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DPO4_PSEMY
ID   DPO4_PSEMY              Reviewed;         352 AA.
AC   A4XT24;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Pmen_1726;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP84490.1; -; Genomic_DNA.
DR   RefSeq; WP_012018239.1; NC_009439.1.
DR   AlphaFoldDB; A4XT24; -.
DR   SMR; A4XT24; -.
DR   STRING; 399739.Pmen_1726; -.
DR   EnsemblBacteria; ABP84490; ABP84490; Pmen_1726.
DR   KEGG; pmy:Pmen_1726; -.
DR   PATRIC; fig|399739.8.peg.1750; -.
DR   eggNOG; COG0389; Bacteria.
DR   HOGENOM; CLU_012348_1_2_6; -.
DR   OMA; VKKFHGV; -.
DR   OrthoDB; 442163at2; -.
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; Transferase.
FT   CHAIN           1..352
FT                   /note="DNA polymerase IV"
FT                   /id="PRO_1000084915"
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   352 AA;  39840 MW;  161D3A129994E955 CRC64;
     MKQRKIIHID CDCFYAAIEM RDDPSLANRP LAVGGSADRR GVIATCNYEA RAYGVRSAMS
     SRHALKLCPD LLIVKPRFEV YRSVSREIHG IFRQFTDLIE PLSLDEAYLD VSDSPHFAGS
     ATRIAQEIRR RVAQELHITV SAGVAPNKFL AKIASDWRKP NGLFVITPDQ VDEFVTALPV
     SKLHGVGKVT ADKLTRLGIR TCLDLRDWNK LALVREFGSF GERLWRLAHG IDEREVKVDS
     RRQSLSVEHT YDQDLPDLQS CLEKLPALLE EMNGRLQRLD ASYRPDKPFV KVKFHDFTQT
     TLEQAGASRD LDSYRQLLAS AHARGDKPVR LLGVGVRLHD LRGRQEQLEL FA
 
 
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