DNA polymerase III subunit beta

Details

Name
DNA polymerase III subunit beta
Synonyms
  • 2.7.7.7
  • Beta clamp
  • Beta sliding clamp
Gene Name
dnaN
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0017219|DNA polymerase III subunit beta
MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGTLSLTGTDLEMEMVARVALV
QPHEPGATTVPARKFFDICRGLPEGAEIAVQLEGERMLVRSGRSRFSLSTLPAADFPNLD
DWQSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVC
SMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGR
FPDYRRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQE
EAEEILDVTYSGAEMEIGFNVSYVLDVLNALKCENVRMMLTDSVSSVQIEDAASQSAAYV
VMPMRL
Number of residues
366
Molecular Weight
40586.255
Theoretical pI
5.05
GO Classification
Functions
3'-5' exonuclease activity / DNA binding / DNA-directed DNA polymerase activity / identical protein binding
Processes
cellular response to DNA damage stimulus / DNA strand elongation involved in DNA replication
Components
cytosol / DNA polymerase III complex
General Function
Identical protein binding
Specific 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. Coordinates protein traffic at the replication fork, where it interacts with multiple DNA polymerases.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0017220|DNA polymerase III subunit beta (dnaN)
ATGAAATTTACCGTAGAACGTGAGCATTTATTAAAACCGCTACAACAGGTGAGCGGTCCG
TTAGGTGGTCGTCCTACGCTACCGATTCTCGGTAATCTGCTGTTACAGGTTGCTGACGGT
ACGTTGTCGCTGACCGGTACTGATCTCGAGATGGAAATGGTGGCACGTGTTGCGCTGGTT
CAGCCACACGAGCCAGGAGCGACGACCGTTCCGGCGCGCAAATTCTTTGATATCTGCCGT
GGTCTGCCTGAAGGCGCGGAAATTGCCGTGCAGCTGGAAGGTGAACGGATGCTGGTACGC
TCCGGGCGTAGCCGTTTTTCGCTGTCTACCCTGCCAGCGGCGGATTTCCCGAACCTCGAT
GACTGGCAGAGTGAAGTCGAATTTACCCTGCCGCAGGCAACGATGAAGCGTCTGATTGAA
GCGACCCAGTTTTCTATGGCGCATCAGGACGTTCGCTATTACTTAAATGGTATGCTGTTT
GAAACCGAAGGTGAAGAACTGCGCACCGTGGCAACCGACGGCCACCGTCTGGCGGTCTGT
TCAATGCCAATTGGTCAATCTTTGCCAAGCCATTCGGTGATCGTACCGCGTAAAGGCGTG
ATTGAACTGATGCGTATGCTCGACGGCGGCGACAATCCGCTGCGCGTACAGATTGGCAGC
AACAACATTCGCGCCCACGTTGGCGACTTTATCTTCACCTCCAAACTGGTGGATGGTCGC
TTCCCGGATTATCGCCGCGTTCTGCCGAAGAACCCGGACAAACATCTGGAAGCTGGCTGC
GATCTGCTCAAGCAGGCGTTTGCTCGCGCGGCGATTCTCTCTAACGAGAAATTCCGCGGC
GTACGTCTTTATGTCAGCGAAAACCAGCTGAAAATCACCGCCAACAACCCGGAACAGGAA
GAAGCGGAAGAGATCCTCGACGTTACCTATAGCGGTGCGGAGATGGAAATCGGCTTCAAC
GTCAGTTATGTGCTGGATGTTCTGAACGCGCTGAAATGCGAAAACGTCCGCATGATGCTG
ACCGATTCGGTTTCCAGCGTGCAGATTGAAGATGCGGCCAGCCAGAGCGCGGCTTATGTT
GTCATGCCAATGAGACTGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A988
UniProtKB Entry NameDPO3B_ECOLI
GenBank Protein ID145759
GenBank Gene IDJ01602
General References
  1. Ohmori H, Kimura M, Nagata T, Sakakibara Y: Structural analysis of the dnaA and dnaN genes of Escherichia coli. Gene. 1984 May;28(2):159-70. [Article]
  2. Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Armengod ME, Garcia-Sogo M, Lambies E: Transcriptional organization of the dnaN and recF genes of Escherichia coli K-12. J Biol Chem. 1988 Aug 25;263(24):12109-14. [Article]
  6. Armengod ME, Lambies E: Overlapping arrangement of the recF and dnaN operons of Escherichia coli; positive and negative control sequences. Gene. 1986;43(3):183-96. [Article]
  7. Blanar MA, Sandler SJ, Armengod ME, Ream LW, Clark AJ: Molecular analysis of the recF gene of Escherichia coli. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4622-6. [Article]
  8. Adachi T, Mizuuchi K, Menzel R, Gellert M: DNA sequence and transcription of the region upstream of the E. coli gyrB gene. Nucleic Acids Res. 1984 Aug 24;12(16):6389-95. [Article]
  9. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  10. Kurz M, Dalrymple B, Wijffels G, Kongsuwan K: Interaction of the sliding clamp beta-subunit and Hda, a DnaA-related protein. J Bacteriol. 2004 Jun;186(11):3508-15. [Article]
  11. Sutton MD: The Escherichia coli dnaN159 mutant displays altered DNA polymerase usage and chronic SOS induction. J Bacteriol. 2004 Oct;186(20):6738-48. [Article]
  12. Su'etsugu M, Nakamura K, Keyamura K, Kudo Y, Katayama T: Hda monomerization by ADP binding promotes replicase clamp-mediated DnaA-ATP hydrolysis. J Biol Chem. 2008 Dec 26;283(52):36118-31. doi: 10.1074/jbc.M803158200. Epub 2008 Oct 30. [Article]
  13. Davies BW, Kohanski MA, Simmons LA, Winkler JA, Collins JJ, Walker GC: Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli. Mol Cell. 2009 Dec 11;36(5):845-60. doi: 10.1016/j.molcel.2009.11.024. [Article]
  14. Baxter JC, Sutton MD: Evidence for roles of the Escherichia coli Hda protein beyond regulatory inactivation of DnaA. Mol Microbiol. 2012 Aug;85(4):648-68. doi: 10.1111/j.1365-2958.2012.08129.x. Epub 2012 Jul 13. [Article]
  15. Ozaki S, Matsuda Y, Keyamura K, Kawakami H, Noguchi Y, Kasho K, Nagata K, Masuda T, Sakiyama Y, Katayama T: A replicase clamp-binding dynamin-like protein promotes colocalization of nascent DNA strands and equipartitioning of chromosomes in E. coli. Cell Rep. 2013 Sep 12;4(5):985-95. doi: 10.1016/j.celrep.2013.07.040. Epub 2013 Aug 30. [Article]
  16. Kong XP, Onrust R, O'Donnell M, Kuriyan J: Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell. 1992 May 1;69(3):425-37. [Article]
  17. Oakley AJ, Prosselkov P, Wijffels G, Beck JL, Wilce MC, Dixon NE: Flexibility revealed by the 1.85 A crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1192-9. Epub 2003 Jun 27. [Article]
  18. Bunting KA, Roe SM, Pearl LH: Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp. EMBO J. 2003 Nov 3;22(21):5883-92. [Article]
  19. O'Donnell M: Accessory protein function in the DNA polymerase III holoenzyme from E. coli. Bioessays. 1992 Feb;14(2):105-11. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB06998[(5R)-5-(2,3-dibromo-5-ethoxy-4-hydroxybenzyl)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acidexperimentalunknownDetails