DPO41_MYCTU
ID DPO41_MYCTU Reviewed; 468 AA.
AC P9WNT3; L0T6Y5; P63985; Q10787;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=DNA polymerase IV 1;
DE Short=Pol IV 1;
DE EC=2.7.7.7;
GN Name=dinB1; Synonyms=dinX; OrderedLocusNames=Rv1537; ORFNames=MTCY48.28c;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- SEQUENCE CAUTION:
CC Sequence=CCP44301.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP44301.1; ALT_INIT; Genomic_DNA.
DR PIR; F70760; F70760.
DR RefSeq; NP_216053.3; NC_000962.3.
DR AlphaFoldDB; P9WNT3; -.
DR SMR; P9WNT3; -.
DR IntAct; P9WNT3; 1.
DR STRING; 83332.Rv1537; -.
DR PaxDb; P9WNT3; -.
DR DNASU; 886414; -.
DR GeneID; 886414; -.
DR KEGG; mtu:Rv1537; -.
DR PATRIC; fig|83332.12.peg.1717; -.
DR TubercuList; Rv1537; -.
DR eggNOG; COG0389; Bacteria.
DR OMA; KVRRYDF; -.
DR PhylomeDB; P9WNT3; -.
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; 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 1: Evidence at protein level;
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..468
FT /note="DNA polymerase IV 1"
FT /id="PRO_0000173924"
FT DOMAIN 6..188
FT /note="UmuC"
FT ACT_SITE 106
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 15
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 49765 MW; F6CF59BC5FAEA1D8 CRC64;
MESRWVLHLD MDAFFASVEQ LTRPTLRGRP VLVGGLGGRG VVAGASYEAR AYGARSAMPM
HQARRLIGVT AVVLPPRGVV YGIASRRVFD TVRGLVPVVE QLSFDEAFAE PPQLAGAVAE
DVETFCERLR RRVRDETGLI ASVGAGSGKQ IAKIASGLAK PDGIRVVRHA EEQALLSGLP
VRRLWGIGPV AEEKLHRLGI ETIGQLAALS DAEAANILGA TIGPALHRLA RGIDDRPVVE
RAEAKQISAE STFAVDLTTM EQLHEAIDSI AEHAHQRLLR DGRGARTITV KLKKSDMSTL
TRSATMPYPT TDAGALFTVA RRLLPDPLQI GPIRLLGVGF SGLSDIRQES LFADSDLTQE
TAAAHYVETP GAVVPAAHDA TMWRVGDDVA HPELGHGWVQ GAGHGVVTVR FETRGSGPGS
ARTFPVDTGD ISNASPLDSL DWPDYIGQLS VEGSAGASAP TVDDVGDR
