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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.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

GO - Biological processi

<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
MetaCyc:EG10893-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10893 rpoA

<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

GO - Cellular componenti

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_and_biotech_section">'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

Drug and drug target database

More...
DrugBanki
DB00615 Rifabutin

<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.<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 residuei297N6-acetyllysine1 Publication1
Modified residuei298N6-acetyllysine; by Pka1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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. Pka controls acetylation of Lys-298 but not of Lys-297.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
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_section">'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_section">'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.4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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

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
316385.ECDH10B_3470

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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0A7Z4

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

More...
SMRi
P0A7Z4

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000218481

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A7Z4

KEGG Orthology (KO)

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KOi
K03040

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

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD001179 RNAP_asu_C, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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

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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_LN832404.1

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
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_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
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[»]
ProteinModelPortaliP0A7Z4
SMRiP0A7Z4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263398, 114 interactors
852106, 1 interactor
DIPiDIP-35879N
IntActiP0A7Z4, 91 interactors
MINTiP0A7Z4
STRINGi316385.ECDH10B_3470

Chemistry databases

BindingDBiP0A7Z4
ChEMBLiCHEMBL2364672
DrugBankiDB00615 Rifabutin

PTM databases

iPTMnetiP0A7Z4

2D gel databases

SWISS-2DPAGEiP0A7Z4

Proteomic databases

EPDiP0A7Z4
PaxDbiP0A7Z4
PRIDEiP0A7Z4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76320; AAC76320; b3295
BAE77996; BAE77996; BAE77996
GeneIDi947794
KEGGiecj:JW3257
eco:b3295
PATRICifig|1411691.4.peg.3436

Organism-specific databases

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

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EchoBASEi
EB0886
EcoGeneiEG10893 rpoA

Phylogenomic databases

eggNOGiCOG0202 LUCA
HOGENOMiHOG000218481
InParanoidiP0A7Z4
KOiK03040
PhylomeDBiP0A7Z4

Enzyme and pathway databases

BioCyciEcoCyc:EG10893-MONOMER
MetaCyc:EG10893-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7Z4

Protein Ontology

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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
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001179 RNAP_asu_C, 1 hit
SMARTiView protein in SMART
SM00662 RPOLD, 1 hit
SUPFAMiSSF55257 SSF55257, 1 hit
SSF56553 SSF56553, 1 hit
TIGRFAMsiTIGR02027 rpoA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry 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_and_isoforms">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: December 5, 2018
This is version 136 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, Complete proteome, 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
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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