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 27-MAR-2024, entry version 143. 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; Pseudomonadota; 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}. 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; 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 PDB; 8HKC; EM; 2.49 A; E=1-284. DR PDBsum; 8HKC; -. DR AlphaFoldDB; P0AGB3; -. DR EMDB; EMD-34849; -. 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; 511145-b3461; -. DR DNASU; 947970; -. DR EnsemblBacteria; AAC76486; AAC76486; b3461. DR GeneID; 75173621; -. 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; MDAPFVQ; -. DR OrthoDB; 9809557at2; -. DR PhylomeDB; P0AGB3; -. DR BioCyc; EcoCyc:RPOH-MONOMER; -. DR BioCyc; MetaCyc:RPOH-MONOMER; -. DR PRO; PR:P0AGB3; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0000345; C:cytosolic DNA-directed RNA polymerase complex; ISS:ComplexPortal. 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:0006351; P:DNA-templated transcription; IDA:CACAO. DR GO; GO:0006352; P:DNA-templated transcription initiation; ISS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:EcoliWiki. DR GO; GO:2000142; P:regulation of DNA-templated transcription initiation; ISS:ComplexPortal. DR GO; GO:0010468; P:regulation of gene expression; IDA:EcoCyc. DR GO; GO:0009408; P:response to heat; IMP:EcoCyc. DR CDD; cd06171; Sigma70_r4; 1. DR Gene3D; 1.20.120.1810; -; 1. DR Gene3D; 1.20.140.160; -; 1. 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 NCBIfam; TIGR02392; rpoH_proteo; 1. DR NCBIfam; TIGR02937; sigma70-ECF; 1. DR PANTHER; PTHR30376:SF3; RNA POLYMERASE SIGMA FACTOR RPOH; 1. DR PANTHER; PTHR30376; SIGMA FACTOR RPOH HEAT SHOCK RELATED; 1. 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; SSF88946; Sigma2 domain of RNA polymerase sigma factors; 1. DR SUPFAM; SSF88659; Sigma3 and sigma4 domains of RNA polymerase sigma factors; 1. DR PROSITE; PS00715; SIGMA70_1; 1. DR PROSITE; PS00716; SIGMA70_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA-binding; Reference proteome; Sigma factor; KW Stress response; 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" FT HELIX 16..25 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 31..44 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 47..56 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 58..65 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 66..71 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 75..91 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 101..120 FT /evidence="ECO:0007829|PDB:8HKC" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 130..142 FT /evidence="ECO:0007829|PDB:8HKC" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 151..161 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 165..176 FT /evidence="ECO:0007829|PDB:8HKC" FT STRAND 200..203 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 208..231 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 234..244 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 253..260 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 264..283 FT /evidence="ECO:0007829|PDB:8HKC" 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 //