RPOE_ECO57
ID RPOE_ECO57 Reviewed; 191 AA.
AC P0AGB8; P34086;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Z3855, ECs3439;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
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DR EMBL; AE005174; AAG57689.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36862.1; -; Genomic_DNA.
DR PIR; E85903; E85903.
DR PIR; G91058; G91058.
DR RefSeq; NP_311466.1; NC_002695.1.
DR RefSeq; WP_001295364.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AGB8; -.
DR SMR; P0AGB8; -.
DR STRING; 155864.EDL933_3738; -.
DR PRIDE; P0AGB8; -.
DR EnsemblBacteria; AAG57689; AAG57689; Z3855.
DR EnsemblBacteria; BAB36862; BAB36862; ECs_3439.
DR GeneID; 67416952; -.
DR GeneID; 914887; -.
DR KEGG; ece:Z3855; -.
DR KEGG; ecs:ECs_3439; -.
DR PATRIC; fig|386585.9.peg.3593; -.
DR eggNOG; COG1595; Bacteria.
DR HOGENOM; CLU_047691_3_0_6; -.
DR OMA; LVDMQGY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Sigma factor; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..191
FT /note="ECF RNA polymerase sigma-E factor"
FT /id="PRO_0000093998"
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
