Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A988

- DPO3B_ECOLI

UniProt

P0A988 - DPO3B_ECOLI

Protein

DNA polymerase III subunit beta

Gene

dnaN

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. 3'-5' exonuclease activity Source: InterPro
    2. DNA binding Source: InterPro
    3. DNA-directed DNA polymerase activity Source: UniProtKB-KW
    4. identical protein binding Source: IntAct
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: EcoliWiki
    2. DNA strand elongation involved in DNA replication Source: EcoCyc

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA replication

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10242-MONOMER.
    ECOL316407:JW3678-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10242. dnaN.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Localizes to midcell position when chromosomes are condensed during DNA replication.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. DNA polymerase III complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi66 – 661G → E in dnaN159; a temperature- and UV-sensitive mutation, displays altered DNA polymerase usage, chronically induced SOS response; when associated with A-174. 1 Publication
    Mutagenesisi174 – 1741G → A in dnaN159; a temperature- and UV-sensitive mutation, displays altered DNA polymerase usage, chronically induced SOS response; when associated with A-66. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366DNA polymerase III subunit betaPRO_0000105434Add
    BLAST

    Proteomic databases

    PaxDbiP0A988.
    PRIDEiP0A988.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A988.

    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.

    Protein-protein interaction databases

    DIPiDIP-36038N.
    IntActiP0A988. 38 interactions.
    STRINGi511145.b3701.

    Structurei

    Secondary structure

    1
    366
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi7 – 1711
    Turni18 – 203
    Beta strandi26 – 283
    Helixi29 – 313
    Beta strandi32 – 387
    Beta strandi41 – 477
    Beta strandi49 – 5810
    Beta strandi66 – 716
    Helixi72 – 8110
    Beta strandi87 – 937
    Beta strandi96 – 1016
    Beta strandi104 – 1096
    Helixi113 – 1153
    Beta strandi126 – 1316
    Helixi132 – 14211
    Helixi143 – 1453
    Helixi153 – 1564
    Beta strandi157 – 1637
    Beta strandi166 – 1727
    Beta strandi174 – 18310
    Beta strandi190 – 1956
    Helixi197 – 2059
    Beta strandi209 – 2113
    Beta strandi213 – 2186
    Beta strandi220 – 2278
    Beta strandi230 – 2356
    Helixi244 – 2463
    Beta strandi254 – 2596
    Helixi260 – 27112
    Turni276 – 2783
    Beta strandi280 – 2867
    Beta strandi289 – 2957
    Beta strandi301 – 3077
    Beta strandi309 – 3124
    Beta strandi315 – 3206
    Helixi321 – 33111
    Beta strandi334 – 3407
    Beta strandi343 – 3453
    Beta strandi347 – 3515
    Beta strandi354 – 3618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP0A988.
    SMRiP0A988. Positions 1-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A988.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 125125IAdd
    BLAST
    Regioni126 – 253128IIAdd
    BLAST
    Regioni254 – 366113IIIAdd
    BLAST

    Phylogenomic databases

    eggNOGiCOG0592.
    HOGENOMiHOG000071791.
    KOiK02338.
    OMAiAVCSMPV.
    OrthoDBiEOG65J53F.
    PhylomeDBiP0A988.

    Family and domain databases

    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

    MKFTVEREHL LKPLQQVSGP LGGRPTLPIL GNLLLQVADG TLSLTGTDLE    50
    MEMVARVALV QPHEPGATTV PARKFFDICR GLPEGAEIAV QLEGERMLVR 100
    SGRSRFSLST LPAADFPNLD DWQSEVEFTL PQATMKRLIE ATQFSMAHQD 150
    VRYYLNGMLF ETEGEELRTV ATDGHRLAVC SMPIGQSLPS HSVIVPRKGV 200
    IELMRMLDGG DNPLRVQIGS NNIRAHVGDF IFTSKLVDGR FPDYRRVLPK 250
    NPDKHLEAGC DLLKQAFARA AILSNEKFRG VRLYVSENQL KITANNPEQE 300
    EAEEILDVTY SGAEMEIGFN VSYVLDVLNA LKCENVRMML TDSVSSVQIE 350
    DAASQSAAYV VMPMRL 366
    Length:366
    Mass (Da):40,587
    Last modified:April 1, 1988 - v1
    Checksum:i7A45646F61255B5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491734.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76724; AAC76724; b3701.
    BAE77593; BAE77593; BAE77593.
    GeneIDi12930541.
    948218.
    KEGGiecj:Y75_p3472.
    eco:b3701.
    PATRICi32122899. VBIEscCol129921_3825.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A91510. DJEC3B.
    RefSeqi NP_418156.1. NC_000913.3.
    YP_491734.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JQJ X-ray 2.90 A/B 1-366 [» ]
    1JQL X-ray 2.50 A 1-366 [» ]
    1MMI X-ray 1.85 A/B 1-366 [» ]
    1OK7 X-ray 1.65 A/B 1-366 [» ]
    1UNN X-ray 1.90 A/B 1-366 [» ]
    1WAI model - A/B 1-366 [» ]
    2POL X-ray 2.50 A/B 1-366 [» ]
    2XUR X-ray 1.90 A/B 1-366 [» ]
    3BEP X-ray 1.92 A/B 1-366 [» ]
    3D1E X-ray 1.90 A/B 1-366 [» ]
    3D1F X-ray 2.00 A/B 1-366 [» ]
    3D1G X-ray 1.64 A/B 1-366 [» ]
    3F1V X-ray 1.77 A/B 1-366 [» ]
    3PWE X-ray 2.20 A/B 1-366 [» ]
    3Q4J X-ray 2.30 A/B/C/D/E/F 1-366 [» ]
    3Q4K X-ray 2.60 A/B 1-366 [» ]
    3Q4L X-ray 1.95 A/B 1-366 [» ]
    3QSB X-ray 1.90 A/B 1-366 [» ]
    4K3K X-ray 1.85 A/B 1-366 [» ]
    4K3L X-ray 1.50 A/B 1-366 [» ]
    4K3M X-ray 1.85 A/B 1-366 [» ]
    4K3O X-ray 2.00 A/B 1-366 [» ]
    4K3P X-ray 2.15 A/B 1-366 [» ]
    4K3Q X-ray 1.85 A/B 1-366 [» ]
    4K3R X-ray 1.86 A/B 1-366 [» ]
    4K3S X-ray 1.75 A/B 1-366 [» ]
    4MJP X-ray 1.86 A/B 1-366 [» ]
    4MJQ X-ray 1.73 A/B 1-366 [» ]
    4MJR X-ray 1.62 A/B 1-366 [» ]
    4N94 X-ray 1.73 A/B 1-366 [» ]
    4N95 X-ray 1.80 A/B 1-366 [» ]
    4N96 X-ray 1.70 A/B 1-366 [» ]
    4N97 X-ray 1.97 A/B 1-366 [» ]
    4N98 X-ray 1.70 A/B 1-366 [» ]
    4N99 X-ray 2.30 A/B 1-366 [» ]
    4N9A X-ray 1.90 A/B 1-366 [» ]
    ProteinModelPortali P0A988.
    SMRi P0A988. Positions 1-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36038N.
    IntActi P0A988. 38 interactions.
    STRINGi 511145.b3701.

    Proteomic databases

    PaxDbi P0A988.
    PRIDEi P0A988.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76724 ; AAC76724 ; b3701 .
    BAE77593 ; BAE77593 ; BAE77593 .
    GeneIDi 12930541.
    948218.
    KEGGi ecj:Y75_p3472.
    eco:b3701.
    PATRICi 32122899. VBIEscCol129921_3825.

    Organism-specific databases

    EchoBASEi EB0238.
    EcoGenei EG10242. dnaN.

    Phylogenomic databases

    eggNOGi COG0592.
    HOGENOMi HOG000071791.
    KOi K02338.
    OMAi AVCSMPV.
    OrthoDBi EOG65J53F.
    PhylomeDBi P0A988.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10242-MONOMER.
    ECOL316407:JW3678-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A988.
    PROi P0A988.

    Gene expression databases

    Genevestigatori P0A988.

    Family and domain databases

    InterProi IPR001001. DNA_polIII_beta.
    IPR022635. DNA_polIII_beta_C.
    IPR022637. DNA_polIII_beta_cen.
    IPR022634. DNA_polIII_beta_N.
    [Graphical view ]
    Pfami PF00712. DNA_pol3_beta. 1 hit.
    PF02767. DNA_pol3_beta_2. 1 hit.
    PF02768. DNA_pol3_beta_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000804. DNA_pol_III_b. 1 hit.
    SMARTi SM00480. POL3Bc. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00663. dnan. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-170.
    7. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-366.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Interaction of the sliding clamp beta-subunit and Hda, a DnaA-related protein."
      Kurz M., Dalrymple B., Wijffels G., Kongsuwan K.
      J. Bacteriol. 186:3508-3515(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDA.
    11. "The Escherichia coli dnaN159 mutant displays altered DNA polymerase usage and chronic SOS induction."
      Sutton M.D.
      J. Bacteriol. 186:6738-6748(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AT REPLICATION FORK, INTERACTION WITH DNAE, MUTAGENESIS OF GLY-66 AND GLY-174.
    12. "Hda monomerization by ADP binding promotes replicase clamp-mediated DnaA-ATP hydrolysis."
      Su'etsugu M., Nakamura K., Keyamura K., Kudo Y., Katayama T.
      J. Biol. Chem. 283:36118-36131(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN RIDA COMPLEX.
    13. "Evidence for roles of the Escherichia coli Hda protein beyond regulatory inactivation of DnaA."
      Baxter J.C., Sutton M.D.
      Mol. Microbiol. 85:648-668(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REPLICATION FORK.
    14. "A replicase clamp-binding dynamin-like protein promotes colocalization of nascent DNA strands and equipartitioning of chromosomes in E. coli."
      Ozaki S., Matsuda Y., Keyamura K., Kawakami H., Noguchi Y., Kasho K., Nagata K., Masuda T., Sakiyama Y., Katayama T.
      Cell Rep. 4:985-995(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRFC, SUBUNIT, SUBCELLULAR LOCATION.
      Strain: K12 / MG1655 / ATCC 47076.
    15. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    16. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    17. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH DINB.
    18. "Accessory protein function in the DNA polymerase III holoenzyme from E. coli."
      O'Donnell M.
      Bioessays 14:105-111(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    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: October 1, 2014
    This is version 94 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

    External Data

    Dasty 3