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Database: UniProt
Entry: N2B181_9FIRM
LinkDB: N2B181_9FIRM
Original site: N2B181_9FIRM 
ID   N2B181_9FIRM            Unreviewed;       415 AA.
AC   N2B181;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=DNA polymerase IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE            Short=Pol IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE            EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01113};
GN   Name=dinB {ECO:0000256|HAMAP-Rule:MF_01113};
GN   ORFNames=C823_01642 {ECO:0000313|EMBL:EMZ30409.1};
OS   Eubacterium plexicaudatum ASF492.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ30409.1, ECO:0000313|Proteomes:UP000012589};
RN   [1] {ECO:0000313|EMBL:EMZ30409.1, ECO:0000313|Proteomes:UP000012589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF492 {ECO:0000313|EMBL:EMZ30409.1,
RC   ECO:0000313|Proteomes:UP000012589};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01113};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01113};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01113};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC       {ECO:0000256|ARBA:ARBA00010945, ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMZ30409.1}.
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DR   EMBL; AQFT01000053; EMZ30409.1; -; Genomic_DNA.
DR   RefSeq; WP_004058762.1; NZ_AQFT02000001.1.
DR   AlphaFoldDB; N2B181; -.
DR   STRING; 1235802.C823_01642; -.
DR   GeneID; 78436544; -.
DR   PATRIC; fig|1235802.3.peg.1743; -.
DR   eggNOG; COG0389; Bacteria.
DR   HOGENOM; CLU_012348_1_1_9; -.
DR   OrthoDB; 9808813at2; -.
DR   Proteomes; UP000012589; Unassembled WGS sequence.
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; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.1170.60; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 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   PANTHER; PTHR11076; DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11076:SF35; DNA REPAIR PROTEIN HOMOLOG YOBH; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_01113};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_01113}; DNA replication {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Mutator protein {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012589};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01113}.
FT   DOMAIN          6..188
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   BINDING         106
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   SITE            15
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ   SEQUENCE   415 AA;  46917 MW;  D1DF520A2B7C6857 CRC64;
     MGDRVILHSD INCCYASIEH LHHPELAGKP LAVGGDPEAR HGIVLTADYI AKKYGVKTGM
     ALWQAKQVCP DITFVSPRMD LYLRFSRMAH EIYAEYTDRQ EPYGIDECWL DVTGSSFLKG
     DGLLIAQEIS RRMKSELGIT VSVGVSFNKI FAKLGSDYKK PDAITTMYKS EFKQKAWSLP
     VADLLYVGKS TNRKLALFGI KTIGDLARAD EDVLNSHLGK MGSILWSFAN GYDDSPVKLE
     NTHAPIKSVG NSTTTPKDLV CDEDVKIVLY ILAESVAARL RENGFRCRVV EISVRDNELF
     SFTRQKKIDH ATNITGEIAA YAYQIFKENY NWSKPIRSVG VRGADLVTDN YWELIDLFSS
     VEKREKQMKM DSAVDEIRRR FGFYSIQRGL MYRDRILSAV NAKEEYTVHP HGYFG
//
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