DPO4_ECOLI
ID DPO4_ECOLI Reviewed; 351 AA.
AC Q47155; Q47683; Q8RJ78; Q8RJ81; Q8RJ86; Q8RJ87; Q8RNI5; Q8RNI6; Q8RNI7;
AC Q8RNI8; Q8RNI9; Q8RNJ0; Q8RNJ1; Q8RNJ2; Q8RNJ3; Q8RNJ4; Q8RNJ5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DNA polymerase IV;
DE Short=Pol IV;
DE EC=2.7.7.7;
DE AltName: Full=Translesion synthesis polymerase IV {ECO:0000303|PubMed:14729336};
DE Short=TSL polymerase IV;
GN Name=dinB; Synonyms=dinP; OrderedLocusNames=b0231, JW0221;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7596361; DOI=10.1016/0165-7992(95)90024-1;
RA Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.;
RT "dinP, a new gene in Escherichia coli, whose product shows similarities to
RT UmuC and its homologues.";
RL Mutat. Res. 347:1-7(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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].
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 7-342.
RC STRAIN=ECOR 10A, ECOR 13A, ECOR 17A, ECOR 1A, ECOR 20A, ECOR 23A, ECOR 24A,
RC ECOR 26B1, ECOR 27B1, ECOR 34B1, ECOR 35D, ECOR 37UG, ECOR 45B1, ECOR 46D,
RC ECOR 49D, ECOR 4A, ECOR 50D, ECOR 51B2, ECOR 52B2, ECOR 57B2, ECOR 58B1,
RC ECOR 59B2, ECOR 60B2, ECOR 62B2, ECOR 68B1, and ECOR 70B1;
RA Bjedov I., Matic I., Denamur E.;
RT "Phylogeny of SOS inducible DNA polymerases of Escherichia coli.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CHARACTERIZATION.
RX PubMed=6771759; DOI=10.1073/pnas.77.5.2819;
RA Kenyon C.J., Walker G.C.;
RT "DNA-damaging agents stimulate gene expression at specific loci in
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:2819-2823(1980).
RN [8]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=9391106; DOI=10.1073/pnas.94.25.13792;
RA Kim S.-R., Maenhaut-Michel G., Yamada M., Yamamoto Y., Matsui K.,
RA Sofuni T., Nohmi T., Ohmori H.;
RT "Multiple pathways for SOS-induced mutagenesis in Escherichia coli: an
RT overexpression of dinB/dinP results in strongly enhancing mutagenesis in
RT the absence of any exogenous treatment to damage DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13792-13797(1997).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ASP-8; ARG-49; ASP-103 AND GLU-104.
RC STRAIN=K12;
RX PubMed=10488344; DOI=10.1016/s1097-2765(00)80376-7;
RA Wagner J., Gruz P., Kim S.-R., Yamada M., Matsui K., Fuchs R.P.P.,
RA Nohmi T.;
RT "The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved
RT in mutagenesis.";
RL Mol. Cell 4:281-286(1999).
RN [10]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11080171; DOI=10.1093/emboj/19.22.6259;
RA Napolitano R., Janel-Bintz R., Wagner J., Fuchs R.P.P.;
RT "All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are
RT involved in induced mutagenesis.";
RL EMBO J. 19:6259-6265(2000).
RN [11]
RP FUNCTION, AND STIMULATION BY BETA SLIDING-CLAMP COMPLEX.
RX PubMed=10801133; DOI=10.1038/35010020;
RA Tang M., Pham P., Shen X., Taylor J.S., O'Donnell M., Woodgate R.,
RA Goodman M.F.;
RT "Roles of E. coli DNA polymerases IV and V in lesion-targeted and
RT untargeted SOS mutagenesis.";
RL Nature 404:1014-1018(2000).
RN [12]
RP FUNCTION.
RX PubMed=11463382; DOI=10.1016/s1097-2765(01)00204-0;
RA McKenzie G.J., Lee P.L., Lombardo M.-J., Hastings P.J., Rosenberg S.M.;
RT "SOS mutator DNA polymerase IV functions in adaptive mutation and not
RT adaptive amplification.";
RL Mol. Cell 7:571-579(2001).
RN [13]
RP FUNCTION.
RX PubMed=11751576; DOI=10.1093/embo-reports/kvf007;
RA Lenne-Samuel N., Wagner J., Etienne H., Fuchs R.P.P.;
RT "The processivity factor beta controls DNA polymerase IV traffic during
RT spontaneous mutagenesis and translesion synthesis in vivo.";
RL EMBO Rep. 3:45-49(2002).
RN [14]
RP FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=12060704; DOI=10.1073/pnas.092269199;
RA Yeiser B., Pepper E.D., Goodman M.F., Finkel S.E.;
RT "SOS-induced DNA polymerases enhance long-term survival and evolutionary
RT fitness.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8737-8741(2002).
RN [15]
RP INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12813093; DOI=10.1128/jb.185.13.3972-3977.2003;
RA McKenzie G.J., Magner D.B., Lee P.L., Rosenberg S.M.;
RT "The dinB operon and spontaneous mutation in Escherichia coli.";
RL J. Bacteriol. 185:3972-3977(2003).
RN [16]
RP SUBUNIT.
RX PubMed=16168375; DOI=10.1016/j.molcel.2005.08.011;
RA Indiani C., McInerney P., Georgescu R., Goodman M.F., O'Donnell M.;
RT "A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases
RT simultaneously.";
RL Mol. Cell 19:805-815(2005).
RN [17]
RP REVIEW.
RX PubMed=11595180; DOI=10.1016/s0092-8674(01)00509-8;
RA Friedberg E.C., Fischhaber P.L., Kisker C.;
RT "Error-prone DNA polymerases: novel structures and the benefits of
RT infidelity.";
RL Cell 107:9-12(2001).
RN [18]
RP REVIEW.
RX PubMed=11587937; DOI=10.1016/s1369-5274(00)00255-1;
RA McKenzie G.J., Rosenberg S.M.;
RT "Adaptive mutations, mutator DNA polymerases and genetic change strategies
RT of pathogens.";
RL Curr. Opin. Microbiol. 4:586-594(2001).
RN [19]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [20]
RP REVIEW.
RX PubMed=12045089; DOI=10.1146/annurev.biochem.71.083101.124707;
RA Goodman M.F.;
RT "Error-prone repair DNA polymerases in prokaryotes and eukaryotes.";
RL Annu. Rev. Biochem. 71:17-50(2002).
RN [21] {ECO:0007744|PDB:1UNN}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 243-351 IN COMPLEX WITH DNAN.
RX PubMed=14592985; DOI=10.1093/emboj/cdg568;
RA Bunting K.A., Roe S.M., Pearl L.H.;
RT "Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB
RT to the beta-clamp.";
RL EMBO J. 22:5883-5892(2003).
RN [22] {ECO:0007744|PDB:1OK7}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 336-351 IN COMPLEX WITH DNAN.
RX PubMed=14729336; DOI=10.1016/j.jmb.2003.11.049;
RA Burnouf D.Y., Olieric V., Wagner J., Fujii S., Reinbolt J., Fuchs R.P.,
RA Dumas P.;
RT "Structural and biochemical analysis of sliding clamp/ligand interactions
RT suggest a competition between replicative and translesion DNA
RT polymerases.";
RL J. Mol. Biol. 335:1187-1197(2004).
CC -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved in
CC translesion repair and untargeted mutagenesis (PubMed:10488344,
CC PubMed:10801133). Copies undamaged DNA at stalled replication forks,
CC which arise in vivo from mismatched or misaligned primer ends. These
CC misaligned primers can be extended by Pol IV. Exhibits no 3'-5'
CC exonuclease (proofreading) activity (PubMed:10488344). Overexpression
CC of Pol IV results in increased frameshift mutagenesis. It is required
CC for stationary-phase adaptive mutation, which provides the bacterium
CC with flexibility in dealing with environmental stress, enhancing long-
CC term survival and evolutionary fitness. Not seen to be involved in
CC translesion snythesis even when stimulated by the beta slding-clamp and
CC clamp-loading complex, which do however increase non-targeted DNA
CC polymerase efficiency 3,000-fold, may be due to targeting to stalled
CC replication forks on nondamaged DNA (PubMed:10801133, PubMed:16168375).
CC Involved in translesional synthesis, in conjunction with the beta clamp
CC from PolIII (PubMed:14592985, PubMed:14729336).
CC {ECO:0000269|PubMed:10488344, ECO:0000269|PubMed:10801133,
CC ECO:0000269|PubMed:11080171, ECO:0000269|PubMed:11463382,
CC ECO:0000269|PubMed:11751576, ECO:0000269|PubMed:12060704,
CC ECO:0000269|PubMed:14592985, ECO:0000269|PubMed:16168375,
CC ECO:0000269|PubMed:9391106, ECO:0000305|PubMed:14729336}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. Interacts with beta sliding clamp, which confers
CC increased processivity (PubMed:14592985,
CC PubMed:14729336,PubMed:16168375). {ECO:0000269|PubMed:14592985,
CC ECO:0000269|PubMed:14729336, ECO:0000269|PubMed:16168375, ECO:0000305}.
CC -!- INTERACTION:
CC Q47155; P0A988: dnaN; NbExp=2; IntAct=EBI-1037359, EBI-542385;
CC Q47155; P0AFF6: nusA; NbExp=3; IntAct=EBI-1037359, EBI-551571;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By SOS response. A member of the dinB-yafNOP operon
CC (PubMed:12813093). Induced by hydroxyurea (PubMed:20005847).
CC {ECO:0000269|PubMed:12813093, ECO:0000269|PubMed:20005847}.
CC -!- DOMAIN: The catalytic core consists of fingers, palm and thumb
CC subdomains, but the fingers and thumb subdomains are much smaller than
CC in high-fidelity polymerases; residues from five sequence motifs of the
CC Y-family cluster around an active site cleft that can accommodate DNA
CC and nucleotide substrates with relaxed geometric constraints, with
CC consequently higher rates of misincorporation and low processivity. It
CC lacks the O helices present in high-fidelity DNA polymerases in the
CC fingers domain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR EMBL; D38582; BAA07593.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08651.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73335.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77901.1; -; Genomic_DNA.
DR EMBL; AF483080; AAL91943.1; -; Genomic_DNA.
DR EMBL; AF483081; AAL91944.1; -; Genomic_DNA.
DR EMBL; AF483082; AAL91945.1; -; Genomic_DNA.
DR EMBL; AF483083; AAL91946.1; -; Genomic_DNA.
DR EMBL; AF483084; AAL91947.1; -; Genomic_DNA.
DR EMBL; AF483085; AAL91948.1; -; Genomic_DNA.
DR EMBL; AF483086; AAL91949.1; -; Genomic_DNA.
DR EMBL; AF483087; AAL91950.1; -; Genomic_DNA.
DR EMBL; AF483088; AAL91951.1; -; Genomic_DNA.
DR EMBL; AF483089; AAL91952.1; -; Genomic_DNA.
DR EMBL; AF483090; AAL91953.1; -; Genomic_DNA.
DR EMBL; AF483091; AAL91954.1; -; Genomic_DNA.
DR EMBL; AF483092; AAL91955.1; -; Genomic_DNA.
DR EMBL; AF483093; AAL91956.1; -; Genomic_DNA.
DR EMBL; AF483094; AAL91957.1; -; Genomic_DNA.
DR EMBL; AF483095; AAL91958.1; -; Genomic_DNA.
DR EMBL; AF483096; AAL91959.1; -; Genomic_DNA.
DR EMBL; AF483097; AAL91960.1; -; Genomic_DNA.
DR EMBL; AF483098; AAL91961.1; -; Genomic_DNA.
DR EMBL; AF483099; AAL91962.1; -; Genomic_DNA.
DR EMBL; AF483100; AAL91963.1; -; Genomic_DNA.
DR EMBL; AF483101; AAL91964.1; -; Genomic_DNA.
DR EMBL; AF483102; AAL91965.1; -; Genomic_DNA.
DR EMBL; AF483103; AAL91966.1; -; Genomic_DNA.
DR EMBL; AF483104; AAL91967.1; -; Genomic_DNA.
DR EMBL; AF483105; AAL91968.1; -; Genomic_DNA.
DR PIR; H64747; H64747.
DR RefSeq; NP_414766.1; NC_000913.3.
DR RefSeq; WP_001226164.1; NZ_SSZK01000050.1.
DR PDB; 1OK7; X-ray; 1.65 A; C=336-351.
DR PDB; 1UNN; X-ray; 1.90 A; C/D=243-351.
DR PDB; 4IR1; X-ray; 2.38 A; A/F=2-351.
DR PDB; 4IR9; X-ray; 2.33 A; A/F=2-351.
DR PDB; 4IRC; X-ray; 2.67 A; A/F=2-341.
DR PDB; 4IRD; X-ray; 2.48 A; A/F=2-341.
DR PDB; 4IRK; X-ray; 2.32 A; A/B=2-341.
DR PDB; 4Q43; X-ray; 2.45 A; A/F=2-351.
DR PDB; 4Q44; X-ray; 2.71 A; A/F=2-341.
DR PDB; 4Q45; X-ray; 2.18 A; A/F=2-341.
DR PDB; 4R8U; X-ray; 2.30 A; A=2-340, B=2-338.
DR PDB; 5C5J; X-ray; 2.10 A; A/F=2-351.
DR PDB; 5YUR; X-ray; 2.04 A; A/F=2-351.
DR PDB; 5YUS; X-ray; 1.94 A; A/F=2-351.
DR PDB; 5YUT; X-ray; 2.15 A; A/F=2-351.
DR PDB; 5YUU; X-ray; 1.89 A; A/F=2-351.
DR PDB; 5YUV; X-ray; 2.06 A; A/F=2-351.
DR PDB; 5YUW; X-ray; 2.12 A; A/F=2-351.
DR PDB; 5YUX; X-ray; 2.04 A; A/F=2-351.
DR PDB; 5YUY; X-ray; 1.74 A; A/F=2-351.
DR PDB; 5YUZ; X-ray; 1.83 A; A/F=2-351.
DR PDB; 5YV0; X-ray; 2.09 A; A/F=2-351.
DR PDB; 5YV1; X-ray; 2.09 A; A/F=2-351.
DR PDB; 5YV2; X-ray; 1.90 A; A/F=2-351.
DR PDB; 5YV3; X-ray; 2.03 A; A/F=2-351.
DR PDB; 5YYD; X-ray; 2.05 A; A/F=2-351.
DR PDB; 5YYE; X-ray; 2.33 A; A/F=2-351.
DR PDB; 5ZLV; X-ray; 2.35 A; A/F=2-351.
DR PDB; 6IG1; X-ray; 1.97 A; A/F=2-351.
DR PDB; 6JUP; X-ray; 2.44 A; A/F=2-341.
DR PDB; 6JUQ; X-ray; 2.74 A; A/F=2-341.
DR PDBsum; 1OK7; -.
DR PDBsum; 1UNN; -.
DR PDBsum; 4IR1; -.
DR PDBsum; 4IR9; -.
DR PDBsum; 4IRC; -.
DR PDBsum; 4IRD; -.
DR PDBsum; 4IRK; -.
DR PDBsum; 4Q43; -.
DR PDBsum; 4Q44; -.
DR PDBsum; 4Q45; -.
DR PDBsum; 4R8U; -.
DR PDBsum; 5C5J; -.
DR PDBsum; 5YUR; -.
DR PDBsum; 5YUS; -.
DR PDBsum; 5YUT; -.
DR PDBsum; 5YUU; -.
DR PDBsum; 5YUV; -.
DR PDBsum; 5YUW; -.
DR PDBsum; 5YUX; -.
DR PDBsum; 5YUY; -.
DR PDBsum; 5YUZ; -.
DR PDBsum; 5YV0; -.
DR PDBsum; 5YV1; -.
DR PDBsum; 5YV2; -.
DR PDBsum; 5YV3; -.
DR PDBsum; 5YYD; -.
DR PDBsum; 5YYE; -.
DR PDBsum; 5ZLV; -.
DR PDBsum; 6IG1; -.
DR PDBsum; 6JUP; -.
DR PDBsum; 6JUQ; -.
DR AlphaFoldDB; Q47155; -.
DR SMR; Q47155; -.
DR BioGRID; 4261678; 55.
DR IntAct; Q47155; 3.
DR MINT; Q47155; -.
DR STRING; 511145.b0231; -.
DR PaxDb; Q47155; -.
DR PRIDE; Q47155; -.
DR EnsemblBacteria; AAC73335; AAC73335; b0231.
DR EnsemblBacteria; BAA77901; BAA77901; BAA77901.
DR GeneID; 944922; -.
DR KEGG; ecj:JW0221; -.
DR KEGG; eco:b0231; -.
DR PATRIC; fig|1411691.4.peg.2052; -.
DR EchoBASE; EB2935; -.
DR eggNOG; COG0389; Bacteria.
DR HOGENOM; CLU_012348_1_2_6; -.
DR InParanoid; Q47155; -.
DR OMA; CKPDGLL; -.
DR PhylomeDB; Q47155; -.
DR BioCyc; EcoCyc:G6115-MON; -.
DR BioCyc; MetaCyc:G6115-MON; -.
DR EvolutionaryTrace; Q47155; -.
DR PRO; PR:Q47155; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IDA:EcoliWiki.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0070987; P:error-free translesion synthesis; IDA:EcoCyc.
DR GO; GO:0042276; P:error-prone translesion synthesis; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEP:EcoCyc.
DR CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR HAMAP; MF_01113; DNApol_IV; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR022880; DNApol_IV.
DR InterPro; IPR024728; PolY_HhH_motif.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF11798; IMS_HHH; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding;
KW Mutator protein; Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..351
FT /note="DNA polymerase IV"
FT /id="PRO_0000173912"
FT DOMAIN 4..185
FT /note="UmuC"
FT ACT_SITE 104
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 13
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT VARIANT 36..38
FT /note="ERR -> ARG (in strain: ECOR 45B1)"
FT VARIANT 124
FT /note="Q -> K (in strain: ECOR 35D)"
FT VARIANT 132
FT /note="N -> S (in strain: ECOR 34B1 and ECOR 37UG)"
FT VARIANT 135
FT /note="Q -> H (in strain: ECOR 70B1)"
FT VARIANT 170
FT /note="P -> S (in strain: ECOR 37UG)"
FT VARIANT 171
FT /note="A -> T (in strain: ECOR 45B1, ECOR 46D, ECOR 49D and
FT ECOR 50D)"
FT VARIANT 176
FT /note="L -> F (in strain: ECOR 37UG)"
FT VARIANT 201
FT /note="G -> S (in strain: ECOR 59B2)"
FT VARIANT 210
FT /note="M -> I (in strain: ECOR 37UG, ECOR 45B1, ECOR 51B2,
FT ECOR 52B2, ECOR 58B1 and ECOR 70B1)"
FT VARIANT 210
FT /note="M -> T (in strain: ECOR 35D, ECOR 46D, ECOR 49D,
FT ECOR 50D, ECOR 57B2, ECOR 59B2, ECOR 60B2 and ECOR 62B2)"
FT VARIANT 225
FT /note="R -> C (in strain: ECOR 59B2 and ECOR 60B2)"
FT VARIANT 310
FT /note="A -> S (in strain: ECOR 57B2, ECOR 59B2, ECOR 60B2
FT and ECOR 62B2)"
FT VARIANT 321
FT /note="D -> N (in strain: ECOR 35D)"
FT MUTAGEN 8
FT /note="D->A,H: Loss of function."
FT /evidence="ECO:0000269|PubMed:10488344"
FT MUTAGEN 49
FT /note="R->A,F: Loss of function."
FT /evidence="ECO:0000269|PubMed:10488344"
FT MUTAGEN 103
FT /note="D->A,N: Loss of function."
FT /evidence="ECO:0000269|PubMed:10488344"
FT MUTAGEN 104
FT /note="E->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10488344"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5YUY"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:5YUY"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:5YUY"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 256..277
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:5YUY"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:5YUY"
FT STRAND 329..337
FT /evidence="ECO:0007829|PDB:5YUY"
SQ SEQUENCE 351 AA; 39516 MW; 74DF44DCA18D405F CRC64;
MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARK FGVRSAMPTG
MALKLCPHLT LLPGRFDAYK EASNHIREIF SRYTSRIEPL SLDEAYLDVT DSVHCHGSAT
LIAQEIRQTI FNELQLTASA GVAPVKFLAK IASDMNKPNG QFVITPAEVP AFLQTLPLAK
IPGVGKVSAA KLEAMGLRTC GDVQKCDLVM LLKRFGKFGR ILWERSQGID ERDVNSERLR
KSVGVERTMA EDIHHWSECE AIIERLYPEL ERRLAKVKPD LLIARQGVKL KFDDFQQTTQ
EHVWPRLNKA DLIATARKTW DERRGGRGVR LVGLHVTLLD PQMERQLVLG L
