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DPO4_UREU1
ID   DPO4_UREU1              Reviewed;         360 AA.
AC   B5ZBT4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=UUR10_0483;
OS   Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=565575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33699 / Western;
RA   Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT   "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL   Submitted (OCT-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; CP001184; ACI59868.1; -; Genomic_DNA.
DR   RefSeq; WP_004027185.1; NC_011374.1.
DR   AlphaFoldDB; B5ZBT4; -.
DR   SMR; B5ZBT4; -.
DR   STRING; 565575.UUR10_0483; -.
DR   PRIDE; B5ZBT4; -.
DR   EnsemblBacteria; ACI59868; ACI59868; UUR10_0483.
DR   GeneID; 45016025; -.
DR   KEGG; uue:UUR10_0483; -.
DR   eggNOG; COG0389; Bacteria.
DR   HOGENOM; CLU_012348_1_1_14; -.
DR   OMA; KVRRYDF; -.
DR   OrthoDB; 442163at2; -.
DR   Proteomes; UP000002018; 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; Transferase.
FT   CHAIN           1..360
FT                   /note="DNA polymerase IV"
FT                   /id="PRO_1000137149"
FT   DOMAIN          9..191
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   SITE            18
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ   SEQUENCE   360 AA;  41339 MW;  8F870781CCDE05D1 CRC64;
     MQSSGQKIIM HLDIDAFYAT VSELLHPEYK NFPIAVGSLN SRTGIISSPN YLARSYGVKS
     AMPIFLAKEL CPNLIILPCE HDIYQTYSNH FFQIVNKYCN KVEITSIDEC FIDATNSIKK
     YHNNVRLLAA KIQNEVKNKL NLSISVGISF NKTIAKMATE LNKPFGISII DENKITNLIH
     ELDISKIPFI GEIKSQELYA INIFKIKELI ASNNKQKASL VLGSMYQNLV NDLKGLNEIK
     TIEDDIYKSI SHSKTFNEDL NDFYEISNEL NELISNVVNR LKKHNLMTNN ISINIKYPNF
     QTKVKQKRLD YYTDDYQTIF LAIKNLFKKV YKDELVRLIG VSLNKLVPKE SVKKQLFLFD
 
 
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