rseB

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

lipid binding Source: UniProtKB-KW
sigma factor antagonist activity
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 9159522

Complete GO annotation...

GO - Biological processⁱ

negative regulation of transcription, DNA-templated
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 9159522
transcription, DNA-templated Source: UniProtKB-KW

Complete GO annotation...

Keywordsⁱ

Biological process	Transcription, Transcription regulation
Ligand	Lipid-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7348-MONOMER.

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	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG13177. rseB.

EcoGeneⁱ

EG13177. rseB.

Subcellular locationⁱ

Periplasm
3 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
- Ref.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.

Note:

Partially associates with the inner membrane via RseA.

GO - Cellular componentⁱ

outer membrane-bounded periplasmic space
Source: EcoCyc
Inferred from direct assayⁱ
- 9159522

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 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

With	Entry	#Exp.	IntAct	Notes
rseA	P0AFX7	6	EBI-1135231,EBI-1117560

With

Entry

#Exp.

IntAct

Notes

rseA

P0AFX7

6

EBI-1135231,EBI-1117560

Protein-protein interaction databases

BioGridⁱ	4260602. 6 interactors.
Database of interacting proteins More...DIPⁱ	DIP-10802N.
IntActⁱ	P0AFX9. 2 interactors.
STRINGⁱ	511145.b2571.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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

Signal

Phylogenomic databases

eggNOGⁱ	ENOG4105VQK. Bacteria. COG3026. LUCA.
HOGENOMⁱ	HOG000272273.
InParanoidⁱ	P0AFX9.
KEGG Orthology (KO) More...KOⁱ	K03598.
OMAⁱ	DDFRYQY.

Family and domain databases

InterProⁱ	View protein in InterPro IPR033436. MucB/RseB_C. IPR033434. MucB/RseB_N. IPR005588. MucB_RseB.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03888. MucB_RseB. 1 hit. PF17188. MucB_RseB_C. 1 hit.
PIRSFⁱ	PIRSF005427. RseB. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P0AFX9-1 [UniParc]FASTA Add 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.
PIRⁱ	I83298.
NCBI Reference Sequences More...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	32120541. 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.
PIRⁱ	I83298.
NCBI Reference Sequences More...RefSeqⁱ	NP_417066.1. NC_000913.3. WP_000812053.1. NZ_LN832404.1.

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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...

Protein-protein interaction databases

BioGridⁱ	4260602. 6 interactors.
Database of interacting proteins More...DIPⁱ	DIP-10802N.
IntActⁱ	P0AFX9. 2 interactors.
STRINGⁱ	511145.b2571.

Proteomic databases

EPDⁱ	P0AFX9.
PaxDbⁱ	P0AFX9.
PRIDEⁱ	P0AFX9.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75624; AAC75624; b2571. BAE76747; BAE76747; BAE76747.
GeneIDⁱ	947054.
KEGGⁱ	ecj:JW2555. eco:b2571.
PATRICⁱ	32120541. VBIEscCol129921_2673.

Organism-specific databases

EchoBASEⁱ	EB2969.
EcoGeneⁱ	EG13177. rseB.

Phylogenomic databases

eggNOGⁱ	ENOG4105VQK. Bacteria. COG3026. LUCA.
HOGENOMⁱ	HOG000272273.
InParanoidⁱ	P0AFX9.
KEGG Orthology (KO) More...KOⁱ	K03598.
OMAⁱ	DDFRYQY.

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7348-MONOMER.

BioCycⁱ

EcoCyc:G7348-MONOMER.

Miscellaneous databases

EvolutionaryTraceⁱ	P0AFX9.
Protein Ontology More...PROⁱ	PR:P0AFX9.

Family and domain databases

InterProⁱ	View protein in InterPro IPR033436. MucB/RseB_C. IPR033434. MucB/RseB_N. IPR005588. MucB_RseB.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03888. MucB_RseB. 1 hit. PF17188. MucB_RseB_C. 1 hit.
PIRSFⁱ	PIRSF005427. RseB. 1 hit.
ProtoNetⁱ	Search...

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:	February 15, 2017
	This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AFX9 (RSEB_ECOLI)

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Sigma-E factor regulatory protein RseB

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ