DPO4_EXIS2
ID DPO4_EXIS2 Reviewed; 360 AA.
AC B1YK83;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Exig_0683;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; 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}.
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DR EMBL; CP001022; ACB60164.1; -; Genomic_DNA.
DR RefSeq; WP_012369588.1; NC_010556.1.
DR AlphaFoldDB; B1YK83; -.
DR SMR; B1YK83; -.
DR STRING; 262543.Exig_0683; -.
DR EnsemblBacteria; ACB60164; ACB60164; Exig_0683.
DR KEGG; esi:Exig_0683; -.
DR eggNOG; COG0389; Bacteria.
DR HOGENOM; CLU_012348_1_2_9; -.
DR OMA; KVRRYDF; -.
DR OrthoDB; 442163at2; -.
DR Proteomes; UP000001681; 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-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProt.
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..360
FT /note="DNA polymerase IV"
FT /id="PRO_1000164001"
FT DOMAIN 6..187
FT /note="UmuC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT ACT_SITE 106
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT SITE 15
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ SEQUENCE 360 AA; 40356 MW; 5BCFAF8D4E5485D3 CRC64;
MVGRKIIHVD MDAFYASVEQ RDRPHLKGVP VIVGGPPHAR GVVATCSYEA RKYGIHSAMP
SRRAFQLCPR AVFVRPRFEV YRAVSAQIME LFLEVTPLVE PLSLDEAYLD VTENNLQMTS
ATHIAQYILA EIKRRTGLTA SAGVSNSKLV AKIASGHQKP NGLTVLPPDA VLPFLSGLKI
GDLHGVGKVT EQTLQKHGFN TVADIQQSPI AELRGLLGRD RGTELYTMAH GEDERMVRPH
RERKSIGSES TFEEDTEDID TIFETLKREA LSVVKTLNQK ELVCRTVTIK WKTEDFQSRS
KRYTFLEETA DEDTLLRVTT KLFNEIEFSG PIRLIGMSVS HLEAPPLSKQ LTWQDIDSYL
