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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000002224924 – 318Sigma-E factor regulatory protein RseBAdd BLAST295

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 interactors.
DIPiDIP-10802N.
IntActiP0AFX9. 2 interactors.
STRINGi511145.b2571.

Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 40Combined sources15
Beta strandi41 – 51Combined sources11
Beta strandi54 – 64Combined sources11
Beta strandi66 – 75Combined sources10
Beta strandi77 – 79Combined sources3
Beta strandi82 – 86Combined sources5
Beta strandi89 – 93Combined sources5
Beta strandi100 – 103Combined sources4
Beta strandi108 – 111Combined sources4
Helixi113 – 116Combined sources4
Helixi119 – 122Combined sources4
Turni123 – 125Combined sources3
Beta strandi126 – 136Combined sources11
Beta strandi139 – 148Combined sources10
Beta strandi155 – 161Combined sources7
Turni162 – 164Combined sources3
Beta strandi167 – 173Combined sources7
Beta strandi179 – 193Combined sources15
Helixi196 – 203Combined sources8
Beta strandi223 – 225Combined sources3
Beta strandi232 – 237Combined sources6
Beta strandi242 – 245Combined sources4
Beta strandi250 – 255Combined sources6
Beta strandi260 – 267Combined sources8
Beta strandi275 – 279Combined sources5
Beta strandi282 – 289Combined sources8
Beta strandi292 – 300Combined sources9
Helixi302 – 309Combined sources8
Beta strandi312 – 314Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFX9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 203Responsible for oligomerizationAdd BLAST180
Regioni222 – 318Interaction with RseAAdd BLAST97

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.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260602. 6 interactors.
DIPiDIP-10802N.
IntActiP0AFX9. 2 interactors.
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.

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...

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: November 2, 2016
This is version 78 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.