DPO2_ECOLI
ID DPO2_ECOLI Reviewed; 783 AA.
AC P21189; Q8KMX7; Q8KMX8;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=DNA polymerase II;
DE Short=Pol II;
DE EC=2.7.7.7;
GN Name=polB; Synonyms=dinA; OrderedLocusNames=b0060, JW0059;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-9.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2034216; DOI=10.1007/bf00273583;
RA Iwasaki H., Ishino Y., Toh H., Nakata A., Shinagawa H.;
RT "Escherichia coli DNA polymerase II is homologous to alpha-like DNA
RT polymerases.";
RL Mol. Gen. Genet. 226:24-33(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2261080; DOI=10.1089/dna.1990.9.631;
RA Chen H., Sun Y., Stark T., Beattie W., Moses R.E.;
RT "Nucleotide sequence and deletion analysis of the polB gene of Escherichia
RT coli.";
RL DNA Cell Biol. 9:631-635(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-458, AND PROTEIN SEQUENCE OF 2-28.
RC STRAIN=K12;
RX PubMed=2217198; DOI=10.1073/pnas.87.19.7663;
RA Bonner C.A., Hays S., McEntee K., Goodman M.F.;
RT "DNA polymerase II is encoded by the DNA damage-inducible dinA gene of
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7663-7667(1990).
RN [7]
RP STIMULATION BY BETA SLIDING-CLAMP (DNAN).
RX PubMed=1999435; DOI=10.1016/s0021-9258(20)64360-5;
RA Hughes A.J. Jr., Bryan S.K., Chen H., Moses R.E., McHenry C.S.;
RT "Escherichia coli DNA polymerase II is stimulated by DNA polymerase III
RT holoenzyme auxiliary subunits.";
RL J. Biol. Chem. 266:4568-4573(1991).
RN [8]
RP STIMULATION BY BETA SLIDING-CLAMP (DNAN).
RX PubMed=1534562; DOI=10.1016/s0021-9258(19)49928-6;
RA Bonner C.A., Stukenberg P.T., Rajagopalan M., Eritja R., O'Donnell M.,
RA McEntee K., Echols H., Goodman M.F.;
RT "Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase
RT III accessory proteins.";
RL J. Biol. Chem. 267:11431-11438(1992).
RN [9]
RP VARIANT MUTANT ALLELE POLB100.
RX PubMed=9079692; DOI=10.1074/jbc.272.13.8611;
RA Qiu Z., Goodman M.F.;
RT "The Escherichia coli polB locus is identical to dinA, the structural gene
RT for DNA polymerase II. Characterization of Pol II purified from a polB
RT mutant.";
RL J. Biol. Chem. 272:8611-8617(1997).
CC -!- FUNCTION: Thought to be involved in DNA repair and/or mutagenesis. Its
CC processivity is enhanced by the beta sliding clamp (dnaN) and clamp
CC loader (PubMed:1999435, PubMed:1534562). {ECO:0000269|PubMed:1534562,
CC ECO:0000269|PubMed:1999435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- ACTIVITY REGULATION: DNA polymerase II activity is regulated by the
CC lexA gene during the SOS response.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; X54847; CAA38616.1; -; Genomic_DNA.
DR EMBL; M62646; AAA24406.1; -; Genomic_DNA.
DR EMBL; M35371; AAA24407.1; -; Genomic_DNA.
DR EMBL; M38283; AAA63764.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73171.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96628.2; -; Genomic_DNA.
DR EMBL; M37727; AAA23684.1; -; Genomic_DNA.
DR PIR; S15943; JDEC22.
DR RefSeq; NP_414602.1; NC_000913.3.
DR RefSeq; WP_000035670.1; NZ_LN832404.1.
DR PDB; 1Q8I; X-ray; 2.00 A; A=1-783.
DR PDB; 3K57; X-ray; 2.08 A; A=1-783.
DR PDB; 3K58; X-ray; 2.05 A; A=1-783.
DR PDB; 3K59; X-ray; 1.92 A; A=1-783.
DR PDB; 3K5L; X-ray; 2.70 A; A=1-783.
DR PDB; 3K5M; X-ray; 2.04 A; A=1-783.
DR PDB; 3K5N; X-ray; 3.15 A; A/B=1-783.
DR PDB; 3K5O; X-ray; 2.20 A; A/B=1-783.
DR PDB; 3MAQ; X-ray; 2.40 A; A=1-783.
DR PDBsum; 1Q8I; -.
DR PDBsum; 3K57; -.
DR PDBsum; 3K58; -.
DR PDBsum; 3K59; -.
DR PDBsum; 3K5L; -.
DR PDBsum; 3K5M; -.
DR PDBsum; 3K5N; -.
DR PDBsum; 3K5O; -.
DR PDBsum; 3MAQ; -.
DR AlphaFoldDB; P21189; -.
DR SMR; P21189; -.
DR BioGRID; 4261621; 107.
DR BioGRID; 849181; 1.
DR IntAct; P21189; 5.
DR STRING; 511145.b0060; -.
DR PaxDb; P21189; -.
DR PRIDE; P21189; -.
DR EnsemblBacteria; AAC73171; AAC73171; b0060.
DR EnsemblBacteria; BAB96628; BAB96628; BAB96628.
DR GeneID; 944779; -.
DR KEGG; ecj:JW0059; -.
DR KEGG; eco:b0060; -.
DR PATRIC; fig|1411691.4.peg.2223; -.
DR EchoBASE; EB0740; -.
DR eggNOG; COG0417; Bacteria.
DR HOGENOM; CLU_018487_0_0_6; -.
DR InParanoid; P21189; -.
DR OMA; FVLTRHW; -.
DR PhylomeDB; P21189; -.
DR BioCyc; EcoCyc:EG10747-MON; -.
DR BioCyc; MetaCyc:EG10747-MON; -.
DR EvolutionaryTrace; P21189; -.
DR PRO; PR:P21189; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0045004; P:DNA replication proofreading; IDA:EcoCyc.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEP:EcoCyc.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 2.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; DNA-directed DNA polymerase; Nucleotidyltransferase;
KW Reference proteome; SOS response; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2034216,
FT ECO:0000269|PubMed:2217198"
FT CHAIN 2..783
FT /note="DNA polymerase II"
FT /id="PRO_0000046473"
FT VARIANT 401
FT /note="G -> D (in allele POLB100)"
FT CONFLICT 172
FT /note="G -> A (in Ref. 2; AAA24406/AAA24407)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..258
FT /note="EH -> DD (in Ref. 6; AAA63764/AAA23684)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="R -> G (in Ref. 6; AAA63764/AAA23684)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="N -> T (in Ref. 2; AAA24406/AAA24407)"
FT /evidence="ECO:0000305"
FT CONFLICT 740..783
FT /note="LDYQRSPLDYEHYLTRQLQPVAEGILPFIEDNFATLMTGQLGLF -> PGLP
FT TFTTGLRTLSDPPATTRGGGNTPFY (in Ref. 2; AAA24406/AAA24407)"
FT /evidence="ECO:0000305"
FT STRAND 2..15
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:3K59"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:3K59"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:3K59"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3K5L"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 325..346
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 348..359
FT /evidence="ECO:0007829|PDB:3K59"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:1Q8I"
FT HELIX 369..383
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 423..431
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 435..443
FT /evidence="ECO:0007829|PDB:3K59"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:3K5O"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 466..482
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 486..501
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 513..536
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 559..582
FT /evidence="ECO:0007829|PDB:3K59"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 592..603
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 617..623
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 626..634
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 643..657
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 663..674
FT /evidence="ECO:0007829|PDB:3K59"
FT TURN 675..678
FT /evidence="ECO:0007829|PDB:1Q8I"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 684..688
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 701..715
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 725..733
FT /evidence="ECO:0007829|PDB:3K59"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 749..755
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 757..762
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 765..768
FT /evidence="ECO:0007829|PDB:3K59"
FT HELIX 772..779
FT /evidence="ECO:0007829|PDB:3K59"
SQ SEQUENCE 783 AA; 90053 MW; 1A12A21B2FDB0E22 CRC64;
MAQAGFILTR HWRDTPQGTE VSFWLATDNG PLQVTLAPQE SVAFIPADQV PRAQHILQGE
QGFRLTPLAL KDFHRQPVYG LYCRAHRQLM NYEKRLREGG VTVYEADVRP PERYLMERFI
TSPVWVEGDM HNGTIVNARL KPHPDYRPPL KWVSIDIETT RHGELYCIGL EGCGQRIVYM
LGPENGDASS LDFELEYVAS RPQLLEKLNA WFANYDPDVI IGWNVVQFDL RMLQKHAERY
RLPLRLGRDN SELEWREHGF KNGVFFAQAK GRLIIDGIEA LKSAFWNFSS FSLETVAQEL
LGEGKSIDNP WDRMDEIDRR FAEDKPALAT YNLKDCELVT QIFHKTEIMP FLLERATVNG
LPVDRHGGSV AAFGHLYFPR MHRAGYVAPN LGEVPPHASP GGYVMDSRPG LYDSVLVLDY
KSLYPSIIRT FLIDPVGLVE GMAQPDPEHS TEGFLDAWFS REKHCLPEIV TNIWHGRDEA
KRQGNKPLSQ ALKIIMNAFY GVLGTTACRF FDPRLASSIT MRGHQIMRQT KALIEAQGYD
VIYGDTDSTF VWLKGAHSEE EAAKIGRALV QHVNAWWAET LQKQRLTSAL ELEYETHFCR
FLMPTIRGAD TGSKKRYAGL IQEGDKQRMV FKGLETVRTD WTPLAQQFQQ ELYLRIFRNE
PYQEYVRETI DKLMAGELDA RLVYRKRLRR PLSEYQRNVP PHVRAARLAD EENQKRGRPL
QYQNRGTIKY VWTTNGPEPL DYQRSPLDYE HYLTRQLQPV AEGILPFIED NFATLMTGQL
GLF
