ID   DPO41_RHILO             Reviewed;         438 AA.
AC   Q98LV1;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=DNA polymerase IV 1;
DE            Short=Pol IV 1;
DE            EC=2.7.7.7;
GN   Name=dinB1; OrderedLocusNames=mlr0866;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(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 (By
CC       similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR   EMBL; BA000012; BAB48362.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q98LV1; -.
DR   SMR; Q98LV1; -.
DR   STRING; 266835.14021750; -.
DR   PRIDE; Q98LV1; -.
DR   EnsemblBacteria; BAB48362; BAB48362; BAB48362.
DR   KEGG; mlo:mlr0866; -.
DR   eggNOG; COG0389; Bacteria.
DR   HOGENOM; CLU_012348_1_0_5; -.
DR   OMA; KVRRYDF; -.
DR   Proteomes; UP000000552; 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; Transferase.
FT   CHAIN           1..438
FT                   /note="DNA polymerase IV 1"
FT                   /id="PRO_0000173936"
FT   DOMAIN          46..226
FT                   /note="UmuC"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            55
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   438 AA;  48490 MW;  48BDE1A21BF9CD4F CRC64;
     MAAPVNNPDH GFCRDCLTFQ RSETRRCERC GSPRLARHPE LYRLHLAHID CDAFYAAIEK
     RDNPALKDKP LIIGGGKRGV VSTACYIARI RGVRSAMPMF KALEACPEAV VIPPNMEKYV
     RVGREVRAMM QTLTPLVEPL SIDEAFLDFA GTERLHGQPP AVVLARFALA VEKEIGITVS
     AGLSYCKFLA KIASDFRKPR GFSVIGEAEA VGFLATKPVT MIWGVGKAFN ATLERDGIRT
     IGQLQTMERG DLMRRYGVMG DRLYRLSRGE DVRRVDPDQD AKSVSAETTF DTDIASLDEL
     VSVLRGLSEK VSARLKKSGI AGRTVVLKLK TQDFKLRTRN RQLGDPTRLA DRIFQAGVEL
     LRKETDGTKF RLLGIGVSDL SDDDKADPPD LVDVQSRKRA MAEGAIDALR DKFGRKAVET
     GYTFGRGRDA HPPEPLED