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DPO4_BACVZ
ID   DPO4_BACVZ              Reviewed;         414 AA.
AC   A7Z6F3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=RBAM_022180;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS74579.1; -; Genomic_DNA.
DR   RefSeq; WP_012117936.1; NC_009725.2.
DR   AlphaFoldDB; A7Z6F3; -.
DR   SMR; A7Z6F3; -.
DR   STRING; 326423.RBAM_022180; -.
DR   PRIDE; A7Z6F3; -.
DR   EnsemblBacteria; ABS74579; ABS74579; RBAM_022180.
DR   KEGG; bay:RBAM_022180; -.
DR   HOGENOM; CLU_012348_1_1_9; -.
DR   OMA; KVRRYDF; -.
DR   Proteomes; UP000001120; 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..414
FT                   /note="DNA polymerase IV"
FT                   /id="PRO_1000084878"
FT   DOMAIN          8..189
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   REGION          394..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   BINDING         12
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            17
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ   SEQUENCE   414 AA;  47144 MW;  7256FE75FD4F2E9F CRC64;
     MAGKGRIIFH IDMNSFYASV EMAYDPSLRG KPIAVAGNVK ERKGIIVTCS YEARARGVKT
     TMPVWRAKRL CPELIVVPPN FDRYRSSSKE MFSILREYTD LVEPVSIDEG YMDITDTPHS
     HRAYETAEDI QARLQKELLL PSSIGIAPNK FLAKMASDMK KPLGITILRK RELPDVLWPL
     PIEEMHGIGT KTAEKIKTLG IKTIGDLAKG DEHALKTLLG INGPRLKDKA NGIHPAEVNP
     ERIYEFKSVG NSSTLSHDSA DWDELTGVFD RLALSVSERL QRKEVMACRL FIMIRYADWK
     TVTRSMTLSN PADQKKDIME AAMELFDKHW NQNPVRLLGI TGTELVEKQQ AYKQLDLFSF
     KEDAKDEPIF QMMNELNEKY GQNLIRKGAV IKKEESKTRG TSFNRDFFQD EKKR
 
 
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