ID   DPO1_LACLA              Reviewed;         877 AA.
AC   Q9CDS1;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=LL2142; ORFNames=L0270;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK06240.1; -; Genomic_DNA.
DR   PIR; F86892; F86892.
DR   RefSeq; NP_268299.1; NC_002662.1.
DR   RefSeq; WP_010906334.1; NC_002662.1.
DR   AlphaFoldDB; Q9CDS1; -.
DR   SMR; Q9CDS1; -.
DR   STRING; 272623.L0270; -.
DR   PaxDb; Q9CDS1; -.
DR   EnsemblBacteria; AAK06240; AAK06240; L0270.
DR   KEGG; lla:L0270; -.
DR   PATRIC; fig|272623.7.peg.2301; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_9; -.
DR   OMA; NRPPMPD; -.
DR   Proteomes; UP000002196; 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; Reference proteome; Transferase.
FT   CHAIN           1..877
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101243"
FT   DOMAIN          180..270
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          308..468
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   877 AA;  98733 MW;  A5C2BEB92FF98FB2 CRC64;
     MENKDRLLLI DGSSVAFRAF FALYNQIDRF KAPNGLHTNA IFAFHTMLSS LMERIEPTHV
     LIAFDAGKTT FRTEMFADYK GGRSKTPDEF REQLPFIKEM IEKLGIRHYE LANYEADDII
     GTLDKMAEAP NVNFDVTIVT GDKDMIQLVD GNTRVEISKK GVAEFEEFTP DYLLEKMGLT
     PAQFIDLKAL MGDSSDNYPG VTKVGEKTGL KLLQEFGSLE NLYENVDSLK ASKMKENLIA
     DKEMAFLSQQ LATINTKAPI EIGLDDTLLK GKKVDELSQF YDEMGFAQFK SKLLAEAGGE
     VTDEKVVDEI DFEIVTDGSI SEKVNADDFF YLETLGENYH REQIVAFAWG NAEKIYVSKN
     IDLLTKMKFP ENTYDFKKNR VLLSHLDIEL PLVKFDAMLA KYLISTTEDN KISTIARLFN
     SGHLATDEEI FGKGTKIALP DDAVLFEHLA RKIKVLALAK EKMMAELLEN EQEHLLSDME
     LPLAEVLAKM EITGIAVSQN TLEEIGAENE EKLASLTREI YDLAGEEFNI NSPKQLGVIL
     FEKLQLPVGK KTKTGYSTAV DVLEDLAALS PVVAKILEYR QINKVQSTYV KGLIPQIADD
     GKIHTRYVQD LTQTGRLSSV DPNLQNIPVR LEEGRKIRKA FVPSKDSLLL SSDYSQIELR
     VLAHISGDEH LIDAFKHGAD IHTSTAMRVF GIEKAEDVTA NDRRNAKAVN FGVVYGISDF
     GLARNLGITR KDAKNYIETY FERYPGIKTY MENIVREARD KGFVETMSHR RRKIPDINAR
     NFNVRGFAER TAINSPIQGS AADILKIAMI NLDKALSARD FKSKLLLQVH DEIILDVPLE
     ELDEIKVLVK QTMEEAIELA VPLKVDENTG KTWYEAK