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P0AGB3 (RPOH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase sigma factor RpoH
Alternative name(s):
Heat shock regulatory protein F33.4
RNA polymerase sigma-32 factor
Gene names
Name:rpoH
Synonyms:fam, hin, htpR
Ordered Locus Names:b3461, JW3426
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quickly degraded, leading to a decrease in the rate of synthesis of heat shock proteins and shut-off of the heat shock response. Ref.3 Ref.7 Ref.9 Ref.16 Ref.18

Subunit structure

Interacts with the RNA polymerase core enzyme. Interacts with DnaK and DnaJ. Ref.10 Ref.12

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00961.

Induction

Subject to complex regulation at multiple levels (transcription, translation, regulation of activity and degradation). In the absence of heat shock, or after heat shock, activity is inhibited by transient association with DnaK and DnaJ, which reduces the amounts of free active RpoH, makes it unstable and mediates its degradation by the FtsH protease. During heat shock, the intracellular concentration of RpoH increases, due to slightly increased transcription, increased synthesis and stabilization of the protein. Induction occurs mainly at the post-transcriptional level, via translational thermoregulation: at low temperature, the structure of the rpoH mRNA blocks its translation, while at high temperature, melting of the mRNA secondary structure facilitates ribosome binding and synthesis of the RpoH protein. In addition, during heat shock, stabilization of RpoH is triggered by the titration of free DnaK/DnaJ by stress-induced misfolded proteins. Can also be induced by other stress conditions, including during the first round of cell division. Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19

Domain

The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC By similarity. HAMAP-Rule MF_00961

The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA By similarity. HAMAP-Rule MF_00961

Disruption phenotype

Mutants exhibit an increased sensitivity to heat shock but only in the exponential phase of aerobic growth. Ref.17

Miscellaneous

May only be involved in heat shocks that occur during exponential phase of growth under aerobic conditions. Different mechanisms may play a prime role during stationary phase and anaerobic growth (Ref.17).

Sequence similarities

Belongs to the sigma-70 factor family. RpoH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284RNA polymerase sigma factor RpoH HAMAP-Rule MF_00961
PRO_0000093957

Regions

DNA binding253 – 27220H-T-H motif By similarity
Region53 – 12270Sigma-70 factor domain-2 By similarity
Region228 – 28053Sigma-70 factor domain-4 By similarity
Motif77 – 804Interaction with polymerase core subunit RpoC HAMAP-Rule MF_00961

Experimental info

Mutagenesis801Q → N or R: Decrease in activity. Exhibits reduced affinity for core RNAP. Ref.12
Sequence conflict1851S → A in AAA23991. Ref.3
Sequence conflict193 – 1942QP → HA in AAA23991. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P0AGB3 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 628A17B4C835D00A

FASTA28432,469
        10         20         30         40         50         60 
MTDKMQSLAL APVGNLDSYI RAANAWPMLS ADEERALAEK LHYHGDLEAA KTLILSHLRF 

        70         80         90        100        110        120 
VVHIARNYAG YGLPQADLIQ EGNIGLMKAV RRFNPEVGVR LVSFAVHWIK AEIHEYVLRN 

       130        140        150        160        170        180 
WRIVKVATTK AQRKLFFNLR KTKQRLGWFN QDEVEMVARE LGVTSKDVRE MESRMAAQDM 

       190        200        210        220        230        240 
TFDLSSDDDS DSQPMAPVLY LQDKSSNFAD GIEDDNWEEQ AANRLTDAMQ GLDERSQDII 

       250        260        270        280 
RARWLDEDNK STLQELADRY GVSAERVRQL EKNAMKKLRA AIEA 

« Hide

References

« Hide 'large scale' references
[1]"Deletion and insertion mutations in the rpoH gene of Escherichia coli that produce functional sigma 32."
Calendar R., Erickson J.W., Halling C., Nolte A.
J. Bacteriol. 170:3479-3484(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence of the heat shock regulatory gene of E. coli suggests its protein product may be a transcription factor."
Landick R., Vaughn V., Lau E.T., Vanbogelen R.A., Erickson J.W., Neidhardt F.C.
Cell 38:175-182(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"Heat shock regulatory gene (htpR) of Escherichia coli is required for growth at high temperature but is dispensable at low temperature."
Yura T., Tobe T., Ito K., Osawa T.
Proc. Natl. Acad. Sci. U.S.A. 81:6803-6807(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[4]"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli."
Grossman A.D., Straus D.B., Walter W.A., Gross C.A.
Genes Dev. 1:179-184(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[8]"Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene."
Erickson J.W., Vaughn V., Walter W.A., Neidhardt F.C., Gross C.A.
Genes Dev. 1:419-432(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[9]"The heat shock response of E. coli is regulated by changes in the concentration of sigma 32."
Straus D.B., Walter W.A., Gross C.A.
Nature 329:348-351(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[10]"A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32."
Gamer J., Multhaup G., Tomoyasu T., McCarty J.S., Rudiger S., Schonfeld H.J., Schirra C., Bujard H., Bukau B.
EMBO J. 15:607-617(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAK AND DNAJ, INDUCTION.
Strain: K12.
[11]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[12]"A sigma32 mutant with a single amino acid change in the highly conserved region 2.2 exhibits reduced core RNA polymerase affinity."
Joo D.M., Ng N., Calendar R.
Proc. Natl. Acad. Sci. U.S.A. 94:4907-4912(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNA POLYMERASE, MUTAGENESIS OF GLN-80.
[13]"Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of sigma32 in vivo."
Tatsuta T., Tomoyasu T., Bukau B., Kitagawa M., Mori H., Karata K., Ogura T.
Mol. Microbiol. 30:583-593(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, DEGRADATION BY FTSH.
Strain: K12.
[14]"Translational induction of heat shock transcription factor sigma32: evidence for a built-in RNA thermosensor."
Morita M.T., Tanaka Y., Kodama T.S., Kyogoku Y., Yanagi H., Yura T.
Genes Dev. 13:655-665(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TRANSLATIONAL THERMOREGULATION.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[15]"Heat-induced synthesis of sigma32 in Escherichia coli: structural and functional dissection of rpoH mRNA secondary structure."
Morita M., Kanemori M., Yanagi H., Yura T.
J. Bacteriol. 181:401-410(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TRANSLATIONAL THERMOREGULATION.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[16]"The global transcriptional response of Escherichia coli to induced sigma 32 protein involves sigma 32 regulon activation followed by inactivation and degradation of sigma 32 in vivo."
Zhao K., Liu M., Burgess R.R.
J. Biol. Chem. 280:17758-17768(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
Strain: K12 / MG1655 / ATCC 47076.
[17]"Effect of anaerobic and stationary phase growth conditions on the heat shock and oxidative stress responses in Escherichia coli K-12."
Diaz-Acosta A., Sandoval M.L., Delgado-Olivares L., Membrillo-Hernandez J.
Arch. Microbiol. 185:429-438(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[18]"Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress."
Nonaka G., Blankschien M., Herman C., Gross C.A., Rhodius V.A.
Genes Dev. 20:1776-1789(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: K12 / MG1655 / ATCC 47076.
[19]"Growth phase- and cell division-dependent activation and inactivation of the {sigma}32 regulon in Escherichia coli."
Wagner M.A., Zahrl D., Rieser G., Koraimann G.
J. Bacteriol. 191:1695-1702(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION DURING CELL DIVISION.
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20668 Genomic DNA. Translation: AAA24587.1.
J05516 Genomic DNA. No translation available.
K02177 Genomic DNA. Translation: AAA23991.1.
U00039 Genomic DNA. Translation: AAB18436.1.
U00096 Genomic DNA. Translation: AAC76486.1.
AP009048 Genomic DNA. Translation: BAE77832.1.
PIRRGECH. H65142.
RefSeqNP_417918.1. NC_000913.3.
YP_491973.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AGB3.
SMRP0AGB3. Positions 35-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46203N.
IntActP0AGB3. 13 interactions.
STRING511145.b3461.

Proteomic databases

PaxDbP0AGB3.
PRIDEP0AGB3.

Protocols and materials databases

DNASU947970.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76486; AAC76486; b3461.
BAE77832; BAE77832; BAE77832.
GeneID12933503.
947970.
KEGGecj:Y75_p3717.
eco:b3461.
PATRIC32122366. VBIEscCol129921_3560.

Organism-specific databases

EchoBASEEB0890.
EcoGeneEG10897. rpoH.

Phylogenomic databases

eggNOGCOG0568.
HOGENOMHOG000270269.
KOK03089.
OMALNNDEVH.
OrthoDBEOG6D5G0W.
PhylomeDBP0AGB3.
ProtClustDBPRK06596.

Enzyme and pathway databases

BioCycEcoCyc:RPOH-MONOMER.
ECOL316407:JW3426-MONOMER.
MetaCyc:RPOH-MONOMER.

Gene expression databases

GenevestigatorP0AGB3.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
HAMAPMF_00961. Sigma70_RpoH.
InterProIPR014284. RNA_pol_sigma-70_dom.
IPR000943. RNA_pol_sigma70.
IPR007627. RNA_pol_sigma70_r2.
IPR007630. RNA_pol_sigma70_r4.
IPR013325. RNA_pol_sigma_r2.
IPR013324. RNA_pol_sigma_r3_r4.
IPR012759. RNA_pol_sigma_RpoH_proteobac.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF04542. Sigma70_r2. 1 hit.
PF04545. Sigma70_r4. 1 hit.
[Graphical view]
PRINTSPR00046. SIGMA70FCT.
SUPFAMSSF88659. SSF88659. 1 hit.
SSF88946. SSF88946. 1 hit.
TIGRFAMsTIGR02392. rpoH_proteo. 1 hit.
TIGR02937. sigma70-ECF. 1 hit.
PROSITEPS00715. SIGMA70_1. 1 hit.
PS00716. SIGMA70_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP0AGB3.

Entry information

Entry nameRPOH_ECOLI
AccessionPrimary (citable) accession number: P0AGB3
Secondary accession number(s): P00580, Q2M7C4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene