RPOE_ECOL6
ID RPOE_ECOL6 Reviewed; 191 AA.
AC P0AGB7; P34086;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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; OrderedLocusNames=c3097;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 heat shock and oxidative stress; it controls protein processing in the
CC extracytoplasmic compartment (By similarity). {ECO:0000250}.
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. 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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associates with the
CC inner membrane via RseA. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN81546.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014075; AAN81546.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001295364.1; NC_004431.1.
DR AlphaFoldDB; P0AGB7; -.
DR BMRB; P0AGB7; -.
DR SMR; P0AGB7; -.
DR STRING; 199310.c3097; -.
DR EnsemblBacteria; AAN81546; AAN81546; c3097.
DR GeneID; 67416952; -.
DR KEGG; ecc:c3097; -.
DR eggNOG; COG1595; Bacteria.
DR HOGENOM; CLU_047691_3_0_6; -.
DR OMA; LVDMQGY; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
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 3: Inferred from homology;
KW Cytoplasm; DNA-binding; Sigma factor; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..191
FT /note="ECF RNA polymerase sigma-E factor"
FT /id="PRO_0000093999"
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 /evidence="ECO:0000250"
FT REGION 129..180
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000250"
FT MOTIF 48..61
FT /note="Polymerase core binding"
FT /evidence="ECO:0000250"
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
