DPO4_STRP6
ID DPO4_STRP6 Reviewed; 364 AA.
AC Q5XA48;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=M6_Spy1580;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
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; CP000003; AAT87715.1; -; Genomic_DNA.
DR RefSeq; WP_002983063.1; NC_006086.1.
DR AlphaFoldDB; Q5XA48; -.
DR SMR; Q5XA48; -.
DR EnsemblBacteria; AAT87715; AAT87715; M6_Spy1580.
DR KEGG; spa:M6_Spy1580; -.
DR HOGENOM; CLU_012348_1_2_9; -.
DR OMA; KVRRYDF; -.
DR Proteomes; UP000001167; 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..364
FT /note="DNA polymerase IV"
FT /id="PRO_0000173958"
FT DOMAIN 14..198
FT /note="UmuC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT SITE 23
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ SEQUENCE 364 AA; 40760 MW; C19C0B44D5E09532 CRC64;
MLIFPLINDT SRKIIHIDMD AFFAAVEERD NPALKGKPVV IGKDPRETGG RGVVSTCNYE
ARKYGIHSAM SSKEAYERCP KAIFISGNYE KYRTVGDQIR RIFKRYTDVV EPMSIDEAYL
DVTNNKLGIK SAVKIAKLIQ HDIWKEVGLT CSAGVSYNKF LAKLASDFEK PHGLTLVLKE
DALCFLAKLP IEKFHGVGKK SVEKLHDMGI YTGQDLLAVP EMTLIDHFGR FGFDLYRKAR
GISNSPVKSD RIRKSIGSER TYAKLLYQET DIKAEISKNA KRVAALLQDH KKLGKTIVLK
VRYADFTTLT KRVTLPELTR NAAQIEQVAG DIFDSLSENP AGIRLLGVTM TNLEDKVADI
SLDL
