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UniProtKB - P0AFX7 (RSEA_ECOLI)

Entry version 117 (23 Feb 2022)
Sequence version 1 (20 Dec 2005)
Previous versions | rss
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Protein

Anti-sigma-E factor RseA

Gene

rseA

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

An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-E. Overexpression of RseA blocks sigma-E from acting, results in cell lysis in stationary phase and temperature-sensitivity above 37 degrees Celsius.

3 Publications

Caution

PubMed:9159522 mis-identifies Trp-33 as residue 32.Curated
In vitro (PubMed:19706448) and in vivo (PubMed:23016873) results on the importance of the identity of residue 148 for cleavage by RseP differ.2 Publications

<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

  • sigma factor antagonist activity Source: EcoCyc
Complete GO annotation on QuickGO ...

<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

Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG12341-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:
Anti-sigma-E factor RseA
Alternative name(s):
Regulator of SigE
Sigma-E anti-sigma factor RseA
Sigma-E factor negative regulatory protein
<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:rseA
Synonyms:mclA, yfiJ
Ordered Locus Names:b2572, JW2556
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 100Cytoplasmic1 PublicationAdd BLAST100
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei101 – 118Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST18
Topological domaini119 – 216Periplasmic1 PublicationAdd BLAST98

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

About 10-fold increased sigma-E activity. Neither sigma-E nor RseB associate with the inner membrane.3 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>Mutagenesisi1 – 28Missing : Loss of anti-sigma factor activity. 1 PublicationAdd BLAST28
Mutagenesisi11D → H: Loss of anti-sigma factor activity. 1 Publication1
Mutagenesisi19L → P: Loss of anti-sigma factor activity. 1 Publication1
Mutagenesisi33W → C: Loss of anti-sigma factor activity. 1 Publication1
Mutagenesisi79Q → A: No binding of N-terminal fragment to SspB. 1 Publication1
Mutagenesisi85W → A: No binding of N-terminal fragment to SspB. 1 Publication1
Mutagenesisi88M → A: Reduced binding of N-terminal fragment to SspB. 1 Publication1
Mutagenesisi107 – 108AA → DD: Significantly less degradation by ClpX-ClpP when present as a 1-108 peptide fragment. 1 Publication2
Mutagenesisi146S → X: No effect on protein cleavage. 1 Publication1
Mutagenesisi147P → X: No effect on protein cleavage in vitro and in vivo. 2 Publications1
Mutagenesisi148V → A, C, I, L, M, N or T: Normal cleavage by DegS and RseP in vitro (PubMed:19706448), for A-148 decreased cleavage by DegS in vivo (PubMed:23016873). 2 Publications1
Mutagenesisi148V → D, E, G, F or P: Not cleaved by DegS nor RseP in vitro (PubMed:19706448). 2 Publications1
Mutagenesisi148V → H, K, Q, R, S or Y: Cleaved by DegS but not by RseP in vitro (PubMed:19706448), for R-148 and S-148 decreased cleavage by DegS in vivo (PubMed:23016873). 2 Publications1
Mutagenesisi162 – 169QQQQVQEQ → AAAAVAEA: RseA is degraded by RseP in the absence of DegS. 1 Publication8
Mutagenesisi172R → A: Still binds RseB. No binding to RseB; when associated with A-185. 1 Publication1
Mutagenesisi172R → D: No binding to RseB. 1 Publication1
Mutagenesisi185R → A: Still binds RseB. No binding to RseB; when associated with A-172. 1 Publication1
Mutagenesisi185R → E: No binding to RseB. 1 Publication1
Mutagenesisi190 – 200QLQFEQAQTQQ → ALAFFAAATAA: RseA is degraded by RseP in the absence of DegS. 1 PublicationAdd BLAST11

<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_00000974801 – 216Anti-sigma-E factor RseAAdd BLAST216

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Sequentially cleaved by DegS (a site-1 protease) in its periplasmic domain between Val-148 and Ser-149, then by RseP (a site-2 protease) between positions Ala-108 and Cys-109. The N-terminal fragment is then degraded by primarily ClpX-ClpP in an ATP-dependent fashion. Sequential cleavage by DegS, RseP and ClpX-ClpP frees RpoE from RseA.10 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei108 – 109Cleavage; by RseP2
Sitei148 – 149Cleavage; by DegS2

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AFX7

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

More...PaxDbi		P0AFX7

PRoteomics IDEntifications database

More...PRIDEi		P0AFX7

<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

Transiently induced by cold shock in a PNPase-dependent fashion. Upon stress induction (OMPs or heat shock) decreases in under 3 minutes (at protein level). Part of the rseD-rpoE-rseA-rseB-rseC operon (PubMed:9159522, PubMed:9159523, PubMed:28924029).5 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 1:1 with ECF RNA polymerase sigma-E (RpoE); this inhibits the interaction of sigma-E with the RNA polymerase catalytic core and leads to a decreased expression of sigma-E-regulated genes.

Interacts with RseB with 1:1 stoichiometry. The liberated N-terminus (residues 1-108) forms a complex with SspB and RpoE; binding to SspB is competitively inhibited by ssrA-tags, although the 2 proteins bind in opposite directions in SspB's peptide-binding groove.

14 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

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261964, 1 interactor
851391, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2532, rpoe-rsea-rseb sigma-antisigma complex

Database of interacting proteins

More...DIPi		DIP-39581N

Protein interaction database and analysis system

More...IntActi		P0AFX7, 6 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2572

<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

1216
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P0AFX7

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		P0AFX7

<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 – 97Sufficient to repress sigma-EAdd BLAST97
Regioni146 – 166DisorderedSequence analysisAdd BLAST21
Regioni169 – 186Primary binding site for RseBAdd BLAST18
Regioni190 – 200Poly-Gln (Q2)Add BLAST11

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili158 – 202Sequence analysisAdd BLAST45

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi152 – 166Polar residuesSequence analysisAdd BLAST15

<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 N-terminal cytosolic domain interacts with sigma-E, and upon overexpression leads to temperature sensitivity above 37 degrees Celsius and cell lysis in stationary phase. After degradation by RseP residues 77-108 bind to SspB, targeting RseA for degradation by the ClpX-ClpP protease.
The C-terminal periplasmic domain (residues 169-186) interacts with RseB and is also the target for DegS; RseB and DegS binding sites do not appreciably overlap. Gln-rich regions (residues 162-169, Q1, and 190-200, Q2) contribute to preventing RseP from acting before DegS. Insertion of 8 consecutive Gln residues into a protein lacking Q1 and Q2 restores DegS-dependence of RseP cleavage.

<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 RseA family.Curated

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG3073, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_108851_1_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AFX7

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AFX7

Family and domain databases

Conserved Domains Database

More...CDDi		cd16328, RseA_N, 1 hit

Database of protein disorder

More...DisProti		DP00552

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.880, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005573, Anti-sigma_E_RseA_C
IPR005572, Anti-sigma_E_RseA_N
IPR036147, Anti-sigma_E_RseA_N_sf
IPR026279, RseA

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03873, RseA_C, 1 hit
PF03872, RseA_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF016938, RseA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF89069, SSF89069, 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.

P0AFX7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQKEQLSALM DGETLDSELL NELAHNPEMQ KTWESYHLIR DSMRGDTPEV 
        60         70         80         90        100
LHFDISSRVM AAIEEEPVRQ PATLIPEAQP APHQWQKMPF WQKVRPWAAQ 
       110        120        130        140        150
LTQMGVAACV SLAVIVGVQH YNGQSETSQQ PETPVFNTLP MMGKASPVSL 
       160        170        180        190        200
GVPSEATANN GQQQQVQEQR RRINAMLQDY ELQRRLHSEQ LQFEQAQTQQ 
       210 
AAVQVPGIQT LGTQSQ
Length:216
Mass (Da):24,321
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:i63BD12131C611C32
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 D13169 differs from that shown. Reason: Frameshift.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
U10148 Genomic DNA Translation: AAA83999.1
U37089 Genomic DNA Translation: AAC45315.1
D64044 Genomic DNA Translation: BAA10919.1
D13169 Genomic DNA No translation available.
U00096 Genomic DNA Translation: AAC75625.1
AP009048 Genomic DNA Translation: BAE76748.1
U37455 Genomic DNA Translation: AAC45318.1

Protein sequence database of the Protein Information Resource

More...PIRi		B57255

NCBI Reference Sequences

More...RefSeqi		NP_417067.1, NC_000913.3
WP_001168459.1, NZ_STEB01000011.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75625; AAC75625; b2572
BAE76748; BAE76748; BAE76748

Database of genes from NCBI RefSeq genomes

More...GeneIDi		66673539
947053

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2556
eco:b2572

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4162

<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
U10148 Genomic DNA Translation: AAA83999.1
U37089 Genomic DNA Translation: AAC45315.1
D64044 Genomic DNA Translation: BAA10919.1
D13169 Genomic DNA No translation available.
U00096 Genomic DNA Translation: AAC75625.1
AP009048 Genomic DNA Translation: BAE76748.1
U37455 Genomic DNA Translation: AAC45318.1
PIRiB57255
RefSeqiNP_417067.1, NC_000913.3
WP_001168459.1, 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-ray2.00C/F1-90[»]
1YFNX-ray1.80E/F/G/H77-108[»]
3M4WX-ray2.30E/F/G/H121-216[»]
SMRiP0AFX7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261964, 1 interactor
851391, 1 interactor
ComplexPortaliCPX-2532, rpoe-rsea-rseb sigma-antisigma complex
DIPiDIP-39581N
IntActiP0AFX7, 6 interactors
STRINGi511145.b2572

Proteomic databases

jPOSTiP0AFX7
PaxDbiP0AFX7
PRIDEiP0AFX7

Genome annotation databases

EnsemblBacteriaiAAC75625; AAC75625; b2572
BAE76748; BAE76748; BAE76748
GeneIDi66673539
947053
KEGGiecj:JW2556
eco:b2572
PATRICifig|1411691.4.peg.4162

Organism-specific databases

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

More...EchoBASEi		EB2245

Phylogenomic databases

eggNOGiCOG3073, Bacteria
HOGENOMiCLU_108851_1_0_6
InParanoidiP0AFX7
PhylomeDBiP0AFX7

Enzyme and pathway databases

BioCyciEcoCyc:EG12341-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AFX7

Protein Ontology

More...PROi		PR:P0AFX7

Family and domain databases

CDDicd16328, RseA_N, 1 hit
DisProtiDP00552
Gene3Di1.10.10.880, 1 hit
InterProiView protein in InterPro
IPR005573, Anti-sigma_E_RseA_C
IPR005572, Anti-sigma_E_RseA_N
IPR036147, Anti-sigma_E_RseA_N_sf
IPR026279, RseA
PfamiView protein in Pfam
PF03873, RseA_C, 1 hit
PF03872, RseA_N, 1 hit
PIRSFiPIRSF016938, RseA, 1 hit
SUPFAMiSSF89069, SSF89069, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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<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 nameiRSEA_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: P0AFX7
Secondary accession number(s): P38106, Q2MAF8
<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: February 23, 2022
This is version 117 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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