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

 RPOE_SALT1              Reviewed;         191 AA.
D0ZSY9;
22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
19-JAN-2010, sequence version 1.
28-MAR-2018, entry version 49.
RecName: Full=ECF RNA polymerase sigma-E factor;
AltName: Full=RNA polymerase sigma-E factor;
Name=rpoE; Synonyms=sigE; OrderedLocusNames=STM14_3234;
Salmonella typhimurium (strain 14028s / SGSC 2262).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=588858;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=14028s / SGSC 2262;
PubMed=19897643; DOI=10.1128/JB.01233-09;
Jarvik T., Smillie C., Groisman E.A., Ochman H.;
"Short-term signatures of evolutionary change in the Salmonella
enterica serovar typhimurium 14028 genome.";
J. Bacteriol. 192:560-567(2010).
[2]
INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=14028s / SGSC 2262;
PubMed=11929531; DOI=10.1046/j.1365-2958.2002.02787.x;
Testerman T.L., Vazquez-Torres A., Xu Y., Jones-Carson J., Libby S.J.,
Fang F.C.;
"The alternative sigma factor sigmaE controls antioxidant defences
required for Salmonella virulence and stationary-phase survival.";
Mol. Microbiol. 43:771-782(2002).
[3]
FUNCTION, ENZYME REGULATION, INDUCTION, AUTOREGULATION, AND DISRUPTION
PHENOTYPE.
STRAIN=14028s / SGSC 2262;
PubMed=19170886; DOI=10.1111/j.1365-2958.2009.06597.x;
Muller C., Bang I.S., Velayudhan J., Karlinsey J., Papenfort K.,
Vogel J., Fang F.C.;
"Acid stress activation of the sigma(E) stress response in Salmonella
enterica serovar Typhimurium.";
Mol. Microbiol. 71:1228-1238(2009).
-!- FUNCTION: Sigma factors are initiation factors that promote the
attachment of RNA polymerase (RNAP) to specific initiation sites
and are then released. Extracytoplasmic function (ECF) sigma-E
controls the envelope stress response, responding to periplasmic
protein stress, increased levels of periplasmic lipopolysaccharide
(LPS) as well as acid stress, heat shock and oxidative stress; it
controls protein processing in the extracytoplasmic compartment.
{ECO:0000269|PubMed:19170886}.
-!- 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, acid or heat stress)
triggers a concerted proteolytic cascade to transmit information
and elicit cellular responses. In S.typhimurium there are 2
cascades, the heat shock response which depends on DegS and RseP,
and acid response which depends only on RseP. 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. 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. OMP stress can be
abrogated by overexpression of the sRNA rybB.
{ECO:0000269|PubMed:19170886}.
-!- 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. Interacts 1:1 with anti-sigma-E factor RseA which
prevents binding to RNAP catalytic core (Probable). {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Associates
with the inner membrane via RseA. {ECO:0000305}.
-!- INDUCTION: Poorly expressed in logarithmic growth, induced in
stationary phase. By acid stress (pH 4.5), heat shock. Has 3
promoters, the first 2 are sigma-70-dependent, the third is
positively auto-regulated. {ECO:0000269|PubMed:11929531,
ECO:0000269|PubMed:19170886}.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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 (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Not essential. Increased sensitivity to
oxidative stress. 100-fold decreased survival in acidified murine
macrophages, slightly reduced growth at pH 7.0, delayed growth at
pH 4.5, severely delayed growth at pH 3.0. Loss of sigma-E-
dpenedent acid tolerance response, loss of acid and heat stress
response. {ECO:0000269|PubMed:11929531,
ECO:0000269|PubMed:19170886}.
-!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
{ECO:0000305}.
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EMBL; CP001363; ACY89663.1; -; Genomic_DNA.
RefSeq; WP_000003307.1; NC_016856.1.
ProteinModelPortal; D0ZSY9; -.
SMR; D0ZSY9; -.
EnsemblBacteria; ACY89663; ACY89663; STM14_3234.
GeneID; 32365800; -.
KEGG; seo:STM14_3234; -.
PATRIC; fig|588858.6.peg.3001; -.
KO; K03088; -.
OMA; EHADRVY; -.
OrthoDB; POG091H04ZH; -.
Proteomes; UP000002695; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016987; F:bacterial sigma factor activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0097533; P:cellular stress response to acid chemical; IMP:UniProtKB.
GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IMP:UniProtKB.
GO; GO:0009266; P:response to temperature stimulus; IEP:UniProtKB.
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.
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.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; DNA-binding; Sigma factor;
Stress response; Transcription; Transcription regulation; Virulence.
CHAIN 1 191 ECF RNA polymerase sigma-E factor.
/FTId=PRO_0000424883.
DNA_BIND 156 175 H-T-H motif. {ECO:0000250}.
REGION 1 153 Binds RNAP core. {ECO:0000250}.
REGION 25 92 Sigma-70 factor domain-2.
REGION 129 180 Sigma-70 factor domain-4.
MOTIF 48 61 Polymerase core binding.
SEQUENCE 191 AA; 21712 MW; D91F0782CF19611E CRC64;
MSEQLTDQVL VERVQKGDQK AFNLLVVRYQ HKVASLVSRY VPSGDVPDVV QESFIKAYRA
LDSFRGDSAF YTWLYRIAVN TAKNYLVAQG RRPPSSDVDA IEAENFESGG ALKEISNPEN
LMLSEELRQI VFRTIESLPE DLRMAITLRE LDGLSYEEIA AIMDCPVGTV RSRIFRAREA
IDNKVQPLIR R


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