Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P0A988 (DPO3B_ECOLI)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA polymerase III subunit beta
    EC=2.7.7.7
Gene names
Name: dnaN
Ordered Locus Names: b3701, JW3678
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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 sliding clamp processivity factor. 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.

Subcellular location

Cytoplasm.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentCytoplasm
   Molecular functionDNA-directed DNA polymerase
Nucleotidyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: UniProtKB

   Molecular function3'-5' exonuclease activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366DNA polymerase III subunit beta
PRO_0000105434

Regions

Region1 – 125125I
Region126 – 253128II
Region254 – 366113III

Secondary structure

................................................................ 366
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A988-1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 7A45646F61255B5A

FASTA36640,587
        10         20         30         40         50         60 
MKFTVEREHL LKPLQQVSGP LGGRPTLPIL GNLLLQVADG TLSLTGTDLE MEMVARVALV 

        70         80         90        100        110        120 
QPHEPGATTV PARKFFDICR GLPEGAEIAV QLEGERMLVR SGRSRFSLST LPAADFPNLD 

       130        140        150        160        170        180 
DWQSEVEFTL PQATMKRLIE ATQFSMAHQD VRYYLNGMLF ETEGEELRTV ATDGHRLAVC 

       190        200        210        220        230        240 
SMPIGQSLPS HSVIVPRKGV IELMRMLDGG DNPLRVQIGS NNIRAHVGDF IFTSKLVDGR 

       250        260        270        280        290        300 
FPDYRRVLPK NPDKHLEAGC DLLKQAFARA AILSNEKFRG VRLYVSENQL KITANNPEQE 

       310        320        330        340        350        360 
EAEEILDVTY SGAEMEIGFN VSYVLDVLNA LKCENVRMML TDSVSSVQIE DAASQSAAYV 


VMPMRL 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of the dnaA and dnaN genes of Escherichia coli."
Ohmori H., Kimura M., Nagata T., Sakakibara Y.
Gene 28:159-170(1984) [PubMed: 6234204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed: 7686882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Transcriptional organization of the dnaN and recF genes of Escherichia coli K-12."
Armengod M.E.E., Garcca-Sogo M., Lambies E.
J. Biol. Chem. 263:12109-12114(1988) [PubMed: 2841344] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
[6]"Overlapping arrangement of the recF and dnaN operons of Escherichia coli; positive and negative control sequences."
Armengod M.E.E., Lambies E.
Gene 43:183-196(1986) [PubMed: 3527871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-170.
[7]"Molecular analysis of the recF gene of Escherichia coli."
Blanar M.A., Sandler S.J., Armengod M.-E., Ream L.W., Clark A.J.
Proc. Natl. Acad. Sci. U.S.A. 81:4622-4626(1984) [PubMed: 6379647] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-366.
[8]"DNA sequence and transcription of the region upstream of the E. coli gyrB gene."
Adachi T., Mizuuchi K., Menzel R., Gellert M.
Nucleic Acids Res. 12:6389-6395(1984) [PubMed: 6089112] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-366.
[9]"Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp."
Kong X.-P., Onrust R., O'Donnell M., Kuriyan J.
Cell 69:425-437(1992) [PubMed: 1349852] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[10]"Flexibility revealed by the 1.85 A crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III."
Oakley A.J., Prosselkov P., Wijffels G., Beck J.L., Wilce M.C., Dixon N.E.
Acta Crystallogr. D 59:1192-1199(2003) [PubMed: 12832762] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[11]"Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp."
Bunting K.A., Roe S.M., Pearl L.H.
EMBO J. 22:5883-5892(2003) [PubMed: 14592985] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH DINB.
[12]"Accessory protein function in the DNA polymerase III holoenzyme from E. coli."
O'Donnell M.
Bioessays 14:105-111(1992) [PubMed: 1575709] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
PIRDJEC3B. A91510.
RefSeqAP_004092.1.
NP_418156.1.

3D structure databases

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[»]
3BEPX-ray1.92A/B1-366[»]
3D1EX-ray1.90A/B1-366[»]
3D1FX-ray2.00A/B1-366[»]
3D1GX-ray1.64A/B1-366[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP0A988. 28 interactions.

2-D gel databases

ECO2DBASEA036.1. 6TH EDITION.
B036.1. 6TH EDITION.

Genome annotation databases

GeneID948218.
GenomeReviewsGene locus JW3678 in contig AP009048_GR.
Gene locus b3701 in contig U00096_GR.
KEGGecj:JW3678.
eco:b3701.

Organism-specific databases

EchoBASEEB0238.
EcoGeneEG10242. dnaN.
CMRSearch...

Phylogenomic databases

HOGENOMP0A988.
OMAP0A988. IGFNARY.

Enzyme and pathway databases

BioCycEcoCyc:EG10242-MON.

Family and domain databases

InterProIPR001001. DNA_polIII_beta.
[Graphical view]
Gene3DG3DSA:3.10.150.10. DNA_polIII_beta. 3 hits.
PfamPF00712. DNA_pol3_beta. 1 hit.
PF02767. DNA_pol3_beta_2. 1 hit.
PF02768. DNA_pol3_beta_3. 1 hit.
[Graphical view]
SMARTSM00480. POL3Bc. 1 hit.
[Graphical view]
TIGRFAMsTIGR00663. dnan. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDPO3B_ECOLI
AccessionPrimary (citable) accession number: P0A988
Secondary accession number(s): P00583, Q2M813
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents