RT temperature.";
RL Res. Microbiol. 154:573-580(2003).
RN [20]
RP ACTIVITY REGULATION BY CLPX-CLPP, AND INTERACTION WITH RSEA AND SSPB.
RX PubMed=15371343; DOI=10.1101/gad.1240104;
RA Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
RT "Modulating substrate choice: the SspB adaptor delivers a regulator of the
RT extracytoplasmic-stress response to the AAA+ protease ClpXP for
RT degradation.";
RL Genes Dev. 18:2292-2301(2004).
RN [21]
RP FUNCTION, AND REGULON.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16336047; DOI=10.1371/journal.pbio.0040002;
RA Rhodius V.A., Suh W.C., Nonaka G., West J., Gross C.A.;
RT "Conserved and variable functions of the sigmaE stress response in related
RT genomes.";
RL PLoS Biol. 4:E2-E2(2006).
RN [22]
RP ACTIVITY REGULATION.
RX PubMed=17210793; DOI=10.1101/gad.1496707;
RA Chaba R., Grigorova I.L., Flynn J.M., Baker T.A., Gross C.A.;
RT "Design principles of the proteolytic cascade governing the sigmaE-mediated
RT envelope stress response in Escherichia coli: keys to graded, buffered, and
RT rapid signal transduction.";
RL Genes Dev. 21:124-136(2007).
RN [23]
RP ACTIVITY REGULATION, AND INDUCTION BY LIPOPOLYSACCHARIDE.
RC STRAIN=K12;
RX PubMed=23687042; DOI=10.1126/science.1235358;
RA Lima S., Guo M.S., Chaba R., Gross C.A., Sauer R.T.;
RT "Dual molecular signals mediate the bacterial response to outer-membrane
RT stress.";
RL Science 340:837-841(2013).
RN [24]
RP FUNCTION, AND MECHANISM OF TRANSLATION REGULATION.
RC STRAIN=K12 / CF7789;
RX PubMed=28924029; DOI=10.1128/jb.00484-17;
RA Yakhnin H., Aichele R., Ades S.E., Romeo T., Babitzke P.;
RT "Circuitry linking the global Csr and sigma(E)-dependent cell envelope
RT stress response systems.";
RL J. Bacteriol. 0:0-0(2017).
RN [25] {ECO:0007744|PDB:1OR7}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RSEA, INTERACTION
RP WITH RNA POLYMERASE, AND SUBUNIT.
RX PubMed=12718891; DOI=10.1016/s1097-2765(03)00148-5;
RA Campbell E.A., Tupy J.L., Gruber T.M., Wang S., Sharp M.M., Gross C.A.,
RA Darst S.A.;
RT "Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain
RT of its anti-sigma RseA.";
RL Mol. Cell 11:1067-1078(2003).
RN [26] {ECO:0007744|PDB:2H27}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 122-191 IN COMPLEX WITH DNA, AND
RP DOMAIN.
RX PubMed=16903784; DOI=10.1371/journal.pbio.0040269;
RA Lane W.J., Darst S.A.;
RT "The structural basis for promoter -35 element recognition by the group IV
RT sigma factors.";
RL PLoS Biol. 4:1491-1500(2006).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase (RNAP) to specific initiation sites and
CC are then released (PubMed:7889935, PubMed:2691330, PubMed:9159522,
CC PubMed:9159523). Extracytoplasmic function (ECF) sigma-E controls the
CC envelope stress response, responding to periplasmic protein stress,
CC increased levels of periplasmic lipopolysaccharide (LPS) as well as
CC heat shock (PubMed:7889935) and oxidative stress; it controls protein
CC processing in the extracytoplasmic compartment. The 90 member regulon
CC consists of the genes necessary for the synthesis and maintenance of
CC both proteins and LPS of the outer membrane (PubMed:7889934,
CC PubMed:11274153, PubMed:16336047). Indirectly activates transcription
CC of csrB and csrC, 2 sRNAs that antagonize translational regulator CsrA,
CC linking envelope stress, the stringent response and the catabolite
CC repression systems (PubMed:28924029). {ECO:0000269|PubMed:11274153,
CC ECO:0000269|PubMed:16336047, ECO:0000269|PubMed:2691330,
CC ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:7889934,
CC ECO:0000269|PubMed:7889935, ECO:0000269|PubMed:9159522,
CC ECO:0000269|PubMed:9159523}.
CC -!- ACTIVITY REGULATION: ECF sigma-E is held in an inactive form by its
CC cognate anti-sigma factor (RseA) until released by regulated
CC intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic
CC signal (periplasmic stress and excess LPS) triggers a concerted
CC proteolytic cascade to transmit information and elicit cellular
CC responses. The anti-sigma factor RseA is an inner membrane protein,
CC binding sigma-E in the cytoplasm and RseB in the periplasm. RseA is
CC first cut extracytoplasmically (site-1 protease, S1P, by DegS), then
CC within the membrane itself (site-2 protease, S2P, by RseP), while
CC cytoplasmic proteases (predominantly ClpX-ClpP) finish degrading the
CC regulatory protein, liberating sigma-E (PubMed:15371343). Degradation
CC of RseA requires 2 signals to activate DegS; an outer membrane protein
CC (OMP) signal activates DegS, while an LPS signal causes release of RseB
CC from RseA, freeing RseA to be cleaved (PubMed:23687042). The rate-
CC limiting step in this protease cascade is the first signal-sensing
CC cleavage (half-life about 1 minute) (PubMed:17210793).
CC {ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:17210793,
CC ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:9159522}.
CC -!- SUBUNIT: Interacts transiently with the RNAP catalytic core formed by
CC RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega
CC subunit) to form the RNAP holoenzyme that can initiate transcription
CC (PubMed:12016219, PubMed:12718891, PubMed:7889935, PubMed:2691330).
CC Interacts 1:1 with anti-sigma-E factor RseA which prevents binding to
CC RNAP catalytic core (PubMed:9159522, PubMed:9159523, PubMed:11777003,
CC PubMed:12016219, PubMed:15371343, PubMed:12718891). An N-terminal
CC (residues 1-108) RseA sigma-E complex also interacts with SspB
CC (PubMed:15371343). {ECO:0000269|PubMed:11777003,
CC ECO:0000269|PubMed:12016219, ECO:0000269|PubMed:12718891,
CC ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:16903784,
CC ECO:0000269|PubMed:2691330, ECO:0000269|PubMed:9159522,
CC ECO:0000269|PubMed:9159523}.
CC -!- INTERACTION:
CC P0AGB6; Q46864: mqsA; NbExp=2; IntAct=EBI-1129580, EBI-1120353;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11777003,
CC ECO:0000269|PubMed:9159522}. Note=Associates with the inner membrane
CC via RseA (PubMed:9159522, PubMed:11777003).
CC {ECO:0000269|PubMed:11777003}.
CC -!- INDUCTION: Induced after shifting to 50 degrees Celsius (at protein
CC level) (PubMed:2691330). Induced when the level of outer membrane
CC proteins (OMP) increases (at protein level) (PubMed:8276244,
CC PubMed:10500101). Induced as periplasmic levels of LPS levels increase
CC (PubMed:23687042). Induced by misfolded periplasmic proteins
CC (PubMed:9351822). Transcription positively autoregulated (via promoter
CC P2) (PubMed:7889935). Transcription slightly induced by elevated
CC temperatures (PubMed:7889934). Transiently induced by cold shock in a
CC PNPase-dependent fashion (PubMed:14527658). Translation repressed by
CC CsrA which binds to 3 sites in the 5'-UTR which occludes the ribosome
CC binding site (PubMed:28924029). Translation is coupled to upstream
CC leader peptide RseD, whose stop codon overlaps with the start codon of
CC rpoE; when coupling is eliminated translation is decreased by about 50%
CC (PubMed:28924029). Part of the rseD-rpoE-rseA-rseB-rseC operon
CC (PubMed:9159522, PubMed:9159523, PubMed:28924029).
CC {ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:14527658,
CC ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:2691330,
CC ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:7889934,
CC ECO:0000269|PubMed:7889935, ECO:0000269|PubMed:8276244,
CC ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523,
CC ECO:0000269|PubMed:9351822}.
CC -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific
CC interaction with the -10 element in promoter DNA, and plays an
CC important role in melting the double-stranded DNA and the formation of
CC the transcription bubble. The sigma-70 factor domain-2 mediates
CC interaction with the RNA polymerase subunits RpoB and RpoC.
CC {ECO:0000269|PubMed:12016219}.
CC -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-
CC H) motif that mediates interaction with the -35 element in promoter
CC DNA. The domain also mediates interaction with the RNA polymerase
CC subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-
CC sigma factors prevents interaction of sigma factors with the RNA
CC polymerase catalytic core. {ECO:0000269|PubMed:12016219,
CC ECO:0000269|PubMed:16903784}.
CC -!- DISRUPTION PHENOTYPE: Reduced viability at 37 degrees Celsius, death at
CC 42 degrees Celsius (PubMed:7889935). Loss of transcription from rpoE-
CC dependent promoters (PubMed:7889935). Increased sensitivity to outer
CC membrane disruption (PubMed:7889934). {ECO:0000269|PubMed:7889934,
CC ECO:0000269|PubMed:7889935}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA10920.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D13169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U37089; AAC45314.1; -; Genomic_DNA.
DR EMBL; D64044; BAA10920.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75626.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76749.1; -; Genomic_DNA.
DR EMBL; U10148; AAA83998.1; -; Genomic_DNA.
DR PIR; I60227; I60227.
DR RefSeq; NP_417068.1; NC_000913.3.
DR RefSeq; WP_001295364.1; NZ_STEB01000011.1.
DR PDB; 1OR7; X-ray; 2.00 A; A/B=1-191.
DR PDB; 2H27; X-ray; 2.30 A; A/D=122-191.
DR PDB; 5OR5; NMR; -; A=1-64, A=79-92.
DR PDB; 6JBQ; EM; 4.02 A; F=1-191.
DR PDBsum; 1OR7; -.
DR PDBsum; 2H27; -.
DR PDBsum; 5OR5; -.
DR PDBsum; 6JBQ; -.
DR AlphaFoldDB; P0AGB6; -.
DR BMRB; P0AGB6; -.
DR EMDB; EMD-9792; -.
DR SMR; P0AGB6; -.
DR BioGRID; 4263046; 226.
DR BioGRID; 851388; 9.
DR ComplexPortal; CPX-2532; rpoe-rsea-rseb sigma-antisigma complex.
DR ComplexPortal; CPX-4885; DNA-directed RNA polymerase holoenzyme complex, SigmaE variant.
DR DIP; DIP-10774N; -.
DR IntAct; P0AGB6; 30.
DR STRING; 511145.b2573; -.
DR jPOST; P0AGB6; -.
DR PaxDb; 511145-b2573; -.
DR EnsemblBacteria; AAC75626; AAC75626; b2573.
DR GeneID; 83579881; -.
DR GeneID; 947050; -.
DR KEGG; ecj:JW2557; -.
DR KEGG; eco:b2573; -.
DR PATRIC; fig|1411691.4.peg.4161; -.
DR EchoBASE; EB1843; -.
DR eggNOG; COG1595; Bacteria.
DR HOGENOM; CLU_047691_3_0_6; -.
DR InParanoid; P0AGB6; -.
DR OMA; QFYTWLY; -.
DR OrthoDB; 9780326at2; -.
DR PhylomeDB; P0AGB6; -.
DR BioCyc; EcoCyc:RPOE-MONOMER; -.
DR BioCyc; MetaCyc:RPOE-MONOMER; -.
DR EvolutionaryTrace; P0AGB6; -.
DR PHI-base; PHI:123198; -.
DR PRO; PR:P0AGB6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0000345; C:cytosolic DNA-directed RNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:1903865; C:sigma factor antagonist complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IBA:GO_Central.
DR GO; GO:0036460; P:cellular response to cell envelope stress; NAS:ComplexPortal.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IDA:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; NAS:ComplexPortal.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:EcoCyc.
DR GO; GO:2000142; P:regulation of DNA-templated transcription initiation; IDA:ComplexPortal.
DR GO; GO:0006970; P:response to osmotic stress; IDA:EcoCyc.
DR GO; GO:0009266; P:response to temperature stimulus; IDA:EcoCyc.
DR GO; GO:0090605; P:submerged biofilm formation; NAS:ComplexPortal.
DR CDD; cd06171; Sigma70_r4; 1.
DR Gene3D; 1.10.1740.10; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR039425; RNA_pol_sigma-70-like.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR013249; RNA_pol_sigma70_r4_t2.
DR InterPro; IPR014286; RNA_pol_sigma70_RpoE.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR02939; RpoE_Sigma70; 1.
DR NCBIfam; TIGR02937; sigma70-ECF; 1.
DR PANTHER; PTHR43133:SF51; ECF RNA POLYMERASE SIGMA-E FACTOR; 1.
DR PANTHER; PTHR43133; RNA POLYMERASE ECF-TYPE SIGMA FACTO; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF08281; Sigma70_r4_2; 1.
DR SUPFAM; SSF88946; Sigma2 domain of RNA polymerase sigma factors; 1.
DR SUPFAM; SSF88659; Sigma3 and sigma4 domains of RNA polymerase sigma factors; 1.
DR PROSITE; PS01063; SIGMA70_ECF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome; Sigma factor; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..191
FT /note="ECF RNA polymerase sigma-E factor"
FT /id="PRO_0000093997"
FT DNA_BIND 156..175
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 1..153
FT /note="Binds RNAP core"
FT /evidence="ECO:0000269|PubMed:12016219"
FT REGION 25..92
FT /note="Sigma-70 factor domain-2"
FT REGION 129..180
FT /note="Sigma-70 factor domain-4"
FT MOTIF 48..61
FT /note="Polymerase core binding"
FT MUTAGEN 25
FT /note="L->P: In SR1576; loss of sigma factor activity."
FT /evidence="ECO:0000269|PubMed:7889935"
FT MUTAGEN 165
FT /note="C->A: Binds RNAP and RseA normally."
FT /evidence="ECO:0000269|PubMed:12016219"
FT MUTAGEN 172
FT /note="S->P: In SR1723; loss of sigma factor activity."
FT /evidence="ECO:0000269|PubMed:7889935"
FT MUTAGEN 178
FT /note="R->G: In SR1502; decreased sigma factor activity.
FT Does not bind RseA, still binds RNAP."
FT /evidence="ECO:0000269|PubMed:12016219,
FT ECO:0000269|PubMed:7889935"
FT MUTAGEN 181
FT /note="I->A: In SR1503; decreased sigma factor activity.
FT Does not bind RseA, still binds RNAP."
FT /evidence="ECO:0000269|PubMed:12016219"
FT MUTAGEN 185
FT /note="V->A: In SR1504; decreased sigma factor activity.
FT Does not bind RseA, still binds RNAP."
FT /evidence="ECO:0000269|PubMed:12016219"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:1OR7"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1OR7"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 70..89
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:1OR7"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 167..185
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2H27"
SQ SEQUENCE 191 AA; 21696 MW; C71EEF5939C3611E CRC64;
MSEQLTDQVL VERVQKGDQK AFNLLVVRYQ HKVASLVSRY VPSGDVPDVV QEAFIKAYRA
LDSFRGDSAF YTWLYRIAVN TAKNYLVAQG RRPPSSDVDA IEAENFESGG ALKEISNPEN
LMLSEELRQI VFRTIESLPE DLRMAITLRE LDGLSYEEIA AIMDCPVGTV RSRIFRAREA
IDNKVQPLIR R
//
