ID   DPO41_ALKHC             Reviewed;         413 AA.
AC   Q9KCU7;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=DNA polymerase IV 1;
DE            Short=Pol IV 1;
DE            EC=2.7.7.7;
GN   Name=dinB1; OrderedLocusNames=BH1472;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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 (By
CC       similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR   EMBL; BA000004; BAB05191.1; -; Genomic_DNA.
DR   PIR; H83833; H83833.
DR   RefSeq; WP_010897637.1; NC_002570.2.
DR   AlphaFoldDB; Q9KCU7; -.
DR   SMR; Q9KCU7; -.
DR   STRING; 272558.10174089; -.
DR   EnsemblBacteria; BAB05191; BAB05191; BAB05191.
DR   KEGG; bha:BH1472; -.
DR   eggNOG; COG0389; Bacteria.
DR   HOGENOM; CLU_012348_1_1_9; -.
DR   OMA; CKPDGLL; -.
DR   OrthoDB; 442163at2; -.
DR   Proteomes; UP000001258; 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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 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..413
FT                   /note="DNA polymerase IV 1"
FT                   /id="PRO_0000173902"
FT   DOMAIN          7..188
FT                   /note="UmuC"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            16
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  47226 MW;  60F14D3356101522 CRC64;
     MGKGRVIFHV DMNSFYASVE MAYDPSLKGK AIAVAGSVKD RRGIVVTSSY EARAKGVRSP
     IPVWQALRKC PELILIPPNF DRYRSASQKI FSLLEEYTPL VEKVSIDEGY MDVTTTIKKV
     HPLELAKEIQ QRILAEMDLP CSIGIAPNKF LAKMASDMKK PLGITVLRKR DIAEKLWSLP
     IEEMYGIGRR SVDTYKKYQL HTIGDLAKAD PAWLEKKFGI NGPRLHCRAN GIDERPVDPE
     AVFHFKSVGN STTLPEDTTN EGRLTDVLHQ LSHSVHVRMK RKHVFCYGVQ LTIRYDDRKT
     ITRSRKLEHP IQEKDDIFTV ALSLWKQAWN GRPIRLLGVT GYDVIDKKYA YEPLDLFRYE
     EQIKQATLAE TISSIHKRYG KPIVAKGKDL DLFKEVDETK KGTSFDRDFF QHD