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UniProtKB - P0A8T7 (RPOC_ECOLI)

Entry version 157 (23 Feb 2022)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
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Protein

DNA-directed RNA polymerase subunit beta'

Gene

rpoC

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.

UniRule annotation2 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>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi70Zinc 1Combined sources1 Publication1
Metal bindingi72Zinc 1Combined sources1 Publication1
Metal bindingi85Zinc 1Combined sources1 Publication1
Metal bindingi88Zinc 1Combined sources1 Publication1
Metal bindingi460MagnesiumCombined sources1 Publication1
Metal bindingi462MagnesiumCombined sources1 Publication1
Metal bindingi464MagnesiumCombined sources1 Publication1
Metal bindingi814Zinc 2Combined sources1 Publication1
Metal bindingi888Zinc 2Combined sources1 Publication1
Metal bindingi895Zinc 2Combined sources1 Publication1
Metal bindingi898Zinc 2Combined sources1 Publication1

<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
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:RPOC-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'UniRule annotation (EC:2.7.7.6UniRule annotation)
Short name:
RNAP subunit beta'UniRule annotation
Alternative name(s):
RNA polymerase subunit beta'UniRule annotation
Transcriptase subunit beta'UniRule 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:rpoCUniRule annotation
Synonyms:tabB
Ordered Locus Names:b3988, JW3951
<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>Mutagenesisi504Q → P: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi690N → D: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi697M → V: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi735A → T: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi738R → C, H, P or S: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi748A → E: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi758P → S or T: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi763F → C: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi775S → A: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi779A → T or V: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi780R → C: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi782G → A or C: Resistant to antibiotics salinamide A and B. 1 Publication1
Mutagenesisi783L → R: Resistant to antibiotics salinamide A and B. 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		P0A8T7

<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_00000677411 – 1407DNA-directed RNA polymerase subunit beta'Add BLAST1407

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 residuei983N6-acetyllysineUniRule annotation1 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		P0A8T7

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

More...PaxDbi		P0A8T7

PRoteomics IDEntifications database

More...PRIDEi		P0A8T7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0A8T7

<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).

UniRule annotation4 Publications

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

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4262959, 70 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-35803N

Protein interaction database and analysis system

More...IntActi		P0A8T7, 117 interactors

Molecular INTeraction database

More...MINTi		P0A8T7

STRING: functional protein association networks

More...STRINGi		511145.b3988

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0A8T7

<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

11407
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		P0A8T7

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		P0A8T7

<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.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0086, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000524_3_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A8T7

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A8T7

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.132.30, 1 hit
1.10.274.100, 1 hit
4.10.860.120, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01322, RNApol_bact_RpoC, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR045867, DNA-dir_RpoC_beta_prime
IPR012754, DNA-dir_RpoC_beta_prime_bact
IPR000722, RNA_pol_asu
IPR006592, RNA_pol_N
IPR007080, RNA_pol_Rpb1_1
IPR007066, RNA_pol_Rpb1_3
IPR042102, RNA_pol_Rpb1_3_sf
IPR007083, RNA_pol_Rpb1_4
IPR007081, RNA_pol_Rpb1_5
IPR044893, RNA_pol_Rpb1_clamp_domain
IPR038120, Rpb1_funnel_sf

The PANTHER Classification System

More...PANTHERi		PTHR19376, PTHR19376, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04997, RNA_pol_Rpb1_1, 1 hit
PF00623, RNA_pol_Rpb1_2, 2 hits
PF04983, RNA_pol_Rpb1_3, 1 hit
PF05000, RNA_pol_Rpb1_4, 1 hit
PF04998, RNA_pol_Rpb1_5, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00663, RPOLA_N, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02386, rpoC_TIGR, 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.

P0A8T7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKDLLKFLKA QTKTEEFDAI KIALASPDMI RSWSFGEVKK PETINYRTFK 
        60         70         80         90        100
PERDGLFCAR IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE 
       110        120        130        140        150
RMGHIELASP TAHIWFLKSL PSRIGLLLDM PLRDIERVLY FESYVVIEGG 
       160        170        180        190        200
MTNLERQQIL TEEQYLDALE EFGDEFDAKM GAEAIQALLK SMDLEQECEQ 
       210        220        230        240        250
LREELNETNS ETKRKKLTKR IKLLEAFVQS GNKPEWMILT VLPVLPPDLR 
       260        270        280        290        300
PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLAAPDI IVRNEKRMLQ 
       310        320        330        340        350
EAVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS 
       360        370        380        390        400
GRSVITVGPY LRLHQCGLPK KMALELFKPF IYGKLELRGL ATTIKAAKKM 
       410        420        430        440        450
VEREEAVVWD ILDEVIREHP VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH 
       460        470        480        490        500
PLVCAAYNAD FDGDQMAVHV PLTLEAQLEA RALMMSTNNI LSPANGEPII 
       510        520        530        540        550
VPSQDVVLGL YYMTRDCVNA KGEGMVLTGP KEAERLYRSG LASLHARVKV 
       560        570        580        590        600
RITEYEKDAN GELVAKTSLK DTTVGRAILW MIVPKGLPYS IVNQALGKKA 
       610        620        630        640        650
ISKMLNTCYR ILGLKPTVIF ADQIMYTGFA YAARSGASVG IDDMVIPEKK 
       660        670        680        690        700
HEIISEAEAE VAEIQEQFQS GLVTAGERYN KVIDIWAAAN DRVSKAMMDN 
       710        720        730        740        750
LQTETVINRD GQEEKQVSFN SIYMMADSGA RGSAAQIRQL AGMRGLMAKP 
       760        770        780        790        800
DGSIIETPIT ANFREGLNVL QYFISTHGAR KGLADTALKT ANSGYLTRRL 
       810        820        830        840        850
VDVAQDLVVT EDDCGTHEGI MMTPVIEGGD VKEPLRDRVL GRVTAEDVLK 
       860        870        880        890        900
PGTADILVPR NTLLHEQWCD LLEENSVDAV KVRSVVSCDT DFGVCAHCYG 
       910        920        930        940        950
RDLARGHIIN KGEAIGVIAA QSIGEPGTQL TMRTFHIGGA ASRAAAESSI 
       960        970        980        990       1000
QVKNKGSIKL SNVKSVVNSS GKLVITSRNT ELKLIDEFGR TKESYKVPYG 
      1010       1020       1030       1040       1050
AVLAKGDGEQ VAGGETVANW DPHTMPVITE VSGFVRFTDM IDGQTITRQT 
      1060       1070       1080       1090       1100
DELTGLSSLV VLDSAERTAG GKDLRPALKI VDAQGNDVLI PGTDMPAQYF 
      1110       1120       1130       1140       1150
LPGKAIVQLE DGVQISSGDT LARIPQESGG TKDITGGLPR VADLFEARRP 
      1160       1170       1180       1190       1200
KEPAILAEIS GIVSFGKETK GKRRLVITPV DGSDPYEEMI PKWRQLNVFE 
      1210       1220       1230       1240       1250
GERVERGDVI SDGPEAPHDI LRLRGVHAVT RYIVNEVQDV YRLQGVKIND 
      1260       1270       1280       1290       1300
KHIEVIVRQM LRKATIVNAG SSDFLEGEQV EYSRVKIANR ELEANGKVGA 
      1310       1320       1330       1340       1350
TYSRDLLGIT KASLATESFI SAASFQETTR VLTEAAVAGK RDELRGLKEN 
      1360       1370       1380       1390       1400
VIVGRLIPAG TGYAYHQDRM RRRAAGEAPA APQVTAEDAS ASLAELLNAG 

LGGSDNE
Length:1,407
Mass (Da):155,160
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:iA6878C61D15F4961
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 conflicti1133 – 1177DITGG…RRLVI → ASPVVCRALRTCSKHVVRKS RQSWLKSAVSFPSVKKPKVN VVWLS no nucleotide entry (PubMed:6278450).CuratedAdd BLAST45

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: CAA23626.1
U00006 Genomic DNA Translation: AAC43086.1
U00096 Genomic DNA Translation: AAC76962.1
AP009048 Genomic DNA Translation: BAE77332.1
M38293 Genomic DNA Translation: AAA24582.1
M38303 Genomic DNA Translation: AAA24584.1
V00340 Genomic DNA Translation: CAA23628.1
M38305 Genomic DNA Translation: AAA24586.1
M38288 Genomic DNA Translation: AAA24408.1

Protein sequence database of the Protein Information Resource

More...PIRi		A00695, RNECC

NCBI Reference Sequences

More...RefSeqi		NP_418415.1, NC_000913.3
WP_000653944.1, NZ_STEB01000045.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76962; AAC76962; b3988
BAE77332; BAE77332; BAE77332

Database of genes from NCBI RefSeq genomes

More...GeneIDi		66672101
948487

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3951
eco:b3988

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2724

<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: CAA23626.1
U00006 Genomic DNA Translation: AAC43086.1
U00096 Genomic DNA Translation: AAC76962.1
AP009048 Genomic DNA Translation: BAE77332.1
M38293 Genomic DNA Translation: AAA24582.1
M38303 Genomic DNA Translation: AAA24584.1
V00340 Genomic DNA Translation: CAA23628.1
M38305 Genomic DNA Translation: AAA24586.1
M38288 Genomic DNA Translation: AAA24408.1
PIRiA00695, RNECC
RefSeqiNP_418415.1, NC_000913.3
WP_000653944.1, 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
2AUKX-ray2.30A/B/C/D/E944-1129[»]
2LMCNMR-B1151-1213[»]
3IYDelectron microscopy-D1-1407[»]
3LU0electron microscopy-D1-1407[»]
4IQZX-ray2.10A/B/C/D/E932-1141[»]
4JK1X-ray3.90D/I1-1407[»]
4JK2X-ray4.20D/I1-1407[»]
4KMUX-ray3.85D/I1-1407[»]
4KN4X-ray3.96D/I1-1407[»]
4KN7X-ray3.69D/I1-1407[»]
4MEXX-ray3.90D/J1-1407[»]
4MEYX-ray3.95D/J1-1407[»]
4XSXX-ray3.71D/J1-1407[»]
4XSYX-ray4.01D/J1-1407[»]
4XSZX-ray3.68D/J1-1407[»]
4YG2X-ray3.70D/J1-1407[»]
4YLNX-ray5.50D/J/P1-1407[»]
4YLOX-ray6.00D/J/P1-1407[»]
4YLPX-ray5.50D/J/P1-1407[»]
4ZH2X-ray4.20D/J1-1407[»]
4ZH3X-ray4.08D/J1-1407[»]
4ZH4X-ray3.99D/J1-1407[»]
5BYHX-ray3.76D1-1407[»]
5EZKX-ray8.50D1-1407[»]
5IPLX-ray3.60D1-1407[»]
5IPMX-ray4.20D1-1407[»]
5IPNX-ray4.61D1-1407[»]
5MS0electron microscopy9.80D1-1407[»]
5MY1electron microscopy7.60Y1-1407[»]
5NSRelectron microscopy3.80D1-1407[»]
5NSSelectron microscopy5.80D1-1407[»]
5NWTX-ray3.76D1-1407[»]
5UACX-ray3.80D/J1-1407[»]
5UAGX-ray3.40D/J1-1407[»]
5UAHX-ray4.10D/J1-1407[»]
5UAJX-ray3.92D/J1-1407[»]
5UALX-ray3.89D/J1-1407[»]
5UAQX-ray3.60D/J1-1407[»]
5VSWX-ray4.29D/J1-1407[»]
5VT0electron microscopy3.78J1-1407[»]
5W1SX-ray3.81D/J1-1407[»]
5W1TX-ray4.50D/J1-1407[»]
6ALFelectron microscopy4.10J1-1407[»]
6ALGelectron microscopy3.70J1-1407[»]
6ALHelectron microscopy4.40J1-1407[»]
6ASXelectron microscopy3.80J1-1407[»]
6BJSelectron microscopy5.50J1-1407[»]
6BYUX-ray3.60D/J1-1407[»]
6C6Selectron microscopy3.70J1-1407[»]
6C6Telectron microscopy3.50J1-1407[»]
6C6Uelectron microscopy3.70J1-1407[»]
6C9Yelectron microscopy4.25D1-1407[»]
6CA0electron microscopy5.75D1-1407[»]
6CUXX-ray4.10D/J1-1407[»]
6FLPelectron microscopy4.10D1-1407[»]
6FLQelectron microscopy4.10D1-1407[»]
6GFWelectron microscopy3.70D1-1407[»]
6GH5electron microscopy3.40D1-1407[»]
6GH6electron microscopy4.10D1-1407[»]
6JBQelectron microscopy4.02D1-1407[»]
6JNXelectron microscopy4.08D1-1407[»]
6K4Yelectron microscopy3.79D1-1407[»]
6KJ6electron microscopy3.80D1-1407[»]
6LDIelectron microscopy3.69D1-1407[»]
6N4Celectron microscopy17.00D15-1376[»]
6N57electron microscopy3.70J2-1407[»]
6N58electron microscopy3.78J2-1407[»]
6N60X-ray3.68D2-1407[»]
6N61X-ray3.25D2-1407[»]
6OMFelectron microscopy3.26D1-1407[»]
6P18electron microscopy3.50D1-1407[»]
6P19electron microscopy3.80D1-1407[»]
6P1Kelectron microscopy4.05J2-1407[»]
6PSQelectron microscopy3.40J2-1407[»]
6PSRelectron microscopy3.40J2-1407[»]
6PSSelectron microscopy3.50J2-1407[»]
6PSTelectron microscopy3.00J2-1407[»]
6PSUelectron microscopy3.90J2-1407[»]
6PSVelectron microscopy3.50J2-1407[»]
6PSWelectron microscopy3.70J2-1407[»]
6R9Belectron microscopy3.80D1-1407[»]
6R9Gelectron microscopy3.70D1-1407[»]
6RH3electron microscopy3.60D1-1407[»]
6RI7electron microscopy3.90D1-1407[»]
6RI9electron microscopy3.70D1-1407[»]
6RINelectron microscopy3.70D1-1407[»]
6RIPelectron microscopy3.40D1-1407[»]
6TQNelectron microscopy3.80Y1-1407[»]
6TQOelectron microscopy4.00Y1-1407[»]
6UTVX-ray3.45DDD1-1407[»]
6UTWX-ray3.85DDD1-1407[»]
6UTXX-ray4.05DDD1-1407[»]
6UTYX-ray4.15DDD1-1407[»]
6UTZX-ray3.80DDD1-1407[»]
6UU0X-ray3.90DDD1-1407[»]
6UU1X-ray4.10DDD1-1407[»]
6UU2X-ray4.40DDD1-1407[»]
6UU3X-ray4.00DDD1-1407[»]
6UU4X-ray4.30DDD1-1407[»]
6UU5X-ray5.40DDD1-1407[»]
6UU6X-ray4.20DDD1-1407[»]
6UU7X-ray4.40DDD1-1407[»]
6UU8X-ray4.40DDD1-1407[»]
6UU9X-ray5.40DDD1-1407[»]
6UUAX-ray4.00DDD1-1407[»]
6UUBX-ray3.96DDD1-1407[»]
6UUCX-ray4.10DDD1-1407[»]
6VJSX-ray4.02D/I1-1407[»]
6WMUelectron microscopy3.18D1-1407[»]
6XASelectron microscopy3.80J2-1407[»]
6XAVelectron microscopy7.70J2-1407[»]
6XH7electron microscopy3.90D1-1407[»]
6XH8electron microscopy4.10D1-1407[»]
6XL5electron microscopy2.50D1-1407[»]
6XL9electron microscopy2.50D1-1407[»]
6XLJelectron microscopy2.70D1-1407[»]
6XLLelectron microscopy2.70D1-1407[»]
6XLMelectron microscopy3.20D1-1407[»]
6XLNelectron microscopy2.80D1-1407[»]
7C17electron microscopy4.22D1-1407[»]
7C97electron microscopy3.68D1-1407[»]
7CHWelectron microscopy3.58D1-1407[»]
7KHBelectron microscopy3.53D1-1407[»]
7KHCelectron microscopy4.14D1-1407[»]
7KHEelectron microscopy3.58D1-1407[»]
7KHIelectron microscopy3.62D1-1407[»]
7MKNelectron microscopy3.30D14-1376[»]
7MKOelectron microscopy3.15D14-1376[»]
7MKQelectron microscopy4.80D14-1376[»]
SMRiP0A8T7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262959, 70 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-35803N
IntActiP0A8T7, 117 interactors
MINTiP0A8T7
STRINGi511145.b3988

Chemistry databases

BindingDBiP0A8T7
ChEMBLiCHEMBL2364672
CHEMBL4296169
DrugBankiDB00615, Rifabutin
DB11753, Rifamycin
DrugCentraliP0A8T7

PTM databases

iPTMnetiP0A8T7

Proteomic databases

jPOSTiP0A8T7
PaxDbiP0A8T7
PRIDEiP0A8T7

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P0A8T7, 1 sequenced antibody

Genome annotation databases

EnsemblBacteriaiAAC76962; AAC76962; b3988
BAE77332; BAE77332; BAE77332
GeneIDi66672101
948487
KEGGiecj:JW3951
eco:b3988
PATRICifig|1411691.4.peg.2724

Organism-specific databases

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

More...EchoBASEi		EB0888

Phylogenomic databases

eggNOGiCOG0086, Bacteria
HOGENOMiCLU_000524_3_1_6
InParanoidiP0A8T7
PhylomeDBiP0A8T7

Enzyme and pathway databases

BioCyciEcoCyc:RPOC-MONOMER
BRENDAi2.7.7.6, 2026

Miscellaneous databases

EvolutionaryTraceiP0A8T7

Protein Ontology

More...PROi		PR:P0A8T7

Family and domain databases

Gene3Di1.10.132.30, 1 hit
1.10.274.100, 1 hit
4.10.860.120, 1 hit
HAMAPiMF_01322, RNApol_bact_RpoC, 1 hit
InterProiView protein in InterPro
IPR045867, DNA-dir_RpoC_beta_prime
IPR012754, DNA-dir_RpoC_beta_prime_bact
IPR000722, RNA_pol_asu
IPR006592, RNA_pol_N
IPR007080, RNA_pol_Rpb1_1
IPR007066, RNA_pol_Rpb1_3
IPR042102, RNA_pol_Rpb1_3_sf
IPR007083, RNA_pol_Rpb1_4
IPR007081, RNA_pol_Rpb1_5
IPR044893, RNA_pol_Rpb1_clamp_domain
IPR038120, Rpb1_funnel_sf
PANTHERiPTHR19376, PTHR19376, 1 hit
PfamiView protein in Pfam
PF04997, RNA_pol_Rpb1_1, 1 hit
PF00623, RNA_pol_Rpb1_2, 2 hits
PF04983, RNA_pol_Rpb1_3, 1 hit
PF05000, RNA_pol_Rpb1_4, 1 hit
PF04998, RNA_pol_Rpb1_5, 1 hit
SMARTiView protein in SMART
SM00663, RPOLA_N, 1 hit
TIGRFAMsiTIGR02386, rpoC_TIGR, 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 nameiRPOC_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: P0A8T7
Secondary accession number(s): P00577
, P00578, P78134, Q2M8S4
<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 157 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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