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ECF RNA polymerase sigma-E factor (RNA polymerase sigma-E factor) (Sigma-24)

 RPOE_ECOLI              Reviewed;         191 AA.
P0AGB6; P34086; Q2MAF7;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
20-JUN-2018, entry version 104.
RecName: Full=ECF RNA polymerase sigma-E factor;
AltName: Full=RNA polymerase sigma-E factor;
AltName: Full=Sigma-24;
Name=rpoE; Synonyms=sigE; OrderedLocusNames=b2573, JW2557;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Nashimoto H.;
"Non-ribosomal proteins affecting the assembly of ribosomes in
Escherichia coli.";
(In) Nierhaus K.H. (eds.);
The translational apparatus, pp.185-195, Plenum Press, New York
(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A SIGMA FACTOR,
SUBUNIT, AUTOREGULATION, GENE IDENTIFICATION, DISRUPTION PHENOTYPE,
AND MUTAGENESIS OF LEU-25; SER-172 AND ARG-178.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and
K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=7889935;
Raina S., Missiakas D., Georgopoulos C.;
"The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor
of Escherichia coli.";
EMBO J. 14:1043-1055(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Nashimoto H., Saito N.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 171-191.
STRAIN=K12 / VD1870;
PubMed=7768826; DOI=10.1128/jb.177.11.3259-3268.1995;
Yu H., Schurr M.J., Deretic V.;
"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.";
J. Bacteriol. 177:3259-3268(1995).
[7]
PROTEIN SEQUENCE OF 40-56, GENE IDENTIFICATION, FUNCTION AS A SIGMA
FACTOR, INDUCTION, REGULON, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=7889934;
Rouviere P.E., de Las Penas A., Mecsas J., Lu C.Z., Rudd K.E.,
Gross C.A.;
"rpoE, the gene encoding the second heat-shock sigma factor, sigma E,
in Escherichia coli.";
EMBO J. 14:1032-1042(1995).
[8]
FUNCTION AS A SIGMA FACTOR, SUBUNIT, AND INDUCTION AT HIGH
TEMPERATURE.
STRAIN=SC122;
PubMed=2691330; DOI=10.1101/gad.3.9.1462;
Erickson J.W., Gross C.A.;
"Identification of the sigma E subunit of Escherichia coli RNA
polymerase: a second alternate sigma factor involved in high-
temperature gene expression.";
Genes Dev. 3:1462-1471(1989).
[9]
INDUCTION IN RESPONSE TO OUTER MEMBRANE PROTEIN LEVELS.
PubMed=8276244; DOI=10.1101/gad.7.12b.2618;
Mecsas J., Rouviere P.E., Erickson J.W., Donohue T.J., Gross C.A.;
"The activity of sigma E, an Escherichia coli heat-inducible sigma-
factor, is modulated by expression of outer membrane proteins.";
Genes Dev. 7:2618-2628(1993).
[10]
GENE IDENTIFICATION.
PubMed=7961422; DOI=10.1128/jb.176.21.6688-6696.1994;
Martin D.W., Schurr M.J., Yu H., Deretic V.;
"Analysis of promoters controlled by the putative sigma factor AlgU
regulating conversion to mucoidy in Pseudomonas aeruginosa:
relationship to sigma E and stress response.";
J. Bacteriol. 176:6688-6696(1994).
[11]
GENE IDENTIFICATION.
PubMed=8052622; DOI=10.1073/pnas.91.16.7573;
Lonetto M.A., Brown K.L., Rudd K.E., Buttner M.J.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 91:7573-7577(1994).
[12]
FUNCTION AS A SIGMA FACTOR, ENZYME REGULATION, INTERACTION WITH RSEA,
SUBUNIT, SUBCELLULAR LOCATION, AND OPERON.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=9159522; DOI=10.1046/j.1365-2958.1997.3601713.x;
Missiakas D., Mayer M.P., Lemaire M., Georgopoulos C., Raina S.;
"Modulation of the Escherichia coli sigmaE (RpoE) heat-shock
transcription-factor activity by the RseA, RseB and RseC proteins.";
Mol. Microbiol. 24:355-371(1997).
[13]
FUNCTION AS A SIGMA FACTOR, INTERACTION WITH RSEA, SUBUNIT, AND
OPERON.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=9159523; DOI=10.1046/j.1365-2958.1997.3611718.x;
De Las Penas A., Connolly L., Gross C.A.;
"The sigmaE-mediated response to extracytoplasmic stress in
Escherichia coli is transduced by RseA and RseB, two negative
regulators of sigmaE.";
Mol. Microbiol. 24:373-385(1997).
[14]
INDUCTION.
PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
"The chaperone-assisted membrane release and folding pathway is sensed
by two signal transduction systems.";
EMBO J. 16:6394-6406(1997).
[15]
INDUCTION.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=10500101; DOI=10.1101/gad.13.18.2449;
Ades S.E., Connolly L.E., Alba B.M., Gross C.A.;
"The Escherichia coli sigma(E)-dependent extracytoplasmic stress
response is controlled by the regulated proteolysis of an anti-sigma
factor.";
Genes Dev. 13:2449-2461(1999).
[16]
INTERACTION WITH RSEA, AND SUBCELLULAR LOCATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11777003; DOI=10.1074/jbc.M006214200;
Collinet B., Yuzawa H., Chen T., Herrera C., Missiakas D.;
"RseB binding to the periplasmic domain of RseA modulates the
RseA:sigmaE interaction in the cytoplasm and the availability of
sigmaE.RNA polymerase.";
J. Biol. Chem. 275:33898-33904(2000).
[17]
REGULON.
PubMed=11274153; DOI=10.1074/jbc.M100464200;
Dartigalongue C., Missiakas D., Raina S.;
"Characterization of the Escherichia coli sigma E regulon.";
J. Biol. Chem. 276:20866-20875(2001).
[18]
INTERACTION WITH RNA POLYMERASE AND RSEA, SUBUNIT, DOMAIN, AND
MUTAGENESIS OF CYS-165; ARG-178; ILE-181 AND VAL-185.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12016219; DOI=10.1074/jbc.M202881200;
Tam C., Collinet B., Lau G., Raina S., Missiakas D.;
"Interaction of the conserved region 4.2 of sigma(E) with the RseA
anti-sigma factor.";
J. Biol. Chem. 277:27282-27287(2002).
[19]
INDUCTION BY COLD SHOCK.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=14527658; DOI=10.1016/S0923-2508(03)00167-0;
Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V.,
Pesole G., Deho G.;
"Changes in Escherichia coli transcriptome during acclimatization at
low temperature.";
Res. Microbiol. 154:573-580(2003).
[20]
ENZYME REGULATION BY CLPX-CLPP, AND INTERACTION WITH RSEA AND SSPB.
PubMed=15371343; DOI=10.1101/gad.1240104;
Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
"Modulating substrate choice: the SspB adaptor delivers a regulator of
the extracytoplasmic-stress response to the AAA+ protease ClpXP for
degradation.";
Genes Dev. 18:2292-2301(2004).
[21]
FUNCTION, AND REGULON.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=16336047; DOI=10.1371/journal.pbio.0040002;
Rhodius V.A., Suh W.C., Nonaka G., West J., Gross C.A.;
"Conserved and variable functions of the sigmaE stress response in
related genomes.";
PLoS Biol. 4:E2-E2(2006).
[22]
ENZYME REGULATION.
PubMed=17210793; DOI=10.1101/gad.1496707;
Chaba R., Grigorova I.L., Flynn J.M., Baker T.A., Gross C.A.;
"Design principles of the proteolytic cascade governing the sigmaE-
mediated envelope stress response in Escherichia coli: keys to graded,
buffered, and rapid signal transduction.";
Genes Dev. 21:124-136(2007).
[23]
ENZYME REGULATION, AND INDUCTION BY LIPOPOLYSACCHARIDE.
STRAIN=K12;
PubMed=23687042; DOI=10.1126/science.1235358;
Lima S., Guo M.S., Chaba R., Gross C.A., Sauer R.T.;
"Dual molecular signals mediate the bacterial response to outer-
membrane stress.";
Science 340:837-841(2013).
[24]
FUNCTION, AND MECHANISM OF TRANSLATION REGULATION.
STRAIN=K12 / CF7789;
PubMed=28924029; DOI=10.1128/JB.00484-17;
Yakhnin H., Aichele R., Ades S.E., Romeo T., Babitzke P.;
"Circuitry linking the global Csr and sigma(E)-dependent cell envelope
stress response systems.";
J. Bacteriol. 0:0-0(2017).
[25] {ECO:0000244|PDB:1OR7}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RSEA,
INTERACTION WITH RNA POLYMERASE, AND SUBUNIT.
PubMed=12718891; DOI=10.1016/S1097-2765(03)00148-5;
Campbell E.A., Tupy J.L., Gruber T.M., Wang S., Sharp M.M.,
Gross C.A., Darst S.A.;
"Crystal structure of Escherichia coli sigmaE with the cytoplasmic
domain of its anti-sigma RseA.";
Mol. Cell 11:1067-1078(2003).
[26] {ECO:0000244|PDB:2H27}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 122-191 IN COMPLEX WITH DNA,
AND DOMAIN.
PubMed=16903784; DOI=10.1371/journal.pbio.0040269;
Lane W.J., Darst S.A.;
"The structural basis for promoter -35 element recognition by the
group IV sigma factors.";
PLoS Biol. 4:1491-1500(2006).
-!- FUNCTION: 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). Indirectly activates
transcription of csrB and csrC, 2 sRNAs that antagonize
translational regulator CsrA, linking envelope stress, the
stringent response and the catabolite repression systems
(PubMed:28924029). {ECO:0000269|PubMed:11274153,
ECO:0000269|PubMed:16336047, ECO:0000269|PubMed:2691330,
ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:7889934,
ECO:0000269|PubMed:7889935, ECO:0000269|PubMed:9159522,
ECO:0000269|PubMed:9159523}.
-!- ENZYME REGULATION: 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).
{ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:17210793,
ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:9159522}.
-!- SUBUNIT: 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 (PubMed:15371343).
{ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12016219,
ECO:0000269|PubMed:12718891, ECO:0000269|PubMed:15371343,
ECO:0000269|PubMed:16903784, ECO:0000269|PubMed:2691330,
ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
-!- INTERACTION:
Q46864:mqsA; NbExp=2; IntAct=EBI-1129580, EBI-1120353;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11777003,
ECO:0000269|PubMed:9159522}. Note=Associates with the inner
membrane via RseA (PubMed:9159522, PubMed:11777003).
{ECO:0000269|PubMed:11777003}.
-!- INDUCTION: Induced after shifting to 50 degrees Celsius (at
protein level) (PubMed:2691330). Induced when the level of outer
membrane proteins (OMP) increases (at protein level)
(PubMed:8276244, PubMed:10500101). Induced as periplasmic levels
of LPS levels increase (PubMed:23687042). Induced by misfolded
periplasmic proteins (PubMed:9351822). Transcription positively
autoregulated (via promoter P2) (PubMed:7889935). Transcription
slightly induced by elevated temperatures (PubMed:7889934).
Transiently induced by cold shock in a PNPase-dependent fashion
(PubMed:14527658). Translation repressed by CsrA which binds to 3
sites in the 5'-UTR which occludes the ribosome binding site
(PubMed:28924029). Translation is coupled to upstream leader
peptide RseD, whose stop codon overlaps with the start codon of
rpoE; when coupling is eliminated translation is decreased by
about 50% (PubMed:28924029). Part of the rseD-rpoE-rseA-rseB-rseC
operon (PubMed:9159522, PubMed:9159523, PubMed:28924029).
{ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:14527658,
ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:2691330,
ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:7889934,
ECO:0000269|PubMed:7889935, ECO:0000269|PubMed:8276244,
ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523,
ECO:0000269|PubMed:9351822}.
-!- DOMAIN: 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. {ECO:0000269|PubMed:12016219}.
-!- DOMAIN: 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.
{ECO:0000269|PubMed:12016219, ECO:0000269|PubMed:16903784}.
-!- DISRUPTION PHENOTYPE: 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). {ECO:0000269|PubMed:7889934,
ECO:0000269|PubMed:7889935}.
-!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA10920.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D13169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U37089; AAC45314.1; -; Genomic_DNA.
EMBL; D64044; BAA10920.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC75626.1; -; Genomic_DNA.
EMBL; AP009048; BAE76749.1; -; Genomic_DNA.
EMBL; U10148; AAA83998.1; -; Genomic_DNA.
PIR; I60227; I60227.
RefSeq; NP_417068.1; NC_000913.3.
RefSeq; WP_001295364.1; NZ_LN832404.1.
PDB; 1OR7; X-ray; 2.00 A; A/B=1-191.
PDB; 2H27; X-ray; 2.30 A; A/D=122-191.
PDBsum; 1OR7; -.
PDBsum; 2H27; -.
ProteinModelPortal; P0AGB6; -.
SMR; P0AGB6; -.
BioGrid; 4263046; 226.
ComplexPortal; CPX-2532; Sigma-E factor negative regulation complex.
DIP; DIP-10774N; -.
IntAct; P0AGB6; 30.
STRING; 316385.ECDH10B_2741; -.
PaxDb; P0AGB6; -.
PRIDE; P0AGB6; -.
EnsemblBacteria; AAC75626; AAC75626; b2573.
EnsemblBacteria; BAE76749; BAE76749; BAE76749.
GeneID; 947050; -.
KEGG; ecj:JW2557; -.
KEGG; eco:b2573; -.
PATRIC; fig|1411691.4.peg.4161; -.
EchoBASE; EB1843; -.
EcoGene; EG11897; rpoE.
eggNOG; ENOG4105EMN; Bacteria.
eggNOG; COG1595; LUCA.
HOGENOM; HOG000094755; -.
InParanoid; P0AGB6; -.
KO; K03088; -.
OMA; EHADRVY; -.
PhylomeDB; P0AGB6; -.
BioCyc; EcoCyc:RPOE-MONOMER; -.
BioCyc; MetaCyc:RPOE-MONOMER; -.
EvolutionaryTrace; P0AGB6; -.
PRO; PR:P0AGB6; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoCyc.
GO; GO:0006970; P:response to osmotic stress; IDA:EcoCyc.
GO; GO:0009266; P:response to temperature stimulus; IDA:EcoCyc.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR014284; RNA_pol_sigma-70_dom.
InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
InterPro; IPR007627; RNA_pol_sigma70_r2.
InterPro; IPR013249; RNA_pol_sigma70_r4_t2.
InterPro; IPR014286; RNA_pol_sigma70_RpoE.
InterPro; IPR013325; RNA_pol_sigma_r2.
InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
InterPro; IPR036388; WH-like_DNA-bd_sf.
Pfam; PF04542; Sigma70_r2; 1.
Pfam; PF08281; Sigma70_r4_2; 1.
SUPFAM; SSF88659; SSF88659; 1.
SUPFAM; SSF88946; SSF88946; 1.
TIGRFAMs; TIGR02939; RpoE_Sigma70; 1.
TIGRFAMs; TIGR02937; sigma70-ECF; 1.
PROSITE; PS01063; SIGMA70_ECF; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
DNA-binding; Reference proteome; Sigma factor; Stress response;
Transcription; Transcription regulation.
CHAIN 1 191 ECF RNA polymerase sigma-E factor.
/FTId=PRO_0000093997.
DNA_BIND 156 175 H-T-H motif. {ECO:0000250}.
REGION 1 153 Binds RNAP core.
{ECO:0000269|PubMed:12016219}.
REGION 25 92 Sigma-70 factor domain-2.
REGION 129 180 Sigma-70 factor domain-4.
MOTIF 48 61 Polymerase core binding.
MUTAGEN 25 25 L->P: In SR1576; loss of sigma factor
activity. {ECO:0000269|PubMed:7889935}.
MUTAGEN 165 165 C->A: Binds RNAP and RseA normally.
{ECO:0000269|PubMed:12016219}.
MUTAGEN 172 172 S->P: In SR1723; loss of sigma factor
activity. {ECO:0000269|PubMed:7889935}.
MUTAGEN 178 178 R->G: In SR1502; decreased sigma factor
activity. Does not bind RseA, still binds
RNAP. {ECO:0000269|PubMed:12016219,
ECO:0000269|PubMed:7889935}.
MUTAGEN 181 181 I->A: In SR1503; decreased sigma factor
activity. Does not bind RseA, still binds
RNAP. {ECO:0000269|PubMed:12016219}.
MUTAGEN 185 185 V->A: In SR1504; decreased sigma factor
activity. Does not bind RseA, still binds
RNAP. {ECO:0000269|PubMed:12016219}.
HELIX 2 15 {ECO:0000244|PDB:1OR7}.
HELIX 19 37 {ECO:0000244|PDB:1OR7}.
TURN 38 40 {ECO:0000244|PDB:1OR7}.
HELIX 43 45 {ECO:0000244|PDB:1OR7}.
HELIX 46 60 {ECO:0000244|PDB:1OR7}.
HELIX 61 63 {ECO:0000244|PDB:1OR7}.
STRAND 66 68 {ECO:0000244|PDB:1OR7}.
HELIX 70 89 {ECO:0000244|PDB:1OR7}.
HELIX 95 104 {ECO:0000244|PDB:1OR7}.
STRAND 121 123 {ECO:0000244|PDB:1OR7}.
HELIX 124 137 {ECO:0000244|PDB:1OR7}.
HELIX 140 150 {ECO:0000244|PDB:1OR7}.
HELIX 156 162 {ECO:0000244|PDB:1OR7}.
HELIX 167 185 {ECO:0000244|PDB:1OR7}.
HELIX 186 188 {ECO:0000244|PDB:2H27}.
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


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