DPO4_LEGPC
ID DPO4_LEGPC Reviewed; 355 AA.
AC A5IH02;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=LPC_2746;
OS Legionella pneumophila (strain Corby).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=400673;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Corby;
RA Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT "Identification and characterization of a new conjugation/ type IVA
RT secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT genomic island.";
RL Submitted (NOV-2006) 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; CP000675; ABQ56652.1; -; Genomic_DNA.
DR RefSeq; WP_011945735.1; NC_009494.2.
DR AlphaFoldDB; A5IH02; -.
DR SMR; A5IH02; -.
DR PRIDE; A5IH02; -.
DR KEGG; lpc:LPC_2746; -.
DR HOGENOM; CLU_012348_1_2_6; -.
DR OMA; KVRRYDF; -.
DR BioCyc; LPNE400673:LPC_RS03215-MON; -.
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..355
FT /note="DNA polymerase IV"
FT /id="PRO_1000137138"
FT DOMAIN 7..188
FT /note="UmuC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT ACT_SITE 107
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT SITE 16
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ SEQUENCE 355 AA; 40305 MW; 8517604104F4AFAC CRC64;
MNPIRKIIHI DMDCFYAAIE MRDFPELANK PIAVGGDAKR RGVIATCNYA ARQFGIRSAM
PTAHALKLCR ELILRPVRMD VYQKESQYIR SLLTEYTDLI EPLSLDEAYL DVTESTQCQG
SATWIAEEIR ARIYQTRQLT ASAGIAPNKS LAKIASDWHK PNGQMVIRPE DVSAFVLDLP
VRKLFGVGPK MEEKLGALNI KTCADLQRYS VEYLLQKFGT MGQRLYELAR GIDNRPVNPE
RIRKSISVEE TYPKDLPNSE ACLAVLPELM ARLEARIQRA GKISGIHNLF VKLKFNDFQQ
TTIERVMDKL DLIVLRQLIQ EGFARRGMPV RLLGIGIKLK QENTYQSVQL PLLDL
