DPO4_SALTY
ID DPO4_SALTY Reviewed; 351 AA.
AC P63989; Q8XET9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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}; Synonyms=dinP;
GN OrderedLocusNames=STM0313;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL19270.1; -; Genomic_DNA.
DR RefSeq; NP_459311.1; NC_003197.2.
DR RefSeq; WP_001226198.1; NC_003197.2.
DR AlphaFoldDB; P63989; -.
DR SMR; P63989; -.
DR STRING; 99287.STM0313; -.
DR PaxDb; P63989; -.
DR EnsemblBacteria; AAL19270; AAL19270; STM0313.
DR GeneID; 1251832; -.
DR KEGG; stm:STM0313; -.
DR PATRIC; fig|99287.12.peg.332; -.
DR HOGENOM; CLU_012348_1_2_6; -.
DR OMA; CKPDGLL; -.
DR PhylomeDB; P63989; -.
DR BioCyc; SENT99287:STM0313-MON; -.
DR Proteomes; UP000001014; 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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR GO; GO:0009432; P:SOS response; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..351
FT /note="DNA polymerase IV"
FT /id="PRO_0000173941"
FT DOMAIN 4..185
FT /note="UmuC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT ACT_SITE 104
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT SITE 13
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ SEQUENCE 351 AA; 39658 MW; EB5E5CAB4F4C11ED CRC64;
MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARQ FGVRSAMPTA
MALKLCPHLT LLPGRFDAYK EASRHVRDIF SRYTSLIEPL SLDEAWLDVT DSPHCYGSAT
LIAREIRQTI FNELQLTASA GVAPVKFLAK IASDLNKPNG QYVITPADVP DFLKTLPLAK
IPGVGKVSAA KLENMGLRTC GDIQQCDLAM LLKRFGKFGR VLWERSQGID ERDVNSERLR
KSVGVERTLA EDIHEWSDCE AIIEHLYPEL ERRLAIVKPD LLIARQGVKL KFNDFQQTTQ
EHVWPQLNKE DLITTARKTW DERRGERGVR LVGLHVTLLD PQLERQLVLG L
