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UniProtKB - P00579 (RPOD_ECOLI)

Entry version 207 (23 Feb 2022)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
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Protein

RNA polymerase sigma factor RpoD

Gene

rpoD

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 to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. Preferentially transcribes genes associated with fast growth, such as ribosomal operons, other protein-synthesis related genes, rRNA- and tRNA-encoding genes and prfB.

UniRule annotation7 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 bindingi573 – 592H-T-H motifUniRule annotationAdd 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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

Molecular functionDNA-binding, Sigma factor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:RPOD-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:
RNA polymerase sigma factor RpoDUniRule annotation
Alternative name(s):
Sigma-70UniRule annotation
<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:rpoDUniRule annotation
Synonyms:alt
Ordered Locus Names:b3067, JW3039
<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

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

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>Mutagenesisi553A → D: Disrupts the interaction with Escherichia phage lambda antitermination protein Q. 1 Publication1
Mutagenesisi596R → D or E: 2-fold reduction in activation of class II Crp-dependent promoters. 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_00000938851 – 613RNA polymerase sigma factor RpoDAdd BLAST613

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P00579

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

More...PaxDbi		P00579

PRoteomics IDEntifications database

More...PRIDEi		P00579

<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 RNA polymerase catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNA polymerase holoenzyme that can initiate transcription.

Identified in a complex containing RpoD, the RNA polymerase subunits RpoA, RpoB and RpoZ, CRP and DNA.

Interacts with Rsd; this prevents interaction with the RNA polymerase catalytic core and with promoter DNA, and as a consequence, promotes transcription from promoters that require alternative sigma factors.

Interacts with phage T4 AsiA; this interferes with binding to DNA and to the RNA polymerase.

UniRule annotation6 Publications

(Microbial infection) Interacts with Escherichia phage lambda antitermination protein Q.

1 Publication

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>Sitei562Interaction with anti-sigma factors1

<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		4261068, 200 interactors
851883, 14 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-4881, DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant
CPX-4901, rpod-rsd sigma-antisigma complex

Database of interacting proteins

More...DIPi		DIP-10773N

Protein interaction database and analysis system

More...IntActi		P00579, 56 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3067

<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

1613
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P00579

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

More...SMRi		P00579

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		P00579

<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>Regioni2 – 80Sigma-70 factor domain-1Add BLAST79
Regioni176 – 213DisorderedSequence analysisAdd BLAST38
Regioni379 – 449Sigma-70 factor domain-2Add BLAST71
Regioni458 – 534Sigma-70 factor domain-3Add BLAST77
Regioni547 – 600Sigma-70 factor domain-4Add BLAST54
Regioni584 – 599Interaction with anti-sigma factorsAdd BLAST16

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>Motifi403 – 406Interaction with polymerase core subunit RpoC4

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 biasi187 – 210Acidic residuesSequence analysisAdd BLAST24

<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

Contains 4 domains, connected by flexible linkers. In the active conformation, the domains are in an extended conformation, each making extensive interactions with the RNA polymerase catalytic core.
In the autoinhibited state, sigma-70 factor domain-1 packs closely together with sigma-70 factor domains-2 and -4, contrary to the extended conformation that is seen when the protein is part of the RNA polymerase holoenzyme.Curated
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.
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 (PubMed:19903881 and PubMed:21829166). This domain is probably also responsible for interaction with Crp (PubMed:10860740).1 Publication

<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. RpoD/SigA subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0568, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_014793_7_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00579

Database for complete collections of gene phylogenies

More...PhylomeDBi		P00579

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.10, 2 hits
1.10.220.120, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00963, Sigma70_RpoD_SigA, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR014284, RNA_pol_sigma-70_dom
IPR000943, RNA_pol_sigma70
IPR009042, RNA_pol_sigma70_r1_2
IPR007627, RNA_pol_sigma70_r2
IPR007624, RNA_pol_sigma70_r3
IPR007630, RNA_pol_sigma70_r4
IPR007631, RNA_pol_sigma_70_non-ess
IPR007127, RNA_pol_sigma_70_r1_1
IPR042189, RNA_pol_sigma_70_r1_1_sf
IPR013325, RNA_pol_sigma_r2
IPR013324, RNA_pol_sigma_r3/r4-like
IPR012760, RNA_pol_sigma_RpoD_C
IPR028630, Sigma70_RpoD
IPR036388, WH-like_DNA-bd_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04546, Sigma70_ner, 1 hit
PF03979, Sigma70_r1_1, 1 hit
PF00140, Sigma70_r1_2, 1 hit
PF04542, Sigma70_r2, 1 hit
PF04539, Sigma70_r3, 1 hit
PF04545, Sigma70_r4, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00046, SIGMA70FCT

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF88659, SSF88659, 2 hits
SSF88946, SSF88946, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02393, RpoD_Cterm, 1 hit
TIGR02937, sigma70-ECF, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00715, SIGMA70_1, 1 hit
PS00716, SIGMA70_2, 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.

P00579-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEQNPQSQLK LLVTRGKEQG YLTYAEVNDH LPEDIVDSDQ IEDIIQMIND 
        60         70         80         90        100
MGIQVMEEAP DADDLMLAEN TADEDAAEAA AQVLSSVESE IGRTTDPVRM 
       110        120        130        140        150
YMREMGTVEL LTREGEIDIA KRIEDGINQV QCSVAEYPEA ITYLLEQYDR 
       160        170        180        190        200
VEAEEARLSD LITGFVDPNA EEDLAPTATH VGSELSQEDL DDDEDEDEED 
       210        220        230        240        250
GDDDSADDDN SIDPELAREK FAELRAQYVV TRDTIKAKGR SHATAQEEIL 
       260        270        280        290        300
KLSEVFKQFR LVPKQFDYLV NSMRVMMDRV RTQERLIMKL CVEQCKMPKK 
       310        320        330        340        350
NFITLFTGNE TSDTWFNAAI AMNKPWSEKL HDVSEEVHRA LQKLQQIEEE 
       360        370        380        390        400
TGLTIEQVKD INRRMSIGEA KARRAKKEMV EANLRLVISI AKKYTNRGLQ 
       410        420        430        440        450
FLDLIQEGNI GLMKAVDKFE YRRGYKFSTY ATWWIRQAIT RSIADQARTI 
       460        470        480        490        500
RIPVHMIETI NKLNRISRQM LQEMGREPTP EELAERMLMP EDKIRKVLKI 
       510        520        530        540        550
AKEPISMETP IGDDEDSHLG DFIEDTTLEL PLDSATTESL RAATHDVLAG 
       560        570        580        590        600
LTAREAKVLR MRFGIDMNTD YTLEEVGKQF DVTRERIRQI EAKALRKLRH 
       610 
PSRSEVLRSF LDD
Length:613
Mass (Da):70,263
Last modified:October 1, 1996 - v2
<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:iCA4F0E30DEC1703D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti149D → N in AAA24601 (PubMed:6269063).Curated1

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
J01687 Genomic DNA Translation: AAA24601.1
U28379 Genomic DNA Translation: AAA89147.1
U00096 Genomic DNA Translation: AAC76103.1
AP009048 Genomic DNA Translation: BAE77118.1

Protein sequence database of the Protein Information Resource

More...PIRi		A65095, RNECS

NCBI Reference Sequences

More...RefSeqi		NP_417539.1, NC_000913.3
WP_000437376.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76103; AAC76103; b3067
BAE77118; BAE77118; BAE77118

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947567

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3039
eco:b3067

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3662

<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
J01687 Genomic DNA Translation: AAA24601.1
U28379 Genomic DNA Translation: AAA89147.1
U00096 Genomic DNA Translation: AAC76103.1
AP009048 Genomic DNA Translation: BAE77118.1
PIRiA65095, RNECS
RefSeqiNP_417539.1, NC_000913.3
WP_000437376.1, 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 entryMethodResolution (Å)ChainPositionsPDBsum
1SIGX-ray2.60A114-448[»]
1TLHNMR-B533-613[»]
2P7VX-ray2.60B546-613[»]
3IYDelectron microscopy19.80F1-613[»]
3T72X-ray4.33o/q533-609[»]
4JK1X-ray3.90X/Y1-613[»]
4JK2X-ray4.20X/Y1-613[»]
4JKRX-ray4.20F/L1-613[»]
4KMUX-ray3.85X/Y1-613[»]
4KN4X-ray3.96X/Y1-613[»]
4KN7X-ray3.69X/Y1-613[»]
4LJZX-ray3.59F/L92-613[»]
4LK0X-ray3.91F/L92-613[»]
4LK1X-ray3.84F/L1-613[»]
4LLGX-ray3.79F/L1-613[»]
4MEXX-ray3.90F/L1-613[»]
4MEYX-ray3.95F/L1-613[»]
4XSXX-ray3.71F/L92-613[»]
4XSYX-ray4.01F/L92-613[»]
4XSZX-ray3.68F/L92-613[»]
4YFKX-ray3.57F/L1-613[»]
4YFNX-ray3.82F/L1-613[»]
4YFXX-ray3.84F/L1-613[»]
4YG2X-ray3.70F/L1-613[»]
4YLNX-ray5.50F/L/R1-613[»]
4YLOX-ray6.00F/L/R1-613[»]
4YLPX-ray5.50F/L/R1-613[»]
4ZH2X-ray4.20F/L1-613[»]
4ZH3X-ray4.08F/L1-613[»]
4ZH4X-ray3.99F/L1-613[»]
5UACX-ray3.80F/L1-613[»]
5UAGX-ray3.40F/L1-613[»]
5UAHX-ray4.10F/L1-613[»]
5UAJX-ray3.92F/L1-613[»]
5UALX-ray3.89F/L1-613[»]
5UAQX-ray3.60F/L1-613[»]
5VSWX-ray4.29F/L1-613[»]
5VT0electron microscopy3.78L94-613[»]
5W1SX-ray3.81F/L1-613[»]
5W1TX-ray4.50F/L1-613[»]
6B6Helectron microscopy3.90F1-613[»]
6BYUX-ray3.60F/L1-613[»]
6C9Yelectron microscopy4.25F1-613[»]
6CA0electron microscopy5.75F1-613[»]
6CUXX-ray4.10F/L1-613[»]
6JNXelectron microscopy4.08F1-613[»]
6K4Yelectron microscopy3.79F1-613[»]
6LDIelectron microscopy3.69F1-613[»]
6N4Celectron microscopy17.00F8-613[»]
6N57electron microscopy3.70L1-613[»]
6N58electron microscopy3.78L1-613[»]
6OULelectron microscopy3.40L1-613[»]
6P18electron microscopy3.50F1-613[»]
6P1Kelectron microscopy4.05L1-613[»]
6PB4electron microscopy4.35F1-613[»]
6PB5electron microscopy4.52F1-613[»]
6PB6electron microscopy4.29F1-613[»]
6PSQelectron microscopy3.40L1-613[»]
6PSRelectron microscopy3.40L1-613[»]
6PSSelectron microscopy3.50L1-613[»]
6PSTelectron microscopy3.00L1-613[»]
6PSUelectron microscopy3.90L1-613[»]
6PSVelectron microscopy3.50L1-613[»]
6PSWelectron microscopy3.70L1-613[»]
6VJSX-ray4.02X/Y1-613[»]
6XH7electron microscopy3.90F1-613[»]
6XH8electron microscopy4.10F1-613[»]
6XL5electron microscopy2.50F1-613[»]
6XL9electron microscopy2.50F1-613[»]
6XLJelectron microscopy2.70F1-613[»]
6XLLelectron microscopy2.70F1-613[»]
6XLMelectron microscopy3.20F1-613[»]
7C17electron microscopy4.22F1-613[»]
7C97electron microscopy3.68F1-613[»]
7CHWelectron microscopy3.58F1-613[»]
7KHBelectron microscopy3.53F1-613[»]
7KHCelectron microscopy4.14F1-613[»]
7KHEelectron microscopy3.58F1-613[»]
7KHIelectron microscopy3.62F1-613[»]
BMRBiP00579
SMRiP00579
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261068, 200 interactors
851883, 14 interactors
ComplexPortaliCPX-4881, DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant
CPX-4901, rpod-rsd sigma-antisigma complex
DIPiDIP-10773N
IntActiP00579, 56 interactors
STRINGi511145.b3067

Proteomic databases

jPOSTiP00579
PaxDbiP00579
PRIDEiP00579

Genome annotation databases

EnsemblBacteriaiAAC76103; AAC76103; b3067
BAE77118; BAE77118; BAE77118
GeneIDi947567
KEGGiecj:JW3039
eco:b3067
PATRICifig|1411691.4.peg.3662

Organism-specific databases

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

More...EchoBASEi		EB0889

Phylogenomic databases

eggNOGiCOG0568, Bacteria
HOGENOMiCLU_014793_7_2_6
InParanoidiP00579
PhylomeDBiP00579

Enzyme and pathway databases

BioCyciEcoCyc:RPOD-MONOMER

Miscellaneous databases

EvolutionaryTraceiP00579

Protein Ontology

More...PROi		PR:P00579

Family and domain databases

Gene3Di1.10.10.10, 2 hits
1.10.220.120, 1 hit
HAMAPiMF_00963, Sigma70_RpoD_SigA, 1 hit
InterProiView protein in InterPro
IPR014284, RNA_pol_sigma-70_dom
IPR000943, RNA_pol_sigma70
IPR009042, RNA_pol_sigma70_r1_2
IPR007627, RNA_pol_sigma70_r2
IPR007624, RNA_pol_sigma70_r3
IPR007630, RNA_pol_sigma70_r4
IPR007631, RNA_pol_sigma_70_non-ess
IPR007127, RNA_pol_sigma_70_r1_1
IPR042189, RNA_pol_sigma_70_r1_1_sf
IPR013325, RNA_pol_sigma_r2
IPR013324, RNA_pol_sigma_r3/r4-like
IPR012760, RNA_pol_sigma_RpoD_C
IPR028630, Sigma70_RpoD
IPR036388, WH-like_DNA-bd_sf
PfamiView protein in Pfam
PF04546, Sigma70_ner, 1 hit
PF03979, Sigma70_r1_1, 1 hit
PF00140, Sigma70_r1_2, 1 hit
PF04542, Sigma70_r2, 1 hit
PF04539, Sigma70_r3, 1 hit
PF04545, Sigma70_r4, 1 hit
PRINTSiPR00046, SIGMA70FCT
SUPFAMiSSF88659, SSF88659, 2 hits
SSF88946, SSF88946, 1 hit
TIGRFAMsiTIGR02393, RpoD_Cterm, 1 hit
TIGR02937, sigma70-ECF, 1 hit
PROSITEiView protein in PROSITE
PS00715, SIGMA70_1, 1 hit
PS00716, SIGMA70_2, 1 hit

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 nameiRPOD_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: P00579
Secondary accession number(s): Q2M9D8
<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: July 21, 1986
Last sequence update: October 1, 1996
Last modified: February 23, 2022
This is version 207 of the entry and version 2 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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