UniProtKB - P0AFX9 (RSEB_ECOLI)
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Protein
Sigma-E factor regulatory protein RseB
Gene
rseB
Organism
Escherichia coli (strain K12)
Status
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 rseD-rpoE-rseA-rseB-rseC operon (PubMed:9159522, PubMed:9159523, PubMed:28924029).3 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
- antisigma factor binding Source: EcoCyc
- identical protein binding Source: IntAct
- lipid binding Source: UniProtKB-KW
GO - Biological processi
- regulation of transcription, DNA-templated Source: UniProtKB-KW
- transcription, DNA-templated Source: UniProtKB-KW
Keywordsi
Biological process | Transcription, Transcription regulation |
Ligand | Lipid-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:G7348-MONOMER. |
Names & Taxonomyi
Protein namesi | Recommended name: Sigma-E factor regulatory protein RseB |
Gene namesi | Name:rseB Ordered Locus Names:b2571, JW2555 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Organism-specific databases
EcoGenei | EG13177. rseB. |
Subcellular locationi
- Periplasm 3 Publications Note: Partially associates with the inner membrane via RseA.
GO - Cellular componenti
- outer membrane-bounded periplasmic space Source: EcoCyc
Keywords - Cellular componenti
PeriplasmPathology & Biotechi
Disruption phenotypei
About 2-fold increased sigma-E activity, 2-fold decrease in stability of RseA.3 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 23 | Sequence analysisAdd BLAST | 23 | |
ChainiPRO_0000022249 | 24 – 318 | Sigma-E factor regulatory protein RseBAdd BLAST | 295 |
Proteomic databases
EPDi | P0AFX9. |
PaxDbi | P0AFX9. |
PRIDEi | P0AFX9. |
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
GO - Molecular functioni
- antisigma factor binding Source: EcoCyc
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGridi | 4260602. 25 interactors. |
DIPi | DIP-10802N. |
IntActi | P0AFX9. 2 interactors. |
STRINGi | 316385.ECDH10B_2739. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 26 – 40 | Combined sources | 15 | |
Beta strandi | 41 – 51 | Combined sources | 11 | |
Beta strandi | 54 – 64 | Combined sources | 11 | |
Beta strandi | 66 – 75 | Combined sources | 10 | |
Beta strandi | 77 – 79 | Combined sources | 3 | |
Beta strandi | 82 – 86 | Combined sources | 5 | |
Beta strandi | 89 – 93 | Combined sources | 5 | |
Beta strandi | 100 – 103 | Combined sources | 4 | |
Beta strandi | 108 – 111 | Combined sources | 4 | |
Helixi | 113 – 116 | Combined sources | 4 | |
Helixi | 119 – 122 | Combined sources | 4 | |
Turni | 123 – 125 | Combined sources | 3 | |
Beta strandi | 126 – 136 | Combined sources | 11 | |
Beta strandi | 139 – 148 | Combined sources | 10 | |
Beta strandi | 155 – 161 | Combined sources | 7 | |
Turni | 162 – 164 | Combined sources | 3 | |
Beta strandi | 167 – 173 | Combined sources | 7 | |
Beta strandi | 179 – 193 | Combined sources | 15 | |
Helixi | 196 – 203 | Combined sources | 8 | |
Beta strandi | 223 – 225 | Combined sources | 3 | |
Beta strandi | 232 – 237 | Combined sources | 6 | |
Beta strandi | 242 – 245 | Combined sources | 4 | |
Beta strandi | 250 – 255 | Combined sources | 6 | |
Beta strandi | 260 – 267 | Combined sources | 8 | |
Beta strandi | 275 – 279 | Combined sources | 5 | |
Beta strandi | 282 – 289 | Combined sources | 8 | |
Beta strandi | 292 – 300 | Combined sources | 9 | |
Helixi | 302 – 309 | Combined sources | 8 | |
Beta strandi | 312 – 314 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2P4B | X-ray | 2.40 | A/B/C | 24-318 | [»] | |
2V42 | X-ray | 2.75 | A/B | 23-318 | [»] | |
2V43 | X-ray | 2.37 | A/B/C | 23-318 | [»] | |
3M4W | X-ray | 2.30 | A/B/C/D | 24-318 | [»] | |
ProteinModelPortali | P0AFX9. | |||||
SMRi | P0AFX9. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AFX9. |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 24 – 203 | Responsible for oligomerizationAdd BLAST | 180 | |
Regioni | 222 – 318 | Interaction with RseAAdd BLAST | 97 |
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
SignalPhylogenomic databases
eggNOGi | ENOG4105VQK. Bacteria. COG3026. LUCA. |
HOGENOMi | HOG000272273. |
InParanoidi | P0AFX9. |
KOi | K03598. |
OMAi | VYERNGS. |
Family and domain databases
CDDi | cd16327. RseB. 1 hit. |
Gene3Di | 3.30.200.100. 1 hit. |
InterProi | View protein in InterPro IPR033436. MucB/RseB_C. IPR038484. MucB/RseB_C_sf. IPR033434. MucB/RseB_N. IPR005588. MucB_RseB. |
PANTHERi | PTHR38782. PTHR38782. 1 hit. |
Pfami | View protein in Pfam PF03888. MucB_RseB. 1 hit. PF17188. MucB_RseB_C. 1 hit. |
PIRSFi | PIRSF005427. RseB. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0AFX9-1 [UniParc]FASTAAdd to basket
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
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. |
PIRi | I83298. |
RefSeqi | NP_417066.1. NC_000913.3. WP_000812053.1. NZ_LN832404.1. |
Genome annotation databases
EnsemblBacteriai | AAC75624; AAC75624; b2571. BAE76747; BAE76747; BAE76747. |
GeneIDi | 947054. |
KEGGi | ecj:JW2555. eco:b2571. |
PATRICi | fig|1411691.4.peg.4163. |
Similar proteinsi
Entry informationi
Entry namei | RSEB_ECOLI | |
Accessioni | P0AFX9Primary (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: | March 28, 2018 | |
This is version 87 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |