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Protein

DNA polymerase III subunit beta

Gene

dnaN

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication; once it is clamped onto DNA it slides freely (bidirectional and ATP-independent) along duplex DNA. Coordinates protein traffic at the replication fork, where it interacts with multiple DNA polymerases.2 Publications

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit beta (EC:2.7.7.7)
Alternative name(s):
Beta sliding clamp
Short name:
Beta clamp
Gene namesi
Name:dnaN
Ordered Locus Names:b3701, JW3678
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10242. dnaN.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • DNA polymerase III complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

Chemistry databases

ChEMBLiCHEMBL3562169.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001054341 – 366DNA polymerase III subunit betaAdd BLAST366

Proteomic databases

PaxDbiP0A988.
PRIDEiP0A988.

Expressioni

Inductioni

Induced 1.5-fold by hydroxyurea.1 Publication

Interactioni

Subunit structurei

The DNA polymerase holoenzyme is a complex that contains 10 different types of subunits. These subunits are 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 beta sliding clamp processivity factor (this entry). The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. This complex contains delta, delta', psi and chi, and copies of either or both of two different DnaX proteins, gamma and tau. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta', psi,chi-beta[4]. The beta chain is a homodimer when not associated with the other components. Can also be part of the RIDA complex (regulatory inactivation of DnaA), consisting of ATP-DnaA, ADP-Hda and DNA-loaded beta clamp. Probably also interacts with components of DNA polymerases I, II, IV and V. Binds to CrfC homooligomers at the midcell position during DNA replication.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-542385,EBI-542385
dinBQ471552EBI-542385,EBI-1037359
dnaEP1044317EBI-542385,EBI-549111
dnaQP030076EBI-542385,EBI-549131
dnaXP067104EBI-542385,EBI-549140
hdaP699318EBI-542385,EBI-545453
holAP2863010EBI-542385,EBI-549153
rpeP0AG073EBI-542385,EBI-546020
tnsEP058454EBI-542385,EBI-2434514From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259535. 176 interactors.
DIPiDIP-36038N.
IntActiP0A988. 38 interactors.
STRINGi511145.b3701.

Structurei

Secondary structure

1366
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi7 – 17Combined sources11
Turni18 – 20Combined sources3
Beta strandi26 – 28Combined sources3
Helixi29 – 31Combined sources3
Beta strandi32 – 38Combined sources7
Beta strandi41 – 47Combined sources7
Beta strandi49 – 58Combined sources10
Beta strandi66 – 71Combined sources6
Helixi72 – 81Combined sources10
Beta strandi87 – 93Combined sources7
Beta strandi96 – 101Combined sources6
Beta strandi104 – 109Combined sources6
Helixi113 – 115Combined sources3
Beta strandi126 – 131Combined sources6
Helixi132 – 142Combined sources11
Helixi143 – 145Combined sources3
Helixi153 – 156Combined sources4
Beta strandi157 – 163Combined sources7
Beta strandi166 – 172Combined sources7
Beta strandi174 – 183Combined sources10
Beta strandi190 – 195Combined sources6
Helixi197 – 205Combined sources9
Beta strandi209 – 211Combined sources3
Beta strandi213 – 218Combined sources6
Beta strandi220 – 227Combined sources8
Beta strandi230 – 235Combined sources6
Helixi244 – 246Combined sources3
Beta strandi254 – 259Combined sources6
Helixi260 – 271Combined sources12
Turni276 – 278Combined sources3
Beta strandi280 – 286Combined sources7
Beta strandi289 – 295Combined sources7
Beta strandi301 – 307Combined sources7
Beta strandi309 – 312Combined sources4
Beta strandi315 – 320Combined sources6
Helixi321 – 331Combined sources11
Beta strandi334 – 340Combined sources7
Beta strandi343 – 345Combined sources3
Beta strandi347 – 351Combined sources5
Beta strandi354 – 361Combined sources8

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[»]
ProteinModelPortaliP0A988.
SMRiP0A988.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A988.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 125IAdd BLAST125
Regioni126 – 253IIAdd BLAST128
Regioni254 – 366IIIAdd BLAST113

Phylogenomic databases

eggNOGiENOG4105CZ8. Bacteria.
COG0592. LUCA.
HOGENOMiHOG000071791.
InParanoidiP0A988.
KOiK02338.
OMAiTHQIRLK.
PhylomeDBiP0A988.

Family and domain databases

CDDicd00140. beta_clamp. 1 hit.
InterProiIPR001001. DNA_polIII_beta.
IPR022635. DNA_polIII_beta_C.
IPR022637. DNA_polIII_beta_cen.
IPR022634. DNA_polIII_beta_N.
[Graphical view]
PfamiPF00712. DNA_pol3_beta. 1 hit.
PF02767. DNA_pol3_beta_2. 1 hit.
PF02768. DNA_pol3_beta_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000804. DNA_pol_III_b. 1 hit.
SMARTiSM00480. POL3Bc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00663. dnan. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A988-1 [UniParc]FASTAAdd to basket

« 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
Checksum:i7A45646F61255B5A
GO

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.

Genome annotation databases

EnsemblBacteriaiAAC76724; AAC76724; b3701.
BAE77593; BAE77593; BAE77593.
GeneIDi948218.
KEGGiecj:JW3678.
eco:b3701.
PATRICi32122899. VBIEscCol129921_3825.

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[»]
ProteinModelPortaliP0A988.
SMRiP0A988.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259535. 176 interactors.
DIPiDIP-36038N.
IntActiP0A988. 38 interactors.
STRINGi511145.b3701.

Chemistry databases

ChEMBLiCHEMBL3562169.

Proteomic databases

PaxDbiP0A988.
PRIDEiP0A988.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76724; AAC76724; b3701.
BAE77593; BAE77593; BAE77593.
GeneIDi948218.
KEGGiecj:JW3678.
eco:b3701.
PATRICi32122899. VBIEscCol129921_3825.

Organism-specific databases

EchoBASEiEB0238.
EcoGeneiEG10242. dnaN.

Phylogenomic databases

eggNOGiENOG4105CZ8. Bacteria.
COG0592. LUCA.
HOGENOMiHOG000071791.
InParanoidiP0A988.
KOiK02338.
OMAiTHQIRLK.
PhylomeDBiP0A988.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A988.
PROiP0A988.

Family and domain databases

CDDicd00140. beta_clamp. 1 hit.
InterProiIPR001001. DNA_polIII_beta.
IPR022635. DNA_polIII_beta_C.
IPR022637. DNA_polIII_beta_cen.
IPR022634. DNA_polIII_beta_N.
[Graphical view]
PfamiPF00712. DNA_pol3_beta. 1 hit.
PF02767. DNA_pol3_beta_2. 1 hit.
PF02768. DNA_pol3_beta_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000804. DNA_pol_III_b. 1 hit.
SMARTiSM00480. POL3Bc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00663. dnan. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDPO3B_ECOLI
AccessioniPrimary (citable) accession number: P0A988
Secondary accession number(s): P00583, Q2M813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: November 30, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The temperature- and UV-sensitive allele dnaN159 does not grow at 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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.