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Entry version 125 (10 Apr 2019)
Sequence version 1 (01 Apr 1988)
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Protein

Beta sliding clamp

Gene

dnaN

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

Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA (PubMed:2040637). DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA (PubMed:18191219). In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent (PubMed:26499492). Coordinates protein traffic at the replication fork, where it interacts with multiple DNA polymerases, repair factors and other proteins (PubMed:15466025, PubMed:16168375, PubMed:22716942, PubMed:14592985, PubMed:14729336, PubMed:26499492, PubMed:15952889). Initially characterized for its ability to contact the alpha subunit (dnaE) of DNA polymerase III (Pol III), tethering it to the DNA and conferring very high processivity (PubMed:2040637). Pol III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; it also exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication (PubMed:3519609, PubMed:2040637). A single clamp can bind both Pol III and IV, allowing the repair Pol IV to access DNA when it is damaged and needs to be fixed, a process the replicative polymerase cannot perform; when DNA is repaired Pol III takes over again (PubMed:16168375). Serves as a processivity factor for DNA polymerases II (PubMed:1999435, PubMed:1534562), IV (PubMed:10801133) and V (PubMed:10801133). A shorter protein beta* may be important for increasing survival after UV irradiation, and stimulates DNA synthesis with increased processivity in the presence of core Pol III plus the clamp loader complex (PubMed:8576210, PubMed:8576212).1 Publication14 Publications

Miscellaneous

The temperature- and UV-sensitive allele dnaN159 does not grow at temperatures higher than 37 degrees Celsius. The global SOS response is chronically induced. The UV-sensitivity of dnaN159 is dependent upon Pol IV (dinB), it has an enhanced Pol V-dependent mutation rate (umuC, umuD), and is absolutely dependent on the polymerase activity of Pol I (polA) for viability.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei24DNA1 Publication1
Binding sitei73DNA1 Publication1
Binding sitei149DNA1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi153 – 154DNA1 Publication2

<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

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • DNA strand elongation involved in DNA replication Source: EcoCyc

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase
Biological processDNA replication

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10242-MONOMER
ECOL316407:JW3678-MONOMER
MetaCyc:EG10242-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:
Beta sliding clamp1 Publication
Short name:
Beta clamp
Short name:
Sliding clamp
Alternative name(s):
Beta-clamp processivity factor
DNA polymerase III beta sliding clamp subunit
<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:dnaN
Ordered Locus Names:b3701, JW3678
<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
EG10242 dnaN

<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

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<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

Small molecules can bind to the hydrophobic cleft and inhibit binding of various protein factors, suggesting this may make and attractive antibiotic target (PubMed:18678908).1 Publication

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>Mutagenesisi24R → A: Mild defect in DNA replication, impaired loading of clamp on DNA, polymerase speed is wild-type. More severe replication defect and very poor clamp loading; when associated with A-149. 1 Publication1
Mutagenesisi66G → E in dnaN159; a temperature- and UV-sensitive mutation, displays altered DNA polymerase usage, chronically induced SOS response; when associated with A-174. 1 Publication1
Mutagenesisi133A → T: Reduction of synthesis of beta*, probably due to mutation of its promoter. 1 Publication1
Mutagenesisi135M → L: 3-fold reduction of synthesis of beta*, probably due to loss of its start codon. 1 Publication1
Mutagenesisi146M → L: No effect on synthesis of beta*. 1 Publication1
Mutagenesisi149Q → A: Mild defect in DNA replication, impaired loading of clamp on DNA, polymerase speed is wild-type. More severe replication defect and very poor clamp loading; when associated with A-24. 1 Publication1
Mutagenesisi153 – 154YY → SS: Very poor loading of clamp on DNA, polymerase speed is wild-type. 1 Publication2
Mutagenesisi174G → A in dnaN159; a temperature- and UV-sensitive mutation, displays altered DNA polymerase usage, chronically induced SOS response; when associated with A-66. 1 Publication1
Mutagenesisi272 – 273IL → AA: Monomeric in solution, binds very tightly to subunit delta (holA). The monomer binds tightly to linear and circular DNA. Cannot bind both Pol III and IV simultaneously. 3 Publications2

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3562169

<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_00001054341 – 366Beta sliding clampAdd BLAST366

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0A988

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

More...
PaxDbi
P0A988

PRoteomics IDEntifications database

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PRIDEi
P0A988

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced 1.5-fold by hydroxyurea (PubMed:20005847). A shorter isoform, beta* is induced by UV treatment and also at low levels in late logarithmic/early stationary phase growth (at protein level) (PubMed:8576210). Beta* transcription induced by naldixic acid (PubMed:8576211).3 Publications

<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

Forms a ring-shaped head-to-tail homodimer (PubMed:2040637, PubMed:9927437, PubMed:1349852, PubMed:12832762, PubMed:14592985, PubMed:14729336, PubMed:18191219, PubMed:18678908) around DNA (PubMed:18191219), which can be opened by the delta subunit (PubMed:9927437, PubMed:11525728). Binds interacting factors in a hydrophobic surface cleft between domains 2 and 3, each monomer is able to bind different proteins simultaneously (PubMed:16168375, PubMed:11525728, PubMed:14592985, PubMed:14729336, PubMed:26499492). The beta* isoform probably forms homotrimers which probably load onto DNA (PubMed:8576212). The DNA polymerase III holoenzyme complex contains at least 10 different subunits organized into 3 functionally essential subassemblies: the Pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The Pol III core (subunits alpha, epsilon and theta) contains the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the dimeric beta sliding clamp processivity factor (this entry) (PubMed:15466025). The clamp loader (also called gamma complex) assembles the beta sliding clamp onto the primed template and plays a central role in the organization and communication at the replication fork. The clamp loader contains delta, delta', psi and chi, and 3 copies of either or both of two different DnaX proteins, gamma and tau. The DNA replisome complex has a single clamp loader (3 tau and 1 each of delta, delta', psi and chi subunits) which binds 3 Pol III cores (1 core on the leading strand and 2 on the lagging strand) each with a beta sliding clamp dimer. Additional proteins in the replisome are other copies of gamma, psi and chi, Ssb, DNA helicase and RNA primase (PubMed:20413500, PubMed:22157955, PubMed:26499492). The beta sliding clamp can also be part of the RIDA complex (regulatory inactivation of DnaA), consisting of ATP-DnaA, ADP-Hda and DNA-loaded beta clamp (PubMed:15150238, PubMed:18977760, PubMed:22716942). Also interacts with a number of other DNA machines such as DNA polymerases I (PubMed:11459978), II (PubMed:1999435, PubMed:1534562), IV (PubMed:14729336) and V, DNA mismatch repair enzyme MutS (PubMed:11459978, PubMed:11573000) and DNA ligase (PubMed:11459978). Binds to CrfC homooligomers at the midcell position during DNA replication (PubMed:23994470). Many proteins that bind the beta sliding clamp have the consensus sequence Gln-Leu[Ser/Asp]Leu-Phe (PubMed:15134440).24 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
4259535, 183 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1927 DNA polymerase III, beta sliding clamp processivity factor complex
CPX-1954 Hda-beta clamp complex

Database of interacting proteins

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DIPi
DIP-36038N

Protein interaction database and analysis system

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IntActi
P0A988, 39 interactors

Molecular INTeraction database

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MINTi
P0A988

STRING: functional protein association networks

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STRINGi
511145.b3701

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0A988

<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

1366
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQJX-ray2.90A/B1-366[»]
1JQLX-ray2.50A1-366[»]
1MMIX-ray1.85A/B1-366[»]
1OK7X-ray1.65A/B1-366[»]
1UNNX-ray1.90A/B1-366[»]
1WAImodel-A/B1-366[»]
2POLX-ray2.50A/B1-366[»]
2XURX-ray1.90A/B1-366[»]
3BEPX-ray1.92A/B1-366[»]
3D1EX-ray1.90A/B1-366[»]
3D1FX-ray2.00A/B1-366[»]
3D1GX-ray1.64A/B1-366[»]
3F1VX-ray1.77A/B1-366[»]
3PWEX-ray2.20A/B1-366[»]
3Q4JX-ray2.30A/B/C/D/E/F1-366[»]
3Q4KX-ray2.60A/B1-366[»]
3Q4LX-ray1.95A/B1-366[»]
3QSBX-ray1.90A/B1-366[»]
4K3KX-ray1.85A/B1-366[»]
4K3LX-ray1.50A/B1-366[»]
4K3MX-ray1.85A/B1-366[»]
4K3OX-ray2.00A/B1-366[»]
4K3PX-ray2.15A/B1-366[»]
4K3QX-ray1.85A/B1-366[»]
4K3RX-ray1.86A/B1-366[»]
4K3SX-ray1.75A/B1-366[»]
4MJPX-ray1.86A/B1-366[»]
4MJQX-ray1.73A/B1-366[»]
4MJRX-ray1.62A/B1-366[»]
4N94X-ray1.73A/B1-366[»]
4N95X-ray1.80A/B1-366[»]
4N96X-ray1.70A/B1-366[»]
4N97X-ray1.97A/B1-366[»]
4N98X-ray1.70A/B1-366[»]
4N99X-ray2.30A/B1-366[»]
4N9AX-ray1.90A/B1-366[»]
5FKUelectron microscopy8.34B/C1-366[»]
5FKVelectron microscopy8.00B/C1-366[»]
5FKWelectron microscopy7.30B/C1-366[»]
5M1Selectron microscopy6.70B/C1-366[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0A988

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

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SMRi
P0A988

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A988

<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 – 1201CuratedAdd BLAST120
Regioni129 – 2432CuratedAdd BLAST115
Regioni245 – 3653CuratedAdd BLAST121

<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 beta sliding clamp family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG4105CZ8 Bacteria
COG0592 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000071791

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0A988

KEGG Orthology (KO)

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KOi
K02338

Database for complete collections of gene phylogenies

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PhylomeDBi
P0A988

Family and domain databases

Conserved Domains Database

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CDDi
cd00140 beta_clamp, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001001 DNA_polIII_beta
IPR022635 DNA_polIII_beta_C
IPR022637 DNA_polIII_beta_cen
IPR022634 DNA_polIII_beta_N

The PANTHER Classification System

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PANTHERi
PTHR30478 PTHR30478, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00712 DNA_pol3_beta, 1 hit
PF02767 DNA_pol3_beta_2, 1 hit
PF02768 DNA_pol3_beta_3, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000804 DNA_pol_III_b, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00480 POL3Bc, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00663 dnan, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage. AlignAdd to basket
Isoform Beta1 Publication (identifier: P0A988-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MKFTVEREHL LKPLQQVSGP LGGRPTLPIL GNLLLQVADG TLSLTGTDLE
60 70 80 90 100
MEMVARVALV QPHEPGATTV PARKFFDICR GLPEGAEIAV QLEGERMLVR
110 120 130 140 150
SGRSRFSLST LPAADFPNLD DWQSEVEFTL PQATMKRLIE ATQFSMAHQD
160 170 180 190 200
VRYYLNGMLF ETEGEELRTV ATDGHRLAVC SMPIGQSLPS HSVIVPRKGV
210 220 230 240 250
IELMRMLDGG DNPLRVQIGS NNIRAHVGDF IFTSKLVDGR FPDYRRVLPK
260 270 280 290 300
NPDKHLEAGC DLLKQAFARA AILSNEKFRG VRLYVSENQL KITANNPEQE
310 320 330 340 350
EAEEILDVTY SGAEMEIGFN VSYVLDVLNA LKCENVRMML TDSVSSVQIE
360
DAASQSAAYV VMPMRL
Length:366
Mass (Da):40,587
Last modified:April 1, 1988 - 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:i7A45646F61255B5A
GO
Isoform Beta*1 Publication (identifier: P0A988-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-134: Missing.

Note: Beta* protein is expressed in late logarithmic/early stationary phase and induced by UV treatment (PubMed:8576210). Mutations in the Shine-Dalgarno region of beta* (some silent at the amino acid level) decrease production of beta* (PubMed:8576211).2 Publications
Show »
Length:232
Mass (Da):25,968
Checksum:iD70A75A4CC15CB43
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0590301 – 134Missing in isoform Beta*. 1 PublicationAdd BLAST134

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J01602 Genomic DNA Translation: AAB59150.1
L10328 Genomic DNA Translation: AAA62052.1
U00096 Genomic DNA Translation: AAC76724.1
AP009048 Genomic DNA Translation: BAE77593.1
M19876 Genomic DNA Translation: AAA23695.1
M13822 Genomic DNA Translation: AAA24512.1
K02179 Genomic DNA Translation: AAA24510.1
X04341 Genomic DNA Translation: CAA27869.1

Protein sequence database of the Protein Information Resource

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PIRi
A91510 DJEC3B

NCBI Reference Sequences

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RefSeqi
NP_418156.1, NC_000913.3
WP_000673464.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAC76724; AAC76724; b3701
BAE77593; BAE77593; BAE77593

Database of genes from NCBI RefSeq genomes

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GeneIDi
948218

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ecj:JW3678
eco:b3701

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|1411691.4.peg.3002

Keywords - Coding sequence diversityi

Alternative promoter usage

<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
J01602 Genomic DNA Translation: AAB59150.1
L10328 Genomic DNA Translation: AAA62052.1
U00096 Genomic DNA Translation: AAC76724.1
AP009048 Genomic DNA Translation: BAE77593.1
M19876 Genomic DNA Translation: AAA23695.1
M13822 Genomic DNA Translation: AAA24512.1
K02179 Genomic DNA Translation: AAA24510.1
X04341 Genomic DNA Translation: CAA27869.1
PIRiA91510 DJEC3B
RefSeqiNP_418156.1, NC_000913.3
WP_000673464.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQJX-ray2.90A/B1-366[»]
1JQLX-ray2.50A1-366[»]
1MMIX-ray1.85A/B1-366[»]
1OK7X-ray1.65A/B1-366[»]
1UNNX-ray1.90A/B1-366[»]
1WAImodel-A/B1-366[»]
2POLX-ray2.50A/B1-366[»]
2XURX-ray1.90A/B1-366[»]
3BEPX-ray1.92A/B1-366[»]
3D1EX-ray1.90A/B1-366[»]
3D1FX-ray2.00A/B1-366[»]
3D1GX-ray1.64A/B1-366[»]
3F1VX-ray1.77A/B1-366[»]
3PWEX-ray2.20A/B1-366[»]
3Q4JX-ray2.30A/B/C/D/E/F1-366[»]
3Q4KX-ray2.60A/B1-366[»]
3Q4LX-ray1.95A/B1-366[»]
3QSBX-ray1.90A/B1-366[»]
4K3KX-ray1.85A/B1-366[»]
4K3LX-ray1.50A/B1-366[»]
4K3MX-ray1.85A/B1-366[»]
4K3OX-ray2.00A/B1-366[»]
4K3PX-ray2.15A/B1-366[»]
4K3QX-ray1.85A/B1-366[»]
4K3RX-ray1.86A/B1-366[»]
4K3SX-ray1.75A/B1-366[»]
4MJPX-ray1.86A/B1-366[»]
4MJQX-ray1.73A/B1-366[»]
4MJRX-ray1.62A/B1-366[»]
4N94X-ray1.73A/B1-366[»]
4N95X-ray1.80A/B1-366[»]
4N96X-ray1.70A/B1-366[»]
4N97X-ray1.97A/B1-366[»]
4N98X-ray1.70A/B1-366[»]
4N99X-ray2.30A/B1-366[»]
4N9AX-ray1.90A/B1-366[»]
5FKUelectron microscopy8.34B/C1-366[»]
5FKVelectron microscopy8.00B/C1-366[»]
5FKWelectron microscopy7.30B/C1-366[»]
5M1Selectron microscopy6.70B/C1-366[»]
ProteinModelPortaliP0A988
SMRiP0A988
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259535, 183 interactors
ComplexPortaliCPX-1927 DNA polymerase III, beta sliding clamp processivity factor complex
CPX-1954 Hda-beta clamp complex
DIPiDIP-36038N
IntActiP0A988, 39 interactors
MINTiP0A988
STRINGi511145.b3701

Chemistry databases

BindingDBiP0A988
ChEMBLiCHEMBL3562169

Proteomic databases

jPOSTiP0A988
PaxDbiP0A988
PRIDEiP0A988

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76724; AAC76724; b3701
BAE77593; BAE77593; BAE77593
GeneIDi948218
KEGGiecj:JW3678
eco:b3701
PATRICifig|1411691.4.peg.3002

Organism-specific databases

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

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EchoBASEi
EB0238
EcoGeneiEG10242 dnaN

Phylogenomic databases

eggNOGiENOG4105CZ8 Bacteria
COG0592 LUCA
HOGENOMiHOG000071791
InParanoidiP0A988
KOiK02338
PhylomeDBiP0A988

Enzyme and pathway databases

BioCyciEcoCyc:EG10242-MONOMER
ECOL316407:JW3678-MONOMER
MetaCyc:EG10242-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A988

Protein Ontology

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PROi
PR:P0A988

Family and domain databases

CDDicd00140 beta_clamp, 1 hit
InterProiView protein in InterPro
IPR001001 DNA_polIII_beta
IPR022635 DNA_polIII_beta_C
IPR022637 DNA_polIII_beta_cen
IPR022634 DNA_polIII_beta_N
PANTHERiPTHR30478 PTHR30478, 1 hit
PfamiView protein in Pfam
PF00712 DNA_pol3_beta, 1 hit
PF02767 DNA_pol3_beta_2, 1 hit
PF02768 DNA_pol3_beta_3, 1 hit
PIRSFiPIRSF000804 DNA_pol_III_b, 1 hit
SMARTiView protein in SMART
SM00480 POL3Bc, 1 hit
TIGRFAMsiTIGR00663 dnan, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiDPO3B_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: P0A988
Secondary accession number(s): P00583, Q2M813
<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: April 1, 1988
Last modified: April 10, 2019
This is version 125 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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