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RPOE_SALTY
ID   RPOE_SALTY              Reviewed;         191 AA.
AC   P0A2F0; P37401;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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; Synonyms=sigE; OrderedLocusNames=STM2640;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C3181;
RX   PubMed=7961422; DOI=10.1128/jb.176.21.6688-6696.1994;
RA   Martin D.W., Schurr M.J., Yu H., Deretic V.;
RT   "Analysis of promoters controlled by the putative sigma factor AlgU
RT   regulating conversion to mucoidy in Pseudomonas aeruginosa: relationship to
RT   sigma E and stress response.";
RL   J. Bacteriol. 176:6688-6696(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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       acid stress, heat shock and oxidative stress; it controls protein
CC       processing in the extracytoplasmic compartment (By similarity).
CC       {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; U05669; AAA57186.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21534.1; -; Genomic_DNA.
DR   RefSeq; NP_461575.1; NC_003197.2.
DR   RefSeq; WP_000003307.1; NC_003197.2.
DR   AlphaFoldDB; P0A2F0; -.
DR   BMRB; P0A2F0; -.
DR   SMR; P0A2F0; -.
DR   STRING; 99287.STM2640; -.
DR   PaxDb; P0A2F0; -.
DR   EnsemblBacteria; AAL21534; AAL21534; STM2640.
DR   GeneID; 1254163; -.
DR   GeneID; 67373980; -.
DR   KEGG; stm:STM2640; -.
DR   PATRIC; fig|99287.12.peg.2790; -.
DR   HOGENOM; CLU_047691_3_0_6; -.
DR   OMA; LVDMQGY; -.
DR   PhylomeDB; P0A2F0; -.
DR   BioCyc; SENT99287:STM2640-MON; -.
DR   PHI-base; PHI:2680; -.
DR   PRO; PR:P0A2F0; -.
DR   Proteomes; UP000001014; 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: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_0000094001"
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;  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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