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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

Miscellaneous

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

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

  • antisigma factor binding Source: EcoCyc
  • identical protein binding Source: IntAct
  • lipid binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Biological processTranscription, Transcription regulation
LigandLipid-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7348-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

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 – 23IEP:Add BLAST23
ChainiPRO_000002224924 – 318Sigma-E factor regulatory protein RseBAdd BLAST295

Proteomic databases

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

Show more details

GO - Molecular functioni

  • antisigma factor binding Source: EcoCyc
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4260602. 6 interactors.
DIPiDIP-10802N.
IntActiP0AFX9. 2 interactors.
STRINGi316385.ECDH10B_2739.

Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 40ND:15
Beta strandi41 – 51ND:11
Beta strandi54 – 64ND:11
Beta strandi66 – 75ND:10
Beta strandi77 – 79ND:3
Beta strandi82 – 86ND:5
Beta strandi89 – 93ND:5
Beta strandi100 – 103ND:4
Beta strandi108 – 111ND:4
Helixi113 – 116ND:4
Helixi119 – 122ND:4
Turni123 – 125ND:3
Beta strandi126 – 136ND:11
Beta strandi139 – 148ND:10
Beta strandi155 – 161ND:7
Turni162 – 164ND:3
Beta strandi167 – 173ND:7
Beta strandi179 – 193ND:15
Helixi196 – 203ND:8
Beta strandi223 – 225ND:3
Beta strandi232 – 237ND:6
Beta strandi242 – 245ND:4
Beta strandi250 – 255ND:6
Beta strandi260 – 267ND:8
Beta strandi275 – 279ND:5
Beta strandi282 – 289ND:8
Beta strandi292 – 300ND:9
Helixi302 – 309ND:8
Beta strandi312 – 314ND:3

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.IKR:

Keywords - Domaini

Signal

Phylogenomic databases

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

Family and domain databases

CDDicd16327. RseB. 1 hit.
Gene3Di2.50.20.10. 1 hit.
InterProiView protein in InterPro
IPR029046. LolA/LolB/LppX.
IPR033436. MucB/RseB_C.
IPR033434. MucB/RseB_N.
IPR005588. MucB_RseB.
PfamiView protein in Pfam
PF03888. MucB_RseB. 1 hit.
PF17188. MucB_RseB_C. 1 hit.
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.
PATRICifig|1411691.4.peg.4163.

Similar proteinsi

Entry informationi

Entry nameiRSEB_ECOLI
AccessioniPrimary (citable) accession number: P0AFX9
Secondary accession number(s): P46186, Q2MAF9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: October 25, 2017
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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