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 24-JAN-2024, entry version 188. 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; Pseudomonadota; 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 RT 0-2.4 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 ASP-401. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 511145-b0060; -. DR EnsemblBacteria; AAC73171; AAC73171; b0060. 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 OrthoDB; 5807460at2; -. DR PhylomeDB; P21189; -. DR BioCyc; EcoCyc:EG10747-MONOMER; -. DR BioCyc; MetaCyc:EG10747-MONOMER; -. DR EvolutionaryTrace; P21189; -. DR PRO; PR:P21189; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0008296; F:3'-5'-DNA exonuclease 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 CDD; cd05784; DNA_polB_II_exo; 1. DR CDD; cd05537; POLBc_Pol_II; 1. DR Gene3D; 2.40.50.590; -; 1. DR Gene3D; 3.30.70.2250; -; 1. DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1. DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. 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 PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1. DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1. DR Pfam; PF00136; DNA_pol_B; 1. DR Pfam; PF03104; DNA_pol_B_exo1; 1. DR Pfam; PF21474; DNApolII_N; 1. DR PRINTS; PR00106; DNAPOLB. DR SMART; SM00486; POLBc; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 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 /evidence="ECO:0000269|PubMed:9079692" 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 //