ID DPO4_CALS4 Reviewed; 384 AA. AC P58965; Q8RD00; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2002, sequence version 1. DT 07-OCT-2020, entry version 105. DE RecName: Full=DNA polymerase IV {ECO:0000255|HAMAP-Rule:MF_01113}; DE Short=Pol IV {ECO:0000255|HAMAP-Rule:MF_01113}; DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01113}; GN Name=dinB {ECO:0000255|HAMAP-Rule:MF_01113}; OrderedLocusNames=TTE0254; OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=273068; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4; RX PubMed=11997336; DOI=10.1101/gr.219302; RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R., RA Wang J., Yu J., Yang H.; RT "A complete sequence of the T. tengcongensis genome."; RL Genome Res. 12:689-700(2002). CC -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved in CC untargeted mutagenesis. Copies undamaged DNA at stalled replication CC forks, which arise in vivo from mismatched or misaligned primer ends. CC These misaligned primers can be extended by PolIV. Exhibits no 3'-5' CC exonuclease (proofreading) activity. May be involved in translesional CC synthesis, in conjunction with the beta clamp from PolIII. CC {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, CC Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01113}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01113}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01113}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. CC {ECO:0000255|HAMAP-Rule:MF_01113}. 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; AE008691; AAM23550.1; -; Genomic_DNA. DR RefSeq; WP_009609988.1; NC_003869.1. DR SMR; P58965; -. DR STRING; 273068.TTE0254; -. DR EnsemblBacteria; AAM23550; AAM23550; TTE0254. DR KEGG; tte:TTE0254; -. DR eggNOG; COG0389; Bacteria. DR HOGENOM; CLU_012348_1_2_9; -. DR KO; K02346; -. DR OMA; KVRRYDF; -. DR OrthoDB; 442163at2; -. DR Proteomes; UP000000555; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Cytoplasm; DNA damage; DNA repair; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Magnesium; Metal-binding; Mutator protein; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1..384 FT /note="DNA polymerase IV" FT /id="PRO_0000173960" FT DOMAIN 5..182 FT /note="UmuC" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT ACT_SITE 104 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT METAL 9 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT METAL 103 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT SITE 14 FT /note="Substrate discrimination" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" SQ SEQUENCE 384 AA; 43916 MW; 01C214516AD9AABB CRC64; MKRKIIHVDM DAFFASIEQQ DNPEYRGKPV IVGGLSGRGV VSTCSYEARK YGIHSAMPMY MAKKLCPQGI FLPVRRKRYE EVSEQIFRIL YDITPFVEPV SIDEAYLDVT HVDKNPEDIA LEIKKRVKDA TGLTVSVGIS YNKFLAKLAS DWNKPDGLMV ITEDMVPEIL KPLPVTKVHG IGEKSAEKLR SIGIETVEDL LKLPQENLIE LFGKTGVEIY NRIRGIDERP VETMREIKSI GKEKTLEKDT KNKELLIQHL KEFSEIVSEE LIKERLYCRT VTVKIKTADF AVHTKSKTVD KYIRFSEDIY EVAKGILEEW KLEQYVRLIG LSVSNLSPVK YEQLSFLDKR LVKVIKAGNL AEEINKRIGK KIIKKGSELL KDNK //