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Protein

Sigma-E factor regulatory protein RseB

Gene

rseB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Negatively modulates the activity of sigma-E (RpoE) by stabilizing RseA under non-stress conditions. Although not essential for association of sigma-E with Rsea it increases their affinity 2- to 3-fold. When bound to RseA it prevents proteolysis by DegS, which is probably relieved by lipopolysaccharide binding (LPS).6 Publications

Enzyme regulationi

Binding to RseA is inhibited by LPS fragments; phosphorylated N-acetylglucosamine (GlcNAc) with N-linked acyl chains are minimally necessary to disrupt binding to RseA. Once RseB is no longer bound to RseA the latter is susceptible to DegS degradation. Thus if periplasmic LPS levels increase the sigma-E regulon is induced.1 Publication

GO - Molecular functioni

  • lipid binding Source: UniProtKB-KW
  • sigma factor antagonist activity Source: EcoCyc

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7348-MONOMER.
ECOL316407:JW2555-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sigma-E factor regulatory protein RseB
Gene namesi
Name:rseB
Ordered Locus Names:b2571, JW2555
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13177. rseB.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

About 2-fold increased sigma-E activity, 2-fold decrease in stability of RseA.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 318295Sigma-E factor regulatory protein RseBPRO_0000022249Add
BLAST

Proteomic databases

EPDiP0AFX9.
PaxDbiP0AFX9.
PRIDEiP0AFX9.

Interactioni

Subunit structurei

Homodimer. Interacts with RseA with 1:1 stoichiometry. Binding to LPS stabilzes a homotetramer that does not bind RseA.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rseAP0AFX76EBI-1135231,EBI-1117560

Protein-protein interaction databases

BioGridi4260602. 6 interactions.
DIPiDIP-10802N.
IntActiP0AFX9. 2 interactions.
STRINGi511145.b2571.

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 4015Combined sources
Beta strandi41 – 5111Combined sources
Beta strandi54 – 6411Combined sources
Beta strandi66 – 7510Combined sources
Beta strandi77 – 793Combined sources
Beta strandi82 – 865Combined sources
Beta strandi89 – 935Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi108 – 1114Combined sources
Helixi113 – 1164Combined sources
Helixi119 – 1224Combined sources
Turni123 – 1253Combined sources
Beta strandi126 – 13611Combined sources
Beta strandi139 – 14810Combined sources
Beta strandi155 – 1617Combined sources
Turni162 – 1643Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi179 – 19315Combined sources
Helixi196 – 2038Combined sources
Beta strandi223 – 2253Combined sources
Beta strandi232 – 2376Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi260 – 2678Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi282 – 2898Combined sources
Beta strandi292 – 3009Combined sources
Helixi302 – 3098Combined sources
Beta strandi312 – 3143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P4BX-ray2.40A/B/C24-318[»]
2V42X-ray2.75A/B23-318[»]
2V43X-ray2.37A/B/C23-318[»]
3M4WX-ray2.30A/B/C/D24-318[»]
ProteinModelPortaliP0AFX9.
SMRiP0AFX9. Positions 23-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFX9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 203180Responsible for oligomerizationAdd
BLAST
Regioni222 – 31897Interacts with RseAAdd
BLAST

Domaini

The N-terminal domain (residues 24-203) is responsible for oligomerization, while the C-terminal domain (residues 222-318) interacts with RseA.1 Publication

Sequence similaritiesi

Belongs to the RseB family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105VQK. Bacteria.
COG3026. LUCA.
HOGENOMiHOG000272273.
InParanoidiP0AFX9.
KOiK03598.
OMAiDDFRYQY.
OrthoDBiEOG6N0HP4.

Family and domain databases

InterProiIPR033436. MucB/RseB_C.
IPR033434. MucB/RseB_N.
IPR005588. MucB_RseB.
[Graphical view]
PfamiPF03888. MucB_RseB. 1 hit.
PF17188. MucB_RseB_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005427. RseB. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AFX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQLWFAMSL VTGSLLFSAN ASATPASGAL LQQMNLASQS LNYELSFISI
60 70 80 90 100
NKQGVESLRY RHARLDNRPL AQLLQMDGPR REVVQRGNEI SYFEPGLEPF
110 120 130 140 150
TLNGDYIVDS LPSLIYTDFK RLSPYYDFIS VGRTRIADRL CEVIRVVARD
160 170 180 190 200
GTRYSYIVWM DTESKLPMRV DLLDRDGETL EQFRVIAFNV NQDISSSMQT
210 220 230 240 250
LAKANLPPLL SVPVGEKAKF SWTPTWLPQG FSEVSSSRRP LPTMDNMPIE
260 270 280 290 300
SRLYSDGLFS FSVNVNRATP SSTDQMLRTG RRTVSTSVRD NAEITIVGEL
310
PPQTAKRIAE NIKFGAAQ
Length:318
Mass (Da):35,750
Last modified:December 20, 2005 - v1
Checksum:i3F8C34DD85600B54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37089 Genomic DNA. Translation: AAC45316.1.
U37455 Genomic DNA. Translation: AAC45319.1.
D64044 Genomic DNA. Translation: BAA10918.1.
U00096 Genomic DNA. Translation: AAC75624.1.
AP009048 Genomic DNA. Translation: BAE76747.1.
PIRiI83298.
RefSeqiNP_417066.1. NC_000913.3.
WP_000812053.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75624; AAC75624; b2571.
BAE76747; BAE76747; BAE76747.
GeneIDi947054.
KEGGiecj:JW2555.
eco:b2571.
PATRICi32120541. VBIEscCol129921_2673.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37089 Genomic DNA. Translation: AAC45316.1.
U37455 Genomic DNA. Translation: AAC45319.1.
D64044 Genomic DNA. Translation: BAA10918.1.
U00096 Genomic DNA. Translation: AAC75624.1.
AP009048 Genomic DNA. Translation: BAE76747.1.
PIRiI83298.
RefSeqiNP_417066.1. NC_000913.3.
WP_000812053.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P4BX-ray2.40A/B/C24-318[»]
2V42X-ray2.75A/B23-318[»]
2V43X-ray2.37A/B/C23-318[»]
3M4WX-ray2.30A/B/C/D24-318[»]
ProteinModelPortaliP0AFX9.
SMRiP0AFX9. Positions 23-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260602. 6 interactions.
DIPiDIP-10802N.
IntActiP0AFX9. 2 interactions.
STRINGi511145.b2571.

Proteomic databases

EPDiP0AFX9.
PaxDbiP0AFX9.
PRIDEiP0AFX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75624; AAC75624; b2571.
BAE76747; BAE76747; BAE76747.
GeneIDi947054.
KEGGiecj:JW2555.
eco:b2571.
PATRICi32120541. VBIEscCol129921_2673.

Organism-specific databases

EchoBASEiEB2969.
EcoGeneiEG13177. rseB.

Phylogenomic databases

eggNOGiENOG4105VQK. Bacteria.
COG3026. LUCA.
HOGENOMiHOG000272273.
InParanoidiP0AFX9.
KOiK03598.
OMAiDDFRYQY.
OrthoDBiEOG6N0HP4.

Enzyme and pathway databases

BioCyciEcoCyc:G7348-MONOMER.
ECOL316407:JW2555-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AFX9.
PROiP0AFX9.

Family and domain databases

InterProiIPR033436. MucB/RseB_C.
IPR033434. MucB/RseB_N.
IPR005588. MucB_RseB.
[Graphical view]
PfamiPF03888. MucB_RseB. 1 hit.
PF17188. MucB_RseB_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005427. RseB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli."
    Raina S., Missiakas D., Georgopoulos C.
    EMBO J. 14:1043-1055(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "The sigmaE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigmaE."
    De Las Penas A., Connolly L., Gross C.A.
    Mol. Microbiol. 24:373-385(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH RSEA, SUBUNIT, SUBCELLULAR LOCATION, OPERON, DISRUPTION PHENOTYPE.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  3. Nashimoto H., Saito N.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins."
    Missiakas D., Mayer M.P., Lemaire M., Georgopoulos C., Raina S.
    Mol. Microbiol. 24:355-371(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RSEA, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, OPERON.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  7. "The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor."
    Ades S.E., Connolly L.E., Alba B.M., Gross C.A.
    Genes Dev. 13:2449-2461(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  8. "RseB binding to the periplasmic domain of RseA modulates the RseA:sigmaE interaction in the cytoplasm and the availability of sigmaE.RNA polymerase."
    Collinet B., Yuzawa H., Chen T., Herrera C., Missiakas D.
    J. Biol. Chem. 275:33898-33904(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSEA, SUBCELLULAR LOCATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  9. Cited for: FUNCTION, INTERACTION WITH RSEA, SUBUNIT.
  10. "Solution structures of RseA and its complex with RseB."
    Jin K.S., Kim D.Y., Rho Y., Le V.B., Kwon E., Kim K.K., Ree M.
    J. Synchrotron Radiat. 15:219-222(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSEA, SUBUNIT.
  11. "Signal integration by DegS and RseB governs the sigma-E-mediated envelope stress response in Escherichia coli."
    Chaba R., Alba B.M., Guo M.S., Sohn J., Ahuja N., Sauer R.T., Gross C.A.
    Proc. Natl. Acad. Sci. U.S.A. 108:2106-2111(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  12. "Dual molecular signals mediate the bacterial response to outer-membrane stress."
    Lima S., Guo M.S., Chaba R., Gross C.A., Sauer R.T.
    Science 340:837-841(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BINDING TO RSEA, BINDING TO LIPID-A, ENZYME REGULATION.
    Strain: K12.
  13. "The structure of RseB: a sensor in periplasmic stress response of E. coli."
    Wollmann P., Zeth K.
    J. Mol. Biol. 372:927-941(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 23-318, INTERACTION WITH RSEA, SUBUNIT, DOMAIN.
  14. "Crystal structure of RseB and a model of its binding mode to RseA."
    Kim D.Y., Jin K.S., Kwon E., Ree M., Kim K.K.
    Proc. Natl. Acad. Sci. U.S.A. 104:8779-8784(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-318, SUBUNIT, BINDING TO RSEA.
  15. "Structural basis for the negative regulation of bacterial stress response by RseB."
    Kim D.Y., Kwon E., Choi J., Hwang H.Y., Kim K.K.
    Protein Sci. 19:1258-1263(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-318 IN COMPLEX WITH RSEA.

Entry informationi

Entry nameiRSEB_ECOLI
AccessioniPrimary (citable) accession number: P0AFX9
Secondary accession number(s): P46186, Q2MAF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 11, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Part of the rpoE-rseA-rseB-rseC operon.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.