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UniProtKB - P0A8V2 (RPOB_ECOLI)

Entry version 159 (23 Feb 2022)
Sequence version 1 (07 Jun 2005)
Previous versions | rss
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Protein

DNA-directed RNA polymerase subunit beta

Gene

rpoB

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.

2 Publications

Resistance to the antibiotics salinamide A, salinamide B, rifampicin, streptolydigin, CBR703, myxopyronin, and lipiarmycin can result from mutations in this protein.

1 Publication1 Publication

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 processAntibiotic resistance, Transcription

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:RPOB-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 beta (EC:2.7.7.6)
Short name:
RNAP subunit beta
Alternative name(s):
RNA polymerase subunit beta
Transcriptase subunit beta
<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:rpoB
Synonyms:groN, nitB, rif, ron, stl, stv, tabD
Ordered Locus Names:b3987, JW3950
<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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Co-administration of salinamide and rifampicin or salinamide and myxopyronin suppresses the emergence of resistance to both antibiotics.1 Publication

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>Mutagenesisi561I → S: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi569I → S: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi665A → E: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi675D → A or G: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi677N → H or K: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi680L → M: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi813E → K: Disrupts the enzyme's active center. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1852

Drug and drug target database

More...DrugBanki		DB00615, Rifabutin
DB04934, Rifalazil
DB01045, Rifampicin
DB11753, Rifamycin
DB01220, Rifaximin

DrugCentral

More...DrugCentrali		P0A8V2

<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_00000478921 – 1342DNA-directed RNA polymerase subunit betaAdd BLAST1342

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 residuei1022N6-acetyllysine1 Publication1
Modified residuei1200N6-acetyllysine1 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 several lysine residues in the presence of glucose.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A8V2

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

More...PaxDbi		P0A8V2

PRoteomics IDEntifications database

More...PRIDEi		P0A8V2

2D gel databases

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

More...SWISS-2DPAGEi		P0A8V2

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P0A8V2

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0A8V2

<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

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. 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).

4 Publications

(Microbial infection) Interacts (via flap domain) with Escherichia phage lambda antitermination protein Q; this interaction renders bacterial RNAP resistant to transcription pausing and allows it to read through termination signals.

2 Publications

(Microbial infection) Interacts (via flap domain) with the late transcription coactivator of enterobacteria phage T4.

1 Publication

<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		4263472, 52 interactors
852782, 2 interactors

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-35777N

Protein interaction database and analysis system

More...IntActi		P0A8V2, 103 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3987

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0A8V2

<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

11342
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		P0A8V2

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		P0A8V2

<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

<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 beta chain family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0085, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000524_4_3_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A8V2

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A8V2

Family and domain databases

Conserved Domains Database

More...CDDi		cd00653, RNA_pol_B_RPB2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.150.10, 1 hit
2.40.270.10, 1 hit
2.40.50.150, 1 hit
3.90.1110.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01321, RNApol_bact_RpoB, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR042107, DNA-dir_RNA_pol_bsu_ext_1_sf
IPR019462, DNA-dir_RNA_pol_bsu_external_1
IPR015712, DNA-dir_RNA_pol_su2
IPR007120, DNA-dir_RNAP_su2_dom
IPR037033, DNA-dir_RNAP_su2_hyb_sf
IPR010243, RNA_pol_bsu_bac
IPR007121, RNA_pol_bsu_CS
IPR007644, RNA_pol_bsu_protrusion
IPR007642, RNA_pol_Rpb2_2
IPR037034, RNA_pol_Rpb2_2_sf
IPR007645, RNA_pol_Rpb2_3
IPR007641, RNA_pol_Rpb2_7
IPR014724, RNA_pol_RPB2_OB-fold

The PANTHER Classification System

More...PANTHERi		PTHR20856, PTHR20856, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04563, RNA_pol_Rpb2_1, 1 hit
PF04561, RNA_pol_Rpb2_2, 2 hits
PF04565, RNA_pol_Rpb2_3, 1 hit
PF10385, RNA_pol_Rpb2_45, 1 hit
PF00562, RNA_pol_Rpb2_6, 1 hit
PF04560, RNA_pol_Rpb2_7, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02013, rpoB, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01166, RNA_POL_BETA, 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.

P0A8V2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE 
        60         70         80         90        100
AAFRSVFPIQ SYSGNSELQY VSYRLGEPVF DVQECQIRGV TYSAPLRVKL 
       110        120        130        140        150
RLVIYEREAP EGTVKDIKEQ EVYMGEIPLM TDNGTFVING TERVIVSQLH 
       160        170        180        190        200
RSPGVFFDSD KGKTHSSGKV LYNARIIPYR GSWLDFEFDP KDNLFVRIDR 
       210        220        230        240        250
RRKLPATIIL RALNYTTEQI LDLFFEKVIF EIRDNKLQME LVPERLRGET 
       260        270        280        290        300
ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVKLIEVPVE YIAGKVVAKD 
       310        320        330        340        350
YIDESTGELI CAANMELSLD LLAKLSQSGH KRIETLFTND LDHGPYISET 
       360        370        380        390        400
LRVDPTNDRL SALVEIYRMM RPGEPPTREA AESLFENLFF SEDRYDLSAV 
       410        420        430        440        450
GRMKFNRSLL REEIEGSGIL SKDDIIDVMK KLIDIRNGKG EVDDIDHLGN 
       460        470        480        490        500
RRIRSVGEMA ENQFRVGLVR VERAVKERLS LGDLDTLMPQ DMINAKPISA 
       510        520        530        540        550
AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR ERAGFEVRDV 
       560        570        580        590        600
HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRKVTDGVVT 
       610        620        630        640        650
DEIHYLSAIE EGNYVIAQAN SNLDEEGHFV EDLVTCRSKG ESSLFSRDQV 
       660        670        680        690        700
DYMDVSTQQV VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV 
       710        720        730        740        750
GTGMERAVAV DSGVTAVAKR GGVVQYVDAS RIVIKVNEDE MYPGEAGIDI 
       760        770        780        790        800
YNLTKYTRSN QNTCINQMPC VSLGEPVERG DVLADGPSTD LGELALGQNM 
       810        820        830        840        850
RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELACVS RDTKLGPEEI 
       860        870        880        890        900
TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK 
       910        920        930        940        950
LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE 
       960        970        980        990       1000
MQLKQAKKDL SEELQILEAG LFSRIRAVLV AGGVEAEKLD KLPRDRWLEL 
      1010       1020       1030       1040       1050
GLTDEEKQNQ LEQLAEQYDE LKHEFEKKLE AKRRKITQGD DLAPGVLKIV 
      1060       1070       1080       1090       1100
KVYLAVKRRI QPGDKMAGRH GNKGVISKIN PIEDMPYDEN GTPVDIVLNP 
      1110       1120       1130       1140       1150
LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK LREFIQRAYD 
      1160       1170       1180       1190       1200
LGADVRQKVD LSTFSDEEVM RLAENLRKGM PIATPVFDGA KEAEIKELLK 
      1210       1220       1230       1240       1250
LGDLPTSGQI RLYDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHARSTGS 
      1260       1270       1280       1290       1300
YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG 
      1310       1320       1330       1340 
RTKMYKNIVD GNHQMEPGMP ESFNVLLKEI RSLGINIELE DE
Length:1,342
Mass (Da):150,632
Last modified:June 7, 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:iF9E95344C54AB118
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 described in Ref. 7 differs from that shown.Curated

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 → R AA sequence (PubMed:1095419).Curated1
Sequence conflicti106 – 107ER → G in CAA23629 (PubMed:7011900).Curated2
Sequence conflicti384 – 391LFENLFFS → CSRTCSSPT in CAA23629 (PubMed:7011900).Curated8
Sequence conflicti516D → V in CAA23625 (PubMed:6266829).Curated1
Sequence conflicti516D → V in CAA23627 (PubMed:6266829).Curated1
Sequence conflicti516D → V in AAA24585 (Ref. 11) 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
V00339 Genomic DNA Translation: CAA23625.1
V00340 Genomic DNA Translation: CAA23627.1
U76222 Genomic DNA Translation: AAB18647.1
U00006 Genomic DNA Translation: AAC43085.1
U00096 Genomic DNA Translation: AAC76961.1
AP009048 Genomic DNA Translation: BAE77333.1
V00341 Genomic DNA Translation: CAA23629.1
M38292 Genomic DNA Translation: AAA24579.1
M38293 Genomic DNA Translation: AAA24581.1
M38287 Genomic DNA Translation: AAA24585.1
M38304 Genomic DNA Translation: AAA24580.1
U77436 Genomic DNA Translation: AAD09605.1
M38303 Genomic DNA Translation: AAA24583.1

Protein sequence database of the Protein Information Resource

More...PIRi		F65205, RNECB

NCBI Reference Sequences

More...RefSeqi		NP_418414.1, NC_000913.3
WP_000263098.1, NZ_STEB01000045.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76961; AAC76961; b3987
BAE77333; BAE77333; BAE77333

Database of genes from NCBI RefSeq genomes

More...GeneIDi		67415312
948488

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3950
eco:b3987

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2725

<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
V00339 Genomic DNA Translation: CAA23625.1
V00340 Genomic DNA Translation: CAA23627.1
U76222 Genomic DNA Translation: AAB18647.1
U00006 Genomic DNA Translation: AAC43085.1
U00096 Genomic DNA Translation: AAC76961.1
AP009048 Genomic DNA Translation: BAE77333.1
V00341 Genomic DNA Translation: CAA23629.1
M38292 Genomic DNA Translation: AAA24579.1
M38293 Genomic DNA Translation: AAA24581.1
M38287 Genomic DNA Translation: AAA24585.1
M38304 Genomic DNA Translation: AAA24580.1
U77436 Genomic DNA Translation: AAD09605.1
M38303 Genomic DNA Translation: AAA24583.1
PIRiF65205, RNECB
RefSeqiNP_418414.1, NC_000913.3
WP_000263098.1, NZ_STEB01000045.1

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
3IYDelectron microscopy-C1-1342[»]
3LTIX-ray1.60A152-443[»]
3LU0electron microscopy-C1-1342[»]
3T72X-ray4.33o/q896-910[»]
3TBIX-ray3.00B831-1057[»]
4JK1X-ray3.90C/H1-1342[»]
4JK2X-ray4.20C/H1-1342[»]
4KMUX-ray3.85C/H1-1342[»]
4KN4X-ray3.96C/H1-1342[»]
4KN7X-ray3.69C/H1-1342[»]
4MEXX-ray3.90C/I1-1342[»]
4MEYX-ray3.95C/I1-1342[»]
4S20X-ray4.70C/H1-1342[»]
4XSXX-ray3.71C/I1-1342[»]
4XSYX-ray4.01C/I1-1342[»]
4XSZX-ray3.68C/I1-1342[»]
4YG2X-ray3.70C/I1-1342[»]
4YLNX-ray5.50C/I/O1-1342[»]
4YLOX-ray6.00C/I/O1-1342[»]
4YLPX-ray5.50C/I/O1-1342[»]
4ZH2X-ray4.20C/I1-1342[»]
4ZH3X-ray4.08C/I1-1342[»]
4ZH4X-ray3.99C/I1-1342[»]
5BYHX-ray3.76C1-1342[»]
5EZKX-ray8.50C1-1342[»]
5IPLX-ray3.60C1-1342[»]
5IPMX-ray4.20C1-1342[»]
5IPNX-ray4.61C1-1342[»]
5MS0electron microscopy9.80C1-1342[»]
5MY1electron microscopy7.60X1-1342[»]
5NSRelectron microscopy3.80C1-1342[»]
5NSSelectron microscopy5.80C1-1342[»]
5NWTX-ray3.76C1-1342[»]
5UACX-ray3.80C/I1-1342[»]
5UAGX-ray3.40C/I1-1342[»]
5UAHX-ray4.10C/I1-1342[»]
5UAJX-ray3.92C/I1-1342[»]
5UALX-ray3.89C/I1-1342[»]
5UAQX-ray3.60C/I1-1342[»]
5VSWX-ray4.29C/I1-1342[»]
5VT0electron microscopy3.78I1-1342[»]
5W1SX-ray3.81C/I1-1342[»]
5W1TX-ray4.50C/I1-1342[»]
6ALFelectron microscopy4.10I1-1342[»]
6ALGelectron microscopy3.70I1-1342[»]
6ALHelectron microscopy4.40I1-1342[»]
6ASXelectron microscopy3.80I1-1342[»]
6BJSelectron microscopy5.50I1-1342[»]
6BYUX-ray3.60C/I1-1342[»]
6C6Selectron microscopy3.70I1-1342[»]
6C6Telectron microscopy3.50I1-1342[»]
6C6Uelectron microscopy3.70I1-1342[»]
6C9Yelectron microscopy4.25C1-1342[»]
6CA0electron microscopy5.75C1-1342[»]
6CUXX-ray4.10C/I1-1342[»]
6FLPelectron microscopy4.10C1-1342[»]
6FLQelectron microscopy4.10C1-1342[»]
6GFWelectron microscopy3.70C1-1342[»]
6GH5electron microscopy3.40C1-1342[»]
6GH6electron microscopy4.10C1-1342[»]
6JBQelectron microscopy4.02C1-1342[»]
6JNXelectron microscopy4.08C1-1342[»]
6K4Yelectron microscopy3.79C1-1342[»]
6KJ6electron microscopy3.80C1-1342[»]
6LDIelectron microscopy3.69C1-1342[»]
6N4Celectron microscopy17.00C2-1342[»]
6N57electron microscopy3.70I1-1342[»]
6N58electron microscopy3.78I1-1342[»]
6N60X-ray3.68C1-1342[»]
6N61X-ray3.25C1-1342[»]
6OMFelectron microscopy3.26C1-1342[»]
6OULelectron microscopy3.40I1-1342[»]
6P18electron microscopy3.50C1-1342[»]
6P19electron microscopy3.80C1-1342[»]
6P1Kelectron microscopy4.05I1-1342[»]
6PSQelectron microscopy3.40I1-1342[»]
6PSRelectron microscopy3.40I1-1342[»]
6PSSelectron microscopy3.50I1-1342[»]
6PSTelectron microscopy3.00I1-1342[»]
6PSUelectron microscopy3.90I1-1342[»]
6PSVelectron microscopy3.50I1-1342[»]
6PSWelectron microscopy3.70I1-1342[»]
6R9Belectron microscopy3.80C1-1342[»]
6R9Gelectron microscopy3.70C1-1342[»]
6RH3electron microscopy3.60C1-1342[»]
6RI7electron microscopy3.90C1-1342[»]
6RI9electron microscopy3.70C1-1342[»]
6RINelectron microscopy3.70C1-1342[»]
6RIPelectron microscopy3.40C1-1342[»]
6TQNelectron microscopy3.80X1-1342[»]
6TQOelectron microscopy4.00X1-1342[»]
6UTVX-ray3.45CCC1-1342[»]
6VJSX-ray4.02C/H1-1342[»]
6WMUelectron microscopy3.18C1-1342[»]
6X26electron microscopy4.10I1-1342[»]
6X2Felectron microscopy4.00I1-1342[»]
6X2Nelectron microscopy3.90I1-1342[»]
6X43electron microscopy3.60I1-1342[»]
6X4Welectron microscopy3.80I1-1342[»]
6X4Yelectron microscopy3.60I1-1342[»]
6X50electron microscopy3.30I1-1342[»]
6XASelectron microscopy3.80I1-1342[»]
6XAVelectron microscopy7.70I1-1342[»]
6XH7electron microscopy3.90C1-1342[»]
6XH8electron microscopy4.10C1-1342[»]
6XL5electron microscopy2.50C1-1342[»]
6XL9electron microscopy2.50C1-1342[»]
6XLJelectron microscopy2.70C1-1342[»]
6XLLelectron microscopy2.70C1-1342[»]
6XLMelectron microscopy3.20C1-1342[»]
6XLNelectron microscopy2.80C1-1342[»]
6Z9Pelectron microscopy3.90X1-1342[»]
6Z9Qelectron microscopy5.70X1-1342[»]
6Z9Relectron microscopy4.10X1-1342[»]
6Z9Selectron microscopy4.40X1-1342[»]
6Z9Telectron microscopy4.10X1-1342[»]
6ZTLelectron microscopy3.50CC1-1342[»]
7ADBelectron microscopy4.40X1-1342[»]
7ADCelectron microscopy4.00X1-1342[»]
7ADDelectron microscopy4.30X1-1342[»]
7ADEelectron microscopy4.20X1-1342[»]
7C17electron microscopy4.22C1-1342[»]
7C97electron microscopy3.68C1-1342[»]
7CHWelectron microscopy3.58C1-1342[»]
7KHBelectron microscopy3.53C1-1342[»]
7KHCelectron microscopy4.14C1-1342[»]
7KHEelectron microscopy3.58C1-1342[»]
7KHIelectron microscopy3.62C1-1342[»]
7MKNelectron microscopy3.30C3-1342[»]
7MKOelectron microscopy3.15C3-1342[»]
7MKQelectron microscopy4.80C3-1342[»]
SMRiP0A8V2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263472, 52 interactors
852782, 2 interactors
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-35777N
IntActiP0A8V2, 103 interactors
STRINGi511145.b3987

Chemistry databases

BindingDBiP0A8V2
ChEMBLiCHEMBL1852
DrugBankiDB00615, Rifabutin
DB04934, Rifalazil
DB01045, Rifampicin
DB11753, Rifamycin
DB01220, Rifaximin
DrugCentraliP0A8V2

PTM databases

CarbonylDBiP0A8V2
iPTMnetiP0A8V2

2D gel databases

SWISS-2DPAGEiP0A8V2

Proteomic databases

jPOSTiP0A8V2
PaxDbiP0A8V2
PRIDEiP0A8V2

Genome annotation databases

EnsemblBacteriaiAAC76961; AAC76961; b3987
BAE77333; BAE77333; BAE77333
GeneIDi67415312
948488
KEGGiecj:JW3950
eco:b3987
PATRICifig|1411691.4.peg.2725

Organism-specific databases

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

More...EchoBASEi		EB0887

Phylogenomic databases

eggNOGiCOG0085, Bacteria
HOGENOMiCLU_000524_4_3_6
InParanoidiP0A8V2
PhylomeDBiP0A8V2

Enzyme and pathway databases

BioCyciEcoCyc:RPOB-MONOMER
BRENDAi2.7.7.6, 2026

Miscellaneous databases

EvolutionaryTraceiP0A8V2

Protein Ontology

More...PROi		PR:P0A8V2

Family and domain databases

CDDicd00653, RNA_pol_B_RPB2, 1 hit
Gene3Di2.30.150.10, 1 hit
2.40.270.10, 1 hit
2.40.50.150, 1 hit
3.90.1110.10, 1 hit
HAMAPiMF_01321, RNApol_bact_RpoB, 1 hit
InterProiView protein in InterPro
IPR042107, DNA-dir_RNA_pol_bsu_ext_1_sf
IPR019462, DNA-dir_RNA_pol_bsu_external_1
IPR015712, DNA-dir_RNA_pol_su2
IPR007120, DNA-dir_RNAP_su2_dom
IPR037033, DNA-dir_RNAP_su2_hyb_sf
IPR010243, RNA_pol_bsu_bac
IPR007121, RNA_pol_bsu_CS
IPR007644, RNA_pol_bsu_protrusion
IPR007642, RNA_pol_Rpb2_2
IPR037034, RNA_pol_Rpb2_2_sf
IPR007645, RNA_pol_Rpb2_3
IPR007641, RNA_pol_Rpb2_7
IPR014724, RNA_pol_RPB2_OB-fold
PANTHERiPTHR20856, PTHR20856, 1 hit
PfamiView protein in Pfam
PF04563, RNA_pol_Rpb2_1, 1 hit
PF04561, RNA_pol_Rpb2_2, 2 hits
PF04565, RNA_pol_Rpb2_3, 1 hit
PF10385, RNA_pol_Rpb2_45, 1 hit
PF00562, RNA_pol_Rpb2_6, 1 hit
PF04560, RNA_pol_Rpb2_7, 1 hit
TIGRFAMsiTIGR02013, rpoB, 1 hit
PROSITEiView protein in PROSITE
PS01166, RNA_POL_BETA, 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 nameiRPOB_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: P0A8V2
Secondary accession number(s): P00575
, P00576, P78242, Q2M8S3
<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: June 7, 2005
Last modified: February 23, 2022
This is version 159 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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