ID   DPO1_LACLM              Reviewed;         877 AA.
AC   O32801; A2RNU5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=llmg_2425;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9226255; DOI=10.1128/jb.179.14.4473-4479.1997;
RA   Duwat P., Cochu A., Ehrlich S.D., Gruss A.;
RT   "Characterization of Lactococcus lactis UV-sensitive mutants obtained by
RT   ISS1 transposition.";
RL   J. Bacteriol. 179:4473-4479(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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   -!- SUBUNIT: Single-chain monomer with multiple functions.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; U78771; AAB64184.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98989.1; -; Genomic_DNA.
DR   RefSeq; WP_011836063.1; NZ_WJVF01000024.1.
DR   AlphaFoldDB; O32801; -.
DR   SMR; O32801; -.
DR   STRING; 416870.llmg_2425; -.
DR   EnsemblBacteria; CAL98989; CAL98989; llmg_2425.
DR   KEGG; llm:llmg_2425; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_9; -.
DR   OMA; NRPPMPD; -.
DR   PhylomeDB; O32801; -.
DR   BioCyc; LLAC416870:LLMG_RS12160-MON; -.
DR   Proteomes; UP000000364; 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..877
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101244"
FT   DOMAIN          180..272
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          312..468
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        585
FT                   /note="V -> E (in Ref. 1; AAB64184)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   877 AA;  98866 MW;  214179C9CDC3A983 CRC64;
     MEDKNRLLLI DGSSVAFRAF FALYNQLDRF KAPNGLHTNA IFAFHTMLSS LMERIQPTHV
     LIAFDAGKTT FRTEMFADYK GGRSKTPDEF REQLPFIKEM IEKLGIRHYE LANYEADDII
     GTLDKMAEAP DVNFDVTIVT GDKDMIQLVD GNTRVEISKK GVAEFEEFTP DYLLEKMGLT
     PSQFIDLKAL MGDSSDNYPG VTKVGEKTGL KLLQEFGSLE NLYENVETLK ASKMKDNLIA
     DKEMAFLSQQ LATINTKAPL EIGLEDTLLK EKNVAELGQF YDEMGFSQFK SKLLADGGGE
     VTDETVSEEI KFEIVTDKSS VASVNADDFF YLETLGENYH REQIVAFAWG NSEKIYVSKN
     LDLLTEMKFP ENTYDFKKNR VLLSHLNIEL PLVKFDAMLA KYLISTTEDN KISTIARLFD
     VGHLATDEEI FGKGTKLALP DDEILFDHLA RKIRVLARAK EKMMAELIEN EQEHLLSDME
     LPLAEVLAKM EITGISVSQN TLEEIGAENE EKLASLTREI YDLAGEEFNI NSPKQLGVIL
     FEKLQLPVGK KTKTGYSTAV DVLEDLAALS PVVAKILEYR QINKVQSTYV KGLIPQIADD
     GKIHTRYVQD LTQTGRLSSV DPNLQNIPVR LEEGRKIRKA FVPSQDSLLL SSDYSQIELR
     VLAHISADEH LIDAFKHGAD IHTSTAMRVF GIEKAEDVTA NDRRNAKAVN FGVVYGISDF
     GLARNLGITR KDAKNYIETY FERYPGIKTY MENIVREARD KGFVETMSHR RRKIPDINAR
     NFNVRGFAER TAINSPIQGS AADILKIAMI NLDKALTERQ SKSKLLLQVH DEIILDVPLE
     ELEDIKALVK QTMEEAIELA VPLKVDDNTG KTWYEAK