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UniProtKB - P0A7Z4 (RPOA_ECOLI)

Entry version 158 (23 Feb 2022)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
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Protein

DNA-directed RNA polymerase subunit alpha

Gene

rpoA

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

DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.

2 Publications

Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNAP. It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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 functionNucleotidyltransferase, Transferase
Biological processTranscription

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10893-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.7.6, 2026

<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:
DNA-directed RNA polymerase subunit alpha (EC:2.7.7.6)
Short name:
RNAP subunit alpha
Alternative name(s):
RNA polymerase subunit alpha
Transcriptase subunit alpha
<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:rpoA
Synonyms:pez, phs, sez
Ordered Locus Names:b3295, JW3257
<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

DNA-directed RNA polymerase

<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>Mutagenesisi45R → C in rpoA112; temperature-sensitive, blocks RNA polymerase assembly. 1 Publication1
Mutagenesisi162 – 165EEDE → AAAA: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication4
Mutagenesisi165E → K: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication1
Mutagenesisi191R → C in rpoA101; temperature-sensitive. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2364672
CHEMBL4296169

Drug and drug target database

More...DrugBanki		DB00615, Rifabutin
DB11753, Rifamycin

DrugCentral

More...DrugCentrali		P0A7Z4

<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_00001753041 – 329DNA-directed RNA polymerase subunit alphaAdd BLAST329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei265ADP-ribosylarginine1 Publication1
Modified residuei297N6-acetyllysine1 Publication1
Modified residuei298N6-acetyllysine; by PatZ1 Publication1

<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

Acetylated on Lys-297 and Lys-298 in the presence of glucose. PatZ controls acetylation of Lys-298 but not of Lys-297.1 Publication
(Microbial infection) ADP-ribosylated on both alpha subunits by the phage T4 protein ModA (PubMed:10634320, PubMed:15489438). ADP-ribosylated on only one of the alpha subunits by the phage T4 protein Alt (PubMed:15489438).2 Publications

Keywords - PTMi

Acetylation, ADP-ribosylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A7Z4

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

More...PaxDbi		P0A7Z4

PRoteomics IDEntifications database

More...PRIDEi		P0A7Z4

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0A7Z4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0A7Z4

<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

Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. Both the N- and C-terminus interact with different regions of transcriptional regulator CRP. The rRNA transcription and antitermination complex (rrnTAC) consists of RNAP, NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than other subunits (PubMed:32871103).

6 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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4263398, 114 interactors
852106, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-4881, DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant
CPX-4883, DNA-directed RNA polymerase holoenzyme complex, SigmaS variant
CPX-4884, DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant
CPX-4885, DNA-directed RNA polymerase holoenzyme complex, SigmaE variant
CPX-4886, DNA-directed RNA polymerase holoenzyme complex, SigmaF variant
CPX-4887, DNA-directed RNA polymerase holoenzyme complex, SigmaH variant
CPX-4888, DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant
CPX-5674, Transcription elongation complex
CPX-5780, lambdaN-dependent processive transcription antitermination complex

Database of interacting proteins

More...DIPi		DIP-35879N

Protein interaction database and analysis system

More...IntActi		P0A7Z4, 91 interactors

Molecular INTeraction database

More...MINTi		P0A7Z4

STRING: functional protein association networks

More...STRINGi		511145.b3295

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0A7Z4

<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

1329
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		P0A7Z4

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		P0A7Z4

<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 – 235Alpha N-terminal domain (alpha-NTD)Add BLAST235
Regioni162 – 165Required for interaction with Crp at class II promoters4
Regioni249 – 329Alpha C-terminal domain (alpha-CTD); not required for RNAP assembly or functionAdd BLAST81

<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 domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators (such as CRP) and with upstream promoter elements.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 RNA polymerase alpha chain family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0202, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_053084_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A7Z4

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A7Z4

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.170.120.12, 1 hit
3.30.1360.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00059, RNApol_bact_RpoA, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011262, DNA-dir_RNA_pol_insert
IPR011263, DNA-dir_RNA_pol_RpoA/D/Rpb3
IPR011773, DNA-dir_RpoA
IPR036603, RBP11-like
IPR011260, RNAP_asu_C
IPR036643, RNApol_insert_sf

The PANTHER Classification System

More...PANTHERi		PTHR32108, PTHR32108, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01000, RNA_pol_A_bac, 1 hit
PF03118, RNA_pol_A_CTD, 1 hit
PF01193, RNA_pol_L, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00662, RPOLD, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55257, SSF55257, 1 hit
SSF56553, SSF56553, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02027, rpoA, 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.

P0A7Z4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQGSVTEFLK PRLVDIEQVS STHAKVTLEP LERGFGHTLG NALRRILLSS 
        60         70         80         90        100
MPGCAVTEVE IDGVLHEYST KEGVQEDILE ILLNLKGLAV RVQGKDEVIL 
       110        120        130        140        150
TLNKSGIGPV TAADITHDGD VEIVKPQHVI CHLTDENASI SMRIKVQRGR 
       160        170        180        190        200
GYVPASTRIH SEEDERPIGR LLVDACYSPV ERIAYNVEAA RVEQRTDLDK 
       210        220        230        240        250
LVIEMETNGT IDPEEAIRRA ATILAEQLEA FVDLRDVRQP EVKEEKPEFD 
       260        270        280        290        300
PILLRPVDDL ELTVRSANCL KAEAIHYIGD LVQRTEVELL KTPNLGKKSL 
       310        320 
TEIKDVLASR GLSLGMRLEN WPPASIADE
Length:329
Mass (Da):36,512
Last modified:July 21, 1986 - 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:i12A14B75A3CAEA19
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 conflicti4S → N AA sequence (PubMed:1095419).Curated1
Sequence conflicti208N → T in CAA26395 (PubMed:2989779).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
J01685 Genomic DNA Translation: AAA24577.1
X00766 Genomic DNA Translation: CAA25337.1
X02543 Genomic DNA Translation: CAA26395.1
U18997 Genomic DNA Translation: AAA58092.1
X53843 Genomic DNA Translation: CAA37838.1
X53844 Genomic DNA Translation: CAA37839.1
U00096 Genomic DNA Translation: AAC76320.1
AP009048 Genomic DNA Translation: BAE77996.1
V00353 Genomic DNA Translation: CAA23646.1
M29822 Genomic DNA Translation: AAA24590.1
M29823 Genomic DNA Translation: AAA24592.1
M29824 Genomic DNA Translation: AAA24594.1

Protein sequence database of the Protein Information Resource

More...PIRi		A22884, RNECA

NCBI Reference Sequences

More...RefSeqi		NP_417754.1, NC_000913.3
WP_001162094.1, NZ_STEB01000038.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76320; AAC76320; b3295
BAE77996; BAE77996; BAE77996

Database of genes from NCBI RefSeq genomes

More...GeneIDi		67415336
947794

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3257
eco:b3295

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3436

<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
J01685 Genomic DNA Translation: AAA24577.1
X00766 Genomic DNA Translation: CAA25337.1
X02543 Genomic DNA Translation: CAA26395.1
U18997 Genomic DNA Translation: AAA58092.1
X53843 Genomic DNA Translation: CAA37838.1
X53844 Genomic DNA Translation: CAA37839.1
U00096 Genomic DNA Translation: AAC76320.1
AP009048 Genomic DNA Translation: BAE77996.1
V00353 Genomic DNA Translation: CAA23646.1
M29822 Genomic DNA Translation: AAA24590.1
M29823 Genomic DNA Translation: AAA24592.1
M29824 Genomic DNA Translation: AAA24594.1
PIRiA22884, RNECA
RefSeqiNP_417754.1, NC_000913.3
WP_001162094.1, NZ_STEB01000038.1

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
1BDFX-ray2.50A/B/C/D1-235[»]
1COONMR-A233-329[»]
1LB2X-ray3.10B/E246-329[»]
1XS9NMR-D249-329[»]
3IYDelectron microscopy-A/B1-329[»]
3K4GX-ray2.05A/B/C/D/E/F/G/H245-329[»]
3LU0electron microscopy-A/B1-329[»]
3N4MX-ray2.99B/C246-329[»]
3N97X-ray3.25B/C246-329[»]
4JK1X-ray3.90A/B/F/G1-329[»]
4JK2X-ray4.20A/B/F/G1-329[»]
4KMUX-ray3.85A/B/F/G1-329[»]
4KN4X-ray3.96A/B/F/G1-329[»]
4KN7X-ray3.69A/B/F/G1-329[»]
4MEXX-ray3.90A/B/G/H1-329[»]
4MEYX-ray3.95A/B/G/H1-329[»]
4S20X-ray4.70A/B/F/G1-329[»]
4XSXX-ray3.71A/B/G/H1-234[»]
4XSYX-ray4.01A/B/G/H1-234[»]
4XSZX-ray3.68A/B/G/H1-234[»]
4YG2X-ray3.70A/B/G/H1-329[»]
4YLNX-ray5.50A/B/G/H/M/N1-235[»]
4YLOX-ray6.00A/B/G/H/M/N1-235[»]
4YLPX-ray5.50A/B/G/H/M/N1-235[»]
4ZH2X-ray4.20A/B/G/H2-329[»]
4ZH3X-ray4.08A/B/G/H2-329[»]
4ZH4X-ray3.99A/B/G/H2-329[»]
5BYHX-ray3.76A/B1-329[»]
5CIZX-ray5.01B246-329[»]
5EZKX-ray8.50A/B1-329[»]
5IPLX-ray3.60A/B1-235[»]
5IPMX-ray4.20A/B1-235[»]
5IPNX-ray4.61A/B1-235[»]
5MS0electron microscopy9.80A/B1-329[»]
5MY1electron microscopy7.60V/W1-329[»]
5NSRelectron microscopy3.80A/B1-329[»]
5NSSelectron microscopy5.80A/B1-329[»]
5NWTX-ray3.76A/B1-329[»]
5UACX-ray3.80A/B/G/H1-329[»]
5UAGX-ray3.40A/B/G/H1-320[»]
5UAHX-ray4.10A/B/G/H1-329[»]
5UAJX-ray3.92A/B/G/H1-329[»]
5UALX-ray3.89A/B/G/H1-329[»]
5UAQX-ray3.60A/B/G/H1-329[»]
5VSWX-ray4.29A/B/G/H1-329[»]
5VT0electron microscopy3.78G/H1-234[»]
5W1SX-ray3.81A/B/G/H1-329[»]
5W1TX-ray4.50A/B/G/H1-329[»]
6ALFelectron microscopy4.10G/H1-234[»]
6ALGelectron microscopy3.70G/H1-234[»]
6ALHelectron microscopy4.40G/H1-234[»]
6ASXelectron microscopy3.80G/H1-234[»]
6BJSelectron microscopy5.50G/H1-234[»]
6BYUX-ray3.60A/B/G/H1-329[»]
6C6Selectron microscopy3.70G/H1-234[»]
6C6Telectron microscopy3.50G/H1-234[»]
6C6Uelectron microscopy3.70G/H1-234[»]
6C9Yelectron microscopy4.25A/B1-329[»]
6CA0electron microscopy5.75A/B1-329[»]
6CUXX-ray4.10A/B/G/H1-329[»]
6FLPelectron microscopy4.10A/B1-329[»]
6FLQelectron microscopy4.10A/B1-329[»]
6GFWelectron microscopy3.70A/B1-329[»]
6GH5electron microscopy3.40A/B1-329[»]
6GH6electron microscopy4.10A/B1-329[»]
6JBQelectron microscopy4.02A/B1-329[»]
6JNXelectron microscopy4.08A/B1-329[»]
6K4Yelectron microscopy3.79A/B1-329[»]
6KJ6electron microscopy3.80A/B1-329[»]
6LDIelectron microscopy3.69A/B1-329[»]
6N4Celectron microscopy17.00A6-321[»]
B6-315[»]
6N57electron microscopy3.70G/H1-329[»]
6N58electron microscopy3.78G/H1-329[»]
6N60X-ray3.68A/B1-234[»]
6N61X-ray3.25A/B1-234[»]
6OMFelectron microscopy3.26A/B1-234[»]
6OULelectron microscopy3.40G/H/R1-329[»]
6P18electron microscopy3.50A/B1-329[»]
6P19electron microscopy3.80A/B1-329[»]
6P1Kelectron microscopy4.05G/H1-329[»]
6PB4electron microscopy4.35A/B1-329[»]
6PB5electron microscopy4.52A/B1-329[»]
6PB6electron microscopy4.29A/B1-329[»]
6PMIelectron microscopy3.86A/B1-329[»]
6PMJelectron microscopy3.91A/B1-329[»]
6PSQelectron microscopy3.40G/H/M1-329[»]
6PSRelectron microscopy3.40G/H/M1-329[»]
6PSSelectron microscopy3.50G/H/M1-329[»]
6PSTelectron microscopy3.00G/H/M1-329[»]
6PSUelectron microscopy3.90G/H/M1-329[»]
6PSVelectron microscopy3.50G/H/M1-329[»]
6PSWelectron microscopy3.70G/H/M1-329[»]
6R9Belectron microscopy3.80A/B1-329[»]
6R9Gelectron microscopy3.70A/B1-329[»]
6RH3electron microscopy3.60A/B1-329[»]
6RI7electron microscopy3.90A/B1-329[»]
6RI9electron microscopy3.70A/B1-329[»]
6RINelectron microscopy3.70A/B1-329[»]
6RIPelectron microscopy3.40A/B1-329[»]
6TQNelectron microscopy3.80U/V1-329[»]
6TQOelectron microscopy3.80U/V1-329[»]
6UTWX-ray3.85AAA/BBB1-235[»]
6UTXX-ray4.05AAA/BBB1-235[»]
6UTYX-ray4.15AAA/BBB1-235[»]
6UU5X-ray5.40AAA/BBB1-235[»]
6UU6X-ray4.20AAA/BBB1-235[»]
6UU7X-ray4.40AAA/BBB1-235[»]
6UU8X-ray4.40AAA/BBB1-235[»]
6UUBX-ray3.96AAA/BBB1-235[»]
6VJSX-ray4.02A/B/F/G1-329[»]
6WMUelectron microscopy3.18A/B1-329[»]
6X26electron microscopy4.10G/H1-329[»]
6X2Felectron microscopy4.00G/H1-329[»]
6X2Nelectron microscopy3.90G/H1-329[»]
6X43electron microscopy3.60G/H1-329[»]
6X4Welectron microscopy3.80G/H1-329[»]
6X4Yelectron microscopy3.60G/H1-329[»]
6X50electron microscopy3.30G/H1-329[»]
6XASelectron microscopy3.80H/K1-329[»]
6XAVelectron microscopy7.70H/K1-329[»]
6XH7electron microscopy3.90A/B1-329[»]
6XH8electron microscopy4.10A/B1-329[»]
6XL5electron microscopy2.50A/B1-329[»]
6XL9electron microscopy2.50A/B1-329[»]
6XLJelectron microscopy2.70A/B1-329[»]
6XLLelectron microscopy2.70A/B1-329[»]
6XLMelectron microscopy3.20A/B1-329[»]
6XLNelectron microscopy2.80A/B1-329[»]
6Z9Pelectron microscopy3.90U/V1-329[»]
6Z9Qelectron microscopy5.70U/V1-329[»]
6Z9Relectron microscopy4.10U/V1-329[»]
6Z9Selectron microscopy4.40U/V1-329[»]
6Z9Telectron microscopy4.10U/V1-329[»]
6ZTJelectron microscopy3.40CA/CB1-329[»]
6ZTLelectron microscopy3.50CA/CB1-329[»]
6ZTMelectron microscopy3.30CA/CB1-329[»]
6ZTNelectron microscopy3.90CA/CB1-329[»]
6ZTOelectron microscopy3.00CA/CB1-329[»]
6ZTPelectron microscopy3.00CA/CB1-329[»]
6ZU1electron microscopy3.00CA/CB1-329[»]
7ADBelectron microscopy4.40U/V1-329[»]
7ADCelectron microscopy4.00U/V1-329[»]
7ADDelectron microscopy4.30U/V1-329[»]
7ADEelectron microscopy4.20U/V1-329[»]
7C17electron microscopy4.22A/B1-329[»]
7C97electron microscopy3.68A/B/K1-329[»]
7CHWelectron microscopy3.58A/B/K1-329[»]
7KHBelectron microscopy3.53A/B1-329[»]
7KHCelectron microscopy4.14A/B1-329[»]
7KHEelectron microscopy3.58A/B1-236[»]
7KHIelectron microscopy3.62A/B1-236[»]
7MKNelectron microscopy3.30A/B1-237[»]
7MKOelectron microscopy3.15A/B1-237[»]
7MKQelectron microscopy4.80A/B1-237[»]
SMRiP0A7Z4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263398, 114 interactors
852106, 1 interactor
ComplexPortaliCPX-4881, DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant
CPX-4883, DNA-directed RNA polymerase holoenzyme complex, SigmaS variant
CPX-4884, DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant
CPX-4885, DNA-directed RNA polymerase holoenzyme complex, SigmaE variant
CPX-4886, DNA-directed RNA polymerase holoenzyme complex, SigmaF variant
CPX-4887, DNA-directed RNA polymerase holoenzyme complex, SigmaH variant
CPX-4888, DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant
CPX-5674, Transcription elongation complex
CPX-5780, lambdaN-dependent processive transcription antitermination complex
DIPiDIP-35879N
IntActiP0A7Z4, 91 interactors
MINTiP0A7Z4
STRINGi511145.b3295

Chemistry databases

BindingDBiP0A7Z4
ChEMBLiCHEMBL2364672
CHEMBL4296169
DrugBankiDB00615, Rifabutin
DB11753, Rifamycin
DrugCentraliP0A7Z4

PTM databases

iPTMnetiP0A7Z4

2D gel databases

SWISS-2DPAGEiP0A7Z4

Proteomic databases

jPOSTiP0A7Z4
PaxDbiP0A7Z4
PRIDEiP0A7Z4

Genome annotation databases

EnsemblBacteriaiAAC76320; AAC76320; b3295
BAE77996; BAE77996; BAE77996
GeneIDi67415336
947794
KEGGiecj:JW3257
eco:b3295
PATRICifig|1411691.4.peg.3436

Organism-specific databases

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

More...EchoBASEi		EB0886

Phylogenomic databases

eggNOGiCOG0202, Bacteria
HOGENOMiCLU_053084_0_0_6
InParanoidiP0A7Z4
PhylomeDBiP0A7Z4

Enzyme and pathway databases

BioCyciEcoCyc:EG10893-MONOMER
BRENDAi2.7.7.6, 2026

Miscellaneous databases

EvolutionaryTraceiP0A7Z4

Protein Ontology

More...PROi		PR:P0A7Z4

Family and domain databases

Gene3Di2.170.120.12, 1 hit
3.30.1360.10, 1 hit
HAMAPiMF_00059, RNApol_bact_RpoA, 1 hit
InterProiView protein in InterPro
IPR011262, DNA-dir_RNA_pol_insert
IPR011263, DNA-dir_RNA_pol_RpoA/D/Rpb3
IPR011773, DNA-dir_RpoA
IPR036603, RBP11-like
IPR011260, RNAP_asu_C
IPR036643, RNApol_insert_sf
PANTHERiPTHR32108, PTHR32108, 1 hit
PfamiView protein in Pfam
PF01000, RNA_pol_A_bac, 1 hit
PF03118, RNA_pol_A_CTD, 1 hit
PF01193, RNA_pol_L, 1 hit
SMARTiView protein in SMART
SM00662, RPOLD, 1 hit
SUPFAMiSSF55257, SSF55257, 1 hit
SSF56553, SSF56553, 1 hit
TIGRFAMsiTIGR02027, rpoA, 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 nameiRPOA_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: P0A7Z4
Secondary accession number(s): P00574, Q2M6W0
<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: July 21, 1986
Last modified: February 23, 2022
This is version 158 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
UniProt is an ELIXIR core data resource
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