ID   DPO1_MYCTO              Reviewed;         904 AA.
AC   P9WNU4; L0TA70; P0A550; Q07700;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=MT1665;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3'-5' and 5'-3' exonuclease activity. {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   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45935.1; -; Genomic_DNA.
DR   PIR; C70559; C70559.
DR   RefSeq; WP_003408063.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNU4; -.
DR   SMR; P9WNU4; -.
DR   PRIDE; P9WNU4; -.
DR   EnsemblBacteria; AAK45935; AAK45935; MT1665.
DR   KEGG; mtc:MT1665; -.
DR   PATRIC; fig|83331.31.peg.1788; -.
DR   HOGENOM; CLU_004675_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10133; PTHR10133; 2.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   TIGRFAMs; TIGR00593; pola; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..904
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000427066"
FT   DOMAIN          186..279
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          317..493
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   904 AA;  98472 MW;  1C8E560FE5F74323 CRC64;
     MVTTASAPSE DRAKPTLMLL DGNSLAFRAF YALPAENFKT RGGLTTNAVY GFTAMLINLL
     RDEAPTHIAA AFDVSRQTFR LQRYPEYKAN RSSTPDEFAG QIDITKEVLG ALGITVLSEP
     GFEADDLIAT LATQAENEGY RVLVVTGDRD ALQLVSDDVT VLYPRKGVSE LTRFTPEAVV
     EKYGLTPRQY PDFAALRGDP SDNLPGIPGV GEKTAAKWIA EYGSLRSLVD NVDAVRGKVG
     DALRANLASV VRNRELTDLV RDVPLAQTPD TLRLQPWDRD HIHRLFDDLE FRVLRDRLFD
     TLAAAGGPEV DEGFDVRGGA LAPGTVRQWL AEHAGDGRRA GLTVVGTHLP HGGDATAMAV
     AAADGEGAYL DTATLTPDDD AALAAWLADP AKPKALHEAK AAVHDLAGRG WTLEGVTSDT
     ALAAYLVRPG QRSFTLDDLS LRYLRRELRA ETPQQQQLSL LDDDDTDAET IQTTILRARA
     VIDLADALDA ELARIDSTAL LGEMELPVQR VLAKMESAGI AVDLPMLTEL QSQFGDQIRD
     AAEAAYGVIG KQINLGSPKQ LQVVLFDELG MPKTKRTKTG YTTDADALQS LFDKTGHPFL
     QHLLAHRDVT RLKVTVDGLL QAVAADGRIH TTFNQTIAAT GRLSSTEPNL QNIPIRTDAG
     RRIRDAFVVG DGYAELMTAD YSQIEMRIMA HLSGDEGLIE AFNTGEDLHS FVASRAFGVP
     IDEVTGELRR RVKAMSYGLA YGLSAYGLSQ QLKISTEEAN EQMDAYFARF GGVRDYLRAV
     VERARKDGYT STVLGRRRYL PELDSSNRQV REAAERAALN APIQGSAADI IKVAMIQVDK
     ALNEAQLASR MLLQVHDELL FEIAPGERER VEALVRDKMG GAYPLDVPLE VSVGYGRSWD
     AAAH