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DPO4_PSEU2
ID   DPO4_PSEU2              Reviewed;         354 AA.
AC   Q4ZWM4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Psyr_1397;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY36448.1; -; Genomic_DNA.
DR   RefSeq; WP_004406165.1; NC_007005.1.
DR   RefSeq; YP_234486.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZWM4; -.
DR   SMR; Q4ZWM4; -.
DR   STRING; 205918.Psyr_1397; -.
DR   EnsemblBacteria; AAY36448; AAY36448; Psyr_1397.
DR   KEGG; psb:Psyr_1397; -.
DR   PATRIC; fig|205918.7.peg.1431; -.
DR   eggNOG; COG0389; Bacteria.
DR   HOGENOM; CLU_012348_1_2_6; -.
DR   OMA; KVRRYDF; -.
DR   Proteomes; UP000000426; 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; Transferase.
FT   CHAIN           1..354
FT                   /note="DNA polymerase IV"
FT                   /id="PRO_1000084919"
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   354 AA;  39305 MW;  C1D35B92C98BD339 CRC64;
     MTQRKIIHID CDCFYAAIEM RDEPDLAGKP LAVGGSAERR GVIATCNYEA RAYGVRSAMS
     SRHALKLCPD LTIVKPRMDA YKEASREIHT IFRDYTDLIE PLSLDEAFLD VSEAGHFSGS
     ATRIAQDIRR RVSNQLHITV SAGVAPNKFL AKIASDWKKP NGLFVITPDQ VEEFVASLPV
     TKLHGVGKVT ADKLGRLGIV DCADLRSRSK LALVREFGSF GERLWSLAHG IDDRPVQNDS
     RRQSVSVENT YDTDLPDLAA CLEKLPDLLE TLSGRMARME GQYRPGKPFV KVKFHDFTQT
     TLEQSGAGRD LGSYEQLLAQ AFARGGKPVR LLGIGVRLHD LRAAHEQLEL FSRQ
 
 
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