ID   DPO42_MYCTU             Reviewed;         346 AA.
AC   P9WNT1; L0TD22; P63987; P95102;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=DNA polymerase IV 2;
DE            Short=Pol IV 2;
DE            EC=2.7.7.7;
GN   Name=dinB2; Synonyms=dinP; OrderedLocusNames=Rv3056; ORFNames=MTCY22D7.25c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL123456; CCP45865.1; -; Genomic_DNA.
DR   PIR; A70649; A70649.
DR   RefSeq; NP_217572.1; NC_000962.3.
DR   RefSeq; WP_003899898.1; NZ_NVQJ01000011.1.
DR   AlphaFoldDB; P9WNT1; -.
DR   SMR; P9WNT1; -.
DR   IntAct; P9WNT1; 1.
DR   STRING; 83332.Rv3056; -.
DR   PaxDb; P9WNT1; -.
DR   DNASU; 887519; -.
DR   GeneID; 887519; -.
DR   KEGG; mtu:Rv3056; -.
DR   TubercuList; Rv3056; -.
DR   eggNOG; COG0389; Bacteria.
DR   OMA; DLDQFQA; -.
DR   PhylomeDB; P9WNT1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:0009432; P:SOS response; IBA:GO_Central.
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..346
FT                   /note="DNA polymerase IV 2"
FT                   /id="PRO_0000173926"
FT   DOMAIN          9..191
FT                   /note="UmuC"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            18
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  37562 MW;  5046A2A8C7274AF5 CRC64;
     MPTAAPRWIL HVDLDQFLAS VELLRHPELA GLPVIVGGNG DPTEPRKVVT CASYEARAYG
     VRAGMPLRTA ARRCPEATFL PSNPAAYNAA SEEVVALLRD LGYPVEVWGW DEAYLAVAPG
     TPDDPIEVAE EIRKVILSQT GLSCSIGISD NKQRAKIATG LAKPAGIYQL TDANWMAIMG
     DRTVEALWGV GPKTTKRLAK LGINTVYQLA HTDSGLLMST FGPRTALWLL LAKGGGDTEV
     SAQAWVPRSR SHAVTFPRDL TCRSEMESAV TELAQRTLNE VVASSRTVTR VAVTVRTATF
     YTRTKIRKLQ APSTDPDVIT AAARHVLDLF ELDRPVRLLG VRLELA