Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 120 (07 Oct 2020)
Sequence version 1 (20 Dec 2005)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

ECF RNA polymerase sigma-E factor

Gene

rpoE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released (PubMed:7889935, PubMed:2691330, PubMed:9159522, PubMed:9159523). Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock (PubMed:7889935) and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS of the outer membrane (PubMed:7889934, PubMed:11274153, PubMed:16336047). Indirectly activates transcription of csrB and csrC, 2 sRNAs that antagonize translational regulator CsrA, linking envelope stress, the stringent response and the catabolite repression systems (PubMed:28924029).8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

ECF sigma-E is held in an inactive form by its cognate anti-sigma factor (RseA) until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal (periplasmic stress and excess LPS) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The anti-sigma factor RseA is an inner membrane protein, binding sigma-E in the cytoplasm and RseB in the periplasm. RseA is first cut extracytoplasmically (site-1 protease, S1P, by DegS), then within the membrane itself (site-2 protease, S2P, by RseP), while cytoplasmic proteases (predominantly ClpX-ClpP) finish degrading the regulatory protein, liberating sigma-E (PubMed:15371343). Degradation of RseA requires 2 signals to activate DegS; an outer membrane protein (OMP) signal activates DegS, while an LPS signal causes release of RseB from RseA, freeing RseA to be cleaved (PubMed:23687042). The rate-limiting step in this protease cascade is the first signal-sensing cleavage (half-life about 1 minute) (PubMed:17210793).4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi156 – 175H-T-H motifBy similarityAdd BLAST20

<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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Sigma factor
Biological processStress response, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:RPOE-MONOMER
MetaCyc:RPOE-MONOMER

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ECF RNA polymerase sigma-E factor
Alternative name(s):
RNA polymerase sigma-E factor
Sigma-24
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:rpoE
Synonyms:sigE
Ordered Locus Names:b2573, JW2557
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<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

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<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 subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Reduced viability at 37 degrees Celsius, death at 42 degrees Celsius (PubMed:7889935). Loss of transcription from rpoE-dependent promoters (PubMed:7889935). Increased sensitivity to outer membrane disruption (PubMed:7889934).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi25L → P in SR1576; loss of sigma factor activity. 1 Publication1
Mutagenesisi165C → A: Binds RNAP and RseA normally. 1 Publication1
Mutagenesisi172S → P in SR1723; loss of sigma factor activity. 1 Publication1
Mutagenesisi178R → G in SR1502; decreased sigma factor activity. Does not bind RseA, still binds RNAP. 2 Publications1
Mutagenesisi181I → A in SR1503; decreased sigma factor activity. Does not bind RseA, still binds RNAP. 1 Publication1
Mutagenesisi185V → A in SR1504; decreased sigma factor activity. Does not bind RseA, still binds RNAP. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000939971 – 191ECF RNA polymerase sigma-E factorAdd BLAST191

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AGB6

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0AGB6

PRoteomics IDEntifications database

More...
PRIDEi
P0AGB6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced after shifting to 50 degrees Celsius (at protein level) (PubMed:2691330). Induced when the level of outer membrane proteins (OMP) increases (at protein level) (PubMed:8276244, PubMed:10500101). Induced as periplasmic levels of LPS levels increase (PubMed:23687042). Induced by misfolded periplasmic proteins (PubMed:9351822). Transcription positively autoregulated (via promoter P2) (PubMed:7889935). Transcription slightly induced by elevated temperatures (PubMed:7889934). Transiently induced by cold shock in a PNPase-dependent fashion (PubMed:14527658). Translation repressed by CsrA which binds to 3 sites in the 5'-UTR which occludes the ribosome binding site (PubMed:28924029). Translation is coupled to upstream leader peptide RseD, whose stop codon overlaps with the start codon of rpoE; when coupling is eliminated translation is decreased by about 50% (PubMed:28924029). Part of the rseD-rpoE-rseA-rseB-rseC operon (PubMed:9159522, PubMed:9159523, PubMed:28924029).11 Publications

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts transiently with the RNAP catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNAP holoenzyme that can initiate transcription (PubMed:12016219, PubMed:12718891, PubMed:7889935, PubMed:2691330).

Interacts 1:1 with anti-sigma-E factor RseA which prevents binding to RNAP catalytic core (PubMed:9159522, PubMed:9159523, PubMed:11777003, PubMed:12016219, PubMed:15371343, PubMed:12718891). An N-terminal (residues 1-108) RseA sigma-E complex also interacts with SspB (PubMed:15371343).

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4263046, 226 interactors
851388, 9 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2532, rpoe-rsea-rseb sigma-antisigma complex
CPX-4885, DNA-directed RNA polymerase holoenzyme complex, SigmaE variant

Database of interacting proteins

More...
DIPi
DIP-10774N

Protein interaction database and analysis system

More...
IntActi
P0AGB6, 30 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2573

<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

1191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P0AGB6

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0AGB6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0AGB6

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 153Binds RNAP core1 PublicationAdd BLAST153
Regioni25 – 92Sigma-70 factor domain-2Add BLAST68
Regioni129 – 180Sigma-70 factor domain-4Add BLAST52

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi48 – 61Polymerase core bindingAdd BLAST14

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC.1 Publication
The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-sigma factors prevents interaction of sigma factors with the RNA polymerase catalytic core.2 Publications

<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

Belongs to the sigma-70 factor family. ECF subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1595, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_047691_3_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AGB6

KEGG Orthology (KO)

More...
KOi
K03088

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AGB6

Family and domain databases

Database of protein disorder

More...
DisProti
DP01505

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039425, RNA_pol_sigma-70-like
IPR014284, RNA_pol_sigma-70_dom
IPR000838, RNA_pol_sigma70_ECF_CS
IPR007627, RNA_pol_sigma70_r2
IPR013249, RNA_pol_sigma70_r4_t2
IPR014286, RNA_pol_sigma70_RpoE
IPR013325, RNA_pol_sigma_r2
IPR013324, RNA_pol_sigma_r3/r4-like
IPR036388, WH-like_DNA-bd_sf

The PANTHER Classification System

More...
PANTHERi
PTHR43133, PTHR43133, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04542, Sigma70_r2, 1 hit
PF08281, Sigma70_r4_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF88659, SSF88659, 1 hit
SSF88946, SSF88946, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02939, RpoE_Sigma70, 1 hit
TIGR02937, sigma70-ECF, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01063, SIGMA70_ECF, 1 hit

<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 <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0AGB6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEQLTDQVL VERVQKGDQK AFNLLVVRYQ HKVASLVSRY VPSGDVPDVV
60 70 80 90 100
QEAFIKAYRA LDSFRGDSAF YTWLYRIAVN TAKNYLVAQG RRPPSSDVDA
110 120 130 140 150
IEAENFESGG ALKEISNPEN LMLSEELRQI VFRTIESLPE DLRMAITLRE
160 170 180 190
LDGLSYEEIA AIMDCPVGTV RSRIFRAREA IDNKVQPLIR R
Length:191
Mass (Da):21,696
Last modified:December 20, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC71EEF5939C3611E
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA10920 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D13169 Genomic DNA No translation available.
U37089 Genomic DNA Translation: AAC45314.1
D64044 Genomic DNA Translation: BAA10920.1 Different initiation.
U00096 Genomic DNA Translation: AAC75626.1
AP009048 Genomic DNA Translation: BAE76749.1
U10148 Genomic DNA Translation: AAA83998.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I60227

NCBI Reference Sequences

More...
RefSeqi
NP_417068.1, NC_000913.3
WP_001295364.1, NZ_STEB01000011.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75626; AAC75626; b2573
BAE76749; BAE76749; BAE76749

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
52077844
947050

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2557
eco:b2573

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4161

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13169 Genomic DNA No translation available.
U37089 Genomic DNA Translation: AAC45314.1
D64044 Genomic DNA Translation: BAA10920.1 Different initiation.
U00096 Genomic DNA Translation: AAC75626.1
AP009048 Genomic DNA Translation: BAE76749.1
U10148 Genomic DNA Translation: AAA83998.1
PIRiI60227
RefSeqiNP_417068.1, NC_000913.3
WP_001295364.1, NZ_STEB01000011.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
1OR7X-ray2.00A/B1-191[»]
2H27X-ray2.30A/D122-191[»]
5OR5NMR-A1-64[»]
A79-92[»]
6JBQelectron microscopy4.02F1-191[»]
BMRBiP0AGB6
SMRiP0AGB6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263046, 226 interactors
851388, 9 interactors
ComplexPortaliCPX-2532, rpoe-rsea-rseb sigma-antisigma complex
CPX-4885, DNA-directed RNA polymerase holoenzyme complex, SigmaE variant
DIPiDIP-10774N
IntActiP0AGB6, 30 interactors
STRINGi511145.b2573

Proteomic databases

jPOSTiP0AGB6
PaxDbiP0AGB6
PRIDEiP0AGB6

Genome annotation databases

EnsemblBacteriaiAAC75626; AAC75626; b2573
BAE76749; BAE76749; BAE76749
GeneIDi52077844
947050
KEGGiecj:JW2557
eco:b2573
PATRICifig|1411691.4.peg.4161

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1843

Phylogenomic databases

eggNOGiCOG1595, Bacteria
HOGENOMiCLU_047691_3_0_6
InParanoidiP0AGB6
KOiK03088
PhylomeDBiP0AGB6

Enzyme and pathway databases

BioCyciEcoCyc:RPOE-MONOMER
MetaCyc:RPOE-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AGB6

Protein Ontology

More...
PROi
PR:P0AGB6

Family and domain databases

DisProtiDP01505
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR039425, RNA_pol_sigma-70-like
IPR014284, RNA_pol_sigma-70_dom
IPR000838, RNA_pol_sigma70_ECF_CS
IPR007627, RNA_pol_sigma70_r2
IPR013249, RNA_pol_sigma70_r4_t2
IPR014286, RNA_pol_sigma70_RpoE
IPR013325, RNA_pol_sigma_r2
IPR013324, RNA_pol_sigma_r3/r4-like
IPR036388, WH-like_DNA-bd_sf
PANTHERiPTHR43133, PTHR43133, 1 hit
PfamiView protein in Pfam
PF04542, Sigma70_r2, 1 hit
PF08281, Sigma70_r4_2, 1 hit
SUPFAMiSSF88659, SSF88659, 1 hit
SSF88946, SSF88946, 1 hit
TIGRFAMsiTIGR02939, RpoE_Sigma70, 1 hit
TIGR02937, sigma70-ECF, 1 hit
PROSITEiView protein in PROSITE
PS01063, SIGMA70_ECF, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRPOE_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AGB6
Secondary accession number(s): P34086, Q2MAF7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: October 7, 2020
This is version 120 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<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

Keywords - Technical termi

3D-structure, Direct protein sequencing, 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again