DPO4_UREPA
ID DPO4_UREPA Reviewed; 360 AA.
AC Q9PQ53;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=UU437;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF30849.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF222894; AAF30849.1; ALT_INIT; Genomic_DNA.
DR PIR; D82891; D82891.
DR RefSeq; WP_006689004.1; NC_002162.1.
DR AlphaFoldDB; Q9PQ53; -.
DR SMR; Q9PQ53; -.
DR STRING; 273119.UU437; -.
DR EnsemblBacteria; AAF30849; AAF30849; UU437.
DR GeneID; 29672432; -.
DR KEGG; uur:UU437; -.
DR eggNOG; COG0389; Bacteria.
DR HOGENOM; CLU_012348_1_1_14; -.
DR OMA; KVRRYDF; -.
DR Proteomes; UP000000423; 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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 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..360
FT /note="DNA polymerase IV"
FT /id="PRO_0000173961"
FT DOMAIN 9..191
FT /note="UmuC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT ACT_SITE 109
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT SITE 18
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ SEQUENCE 360 AA; 41723 MW; 9BCEE8FD496C86FD CRC64;
MKNNHQKIIM HLDIDAFYAT VSELLHPEYK NFPIAVGSLN SRTGIISSPN YLARSYGVKA
AMPIFLAKEL CPNLIILPSE HNIYQSYSKH FFQIINKYTN KIEITSIDEC FIDATDLVKK
YHNNIRLLAT KIQKEIKNKL NLSISIGISY NKTIAKMATE LNKPSGISII DENKIINLIY
ELNINKIPYI GEIKSQELYA INIFKIKELI ATENKQKISL VLGSIYQNLV NDLKGLSKIK
IIDEDIYKTI SHSKTFNEDL NDFYEISNEM NDLILTVTNR LKKCNLMTNN ISIYIKYPSF
KTKIKQKQLT YYTDDYQTIF LAIKNLFKIM YKDETIRLIG ISLNKLVKKE NVKKQLFLFD
