RPOE_SALT1
ID RPOE_SALT1 Reviewed; 191 AA.
AC D0ZSY9;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ECF RNA polymerase sigma-E factor;
DE AltName: Full=RNA polymerase sigma-E factor;
GN Name=rpoE; Synonyms=sigE; OrderedLocusNames=STM14_3234;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=11929531; DOI=10.1046/j.1365-2958.2002.02787.x;
RA Testerman T.L., Vazquez-Torres A., Xu Y., Jones-Carson J., Libby S.J.,
RA Fang F.C.;
RT "The alternative sigma factor sigmaE controls antioxidant defences required
RT for Salmonella virulence and stationary-phase survival.";
RL Mol. Microbiol. 43:771-782(2002).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, INDUCTION, AUTOREGULATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19170886; DOI=10.1111/j.1365-2958.2009.06597.x;
RA Muller C., Bang I.S., Velayudhan J., Karlinsey J., Papenfort K., Vogel J.,
RA Fang F.C.;
RT "Acid stress activation of the sigma(E) stress response in Salmonella
RT enterica serovar Typhimurium.";
RL Mol. Microbiol. 71:1228-1238(2009).
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. 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 acid stress, heat shock and oxidative stress; it controls protein
CC processing in the extracytoplasmic compartment.
CC {ECO:0000269|PubMed:19170886}.
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, acid or heat stress) triggers a concerted
CC proteolytic cascade to transmit information and elicit cellular
CC responses. In S.typhimurium there are 2 cascades, the heat shock
CC response which depends on DegS and RseP, and acid response which
CC depends only on RseP. The anti-sigma factor RseA is an inner membrane
CC protein, binding sigma-E in the cytoplasm and RseB in the periplasm.
CC RseA is first cut extracytoplasmically (site-1 protease, S1P, by DegS),
CC then 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. Degradation of RseA requires 2
CC signals to activate DegS; an outer membrane protein (OMP) signal
CC activates DegS, while an LPS signal causes release of RseB from RseA,
CC freeing RseA to be cleaved. OMP stress can be abrogated by
CC overexpression of the sRNA rybB. {ECO:0000269|PubMed:19170886}.
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 Interacts 1:1 with anti-sigma-E factor RseA which prevents binding to
CC RNAP catalytic core (Probable). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Associates with the
CC inner membrane via RseA. {ECO:0000305}.
CC -!- INDUCTION: Poorly expressed in logarithmic growth, induced in
CC stationary phase. By acid stress (pH 4.5), heat shock. Has 3 promoters,
CC the first 2 are sigma-70-dependent, the third is positively auto-
CC regulated. {ECO:0000269|PubMed:11929531, ECO:0000269|PubMed:19170886}.
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Not essential. Increased sensitivity to oxidative
CC stress. 100-fold decreased survival in acidified murine macrophages,
CC slightly reduced growth at pH 7.0, delayed growth at pH 4.5, severely
CC delayed growth at pH 3.0. Loss of sigma-E-dependent acid tolerance
CC response, loss of acid and heat stress response.
CC {ECO:0000269|PubMed:11929531, ECO:0000269|PubMed:19170886}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
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DR EMBL; CP001363; ACY89663.1; -; Genomic_DNA.
DR RefSeq; WP_000003307.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZSY9; -.
DR BMRB; D0ZSY9; -.
DR SMR; D0ZSY9; -.
DR EnsemblBacteria; ACY89663; ACY89663; STM14_3234.
DR GeneID; 67373980; -.
DR KEGG; seo:STM14_3234; -.
DR PATRIC; fig|588858.6.peg.3001; -.
DR HOGENOM; CLU_047691_3_0_6; -.
DR OMA; LVDMQGY; -.
DR BioCyc; SENT588858:STM14_RS14455-MON; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0097533; P:cellular stress response to acid chemical; IMP:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 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 PANTHER; PTHR43133; PTHR43133; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF08281; Sigma70_r4_2; 1.
DR SUPFAM; SSF88659; SSF88659; 1.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02939; RpoE_Sigma70; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS01063; SIGMA70_ECF; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Sigma factor; Stress response; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..191
FT /note="ECF RNA polymerase sigma-E factor"
FT /id="PRO_0000424883"
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:0000250"
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"
SQ 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
