ID   DPO42_ALKHC             Reviewed;         409 AA.
AC   Q9K9A8;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=DNA polymerase IV 2;
DE            Short=Pol IV 2;
DE            EC=2.7.7.7;
GN   Name=dinB2; OrderedLocusNames=BH2741;
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; BAB06460.1; -; Genomic_DNA.
DR   PIR; E83992; E83992.
DR   AlphaFoldDB; Q9K9A8; -.
DR   SMR; Q9K9A8; -.
DR   STRING; 272558.10175362; -.
DR   EnsemblBacteria; BAB06460; BAB06460; BAB06460.
DR   KEGG; bha:BH2741; -.
DR   eggNOG; COG0389; Bacteria.
DR   HOGENOM; CLU_012348_5_0_9; -.
DR   OMA; VKKFHGV; -.
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   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..409
FT                   /note="DNA polymerase IV 2"
FT                   /id="PRO_0000173903"
FT   DOMAIN          5..190
FT                   /note="UmuC"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            14
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  46251 MW;  5721AC1D8FDD3722 CRC64;
     MDKVIFMVDM ESFFASVERA NHPELSGRPL LVSGDPERRS GVILAACPVA KARGVTNGER
     LWEAQQKCPE AVVVRPHMQQ YVTVSVQITE ILERFTDLIE PFSIDEQFMD VTHSQRLFGA
     PREIAQKVQQ AIWHETGVRA RIGMGESKVL AKMACDNFAK KMPSGVFHLT KERMERLLWP
     LPIECLYGVG RQMTKYFRNQ GIRTIGQLAN TSLERIKGKW GVNGHVLWLT AHGIDPSPVT
     PHSHDKQKGI GHGMTLPHDY VKAEDIHVVL LELCEEVCKR ARRAHLMGRT VAIGVSGANM
     ETPTGFHRQM KLTNHTNITM EVYEGAATLF ERFWDGKPIR RLHVNLSNLT SDEAWQLSFF
     GNRDRAHQLG YTMDTIKEKF GDTAIRRAVS FLSASQAEER AKKIGGHYK