RPOH_ECOLI
ID RPOH_ECOLI Reviewed; 284 AA.
AC P0AGB3; P00580; Q2M7C4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=RNA polymerase sigma factor RpoH {ECO:0000255|HAMAP-Rule:MF_00961};
DE AltName: Full=Heat shock regulatory protein F33.4;
DE AltName: Full=RNA polymerase sigma-32 factor {ECO:0000255|HAMAP-Rule:MF_00961};
GN Name=rpoH {ECO:0000255|HAMAP-Rule:MF_00961}; Synonyms=fam, hin, htpR;
GN OrderedLocusNames=b3461, JW3426;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841288; DOI=10.1128/jb.170.8.3479-3484.1988;
RA Calendar R., Erickson J.W., Halling C., Nolte A.;
RT "Deletion and insertion mutations in the rpoH gene of Escherichia coli that
RT produce functional sigma 32.";
RL J. Bacteriol. 170:3479-3484(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6088062; DOI=10.1016/0092-8674(84)90538-5;
RA Landick R., Vaughn V., Lau E.T., Vanbogelen R.A., Erickson J.W.,
RA Neidhardt F.C.;
RT "Nucleotide sequence of the heat shock regulatory gene of E. coli suggests
RT its protein product may be a transcription factor.";
RL Cell 38:175-182(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=6387714; DOI=10.1073/pnas.81.21.6803;
RA Yura T., Tobe T., Ito K., Osawa T.;
RT "Heat shock regulatory gene (htpR) of Escherichia coli is required for
RT growth at high temperature but is dispensable at low temperature.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6803-6807(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=3315848; DOI=10.1101/gad.1.2.179;
RA Grossman A.D., Straus D.B., Walter W.A., Gross C.A.;
RT "Sigma 32 synthesis can regulate the synthesis of heat shock proteins in
RT Escherichia coli.";
RL Genes Dev. 1:179-184(1987).
RN [8]
RP INDUCTION.
RX PubMed=3315851; DOI=10.1101/gad.1.5.419;
RA Erickson J.W., Vaughn V., Walter W.A., Neidhardt F.C., Gross C.A.;
RT "Regulation of the promoters and transcripts of rpoH, the Escherichia coli
RT heat shock regulatory gene.";
RL Genes Dev. 1:419-432(1987).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=3306410; DOI=10.1038/329348a0;
RA Straus D.B., Walter W.A., Gross C.A.;
RT "The heat shock response of E. coli is regulated by changes in the
RT concentration of sigma 32.";
RL Nature 329:348-351(1987).
RN [10]
RP INTERACTION WITH DNAK AND DNAJ, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=8599944; DOI=10.1002/j.1460-2075.1996.tb00393.x;
RA Gamer J., Multhaup G., Tomoyasu T., McCarty J.S., Rudiger S.,
RA Schonfeld H.J., Schirra C., Bujard H., Bukau B.;
RT "A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones
RT regulates activity of the Escherichia coli heat shock transcription factor
RT sigma32.";
RL EMBO J. 15:607-617(1996).
RN [11]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [12]
RP INTERACTION WITH RNA POLYMERASE, AND MUTAGENESIS OF GLN-80.
RX PubMed=9144163; DOI=10.1073/pnas.94.10.4907;
RA Joo D.M., Ng N., Calendar R.;
RT "A sigma32 mutant with a single amino acid change in the highly conserved
RT region 2.2 exhibits reduced core RNA polymerase affinity.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4907-4912(1997).
RN [13]
RP INDUCTION, AND DEGRADATION BY FTSH.
RC STRAIN=K12;
RX PubMed=9822823; DOI=10.1046/j.1365-2958.1998.01091.x;
RA Tatsuta T., Tomoyasu T., Bukau B., Kitagawa M., Mori H., Karata K.,
RA Ogura T.;
RT "Heat shock regulation in the ftsH null mutant of Escherichia coli:
RT dissection of stability and activity control mechanisms of sigma32 in
RT vivo.";
RL Mol. Microbiol. 30:583-593(1998).
RN [14]
RP INDUCTION, AND TRANSLATIONAL THERMOREGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10090722; DOI=10.1101/gad.13.6.655;
RA Morita M.T., Tanaka Y., Kodama T.S., Kyogoku Y., Yanagi H., Yura T.;
RT "Translational induction of heat shock transcription factor sigma32:
RT evidence for a built-in RNA thermosensor.";
RL Genes Dev. 13:655-665(1999).
RN [15]
RP INDUCTION, AND TRANSLATIONAL THERMOREGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9882652; DOI=10.1128/jb.181.2.401-410.1999;
RA Morita M., Kanemori M., Yanagi H., Yura T.;
RT "Heat-induced synthesis of sigma32 in Escherichia coli: structural and
RT functional dissection of rpoH mRNA secondary structure.";
RL J. Bacteriol. 181:401-410(1999).
RN [16]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15757896; DOI=10.1074/jbc.m500393200;
RA Zhao K., Liu M., Burgess R.R.;
RT "The global transcriptional response of Escherichia coli to induced sigma
RT 32 protein involves sigma 32 regulon activation followed by inactivation
RT and degradation of sigma 32 in vivo.";
RL J. Biol. Chem. 280:17758-17768(2005).
RN [17]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=16775749; DOI=10.1007/s00203-006-0113-9;
RA Diaz-Acosta A., Sandoval M.L., Delgado-Olivares L., Membrillo-Hernandez J.;
RT "Effect of anaerobic and stationary phase growth conditions on the heat
RT shock and oxidative stress responses in Escherichia coli K-12.";
RL Arch. Microbiol. 185:429-438(2006).
RN [18]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16818608; DOI=10.1101/gad.1428206;
RA Nonaka G., Blankschien M., Herman C., Gross C.A., Rhodius V.A.;
RT "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32,
RT reveals a multifaceted cellular response to heat stress.";
RL Genes Dev. 20:1776-1789(2006).
RN [19]
RP INDUCTION DURING CELL DIVISION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19114495; DOI=10.1128/jb.01536-08;
RA Wagner M.A., Zahrl D., Rieser G., Koraimann G.;
RT "Growth phase- and cell division-dependent activation and inactivation of
RT the {sigma}32 regulon in Escherichia coli.";
RL J. Bacteriol. 191:1695-1702(2009).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. This sigma factor is involved in regulation of expression of
CC heat shock genes. Intracellular concentration of free RpoH protein
CC increases in response to heat shock, which causes association with RNA
CC polymerase (RNAP) and initiation of transcription of heat shock genes,
CC including numerous global transcriptional regulators and genes involved
CC in maintaining membrane functionality and homeostasis. RpoH is then
CC quickly degraded, leading to a decrease in the rate of synthesis of
CC heat shock proteins and shut-off of the heat shock response.
CC {ECO:0000255|HAMAP-Rule:MF_00961, ECO:0000269|PubMed:15757896,
CC ECO:0000269|PubMed:16818608, ECO:0000269|PubMed:3306410,
CC ECO:0000269|PubMed:3315848, ECO:0000269|PubMed:6387714}.
CC -!- SUBUNIT: Interacts with the RNA polymerase core enzyme. Interacts with
CC DnaK and DnaJ. {ECO:0000255|HAMAP-Rule:MF_00961,
CC ECO:0000269|PubMed:8599944, ECO:0000269|PubMed:9144163}.
CC -!- INTERACTION:
CC P0AGB3; P0A6Y8: dnaK; NbExp=7; IntAct=EBI-555342, EBI-542092;
CC P0AGB3; P0AGD7: ffh; NbExp=4; IntAct=EBI-555342, EBI-369938;
CC P0AGB3; P0AAI3: ftsH; NbExp=4; IntAct=EBI-555342, EBI-548381;
CC P0AGB3; P0A6F5: groEL; NbExp=3; IntAct=EBI-555342, EBI-543750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00961}.
CC -!- INDUCTION: Subject to complex regulation at multiple levels
CC (transcription, translation, regulation of activity and degradation).
CC In the absence of heat shock, or after heat shock, activity is
CC inhibited by transient association with DnaK and DnaJ, which reduces
CC the amounts of free active RpoH, makes it unstable and mediates its
CC degradation by the FtsH protease. During heat shock, the intracellular
CC concentration of RpoH increases, due to slightly increased
CC transcription, increased synthesis and stabilization of the protein.
CC Induction occurs mainly at the post-transcriptional level, via
CC translational thermoregulation: at low temperature, the structure of
CC the rpoH mRNA blocks its translation, while at high temperature,
CC melting of the mRNA secondary structure facilitates ribosome binding
CC and synthesis of the RpoH protein. In addition, during heat shock,
CC stabilization of RpoH is triggered by the titration of free DnaK/DnaJ
CC by stress-induced misfolded proteins. Can also be induced by other
CC stress conditions, including during the first round of cell division.
CC {ECO:0000269|PubMed:10090722, ECO:0000269|PubMed:15757896,
CC ECO:0000269|PubMed:19114495, ECO:0000269|PubMed:3306410,
CC ECO:0000269|PubMed:3315848, ECO:0000269|PubMed:3315851,
CC ECO:0000269|PubMed:8599944, ECO:0000269|PubMed:9822823,
CC ECO:0000269|PubMed:9882652}.
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 (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit an increased sensitivity to heat
CC shock but only in the exponential phase of aerobic growth.
CC {ECO:0000269|PubMed:16775749}.
CC -!- MISCELLANEOUS: May only be involved in heat shocks that occur during
CC exponential phase of growth under aerobic conditions. Different
CC mechanisms may play a prime role during stationary phase and anaerobic
CC growth (PubMed:16775749). {ECO:0000305|PubMed:16775749}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoH subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00961}.
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DR EMBL; M20668; AAA24587.1; -; Genomic_DNA.
DR EMBL; J05516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K02177; AAA23991.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18436.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76486.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77832.1; -; Genomic_DNA.
DR PIR; H65142; RGECH.
DR RefSeq; NP_417918.1; NC_000913.3.
DR RefSeq; WP_000130217.1; NZ_STEB01000004.1.
DR AlphaFoldDB; P0AGB3; -.
DR SMR; P0AGB3; -.
DR BioGRID; 4262497; 257.
DR ComplexPortal; CPX-4887; DNA-directed RNA polymerase holoenzyme complex, SigmaH variant.
DR DIP; DIP-46203N; -.
DR IntAct; P0AGB3; 19.
DR MINT; P0AGB3; -.
DR STRING; 511145.b3461; -.
DR jPOST; P0AGB3; -.
DR PaxDb; P0AGB3; -.
DR PRIDE; P0AGB3; -.
DR DNASU; 947970; -.
DR EnsemblBacteria; AAC76486; AAC76486; b3461.
DR EnsemblBacteria; BAE77832; BAE77832; BAE77832.
DR GeneID; 66672655; -.
DR GeneID; 947970; -.
DR KEGG; ecj:JW3426; -.
DR KEGG; eco:b3461; -.
DR PATRIC; fig|1411691.4.peg.3264; -.
DR EchoBASE; EB0890; -.
DR eggNOG; COG0568; Bacteria.
DR HOGENOM; CLU_014793_3_5_6; -.
DR InParanoid; P0AGB3; -.
DR OMA; YQRWLAE; -.
DR PhylomeDB; P0AGB3; -.
DR BioCyc; EcoCyc:RPOH-MON; -.
DR BioCyc; MetaCyc:RPOH-MON; -.
DR PRO; PR:P0AGB3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0031421; C:invertasome; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0001000; F:bacterial-type RNA polymerase core enzyme binding; IDA:EcoCyc.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:CAFA.
DR GO; GO:0016987; F:sigma factor activity; IDA:CACAO.
DR GO; GO:0009009; F:site-specific recombinase activity; IDA:CAFA.
DR GO; GO:0006310; P:DNA recombination; IDA:CAFA.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoliWiki.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:CAFA.
DR HAMAP; MF_00961; Sigma70_RpoH; 1.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR000943; RNA_pol_sigma70.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR007630; RNA_pol_sigma70_r4.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR012759; RNA_pol_sigma_RpoH_proteobac.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF04545; Sigma70_r4; 1.
DR PIRSF; PIRSF000770; RNA_pol_sigma-SigE/K; 1.
DR PRINTS; PR00046; SIGMA70FCT.
DR SUPFAM; SSF88659; SSF88659; 1.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02392; rpoH_proteo; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS00715; SIGMA70_1; 1.
DR PROSITE; PS00716; SIGMA70_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Reference proteome; Sigma factor; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..284
FT /note="RNA polymerase sigma factor RpoH"
FT /id="PRO_0000093957"
FT DNA_BIND 253..272
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00961"
FT REGION 53..122
FT /note="Sigma-70 factor domain-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00961"
FT REGION 228..280
FT /note="Sigma-70 factor domain-4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00961"
FT MOTIF 77..80
FT /note="Interaction with polymerase core subunit RpoC"
FT MUTAGEN 80
FT /note="Q->N,R: Decrease in activity. Exhibits reduced
FT affinity for core RNAP."
FT /evidence="ECO:0000269|PubMed:9144163"
FT CONFLICT 185
FT /note="S -> A (in Ref. 3; AAA23991)"
FT /evidence="ECO:0000305"
FT CONFLICT 193..194
FT /note="QP -> HA (in Ref. 3; AAA23991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32469 MW; 628A17B4C835D00A CRC64;
MTDKMQSLAL APVGNLDSYI RAANAWPMLS ADEERALAEK LHYHGDLEAA KTLILSHLRF
VVHIARNYAG YGLPQADLIQ EGNIGLMKAV RRFNPEVGVR LVSFAVHWIK AEIHEYVLRN
WRIVKVATTK AQRKLFFNLR KTKQRLGWFN QDEVEMVARE LGVTSKDVRE MESRMAAQDM
TFDLSSDDDS DSQPMAPVLY LQDKSSNFAD GIEDDNWEEQ AANRLTDAMQ GLDERSQDII
RARWLDEDNK STLQELADRY GVSAERVRQL EKNAMKKLRA AIEA
